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CST11_MOUSE
ID   CST11_MOUSE             Reviewed;         139 AA.
AC   Q9D269; Q7M731;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Cystatin-11;
DE   AltName: Full=Cystatin-E1 {ECO:0000303|PubMed:12586767};
DE   AltName: Full=Cystatin-related epididymal spermatogenic protein 2 {ECO:0000303|PubMed:12586767};
DE   Flags: Precursor;
GN   Name=Cst11 {ECO:0000312|MGI:MGI:1925490};
GN   Synonyms=Cres2 {ECO:0000303|PubMed:12586767},
GN   CSTE1 {ECO:0000303|PubMed:12700194};
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], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:DAA01199.1};
RC   TISSUE=Epididymis {ECO:0000312|EMBL:DAA01199.1};
RX   PubMed=12700194; DOI=10.1095/biolreprod.102.014100;
RA   Li Y., Friel P.J., McLean D.J., Griswold M.D.;
RT   "Cystatin E1 and E2, new members of male reproductive tract subgroup within
RT   cystatin type 2 family.";
RL   Biol. Reprod. 69:489-500(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=ICR {ECO:0000312|EMBL:AAL51004.1};
RC   TISSUE=Epididymis {ECO:0000312|EMBL:AAL51004.1};
RX   PubMed=12586767; DOI=10.1210/en.2002-220890;
RA   Hsia N., Cornwall G.A.;
RT   "Cres2 and Cres3: new members of the cystatin-related epididymal
RT   spermatogenic subgroup of family 2 cystatins.";
RL   Endocrinology 144:909-915(2003).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000312|EMBL:AAI00527.1};
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: Has antibacterial activity against the Gram-negative bacteria
CC       E.coli. May play a role in sperm maturation and fertilization.
CC       {ECO:0000250|UniProtKB:Q9H112}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9H112}.
CC       Note=Probably secreted into the epididymis lumen, where it localizes to
CC       the outer surface of sperm. Specifically localizes to the postacrosomal
CC       and tail regions of sperm. {ECO:0000250|UniProtKB:Q9H112}.
CC   -!- TISSUE SPECIFICITY: Expressed in epididymis, where it localizes to the
CC       proximal caput and also part of the midcaput. Not detected in other
CC       tissues tested. {ECO:0000269|PubMed:12586767,
CC       ECO:0000269|PubMed:12700194}.
CC   -!- INDUCTION: Up-regulated by testicular factors. However, does not seem
CC       to be directly regulated by androgens or estrogen.
CC       {ECO:0000269|PubMed:12586767, ECO:0000269|PubMed:12700194}.
CC   -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR   EMBL; BK001265; DAA01199.1; -; mRNA.
DR   EMBL; AF454373; AAL51004.1; -; mRNA.
DR   EMBL; AK020300; BAB32061.1; -; mRNA.
DR   EMBL; BC100526; AAI00527.1; -; mRNA.
DR   CCDS; CCDS16845.1; -.
DR   RefSeq; NP_084335.1; NM_030059.2.
DR   AlphaFoldDB; Q9D269; -.
DR   SMR; Q9D269; -.
DR   BioGRID; 219272; 1.
DR   STRING; 10090.ENSMUSP00000028934; -.
DR   GlyGen; Q9D269; 1 site.
DR   PhosphoSitePlus; Q9D269; -.
DR   PaxDb; Q9D269; -.
DR   PRIDE; Q9D269; -.
DR   ProteomicsDB; 283966; -.
DR   Antibodypedia; 54198; 90 antibodies from 16 providers.
DR   DNASU; 78240; -.
DR   Ensembl; ENSMUST00000028934; ENSMUSP00000028934; ENSMUSG00000036958.
DR   GeneID; 78240; -.
DR   KEGG; mmu:78240; -.
DR   UCSC; uc008mtl.1; mouse.
DR   CTD; 140880; -.
DR   MGI; MGI:1925490; Cst11.
DR   VEuPathDB; HostDB:ENSMUSG00000036958; -.
DR   eggNOG; ENOG502RWFM; Eukaryota.
DR   GeneTree; ENSGT00910000144356; -.
DR   HOGENOM; CLU_118168_2_1_1; -.
DR   InParanoid; Q9D269; -.
DR   OMA; ETTNCVP; -.
DR   OrthoDB; 1565344at2759; -.
DR   PhylomeDB; Q9D269; -.
DR   BioGRID-ORCS; 78240; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q9D269; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9D269; protein.
DR   Bgee; ENSMUSG00000036958; Expressed in morula and 8 other tissues.
DR   Genevisible; Q9D269; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR   GO; GO:0061827; C:sperm head; ISS:UniProtKB.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; ISS:UniProtKB.
DR   CDD; cd00042; CY; 1.
DR   InterPro; IPR042930; CST11.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR046350; Cystatin_sf.
DR   PANTHER; PTHR47886; PTHR47886; 1.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Signal; Thiol protease inhibitor.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..139
FT                   /note="Cystatin-11"
FT                   /id="PRO_0000006659"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..102
FT                   /evidence="ECO:0000250|UniProtKB:O76096"
FT   DISULFID        115..135
FT                   /evidence="ECO:0000250|UniProtKB:O76096"
SQ   SEQUENCE   139 AA;  16217 MW;  F228D9815FA32640 CRC64;
     MAAGSWKATR LLLAILVALV AFSYQVKRKT FIRIEEVSAL ESSVKETLEY VTDEYNKKSE
     DLYNFRILRI LKIMKQVTGH LEYHITVEMQ RTTCLKTETS LCDIQKGELH KKIQCYFSVY
     AIPWVEVFKI LKKNCTDIS
 
 
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