MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Atrial natriuretic peptide-converting enzyme; EC=3.4.21.-; AltName: Full=Corin; AltName: Full=Heart-specific serine proteinase ATC2; AltName: Full=Pro-ANP-converting enzyme; AltName: Full=Transmembrane protease serine 10; Contains: RecName: Full=Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Contains: RecName: Full=Atrial natriuretic peptide-converting enzyme, activated protease fragment; Contains: RecName: Full=Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment; Contains: RecName: Full=Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment; Contains: RecName: Full=Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment; |
 |
|
| MyHits synonyms | CORIN_HUMAN , Q9Y5Q5 , B0ZBE3 , Q2TBD2 , Q4W5E5 , Q4W5G6 , Q9UHY2 , A3F1CB8EBB676F78 |
 Legends: 1, ACT_SITE Charge relay system. {ECO:0000250}; 2, ACT_SITE Charge relay system; 3, N-linked (GlcNAc...) asparagine. {ECO:0000255}; 4, VARIANT C -> Y (in dbSNP:rs2289433). {ECO:0000269|PubMed:10329693, ECO:0000269|PubMed:15489334}; 5, VARIANT K -> E (in PEE5; dbSNP:rs387906894). {ECO:0000269|PubMed:22437503}; 6, VARIANT D -> G (in dbSNP:rs13105608); 7, VARIANT S -> G (in PEE5; dbSNP:rs387906895). {ECO:0000269|PubMed:22437503}; 8, VARIANT H -> R (in dbSNP:rs11934749). {ECO:0000269|PubMed:10329693, ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17918732}; 9, MUTAGEN D->A: Impairs cell membrane targeting; when associated with A-30. {ECO:0000269|PubMed:21518754}; 10, MUTAGEN M->A: Impairs cell membrane targeting; when associated with A-26. {ECO:0000269|PubMed:21518754}; 11, MUTAGEN R->A: Does not affect autocatalytic cleavage. {ECO:0000269|PubMed:21288900}; 12, MUTAGEN R->A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide- converting enzyme, 160 kDa soluble fragment. {ECO:0000269|PubMed:21288900}; 13, MUTAGEN R->A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide- converting enzyme, 100 kDa soluble fragment. {ECO:0000269|PubMed:21288900}; 14, MUTAGEN R->A: Loss of activity towards NPPA. {ECO:0000269|PubMed:14559895, ECO:0000269|PubMed:21288900}; 15, MUTAGEN S->A: Loss of activity towards NPPA. {ECO:0000269|PubMed:10880574, ECO:0000269|PubMed:14559895, ECO:0000269|PubMed:21288900}; 16, CONFLICT W -> R (in Ref. 4; AAF21966). {ECO:0000305}; 17, CONFLICT K -> R (in Ref. 4; AAF21966). {ECO:0000305}; 18, CHAIN Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment. {ECO:0000305}; 19, CHAIN Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment. {ECO:0000305}; 20, CHAIN Atrial natriuretic peptide-converting enzyme, activated protease fragment. {ECO:0000305}; 21, TOPO_DOM Cytoplasmic. {ECO:0000255}; 22, TRANSMEM Helical; Signal-anchor for type II membrane protein. {ECO:0000255}; 23, FZ 1. {ECO:0000255|PROSITE- ProRule:PRU00090}; 24, LDL-receptor class A 1. {ECO:0000255|PROSITE-ProRule:PRU00124}; 25, LDL-receptor class A 2. {ECO:0000255|PROSITE-ProRule:PRU00124}; 26, LDL-receptor class A 3. {ECO:0000255|PROSITE-ProRule:PRU00124}; 27, LDL-receptor class A 4. {ECO:0000255|PROSITE-ProRule:PRU00124}; 28, FZ 2. {ECO:0000255|PROSITE- ProRule:PRU00090}; 29, LDL-receptor class A 5. {ECO:0000255|PROSITE-ProRule:PRU00124}; 30, LDL-receptor class A 6. {ECO:0000255|PROSITE-ProRule:PRU00124}; 31, LDL-receptor class A 7. {ECO:0000255|PROSITE-ProRule:PRU00124}; 32, Peptidase S1. {ECO:0000255|PROSITE- ProRule:PRU00274}; 33, MOTIF DDNN motif; 34, SITE Cleavage; by autolysis; 35, SITE Cleavage. {ECO:0000305}; 36, VAR_SEQ Missing (in isoform 2). {ECO:0000305}; 37, ismart:LDLa [T]; 38, ismart:SR [T]; 39, ipat:TRYPSIN_SER [T]; 40, ipfam:Ldl_recept_a [T]; 41, ipat:LDLRA_1 [T]; 42, ipfam:Fz [T]; 43, iprf:LDLRA_2 [T]; 44, ismart:FRI [T]; 45, ipfam:SRCR_2 [T].
