CPVL_RAT
ID CPVL_RAT Reviewed; 478 AA.
AC Q4QR71;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine carboxypeptidase CPVL;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=CPVL;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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: May be involved in the digestion of phagocytosed particles in
CC the lysosome, participation in an inflammatory protease cascade, and
CC trimming of peptides for antigen presentation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; BC097471; AAH97471.1; -; mRNA.
DR RefSeq; NP_001025098.1; NM_001029927.1.
DR RefSeq; XP_008761137.1; XM_008762915.2.
DR AlphaFoldDB; Q4QR71; -.
DR SMR; Q4QR71; -.
DR STRING; 10116.ENSRNOP00000012196; -.
DR ESTHER; ratno-CPVL; Carboxypeptidase_S10.
DR MEROPS; S10.003; -.
DR GlyGen; Q4QR71; 4 sites.
DR PhosphoSitePlus; Q4QR71; -.
DR PaxDb; Q4QR71; -.
DR Ensembl; ENSRNOT00000012196; ENSRNOP00000012196; ENSRNOG00000009172.
DR GeneID; 502774; -.
DR KEGG; rno:502774; -.
DR UCSC; RGD:1563609; rat.
DR CTD; 54504; -.
DR RGD; 1563609; Cpvl.
DR eggNOG; KOG1282; Eukaryota.
DR GeneTree; ENSGT00940000159498; -.
DR InParanoid; Q4QR71; -.
DR OMA; PFHDLDK; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q4QR71; -.
DR TreeFam; TF354323; -.
DR PRO; PR:Q4QR71; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009172; Expressed in testis and 6 other tissues.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000331565"
FT CHAIN ?..478
FT /note="Probable serine carboxypeptidase CPVL"
FT /id="PRO_0000331566"
FT ACT_SITE 206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 55146 MW; BA1ED40D3776355C CRC64;
MVRAQWKVII LLILLMVIPS DGLFHSIYRS ILVAQPFKGN AGQPLFLSPY IRTGKIKEGQ
RKSMVSPFPG MYDKSYAGYI TVNQTYNSNL FFWFFPARTQ PADAPVVLWL QGGPGGSSMF
GLFVEHGPYI ITSNMTVLSR DFPWTFSLSM LYIDNPVGTG FSFTDHIQGY AIDEDDVAQD
LYSALVQFFK LFPEYAKNDF YITGESYAGK YVPAIAYYIH SLNPVRRFKI RLKGIALGDA
YTDPETIIGG YATFLYEVGL LDEQQRRHFR KQCRKCIKYI KEQEWMKAFE VLDELLDGDL
TAGPSFFQNV TGCTNYYNIL QCTEPEDQSY FSKFLSLPQV RQAIHVGNRN FSDGAEVEKY
LREDTVKSVK PWLAEIMNYY KVLIYNGQLD IIVAAALTER SLMTMDWKGS YAYRRTHKKI
WKIFESDDEV AGYVRRVGKF HQVIVRGGGH ILPYDQPLRS FDMINRFIYD RGWEPYKL