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DescriptionRecName: Full=Serine protease inhibitor Kazal-type 2; AltName: Full=Acrosin-trypsin inhibitor; AltName: Full=Epididymis tissue protein Li 172; AltName: Full=HUSI-II; Flags: Precursor;
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MyHits synonymsISK2_HUMAN , P20155 , Q6FGH2 , E1DE1792BFB1BB85
match map segment
iprf:KAZAL_2 ipat:KAZAL_1 ipfam:Kazal_1 ismart:KAZAL  
Legends: 1, Pyrrolidone carboxylic acid. {ECO:0000269|PubMed:2226783}; 2, MUTAGEN P->A: No effect on inhibitory activity towards trypsin. {ECO:0000269|PubMed:19422058}; 3, MUTAGEN R->A: Loss of inhibitory activity towards trypsin. {ECO:0000269|PubMed:19422058}; 4, MUTAGEN H->A: Reduces inhibitory activity towards trypsin. {ECO:0000269|PubMed:19422058}; 5, MUTAGEN F->A: Reduces inhibitory activity towards trypsin. {ECO:0000269|PubMed:19422058}; 6, SIGNAL {ECO:0000269|PubMed:2226783}; 7, CHAIN Serine protease inhibitor Kazal-type 2; 8, Kazal-like. {ECO:0000255|PROSITE- ProRule:PRU00798}; 9, SITE Reactive bond; 10, ipat:KAZAL_1 [T]; 11, STRAND {ECO:0000244|PDB:2JXD}; 12, TURN {ECO:0000244|PDB:2JXD}; 13, HELIX {ECO:0000244|PDB:2JXD}.
ID   ISK2_HUMAN              Reviewed;          84 AA.
AC   P20155; Q6FGH2;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   02-NOV-2016, entry version 143.
DE   RecName: Full=Serine protease inhibitor Kazal-type 2;
DE   AltName: Full=Acrosin-trypsin inhibitor;
DE   AltName: Full=Epididymis tissue protein Li 172;
DE   AltName: Full=HUSI-II;
DE   Flags: Precursor;
GN   Name=SPINK2;
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].
RX   PubMed=1704312; DOI=10.1016/0014-5793(91)80099-O;
RA   Moeritz A., Lilja H., Fink E.;
RT   "Molecular cloning and sequence analysis of the cDNA encoding the
RT   human acrosin-trypsin inhibitor (HUSI-II).";
RL   FEBS Lett. 278:127-130(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8428671; DOI=10.1016/0378-1119(93)90138-S;
RA   Moeritz A., Grzeschik K.H., Wingender E., Fink E.;
RT   "Organization and sequence of the gene encoding the human acrosin-
RT   trypsin inhibitor (HUSI-II).";
RL   Gene 123:277-281(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
RX   PubMed=20736409; DOI=10.1074/mcp.M110.001719;
RA   Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W.,
RA   Zhang C., Jin S., Liu J., Zhu P., Liu Y.;
RT   "Systematic mapping and functional analysis of a family of human
RT   epididymal secretory sperm-located proteins.";
RL   Mol. Cell. Proteomics 9:2517-2528(2010).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   PROTEIN SEQUENCE OF 24-84, AND PYROGLUTAMATE FORMATION AT GLN-24.
RC   TISSUE=Semen;
RX   PubMed=2226783; DOI=10.1016/0014-5793(90)81273-Q;
RA   Fink E., Hehlein-Fink C., Eulitz M.;
RT   "Amino acid sequence elucidation of human acrosin-trypsin inhibitor
RT   (HUSI-II) reveals that Kazal-type proteinase inhibitors are
RT   structurally related to beta-subunits of glycoprotein hormones.";
RL   FEBS Lett. 270:222-224(1990).
RN   [9]
RP   STRUCTURE BY NMR OF 23-84, FUNCTION, MUTAGENESIS OF PRO-45; ARG-46;
RP   HIS-47 AND PHE-48, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE
RP   BONDS.
RX   PubMed=19422058; DOI=10.1002/prot.22432;
RA   Chen T., Lee T.-R., Liang W.-G., Chang W.-S., Lyu P.-C.;
RT   "Identification of trypsin-inhibitory site and structure determination
RT   of human SPINK2 serine proteinase inhibitor.";
RL   Proteins 77:209-219(2009).
CC   -!- FUNCTION: Strong inhibitor of acrosin in male and/or female
CC       genital tract. Also inhibits trypsin.
CC       {ECO:0000269|PubMed:19422058}.
CC   -!- INTERACTION:
CC       Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-10200479, EBI-10173507;
CC       P26371:KRTAP5-9; NbExp=3; IntAct=EBI-10200479, EBI-3958099;
CC       Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-10200479, EBI-945833;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in epididymis (at protein level).
CC       {ECO:0000269|PubMed:20736409}.
CC   -!- SIMILARITY: Contains 1 Kazal-like domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00798}.
DR   EMBL; M91438; AAB59431.1; -; Genomic_DNA.
DR   EMBL; X57655; CAB37834.1; -; mRNA.
DR   EMBL; M84967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GU727622; ADU87624.1; -; mRNA.
DR   EMBL; AK312222; BAG35155.1; -; mRNA.
DR   EMBL; CR542135; CAG46932.1; -; mRNA.
DR   EMBL; CH471057; EAX05513.1; -; Genomic_DNA.
DR   EMBL; BC022514; AAH22514.1; -; mRNA.