| |
ID CORIN_HUMAN Reviewed; 1042 AA.
AC Q9Y5Q5; B0ZBE3; Q2TBD2; Q4W5E5; Q4W5G6; Q9UHY2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 10-MAY-2017, entry version 164.
DE RecName: Full=Atrial natriuretic peptide-converting enzyme;
DE EC=3.4.21.-;
DE AltName: Full=Corin;
DE AltName: Full=Heart-specific serine proteinase ATC2;
DE AltName: Full=Pro-ANP-converting enzyme;
DE AltName: Full=Transmembrane protease serine 10;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, N-terminal propeptide;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, activated protease fragment;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment;
GN Name=CORIN; Synonyms=CRN, TMPRSS10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP VARIANTS TYR-13 AND ARG-525.
RC TISSUE=Heart;
RX PubMed=10329693; DOI=10.1074/jbc.274.21.14926;
RA Yan W., Sheng N., Seto M., Morser J., Wu Q.;
RT "Corin, a mosaic transmembrane serine protease encoded by a novel cDNA
RT from human heart.";
RL J. Biol. Chem. 274:14926-14935(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP TYR-13 AND ARG-525.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 734-1040.
RC TISSUE=Heart;
RX PubMed=11082206; DOI=10.1046/j.1432-1033.2000.01806.x;
RA Hooper J.D., Scarman A.L., Clarke B.E., Normyle J.F., Antalis T.M.;
RT "Localization of the mosaic transmembrane serine protease corin to
RT heart myocytes.";
RL Eur. J. Biochem. 267:6931-6937(2000).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF SER-985.
RX PubMed=10880574; DOI=10.1073/pnas.150149097;
RA Yan W., Wu F., Morser J., Wu Q.;
RT "Corin, a transmembrane cardiac serine protease, acts as a pro-atrial
RT natriuretic peptide-converting enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8525-8529(2000).
RN [6]
RP ACTIVATION, MUTAGENESIS OF ARG-801 AND SER-985, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=14559895; DOI=10.1074/jbc.M309991200;
RA Knappe S., Wu F., Masikat M.R., Morser J., Wu Q.;
RT "Functional analysis of the transmembrane domain and activation
RT cleavage of human corin: design and characterization of a soluble
RT corin.";
RL J. Biol. Chem. 278:52363-52370(2003).
RN [7]
RP PROTEOLYTIC PROCESSING, GLYCOSYLATION, AND DISULFIDE BONDS.
RX PubMed=17660514; DOI=10.1074/jbc.M703687200;
RA Liao X., Wang W., Chen S., Wu Q.;
RT "Role of glycosylation in corin zymogen activation.";
RL J. Biol. Chem. 282:27728-27735(2007).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19751717; DOI=10.1016/j.cca.2009.09.004;
RA Peleg A., Jaffe A.S., Hasin Y.;
RT "Enzyme-linked immunoabsorbent assay for detection of human serine
RT protease corin in blood.";
RL Clin. Chim. Acta 409:85-89(2009).
