ID SEMG1_HUMAN Reviewed; 462 AA.
AC P04279; Q53ZV0; Q53ZV1; Q53ZV2; Q6X4I9; Q6Y809; Q6Y822; Q6Y823;
AC Q86U64; Q96QM3;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 10-MAY-2017, entry version 177.
DE RecName: Full=Semenogelin-1;
DE AltName: Full=Cancer/testis antigen 103;
DE AltName: Full=Semenogelin I;
DE Short=SGI;
DE Contains:
DE RecName: Full=Alpha-inhibin-92;
DE Contains:
DE RecName: Full=Alpha-inhibin-31;
DE Contains:
DE RecName: Full=Seminal basic protein;
DE Flags: Precursor;
GN Name=SEMG1; Synonyms=SEMG;
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).
RX PubMed=2912989;
RA Lilja H., Abrahamsson P.-A., Lundwall A.;
RT "Semenogelin, the predominant protein in human semen. Primary
RT structure and identification of closely related proteins in the male
RT accessory sex glands and on the spermatozoa.";
RL J. Biol. Chem. 264:1894-1900(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=1517240;
RA Ulvsbaeck M., Lazure C., Lilja H., Spurr N.K., Rao V.V., Loeffler C.,
RA Hansmann I., Lundwall A.;
RT "Gene structure of semenogelin I and II. The predominant proteins in
RT human semen are encoded by two homologous genes on chromosome 20.";
RL J. Biol. Chem. 267:18080-18084(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-79 AND LEU-372.
RX PubMed=14629036; DOI=10.1007/s00239-003-2474-x;
RA Jensen-Seaman M.I., Li W.-H.;
RT "Evolution of the hominoid semenogelin genes, the major proteins of
RT ejaculated semen.";
RL J. Mol. Evol. 57:261-270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-237 AND 241-449, AND VARIANT
RP THR-79.
RX PubMed=14562960; DOI=10.1007/s00239-002-2463-0;
RA Kingan S.B., Tatar M., Rand D.M.;
RT "Reduced polymorphism in the chimpanzee semen coagulating protein,
RT semenogelin I.";
RL J. Mol. Evol. 57:159-169(2003).
RN [9]
RP PROTEIN SEQUENCE OF 108-159.
RX PubMed=3972122; DOI=10.1016/0014-5793(85)81179-0;
RA Lilja H., Jeppsson J.-O.;
RT "Amino acid sequence of the predominant basic protein in human seminal
RT plasma.";
RL FEBS Lett. 182:181-184(1985).
RN [10]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6698208; DOI=10.1016/0014-5793(84)80840-6;
RA Seidah N.G., Ramasharma K., Sairam M.R., Chretien M.;
RT "Partial amino acid sequence of a human seminal plasma peptide with
RT inhibin-like activity.";
RL FEBS Lett. 167:98-102(1984).
RN [11]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6422553; DOI=10.1126/science.6422553;
RA Ramasharma K., Sairam M.R., Seidah N.G., Chretien M., Manjunath P.,
RA Schiller P.W., Yamashiro D., Li C.H.;
RT "Isolation, structure, and synthesis of a human seminal plasma peptide
RT with inhibin-like activity.";
RL Science 223:1199-1202(1984).
RN [12]
RP PROTEIN SEQUENCE OF 316-344.
RX PubMed=2757795;
RA Schneider K., Kausler W., Tripier D., Jouvenal K., Spiteller G.;
RT "Isolation and structure determination of two peptides occurring in
RT human seminal plasma.";
RL Biol. Chem. Hoppe-Seyler 370:353-356(1989).
RN [13]
RP PROTEIN SEQUENCE OF 373-397.
RX PubMed=8444163; DOI=10.1111/j.1432-1033.1993.tb17629.x;
RA Khan Z., Smyth D.G.;
RT "Isolation and identification of N-terminally extended forms of 5-
RT oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-
RT releasing-hormone (TRH)-like peptide present in human semen.";
RL Eur. J. Biochem. 212:35-40(1993).
RN [14]
RP PROTEIN SEQUENCE OF 68-159.
RX PubMed=3889920; DOI=10.1073/pnas.82.12.4041;
RA Li C.H., Hammonds R.G., Ramasharma K., Chung D.;
RT "Human seminal alpha inhibins: isolation, characterization, and
RT structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4041-4044(1985).
RN [15]
RP REVIEW.
RX PubMed=10412373; DOI=10.1007/s000180050346;
RA Robert M., Gagnon C.;
RT "Semenogelin I: a coagulum forming, multifunctional seminal vesicle
RT protein.";
RL Cell. Mol. Life Sci. 55:944-960(1999).
