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Serine protease inhibitor Kazal-type 2 (Acrosin-trypsin inhibitor) (Epididymis tissue protein Li 172) (HUSI-II)

 ISK2_HUMAN              Reviewed;          84 AA.
P20155; Q6FGH2;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
20-JUN-2018, entry version 150.
RecName: 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;
Name=SPINK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1704312; DOI=10.1016/0014-5793(91)80099-O;
Moeritz A., Lilja H., Fink E.;
"Molecular cloning and sequence analysis of the cDNA encoding the
human acrosin-trypsin inhibitor (HUSI-II).";
FEBS Lett. 278:127-130(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8428671; DOI=10.1016/0378-1119(93)90138-S;
Moeritz A., Grzeschik K.H., Wingender E., Fink E.;
"Organization and sequence of the gene encoding the human acrosin-
trypsin inhibitor (HUSI-II).";
Gene 123:277-281(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Epididymis;
PubMed=20736409; DOI=10.1074/mcp.M110.001719;
Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W.,
Zhang C., Jin S., Liu J., Zhu P., Liu Y.;
"Systematic mapping and functional analysis of a family of human
epididymal secretory sperm-located proteins.";
Mol. Cell. Proteomics 9:2517-2528(2010).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 24-84, AND PYROGLUTAMATE FORMATION AT GLN-24.
TISSUE=Semen;
PubMed=2226783; DOI=10.1016/0014-5793(90)81273-Q;
Fink E., Hehlein-Fink C., Eulitz M.;
"Amino acid sequence elucidation of human acrosin-trypsin inhibitor
(HUSI-II) reveals that Kazal-type proteinase inhibitors are
structurally related to beta-subunits of glycoprotein hormones.";
FEBS Lett. 270:222-224(1990).
[9]
STRUCTURE BY NMR OF 23-84, FUNCTION, MUTAGENESIS OF PRO-45; ARG-46;
HIS-47 AND PHE-48, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE
BONDS.
PubMed=19422058; DOI=10.1002/prot.22432;
Chen T., Lee T.-R., Liang W.-G., Chang W.-S., Lyu P.-C.;
"Identification of trypsin-inhibitory site and structure determination
of human SPINK2 serine proteinase inhibitor.";
Proteins 77:209-219(2009).
-!- FUNCTION: Strong inhibitor of acrosin in male and/or female
genital tract. Also inhibits trypsin.
{ECO:0000269|PubMed:19422058}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-10200479, EBI-10173507;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-10200479, EBI-3958099;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-10200479, EBI-945833;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed in epididymis (at protein level).
{ECO:0000269|PubMed:20736409}.
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EMBL; M91438; AAB59431.1; -; Genomic_DNA.
EMBL; X57655; CAB37834.1; -; mRNA.
EMBL; M84967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; GU727622; ADU87624.1; -; mRNA.
EMBL; AK312222; BAG35155.1; -; mRNA.
EMBL; CR542135; CAG46932.1; -; mRNA.
EMBL; CH471057; EAX05513.1; -; Genomic_DNA.
EMBL; BC022514; AAH22514.1; -; mRNA.
CCDS; CCDS3508.1; -.
PIR; JU0152; JU0152.
RefSeq; NP_001258650.1; NM_001271721.1.
RefSeq; NP_001258651.1; NM_001271722.1.
RefSeq; NP_066937.1; NM_021114.3.
UniGene; Hs.98243; -.
PDB; 2JXD; NMR; -; A=23-84.
PDBsum; 2JXD; -.
ProteinModelPortal; P20155; -.
SMR; P20155; -.
BioGrid; 112569; 27.
IntAct; P20155; 4.
MEROPS; I01.012; -.
iPTMnet; P20155; -.
PhosphoSitePlus; P20155; -.
DMDM; 123985; -.
PaxDb; P20155; -.
PeptideAtlas; P20155; -.
PRIDE; P20155; -.
ProteomicsDB; 53731; -.
DNASU; 6691; -.
Ensembl; ENST00000248701; ENSP00000248701; ENSG00000128040.
GeneID; 6691; -.
KEGG; hsa:6691; -.
UCSC; uc003hcg.3; human.
CTD; 6691; -.
DisGeNET; 6691; -.
EuPathDB; HostDB:ENSG00000128040.10; -.
GeneCards; SPINK2; -.
HGNC; HGNC:11245; SPINK2.
HPA; CAB020824; -.
HPA; HPA026813; -.
MIM; 605753; gene.
neXtProt; NX_P20155; -.
OpenTargets; ENSG00000128040; -.
PharmGKB; PA36075; -.
eggNOG; ENOG410IP08; Eukaryota.
eggNOG; ENOG410ZF57; LUCA.
GeneTree; ENSGT00530000064285; -.
HOGENOM; HOG000090244; -.
InParanoid; P20155; -.
PhylomeDB; P20155; -.
EvolutionaryTrace; P20155; -.
GeneWiki; SPINK2; -.
GenomeRNAi; 6691; -.
PRO; PR:P20155; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000128040; -.
CleanEx; HS_SPINK2; -.
ExpressionAtlas; P20155; baseline and differential.
Genevisible; P20155; HS.
GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0060046; P:regulation of acrosome reaction; IBA:GO_Central.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
Pfam; PF00050; Kazal_1; 1.
SMART; SM00280; KAZAL; 1.
SUPFAM; SSF100895; SSF100895; 1.
PROSITE; PS00282; KAZAL_1; 1.
PROSITE; PS51465; KAZAL_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Protease inhibitor; Pyrrolidone carboxylic acid;
Reference proteome; Secreted; Serine protease inhibitor; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:2226783}.
CHAIN 24 84 Serine protease inhibitor Kazal-type 2.
/FTId=PRO_0000016561.
DOMAIN 30 84 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
SITE 46 47 Reactive bond.
MOD_RES 24 24 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2226783}.
DISULFID 36 66 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:19422058}.
DISULFID 44 63 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:19422058}.
DISULFID 52 84 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:19422058}.
MUTAGEN 45 45 P->A: No effect on inhibitory activity
towards trypsin.
{ECO:0000269|PubMed:19422058}.
MUTAGEN 46 46 R->A: Loss of inhibitory activity towards
trypsin. {ECO:0000269|PubMed:19422058}.
MUTAGEN 47 47 H->A: Reduces inhibitory activity towards
trypsin. {ECO:0000269|PubMed:19422058}.
MUTAGEN 48 48 F->A: Reduces inhibitory activity towards
trypsin. {ECO:0000269|PubMed:19422058}.
STRAND 27 32 {ECO:0000244|PDB:2JXD}.
STRAND 51 53 {ECO:0000244|PDB:2JXD}.
TURN 62 64 {ECO:0000244|PDB:2JXD}.
HELIX 65 70 {ECO:0000244|PDB:2JXD}.
STRAND 73 75 {ECO:0000244|PDB:2JXD}.
STRAND 78 82 {ECO:0000244|PDB:2JXD}.
SEQUENCE 84 AA; 9291 MW; E1DE1792BFB1BB85 CRC64;
MALSVLRLAL LLLAVTFAAS LIPQFGLFSK YRTPNCSQYR LPGCPRHFNP VCGSDMSTYA
NECTLCMKIR EGGHNIKIIR NGPC


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