RN [9]
RP SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP ARG-134; ARG-164; ARG-180; ARG-213; ARG-239; ARG-244; ARG-427; ARG-801
RP AND SER-985.
RX PubMed=21288900; DOI=10.1074/jbc.M110.185082;
RA Jiang J., Wu S., Wang W., Chen S., Peng J., Zhang X., Wu Q.;
RT "Ectodomain shedding and autocleavage of the cardiac membrane protease
RT corin.";
RL J. Biol. Chem. 286:10066-10072(2011).
RN [10]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF ASP-26 AND MET-30.
RX PubMed=21518754; DOI=10.1074/jbc.M110.217570;
RA Qi X., Jiang J., Zhu M., Wu Q.;
RT "Human corin isoforms with different cytoplasmic tails that alter cell
RT surface targeting.";
RL J. Biol. Chem. 286:20963-20969(2011).
RN [11]
RP FUNCTION, INVOLVEMENT IN PEE5, TISSUE SPECIFICITY, AND VARIANTS PEE5
RP GLU-317 AND GLY-472.
RX PubMed=22437503; DOI=10.1038/nature10897;
RA Cui Y., Wang W., Dong N., Lou J., Srinivasan D.K., Cheng W., Huang X.,
RA Liu M., Fang C., Peng J., Chen S., Wu S., Liu Z., Dong L., Zhou Y.,
RA Wu Q.;
RT "Role of corin in trophoblast invasion and uterine spiral artery
RT remodelling in pregnancy.";
RL Nature 484:246-250(2012).
RN [12]
RP VARIANT ARG-525.
RX PubMed=17918732; DOI=10.1002/humu.20617;
RA Guipponi M., Toh M.-Y., Tan J., Park D., Hanson K., Ballana E.,
RA Kwong D., Cannon P.Z.F., Wu Q., Gout A., Delorenzi M., Speed T.P.,
RA Smith R.J.H., Dahl H.-H.M., Petersen M., Teasdale R.D., Estivill X.,
RA Park W.J., Scott H.S.;
RT "An integrated genetic and functional analysis of the role of type II
RT transmembrane serine proteases (TMPRSSs) in hearing loss.";
RL Hum. Mutat. 29:130-141(2008).
CC -!- FUNCTION: Serine-type endopeptidase involved in atrial natriuretic
CC peptide hormone (NPPA) processing. Converts through proteolytic
CC cleavage the non-functional propeptide NPPA into the active
CC hormone, thereby regulating blood pressure in heart and promoting
CC natriuresis, diuresis and vasodilation. Proteolytic cleavage of
CC pro-NPPA also plays a role in female pregnancy by promoting
CC trophoblast invasion and spiral artery remodeling in uterus. Also
CC acts as a regulator of sodium reabsorption in kidney. May also
CC process pro-NPPB the B-type natriuretic peptide.
CC -!- FUNCTION: Isoform 2: has weaker endopeptidase activity compared to
CC isoform 1.
CC -!- ENZYME REGULATION: Inhibited in a dose-dependent manner by non-
CC specific trypsin-like serine protease inhibitors including
CC benzamidine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.28 mM for pyroGlu-Phe-Lys-pNA.HCl
CC {ECO:0000269|PubMed:14559895};
CC KM=3.52 mM for pyroGlu-Pro-Arg-pNA.HCl
CC {ECO:0000269|PubMed:14559895};
CC KM=2.95 mM for H-D-Pro-Phe-Arg-pNA.2HCl
CC {ECO:0000269|PubMed:14559895};
CC KM=1.92 mM for Bz-Ile-Glu-(gamma-OR)-Gly-Arg-pNA.HCl
CC {ECO:0000269|PubMed:14559895};
CC KM=16 mM for pyroGlu-Gly-Arg-pNA.HCl
CC {ECO:0000269|PubMed:14559895};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19751717,
CC ECO:0000269|PubMed:21288900, ECO:0000269|PubMed:21518754}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:19751717,
CC ECO:0000269|PubMed:21288900, ECO:0000269|PubMed:21518754}.
