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RISC_MOUSE
ID   RISC_MOUSE              Reviewed;         452 AA.
AC   Q920A5; Q9D625;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Retinoid-inducible serine carboxypeptidase;
DE            EC=3.4.16.-;
DE   AltName: Full=Serine carboxypeptidase 1;
DE   Flags: Precursor;
GN   Name=Scpep1; Synonyms=Risc;
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].
RX   PubMed=11447226; DOI=10.1074/jbc.m104162200;
RA   Chen J., Streb J.W., Maltby K.M., Kitchen C.M., Miano J.M.;
RT   "Cloning of a novel retinoid-inducible serine carboxypeptidase from
RT   vascular smooth muscle cells.";
RL   J. Biol. Chem. 276:34175-34181(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Head, and Liver;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in vascular wall and kidney homeostasis.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AF330052; AAK84662.1; -; mRNA.
DR   EMBL; AK014680; BAB29501.1; -; mRNA.
DR   EMBL; AK050181; BAC34111.1; -; mRNA.
DR   EMBL; AK153225; BAE31818.1; -; mRNA.
DR   EMBL; AL646096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS25230.1; -.
DR   RefSeq; NP_083299.3; NM_029023.3.
DR   AlphaFoldDB; Q920A5; -.
DR   SMR; Q920A5; -.
DR   BioGRID; 216886; 9.
DR   STRING; 10090.ENSMUSP00000000287; -.
DR   ChEMBL; CHEMBL3259511; -.
DR   ESTHER; mouse-RISC; Carboxypeptidase_S10.
DR   MEROPS; S10.013; -.
DR   GlyGen; Q920A5; 5 sites.
DR   iPTMnet; Q920A5; -.
DR   PhosphoSitePlus; Q920A5; -.
DR   SwissPalm; Q920A5; -.
DR   EPD; Q920A5; -.
DR   jPOST; Q920A5; -.
DR   MaxQB; Q920A5; -.
DR   PaxDb; Q920A5; -.
DR   PeptideAtlas; Q920A5; -.
DR   PRIDE; Q920A5; -.
DR   ProteomicsDB; 253295; -.
DR   Antibodypedia; 30882; 121 antibodies from 20 providers.
DR   DNASU; 74617; -.
DR   Ensembl; ENSMUST00000000287; ENSMUSP00000000287; ENSMUSG00000000278.
DR   GeneID; 74617; -.
DR   KEGG; mmu:74617; -.
DR   UCSC; uc007kvx.2; mouse.
DR   CTD; 59342; -.
DR   MGI; MGI:1921867; Scpep1.
DR   VEuPathDB; HostDB:ENSMUSG00000000278; -.
DR   eggNOG; KOG1283; Eukaryota.
DR   GeneTree; ENSGT00940000156193; -.
DR   HOGENOM; CLU_008523_1_0_1; -.
DR   InParanoid; Q920A5; -.
DR   OMA; FMNMEGD; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q920A5; -.
DR   TreeFam; TF313740; -.
DR   BRENDA; 3.4.16.5; 3474.
DR   BioGRID-ORCS; 74617; 5 hits in 72 CRISPR screens.
DR   ChiTaRS; Scpep1; mouse.
DR   PRO; PR:Q920A5; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q920A5; protein.
DR   Bgee; ENSMUSG00000000278; Expressed in decidua and 263 other tissues.
DR   Genevisible; Q920A5; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:UniProtKB.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; IGI:GO_Central.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IGI:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..452
FT                   /note="Retinoid-inducible serine carboxypeptidase"
FT                   /id="PRO_0000004285"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        229
FT                   /note="E -> M (in Ref. 1; AAK84662)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   452 AA;  50965 MW;  E0E59F635B21B051 CRC64;
     MELSRRICLV RLWLLLLSFL LGFSAGSAID WREPEGKEVW DYVTVRKDAH MFWWLYYATN
     PCKNFSELPL VMWLQGGPGG SSTGFGNFEE IGPLDTQLKP RNTTWLQWAS LLFVDNPVGT
     GFSYVNTTDA YAKDLDTVAS DMMVLLKSFF DCHKEFQTVP FYIFSESYGG KMAAGISVEL
     YKAVQQGTIK CNFSGVALGD SWISPVDSVL SWGPYLYSMS LLDNQGLAEV SDIAEQVLDA
     VNKGFYKEAT QLWGKAEMII EKNTDGVNFY NILTKSSPEK AMESSLEFLR SPLVRLCQRH
     VRHLQGDALS QLMNGPIKKK LKIIPEDISW GAQASYVFLS MEGDFMKPAI DVVDKLLAAG
     VNVTVYNGQL DLIVDTIGQE SWVQKLKWPQ LSKFNQLKWK ALYTDPKSSE TAAFVKSYEN
     LAFYWILKAG HMVPSDQGEM ALKMMKLVTK QE
 
 
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