DR   CCDS; CCDS3508.1; -.
DR   PIR; JU0152; JU0152.
DR   RefSeq; NP_001258650.1; NM_001271721.1.
DR   RefSeq; NP_001258651.1; NM_001271722.1.
DR   RefSeq; NP_066937.1; NM_021114.3.
DR   UniGene; Hs.98243; -.
DR   PDB; 2JXD; NMR; -; A=23-84.
DR   PDBsum; 2JXD; -.
DR   ProteinModelPortal; P20155; -.
DR   SMR; P20155; -.
DR   BioGrid; 112569; 26.
DR   IntAct; P20155; 4.
DR   STRING; 9606.ENSP00000248701; -.
DR   MEROPS; I01.012; -.
DR   iPTMnet; P20155; -.
DR   PhosphoSitePlus; P20155; -.
DR   DMDM; 123985; -.
DR   EPD; P20155; -.
DR   PaxDb; P20155; -.
DR   PeptideAtlas; P20155; -.
DR   PRIDE; P20155; -.
DR   DNASU; 6691; -.
DR   Ensembl; ENST00000248701; ENSP00000248701; ENSG00000128040.
DR   GeneID; 6691; -.
DR   KEGG; hsa:6691; -.
DR   UCSC; uc003hcg.3; human.
DR   CTD; 6691; -.
DR   DisGeNET; 6691; -.
DR   GeneCards; SPINK2; -.
DR   HGNC; HGNC:11245; SPINK2.
DR   HPA; CAB020824; -.
DR   HPA; HPA026813; -.
DR   MIM; 605753; gene.
DR   neXtProt; NX_P20155; -.
DR   OpenTargets; ENSG00000128040; -.
DR   PharmGKB; PA36075; -.
DR   eggNOG; ENOG410IP08; Eukaryota.
DR   eggNOG; ENOG410ZF57; LUCA.
DR   GeneTree; ENSGT00530000064285; -.
DR   HOGENOM; HOG000090244; -.
DR   InParanoid; P20155; -.
DR   PhylomeDB; P20155; -.
DR   BioCyc; ZFISH:ENSG00000128040-MONOMER; -.
DR   EvolutionaryTrace; P20155; -.
DR   GeneWiki; SPINK2; -.
DR   GenomeRNAi; 6691; -.
DR   PRO; PR:P20155; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000128040; -.
DR   CleanEx; HS_SPINK2; -.
DR   ExpressionAtlas; P20155; baseline and differential.
DR   Genevisible; P20155; HS.
DR   GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0060046; P:regulation of acrosome reaction; IBA:GO_Central.
DR   InterPro; IPR002350; Kazal_dom.
DR   Pfam; PF00050; Kazal_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   PROSITE; PS00282; KAZAL_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Protease inhibitor; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL        1     23       {ECO:0000269|PubMed:2226783}.
FT   CHAIN        24     84       Serine protease inhibitor Kazal-type 2.
FT                                /FTId=PRO_0000016561.
FT   DOMAIN       30     84       Kazal-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   SITE         46     47       Reactive bond.
FT   MOD_RES      24     24       Pyrrolidone carboxylic acid.
FT                                {ECO:0000269|PubMed:2226783}.
FT   DISULFID     36     66       {ECO:0000255|PROSITE-ProRule:PRU00798,
FT                                ECO:0000269|PubMed:19422058}.
FT   DISULFID     44     63       {ECO:0000255|PROSITE-ProRule:PRU00798,
FT                                ECO:0000269|PubMed:19422058}.
FT   DISULFID     52     84       {ECO:0000255|PROSITE-ProRule:PRU00798,
FT                                ECO:0000269|PubMed:19422058}.
FT   MUTAGEN      45     45       P->A: No effect on inhibitory activity
FT                                towards trypsin.
FT                                {ECO:0000269|PubMed:19422058}.
FT   MUTAGEN      46     46       R->A: Loss of inhibitory activity towards
FT                                trypsin. {ECO:0000269|PubMed:19422058}.
FT   MUTAGEN      47     47       H->A: Reduces inhibitory activity towards
FT                                trypsin. {ECO:0000269|PubMed:19422058}.
FT   MUTAGEN      48     48       F->A: Reduces inhibitory activity towards
FT                                trypsin. {ECO:0000269|PubMed:19422058}.
FT   STRAND       27     32       {ECO:0000244|PDB:2JXD}.
FT   STRAND       51     53       {ECO:0000244|PDB:2JXD}.
FT   TURN         62     64       {ECO:0000244|PDB:2JXD}.
FT   HELIX        65     70       {ECO:0000244|PDB:2JXD}.
FT   STRAND       73     75       {ECO:0000244|PDB:2JXD}.
FT   STRAND       78     82       {ECO:0000244|PDB:2JXD}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        30     84       iprf:KAZAL_2 [T]
FT   MYHIT        44     66       ipat:KAZAL_1 [T]
FT   MYHIT        36     84       ipfam:Kazal_1 [T]
FT   MYHIT        35     84       ismart:KAZAL [T]
SQ   SEQUENCE   84 AA;  9291 MW;  E1DE1792BFB1BB85 CRC64;
     MALSVLRLAL LLLAVTFAAS LIPQFGLFSK YRTPNCSQYR LPGCPRHFNP VCGSDMSTYA
     NECTLCMKIR EGGHNIKIIR NGPC
//