CC Note=May easily detached from the endothelial cell membrane.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type
CC II membrane protein. Note=Less efficiently targeted to the cell
CC membrane compared to isoform 1.
CC -!- SUBCELLULAR LOCATION: Atrial natriuretic peptide-converting
CC enzyme, 180 kDa soluble fragment: Secreted. Note=Soluble form
CC produced following cleavage by ADAM10.
CC -!- SUBCELLULAR LOCATION: Atrial natriuretic peptide-converting
CC enzyme, 160 kDa soluble fragment: Secreted. Note=Soluble form
CC produced following autocatalytic cleavage.
CC -!- SUBCELLULAR LOCATION: Atrial natriuretic peptide-converting
CC enzyme, 100 kDa soluble fragment: Secreted. Note=Soluble form
CC produced following autocatalytic cleavage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=E1, hE1;
CC IsoId=Q9Y5Q5-1; Sequence=Displayed;
CC Name=2; Synonyms=E1a, hE1a;
CC IsoId=Q9Y5Q5-2; Sequence=VSP_043952;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart. Expressed in heart
CC myocytes. Also expressed in pregnant uterus. Detected in blood, in
CC plasma as well as in serum (at protein level).
CC {ECO:0000269|PubMed:10329693, ECO:0000269|PubMed:19751717,
CC ECO:0000269|PubMed:22437503}.
CC -!- DOMAIN: The DDNN motif is required for targeting to the cell
CC membrane and enzyme activation. {ECO:0000269|PubMed:21518754}.
CC -!- PTM: N-glycosylated; required for processing and activation.
CC {ECO:0000269|PubMed:17660514, ECO:0000269|PubMed:21518754}.
CC -!- PTM: Activated through proteolytic processing by a trypsin-like
CC protease; cleaved into a N-terminal propeptide and an activated
CC corin protease fragment. Different soluble forms are produced by
CC cleavage and autocatalytic cleavage: Atrial natriuretic peptide-
CC converting enzyme, 180 kDa soluble fragment is produced by
CC cleavage by ADAM10, while 160 kDa and 100 kDa soluble fragments
CC are produced by autocatalytic cleavage. Cleavage by ADAM10 to
CC produce soluble 180 kDa soluble fragment takes place after the
CC transmembrane region and before FZ 1.
CC -!- PTM: A disulfide bond links the activated corin protease fragment
CC and the N-terminal propeptide. The disulfide bond also links the
CC activated corin protease fragment with soluble fragments (100 kDa,
CC 160 kDa and 180 kDa fragments).
CC -!- DISEASE: Pre-eclampsia/eclampsia 5 (PEE5) [MIM:614595]: A
CC hypertensive disorder of pregnancy characterized by new
CC hypertension (blood pressure 140/90 or greater) presenting after
CC 20 weeks' gestation with clinically relevant proteinuria. It
CC impacts 2 individuals, the mother and her child, both of whom can
CC be severely affected. Preeclampsia is one of the causes of
CC maternal mortality and morbidity worldwide.
CC {ECO:0000269|PubMed:22437503}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Initially named CORIN due to its abundant
CC expression in the heart. {ECO:0000305|PubMed:10329693}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF133845; AAD31850.1; -; mRNA.
DR EMBL; AC092597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104646; AAY40991.1; -; Genomic_DNA.
DR EMBL; AC107068; AAY40917.1; -; Genomic_DNA.
DR EMBL; EU326305; ACA05911.1; -; Genomic_DNA.
DR EMBL; BC110451; AAI10452.1; -; mRNA.
DR EMBL; AF113248; AAF21966.1; -; mRNA.
DR CCDS; CCDS3477.1; -. [Q9Y5Q5-1]
DR RefSeq; NP_001265514.1; NM_001278585.1.
DR RefSeq; NP_006578.2; NM_006587.3. [Q9Y5Q5-1]
DR UniGene; Hs.518618; -.
