位置:首页 > 蛋白库 > ISK13_RAT
ISK13_RAT
ID   ISK13_RAT               Reviewed;          97 AA.
AC   D3ZVP0;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Serine protease inhibitor Kazal-type 13;
DE   Flags: Precursor;
GN   Name=Spink13;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND INDUCTION.
RX   PubMed=23430248; DOI=10.1074/jbc.m112.445866;
RA   Ma L., Yu H., Ni Z., Hu S., Ma W., Chu C., Liu Q., Zhang Y.;
RT   "Spink13, an epididymis-specific gene of the Kazal-type serine protease
RT   inhibitor (SPINK) family, is essential for the acrosomal integrity and male
RT   fertility.";
RL   J. Biol. Chem. 288:10154-10165(2013).
CC   -!- FUNCTION: May be a serine protease inhibitor (By similarity). Essential
CC       for sperm maturation and fertility. Inhibits sperm acrosome reaction,
CC       protecting sperm from premature reaction. {ECO:0000250,
CC       ECO:0000269|PubMed:23430248}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23430248}.
CC       Note=Secreted into the lumen of the initial segment of the epididymis
CC       and binds to sperm. In the initial segment of epididymis, localizes on
CC       the dorsal surface of the acrosomal region of sperm, gradually becomes
CC       more restricted to the acrosomal region in spermatozoa during
CC       epididymal transit.
CC   -!- TISSUE SPECIFICITY: Restricted to the epididymis, with highest levels
CC       in the initial segment, including epithelial cells, lumen, and sperm
CC       (at protein level). Localizes to the sperm heads, where it is
CC       restricted to the acrosomal region in epididymal spermatozoa, but not
CC       in testicular spermatozoa (at protein level).
CC       {ECO:0000269|PubMed:23430248}.
CC   -!- DEVELOPMENTAL STAGE: First expressed at low levels at P15 in the
CC       epididymis. Expression increases from P30 onward. Reaches its highest
CC       level at P120 and remains at a stable level in mature animals.
CC       {ECO:0000269|PubMed:23430248}.
CC   -!- INDUCTION: Up-regulated by testosterone. {ECO:0000269|PubMed:23430248}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR06095461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06095462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06095463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06095464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473971; EDM14640.1; -; Genomic_DNA.
DR   RefSeq; NP_001103009.1; NM_001109539.1.
DR   RefSeq; XP_008770397.1; XM_008772175.2.
DR   AlphaFoldDB; D3ZVP0; -.
DR   SMR; D3ZVP0; -.
DR   STRING; 10116.ENSRNOP00000056043; -.
DR   PaxDb; D3ZVP0; -.
DR   Ensembl; ENSRNOT00000059276; ENSRNOP00000056043; ENSRNOG00000038793.
DR   GeneID; 689570; -.
DR   KEGG; rno:689570; -.
DR   UCSC; RGD:1591057; rat.
DR   CTD; 153218; -.
DR   RGD; 1591057; Spink13.
DR   eggNOG; KOG3649; Eukaryota.
DR   GeneTree; ENSGT00400000023784; -.
DR   HOGENOM; CLU_161738_0_0_1; -.
DR   InParanoid; D3ZVP0; -.
DR   OMA; FFCVEQW; -.
DR   OrthoDB; 1550974at2759; -.
DR   PhylomeDB; D3ZVP0; -.
DR   PRO; PR:D3ZVP0; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Proteomes; UP000234681; Chromosome 18.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:1902225; P:negative regulation of acrosome reaction; IMP:UniProtKB.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF00050; Kazal_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   PROSITE; PS00282; KAZAL_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..97
FT                   /note="Serine protease inhibitor Kazal-type 13"
FT                   /id="PRO_0000423009"
FT   DOMAIN          36..97
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            58..59
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        42..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        56..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        64..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   97 AA;  11415 MW;  8890820824783120 CRC64;
     MTRRGCWPHR IIFSLILLTW THVTLAALIR SHTFSNWPKP PCKMYYPIDP DYEANCPDVI
     ALVCATNGLN YKNECFFCID RWEFGPHIEF VKYGKCE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025