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}.
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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