DR UniGene; Hs.604887; -.
DR ProteinModelPortal; Q9Y5Q5; -.
DR SMR; Q9Y5Q5; -.
DR STRING; 9606.ENSP00000273857; -.
DR MEROPS; S01.019; -.
DR iPTMnet; Q9Y5Q5; -.
DR PhosphoSitePlus; Q9Y5Q5; -.
DR DMDM; 317373348; -.
DR PaxDb; Q9Y5Q5; -.
DR PeptideAtlas; Q9Y5Q5; -.
DR PRIDE; Q9Y5Q5; -.
DR Ensembl; ENST00000273857; ENSP00000273857; ENSG00000145244. [Q9Y5Q5-1]
DR GeneID; 10699; -.
DR KEGG; hsa:10699; -.
DR UCSC; uc003gxm.5; human. [Q9Y5Q5-1]
DR CTD; 10699; -.
DR DisGeNET; 10699; -.
DR GeneCards; CORIN; -.
DR H-InvDB; HIX0024555; -.
DR HGNC; HGNC:19012; CORIN.
DR HPA; HPA070941; -.
DR MalaCards; CORIN; -.
DR MIM; 605236; gene.
DR MIM; 614595; phenotype.
DR neXtProt; NX_Q9Y5Q5; -.
DR OpenTargets; ENSG00000145244; -.
DR PharmGKB; PA134972424; -.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR eggNOG; COG5640; LUCA.
DR GeneTree; ENSGT00870000136375; -.
DR HOGENOM; HOG000060148; -.
DR HOVERGEN; HBG051079; -.
DR InParanoid; Q9Y5Q5; -.
DR KO; K09614; -.
DR OMA; HHVCADG; -.
DR OrthoDB; EOG091G0DF7; -.
DR PhylomeDB; Q9Y5Q5; -.
DR TreeFam; TF351678; -.
DR Reactome; R-HSA-5578768; Physiological factors.
DR ChiTaRS; CORIN; human.
DR GeneWiki; CORIN; -.
DR GenomeRNAi; 10699; -.
DR PRO; PR:Q9Y5Q5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; ENSG00000145244; -.
DR CleanEx; HS_CORIN; -.
DR ExpressionAtlas; Q9Y5Q5; baseline and differential.
DR Genevisible; Q9Y5Q5; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IMP:UniProtKB.
DR GO; GO:0016486; P:peptide hormone processing; IDA:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
DR GO; GO:0035813; P:regulation of renal sodium excretion; ISS:UniProtKB.
DR GO; GO:0003050; P:regulation of systemic arterial blood pressure by atrial natriuretic peptide; IMP:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.10.2000.10; -; 2.
DR InterPro; IPR017052; Corin.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF01392; Fz; 2.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 7.
DR SUPFAM; SSF63501; SSF63501; 2.
DR PROSITE; PS50038; FZ; 2.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autocatalytic cleavage; Cell membrane;
KW Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Polymorphism; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zymogen.
FT CHAIN 1 1042 Atrial natriuretic peptide-converting
FT enzyme.
FT /FTId=PRO_0000088673.
FT CHAIN 1 801 Atrial natriuretic peptide-converting
FT enzyme, N-terminal propeptide.
FT {ECO:0000305}.
FT /FTId=PRO_0000391765.
FT CHAIN 165 801 Atrial natriuretic peptide-converting
FT enzyme, 160 kDa soluble fragment.
FT {ECO:0000305}.
FT /FTId=PRO_0000417984.
FT CHAIN 428 801 Atrial natriuretic peptide-converting
FT enzyme, 100 kDa soluble fragment.
FT {ECO:0000305}.
FT /FTId=PRO_0000417985.
FT CHAIN ? 801 Atrial natriuretic peptide-converting
FT enzyme, 180 kDa soluble fragment.
FT {ECO:0000305}.
FT /FTId=PRO_0000417986.
