ISK12_MOUSE
ID ISK12_MOUSE Reviewed; 87 AA.
AC Q9D256;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serine protease inhibitor Kazal-type 12;
DE Flags: Precursor;
GN Name=Spink12;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=FVB/N; TISSUE=Epididymis;
RX PubMed=16930550; DOI=10.1016/j.bbrc.2006.08.023;
RA Jalkanen J., Kotimaeki M., Huhtaniemi I., Poutanen M.;
RT "Novel epididymal protease inhibitors with Kazal or WAP family domain.";
RL Biochem. Biophys. Res. Commun. 349:245-254(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
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).
RN [3]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Inhibits trypsin. {ECO:0000269|PubMed:16930550}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in epydiymis, in the caput.
CC {ECO:0000269|PubMed:16930550}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI45915.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI45917.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABD93327.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB32081.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; DQ437332; ABD93327.1; ALT_INIT; mRNA.
DR EMBL; AK020352; BAB32081.2; ALT_INIT; mRNA.
DR EMBL; AK136616; BAE23072.1; ALT_INIT; mRNA.
DR EMBL; BC145914; AAI45915.1; ALT_INIT; mRNA.
DR EMBL; BC145916; AAI45917.1; ALT_INIT; mRNA.
DR CCDS; CCDS29225.1; -.
DR RefSeq; NP_084337.1; NM_030061.3.
DR AlphaFoldDB; Q9D256; -.
DR SMR; Q9D256; -.
DR STRING; 10090.ENSMUSP00000080025; -.
DR MEROPS; I01.976; -.
DR PaxDb; Q9D256; -.
DR PRIDE; Q9D256; -.
DR ProteomicsDB; 269100; -.
DR DNASU; 78242; -.
DR Ensembl; ENSMUST00000081271; ENSMUSP00000080025; ENSMUSG00000061144.
DR GeneID; 78242; -.
DR KEGG; mmu:78242; -.
DR UCSC; uc008eus.1; mouse.
DR CTD; 78242; -.
DR MGI; MGI:1925492; Spink12.
DR VEuPathDB; HostDB:ENSMUSG00000061144; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00900000141664; -.
DR InParanoid; Q9D256; -.
DR OMA; IHKPVCG; -.
DR OrthoDB; 1636538at2759; -.
DR PhylomeDB; Q9D256; -.
DR BioGRID-ORCS; 78242; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9D256; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D256; protein.
DR Bgee; ENSMUSG00000061144; Expressed in uterine cervix and 23 other tissues.
DR ExpressionAtlas; Q9D256; baseline and differential.
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:0045861; P:negative regulation of proteolysis; IDA:MGI.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001239; Prot_inh_Kazal-m.
DR Pfam; PF00050; Kazal_1; 1.
DR PRINTS; PR00290; KAZALINHBTR.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR PROSITE; PS00282; KAZAL_1; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..87
FT /note="Serine protease inhibitor Kazal-type 12"
FT /id="PRO_0000302143"
FT DOMAIN 26..87
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 48..49
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 32..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 54..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 87 AA; 9353 MW; 17E61BC003F830CB CRC64;
MKPAGAFLLL ISLACLFLSV DAVSQGGFQA FCSNYEKTLA PDGKSCPKTH KPVCGTDGKT
YQNRCAFCQT AMERSLGKLG FKHEGKC