RN [16]
RP INTERACTION WITH EPPIN.
RX PubMed=15590901; DOI=10.1095/biolreprod.104.036483;
RA Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.;
RT "Association of eppin with semenogelin on human spermatozoa.";
RL Biol. Reprod. 72:1064-1070(2005).
RN [17]
RP IDENTIFICATION IN A COMPLEX WITH LTF; CLU AND EPPIN.
RX PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
RA Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
RT "Characterization of an eppin protein complex from human semen and
RT spermatozoa.";
RL Biol. Reprod. 77:476-484(2007).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF CYS-239.
RX PubMed=19889947; DOI=10.1095/biolreprod.109.081331;
RA Mitra A., Richardson R.T., O'Rand M.G.;
RT "Analysis of recombinant human semenogelin as an inhibitor of human
RT sperm motility.";
RL Biol. Reprod. 82:489-496(2010).
CC -!- FUNCTION: Predominant protein in semen. It participates in the
CC formation of a gel matrix entrapping the accessory gland
CC secretions and ejaculated spermatozoa. Fragments of semenogelin
CC and/or fragments of the related proteins may contribute to the
CC activation of progressive sperm movements as the gel-forming
CC proteins are fragmented by KLK3/PSA.
CC {ECO:0000269|PubMed:19889947}.
CC -!- FUNCTION: Alpha-inhibin-92 and alpha-inhibin-31, derived from the
CC proteolytic degradation of semenogelin, inhibit the secretion of
CC pituitary follicle-stimulating hormone.
CC {ECO:0000269|PubMed:19889947}.
CC -!- SUBUNIT: Occurs in disulfide-linked complexes which may also
CC contain two less abundant 71- and 76-kDa semenogelin-related
CC polypeptides. Interacts with EPPIN (via C-terminus); Cys-239 is a
CC critical amino acid for both binding to EPPIN.
CC {ECO:0000269|PubMed:15590901, ECO:0000269|PubMed:17567961}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04279-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04279-2; Sequence=VSP_004385;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Seminal vesicle.
CC -!- PTM: Transglutaminase substrate.
CC -!- PTM: Rapidly cleaved after ejaculation by KLK3/PSA, resulting in
CC liquefaction of the semen coagulum and the progressive release of
CC motile spermatozoa.
CC -!- SIMILARITY: Belongs to the semenogelin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shackled sperm - Issue
CC 62 of September 2005;
CC URL="http://web.expasy.org/spotlight/back_issues/062";
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DR EMBL; J04440; AAB59506.1; -; mRNA.
DR EMBL; Z47556; CAA87636.1; -; Genomic_DNA.
DR EMBL; M81650; AAA18168.1; -; Genomic_DNA.
DR EMBL; AY256465; AAP82462.1; -; Genomic_DNA.
DR EMBL; AY256466; AAP82463.1; -; Genomic_DNA.
DR EMBL; AY256467; AAP82464.1; -; Genomic_DNA.
DR EMBL; AY256468; AAP82465.1; -; Genomic_DNA.
DR EMBL; AY256469; AAP82466.1; -; Genomic_DNA.
DR EMBL; BT007177; AAP35841.1; -; mRNA.
DR EMBL; AL049767; CAB53523.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75871.1; -; Genomic_DNA.
DR EMBL; BC007096; AAH07096.1; -; mRNA.
DR EMBL; BC055416; AAH55416.1; -; mRNA.
DR EMBL; AY174423; AAO20112.1; -; Genomic_DNA.
DR EMBL; AY174424; AAO20113.1; -; Genomic_DNA.
DR EMBL; AY174437; AAO20126.1; -; Genomic_DNA.
DR CCDS; CCDS13345.1; -. [P04279-1]
DR PIR; B43412; WTHUB.
DR RefSeq; NP_002998.1; NM_003007.4. [P04279-1]
DR UniGene; Hs.1968; -.
DR ProteinModelPortal; P04279; -.
DR BioGrid; 112306; 29.
DR IntAct; P04279; 6.
DR MINT; MINT-2862979; -.
DR STRING; 9606.ENSP00000361867; -.
DR iPTMnet; P04279; -.
DR PhosphoSitePlus; P04279; -.
DR BioMuta; SEMG1; -.
DR DMDM; 134426; -.
DR MaxQB; P04279; -.
DR PaxDb; P04279; -.
DR PeptideAtlas; P04279; -.
DR PRIDE; P04279; -.
DR DNASU; 6406; -.
DR Ensembl; ENST00000372781; ENSP00000361867; ENSG00000124233. [P04279-1]
DR GeneID; 6406; -.
