ID   RISC_RAT                Reviewed;         452 AA.
AC   Q920A6;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
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   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 [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).
CC   -!- FUNCTION: May be involved in vascular wall and kidney homeostasis.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in aorta, bladder, and kidney with
CC       much lower levels in all other tissues analyzed. Expression in kidney
CC       is restricted to proximal convoluted tubules.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AF330051; AAK84661.1; -; mRNA.
DR   RefSeq; NP_596874.1; NM_133383.1.
DR   AlphaFoldDB; Q920A6; -.
DR   SMR; Q920A6; -.
DR   IntAct; Q920A6; 1.
DR   STRING; 10116.ENSRNOP00000003219; -.
DR   ESTHER; ratno-RISC; Carboxypeptidase_S10.
DR   MEROPS; S10.013; -.
DR   GlyGen; Q920A6; 5 sites.
DR   iPTMnet; Q920A6; -.
DR   PhosphoSitePlus; Q920A6; -.
DR   jPOST; Q920A6; -.
DR   PaxDb; Q920A6; -.
DR   PRIDE; Q920A6; -.
DR   GeneID; 114861; -.
DR   KEGG; rno:114861; -.
DR   CTD; 59342; -.
DR   RGD; 620067; Scpep1.
DR   VEuPathDB; HostDB:ENSRNOG00000002358; -.
DR   eggNOG; KOG1283; Eukaryota.
DR   HOGENOM; CLU_008523_1_0_1; -.
DR   InParanoid; Q920A6; -.
DR   OMA; FMNMEGD; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; Q920A6; -.
DR   TreeFam; TF313740; -.
DR   PRO; PR:Q920A6; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000002358; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; Q920A6; RN.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; ISO:RGD.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; ISO:RGD.
DR   GO; GO:0045776; P:negative regulation of blood pressure; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IEP:RGD.
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   2: Evidence at transcript 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_0000004286"
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"
SQ   SEQUENCE   452 AA;  51175 MW;  9195A0E773E7853B CRC64;
     MELSRRICLV RLWLLLLSFL LGFSAGSALN WREQEGKEVW DYVTVREDAR MFWWLYYATN
     PCKNFSELPL VMWLQGGPGG SSTGFGNFEE IGPLDTRLKP RNTTWLQWAS LLFVDNPVGT
     GFSYVNTTDA YAKDLDTVAS DMMVLLKSFF DCHKEFQTVP FYIFSESYGG KMAAGISLEL
     HKAIQQGTIK CNFSGVALGD SWISPVDSVL SWGPYLYSVS LLDNKGLAEV SDIAEQVLNA
     VNKGFYKEAT QLWGKAEMII EKNTDGVNFY NILTKSTPDT SMESSLEFFR SPLVRLCQRH
     VRHLQGDALS QLMNGPIKKK LKIIPDDVSW GAQSSSVFIS MEEDFMKPVI DIVDTLLELG
     VNVTVYNGQL DLIVDTIGQE SWVQKLKWPQ LSRFNQLKWK ALYTNPKSSE TSAFVKSYEN
     LAFYWILKAG HMVPADQGDM ALKMMRLVTQ QE