FT CHAIN 802 1042 Atrial natriuretic peptide-converting
FT enzyme, activated protease fragment.
FT {ECO:0000305}.
FT /FTId=PRO_0000391766.
FT TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 46 66 Helical; Signal-anchor for type II
FT membrane protein. {ECO:0000255}.
FT TOPO_DOM 67 1042 Extracellular. {ECO:0000255}.
FT DOMAIN 134 259 FZ 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00090}.
FT DOMAIN 268 304 LDL-receptor class A 1.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 305 340 LDL-receptor class A 2.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 341 377 LDL-receptor class A 3.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 378 415 LDL-receptor class A 4.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 450 573 FZ 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00090}.
FT DOMAIN 579 614 LDL-receptor class A 5.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 615 653 LDL-receptor class A 6.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 654 689 LDL-receptor class A 7.
FT {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT DOMAIN 690 801 SRCR.
FT DOMAIN 802 1035 Peptidase S1. {ECO:0000255|PROSITE-
FT ProRule:PRU00274}.
FT MOTIF 26 29 DDNN motif.
FT ACT_SITE 843 843 Charge relay system. {ECO:0000250}.
FT ACT_SITE 892 892 Charge relay system. {ECO:0000250}.
FT ACT_SITE 985 985 Charge relay system.
FT SITE 164 165 Cleavage; by autolysis.
FT SITE 427 428 Cleavage; by autolysis.
FT SITE 801 802 Cleavage. {ECO:0000305}.
FT CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 305 305 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 376 376 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 446 446 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 451 451 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 469 469 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 567 567 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 651 651 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 697 697 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 761 761 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1022 1022 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT DISULFID 139 199 {ECO:0000250}.
FT DISULFID 147 192 {ECO:0000250}.
FT DISULFID 183 223 {ECO:0000250}.
FT DISULFID 212 256 {ECO:0000250}.
FT DISULFID 216 240 {ECO:0000250}.
FT DISULFID 269 282 {ECO:0000250}.
FT DISULFID 277 295 {ECO:0000250}.
FT DISULFID 289 304 {ECO:0000250}.
FT DISULFID 306 318 {ECO:0000250}.
FT DISULFID 313 331 {ECO:0000250}.
FT DISULFID 325 340 {ECO:0000250}.
FT DISULFID 342 355 {ECO:0000250}.
FT DISULFID 350 368 {ECO:0000250}.
FT DISULFID 362 377 {ECO:0000250}.
FT DISULFID 379 392 {ECO:0000250}.
FT DISULFID 387 405 {ECO:0000250}.
FT DISULFID 399 414 {ECO:0000250}.
FT DISULFID 455 518 {ECO:0000250}.
FT DISULFID 463 511 {ECO:0000250}.
FT DISULFID 502 540 {ECO:0000250}.
FT DISULFID 529 570 {ECO:0000250}.
FT DISULFID 533 557 {ECO:0000250}.
FT DISULFID 580 592 {ECO:0000250}.
FT DISULFID 587 605 {ECO:0000250}.
FT DISULFID 599 614 {ECO:0000250}.
FT DISULFID 616 630 {ECO:0000250}.
FT DISULFID 624 643 {ECO:0000250}.
FT DISULFID 637 652 {ECO:0000250}.
FT DISULFID 655 667 {ECO:0000250}.
FT DISULFID 662 680 {ECO:0000250}.
FT DISULFID 674 689 {ECO:0000250}.
FT DISULFID 790 912 Interchain (between N-terminal propeptide
FT and activated protease fragment chains).
FT {ECO:0000305|PubMed:17660514}.
FT DISULFID 828 844 {ECO:0000250}.
FT DISULFID 926 991 {ECO:0000250}.
FT DISULFID 955 970 {ECO:0000250}.
FT DISULFID 981 1010 {ECO:0000250}.
FT VAR_SEQ 1 29 Missing (in isoform 2). {ECO:0000305}.
FT /FTId=VSP_043952.