DR KEGG; hsa:6406; -.
DR UCSC; uc002xni.3; human. [P04279-1]
DR CTD; 6406; -.
DR DisGeNET; 6406; -.
DR GeneCards; SEMG1; -.
DR HGNC; HGNC:10742; SEMG1.
DR HPA; HPA042476; -.
DR MIM; 182140; gene.
DR neXtProt; NX_P04279; -.
DR OpenTargets; ENSG00000124233; -.
DR PharmGKB; PA35664; -.
DR eggNOG; ENOG410KG9B; Eukaryota.
DR eggNOG; ENOG4110SI0; LUCA.
DR GeneTree; ENSGT00390000020321; -.
DR HOVERGEN; HBG054194; -.
DR InParanoid; P04279; -.
DR OMA; FHVIVIH; -.
DR OrthoDB; EOG091G03E6; -.
DR PhylomeDB; P04279; -.
DR TreeFam; TF342360; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR GeneWiki; Semenogelin_I; -.
DR GenomeRNAi; 6406; -.
DR PMAP-CutDB; P04279; -.
DR PRO; PR:P04279; -.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; ENSG00000124233; -.
DR CleanEx; HS_SEMG1; -.
DR Genevisible; P04279; HS.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IMP:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0050817; P:coagulation; IDA:UniProtKB.
DR GO; GO:0007320; P:insemination; TAS:UniProtKB.
DR GO; GO:0090281; P:negative regulation of calcium ion import; IDA:CACAO.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; IDA:CACAO.
DR GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
DR InterPro; IPR008836; Semenogelin.
DR Pfam; PF05474; Semenogelin; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Polymorphism; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 23
FT CHAIN 24 462 Semenogelin-1.
FT /FTId=PRO_0000032351.
FT PEPTIDE 68 159 Alpha-inhibin-92.
FT /FTId=PRO_0000032352.
FT PEPTIDE 108 159 Seminal basic protein.
FT /FTId=PRO_0000032353.
FT PEPTIDE 108 138 Alpha-inhibin-31.
FT /FTId=PRO_0000032354.
FT REPEAT 70 129 3-1.
FT REPEAT 141 200 2-1.
FT REPEAT 201 260 2-2.
FT REPEAT 381 439 3-2.
FT REGION 70 439 Repeat-rich region. {ECO:0000250}.
FT REGION 164 283 Interaction with EPPIN.
FT {ECO:0000269|PubMed:15590901}.
FT REGION 261 380 2 X 60 AA tandem repeats, type 1.
FT MOD_RES 24 24 Pyrrolidone carboxylic acid.
FT {ECO:0000305}.
FT DISULFID 239 239 Interchain.
FT VAR_SEQ 312 371 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.4}.
FT /FTId=VSP_004385.
FT VARIANT 58 58 E -> G (in dbSNP:rs11559137).
FT /FTId=VAR_053650.
FT VARIANT 79 79 S -> T (less common genetic variant;
FT dbSNP:rs2301366).
FT {ECO:0000269|PubMed:14562960,
FT ECO:0000269|PubMed:14629036}.
FT /FTId=VAR_005610.
FT VARIANT 108 108 H -> R (in dbSNP:rs2233884).
FT /FTId=VAR_053651.
FT VARIANT 372 372 R -> L (in dbSNP:rs2233887).
FT {ECO:0000269|PubMed:14629036}.
FT /FTId=VAR_022679.
FT MUTAGEN 239 239 C->G: Abrogates binding to EPPIN and do
FT not inhibit spem motility.
FT {ECO:0000269|PubMed:19889947}.
FT CONFLICT 100 100 L -> Q (in Ref. 3; AAP82463).
FT {ECO:0000305}.
FT CONFLICT 235 237 QTS -> LRT (in Ref. 8; AAO20112/
FT AAO20113). {ECO:0000305}.
FT CONFLICT 321 321 K -> L (in Ref. 12; AA sequence).
FT {ECO:0000305}.
FT CONFLICT 423 423 K -> N (in Ref. 2; CAA87636/AAA18168).
FT {ECO:0000305}.
FT CONFLICT 457 457 R -> Q (in Ref. 4 and 7). {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 313 461 ipfam:Semenogelin [T]
FT MYHIT 1 332 ipfam:Semenogelin [T]
SQ SEQUENCE 462 AA; 52131 MW; 760F48EFCF2FA702 CRC64;
MKPNIIFVLS LLLILEKQAA VMGQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK
GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK
GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG
AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP
AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY
GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY
GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH
EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT
//
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