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ISK13_MOUSE
ID   ISK13_MOUSE             Reviewed;          97 AA.
AC   Q3UTS8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Serine protease inhibitor Kazal-type 13;
DE   AltName: Full=Serine protease inhibitor Kazal-type 5-like 3;
DE   Flags: Precursor;
GN   Name=Spink13; Synonyms=Spink5l3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted into the
CC       lumen of the initial segment of the epididymis and binds to sperm. In
CC       the initial segment of epididymis, localizes on the dorsal surface of
CC       the acrosomal region of sperm, gradually becomes more restricted to the
CC       acrosomal region in spermatozoa during epididymal transit (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; AK139149; BAE23902.1; -; mRNA.
DR   CCDS; CCDS50305.1; -.
DR   RefSeq; NP_001161895.1; NM_001168423.2.
DR   AlphaFoldDB; Q3UTS8; -.
DR   SMR; Q3UTS8; -.
DR   STRING; 10090.ENSMUSP00000095165; -.
DR   GlyGen; Q3UTS8; 1 site.
DR   PaxDb; Q3UTS8; -.
DR   PRIDE; Q3UTS8; -.
DR   ProteomicsDB; 267011; -.
DR   Antibodypedia; 49010; 14 antibodies from 7 providers.
DR   Ensembl; ENSMUST00000097557; ENSMUSP00000095165; ENSMUSG00000073551.
DR   Ensembl; ENSMUST00000235190; ENSMUSP00000157623; ENSMUSG00000073551.
DR   GeneID; 100038417; -.
DR   KEGG; mmu:100038417; -.
DR   UCSC; uc012bdy.1; mouse.
DR   CTD; 153218; -.
DR   MGI; MGI:3642511; Spink13.
DR   VEuPathDB; HostDB:ENSMUSG00000073551; -.
DR   eggNOG; KOG3649; Eukaryota.
DR   GeneTree; ENSGT00400000023784; -.
DR   HOGENOM; CLU_161738_0_0_1; -.
DR   InParanoid; Q3UTS8; -.
DR   OMA; FFCVEQW; -.
DR   OrthoDB; 1636538at2759; -.
DR   PhylomeDB; Q3UTS8; -.
DR   BioGRID-ORCS; 100038417; 2 hits in 70 CRISPR screens.
DR   ChiTaRS; Spink13; mouse.
DR   PRO; PR:Q3UTS8; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q3UTS8; protein.
DR   Bgee; ENSMUSG00000073551; Expressed in cortical plate and 10 other tissues.
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; ISS: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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; 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_0000344511"
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   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  11530 MW;  44018E2B02721C5B CRC64;
     MKRSGCWHQR MLLSLVLLTW THVTFSALIR SHNFSRWPKP PCKMYYPIDP DYEANCPDVK
     AYVCATNGLT YKNECFFCID RWEFGPHIQF VKYGKCE
 
 
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