FT VARIANT 13 13 C -> Y (in dbSNP:rs2289433).
FT {ECO:0000269|PubMed:10329693,
FT ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_038000.
FT VARIANT 317 317 K -> E (in PEE5; dbSNP:rs387906894).
FT {ECO:0000269|PubMed:22437503}.
FT /FTId=VAR_067795.
FT VARIANT 444 444 D -> G (in dbSNP:rs13105608).
FT /FTId=VAR_067796.
FT VARIANT 472 472 S -> G (in PEE5; dbSNP:rs387906895).
FT {ECO:0000269|PubMed:22437503}.
FT /FTId=VAR_067797.
FT VARIANT 525 525 H -> R (in dbSNP:rs11934749).
FT {ECO:0000269|PubMed:10329693,
FT ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17918732}.
FT /FTId=VAR_038001.
FT MUTAGEN 26 26 D->A: Impairs cell membrane targeting;
FT when associated with A-30.
FT {ECO:0000269|PubMed:21518754}.
FT MUTAGEN 30 30 M->A: Impairs cell membrane targeting;
FT when associated with A-26.
FT {ECO:0000269|PubMed:21518754}.
FT MUTAGEN 134 134 R->A: Does not affect autocatalytic
FT cleavage. {ECO:0000269|PubMed:21288900}.
FT MUTAGEN 164 164 R->A: Affects autocatalytic cleavage and
FT production of Atrial natriuretic peptide-
FT converting enzyme, 160 kDa soluble
FT fragment. {ECO:0000269|PubMed:21288900}.
FT MUTAGEN 180 180 R->A: Does not affect autocatalytic
FT cleavage. {ECO:0000269|PubMed:21288900}.
FT MUTAGEN 213 213 R->A: Does not affect autocatalytic
FT cleavage. {ECO:0000269|PubMed:21288900}.
FT MUTAGEN 239 239 R->A: Does not affect autocatalytic
FT cleavage. {ECO:0000269|PubMed:21288900}.
FT MUTAGEN 244 244 R->A: Does not affect autocatalytic
FT cleavage. {ECO:0000269|PubMed:21288900}.
FT MUTAGEN 427 427 R->A: Affects autocatalytic cleavage and
FT production of Atrial natriuretic peptide-
FT converting enzyme, 100 kDa soluble
FT fragment. {ECO:0000269|PubMed:21288900}.
FT MUTAGEN 801 801 R->A: Loss of activity towards NPPA.
FT {ECO:0000269|PubMed:14559895,
FT ECO:0000269|PubMed:21288900}.
FT MUTAGEN 985 985 S->A: Loss of activity towards NPPA.
FT {ECO:0000269|PubMed:10880574,
FT ECO:0000269|PubMed:14559895,
FT ECO:0000269|PubMed:21288900}.
FT CONFLICT 854 854 W -> R (in Ref. 4; AAF21966).
FT {ECO:0000305}.
FT CONFLICT 876 876 K -> R (in Ref. 4; AAF21966).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 380 416 ismart:LDLa [T]
FT MYHIT 690 786 ismart:SR [T]
FT MYHIT 617 654 ismart:LDLa [T]
FT MYHIT 979 990 ipat:TRYPSIN_SER [T]
FT MYHIT 305 340 ismart:LDLa [T]
FT MYHIT 802 1030 ipfam:Trypsin [T]
FT MYHIT 579 614 ipfam:Ldl_recept_a [T]
FT MYHIT 667 689 ipat:LDLRA_1 [T]
FT MYHIT 801 1030 ismart:Tryp_SPc [T]
FT MYHIT 139 247 ipfam:Fz [T]
FT MYHIT 305 341 iprf:LDLRA_2 [T]
FT MYHIT 450 573 iprf:FZ [T]
FT MYHIT 579 615 iprf:LDLRA_2 [T]
FT MYHIT 268 304 ismart:LDLa [T]
FT MYHIT 138 248 ismart:FRI [T]
FT MYHIT 711 793 ipfam:SRCR_2 [T]
FT MYHIT 305 340 ipfam:Ldl_recept_a [T]
FT MYHIT 392 414 ipat:LDLRA_1 [T]
FT MYHIT 454 575 ismart:FRI [T]
FT MYHIT 342 377 ipfam:Ldl_recept_a [T]
FT MYHIT 654 690 iprf:LDLRA_2 [T]
FT MYHIT 134 259 iprf:FZ [T]
FT MYHIT 269 304 ipfam:Ldl_recept_a [T]
FT MYHIT 615 653 iprf:LDLRA_2 [T]
FT MYHIT 341 378 iprf:LDLRA_2 [T]
FT MYHIT 455 564 ipfam:Fz [T]
FT MYHIT 655 691 ismart:LDLa [T]
FT MYHIT 579 616 ismart:LDLa [T]
FT MYHIT 341 379 ismart:LDLa [T]
FT MYHIT 268 305 iprf:LDLRA_2 [T]
FT MYHIT 378 415 iprf:LDLRA_2 [T]
FT MYHIT 655 689 ipfam:Ldl_recept_a [T]
FT MYHIT 383 414 ipfam:Ldl_recept_a [T]
FT MYHIT 802 1035 iprf:TRYPSIN_DOM [T]
SQ SEQUENCE 1042 AA; 116486 MW; A3F1CB8EBB676F78 CRC64;
MKQSPALAPE ERCRRAGSPK PVLRADDNNM GNGCSQKLAT ANLLRFLLLV LIPCICALVL
LLVILLSYVG TLQKVYFKSN GSEPLVTDGE IQGSDVILTN TIYNQSTVVS TAHPDQHVPA
WTTDASLPGD QSHRNTSACM NITHSQCQML PYHATLTPLL SVVRNMEMEK FLKFFTYLHR
LSCYQHIMLF GCTLAFPECI IDGDDSHGLL PCRSFCEAAK EGCESVLGMV NYSWPDFLRC
SQFRNQTESS NVSRICFSPQ QENGKQLLCG RGENFLCASG ICIPGKLQCN GYNDCDDWSD
EAHCNCSENL FHCHTGKCLN YSLVCDGYDD CGDLSDEQNC DCNPTTEHRC GDGRCIAMEW
VCDGDHDCVD KSDEVNCSCH SQGLVECRNG QCIPSTFQCD GDEDCKDGSD EENCSVIQTS
CQEGDQRCLY NPCLDSCGGS SLCDPNNSLN NCSQCEPITL ELCMNLPYNS TSYPNYFGHR
TQKEASISWE SSLFPALVQT NCYKYLMFFS CTILVPKCDV NTGEHIPPCR ALCEHSKERC
ESVLGIVGLQ WPEDTDCSQF PEENSDNQTC LMPDEYVEEC SPSHFKCRSG QCVLASRRCD
GQADCDDDSD EENCGCKERD LWECPSNKQC LKHTVICDGF PDCPDYMDEK NCSFCQDDEL
ECANHACVSR DLWCDGEADC SDSSDEWDCV TLSINVNSSS FLMVHRAATE HHVCADGWQE
ILSQLACKQM GLGEPSVTKL IQEQEKEPRW LTLHSNWESL NGTTLHELLV NGQSCESRSK
ISLLCTKQDC GRRPAARMNK RILGGRTSRP GRWPWQCSLQ SEPSGHICGC VLIAKKWVLT
VAHCFEGREN AAVWKVVLGI NNLDHPSVFM QTRFVKTIIL HPRYSRAVVD YDISIVELSE
DISETGYVRP VCLPNPEQWL EPDTYCYITG WGHMGNKMPF KLQEGEVRII SLEHCQSYFD
MKTITTRMIC AGYESGTVDS CMGDSGGPLV CEKPGGRWTL FGLTSWGSVC FSKVLGPGVY
SNVSYFVEWI KRQIYIQTFL LN
//
| |