CTS41_CAEEL
ID CTS41_CAEEL Reviewed; 470 AA.
AC Q09991; Q86NG2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine carboxypeptidase ctsa-4.1 {ECO:0000305};
DE AltName: Full=Carboxypeptidase C {ECO:0000255|PROSITE-ProRule:PRU10074};
DE EC=3.4.16.5 {ECO:0000255|PROSITE-ProRule:PRU10074};
DE Flags: Precursor;
GN Name=ctsa-4.1 {ECO:0000312|WormBase:K10B2.2a};
GN Synonyms=ctsa-1 {ECO:0000312|WormBase:K10B2.2a},
GN drd-7 {ECO:0000312|WormBase:K10B2.2a};
GN ORFNames=K10B2.2 {ECO:0000312|WormBase:K10B2.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity.;
CC EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:K10B2.2a};
CC IsoId=Q09991-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:K10B2.2b};
CC IsoId=Q09991-2; Sequence=VSP_060208;
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {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; BX284602; CCD66392.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD66393.1; -; Genomic_DNA.
DR PIR; T16606; T16606.
DR RefSeq; NP_495284.1; NM_062883.4. [Q09991-1]
DR RefSeq; NP_871927.1; NM_182127.1. [Q09991-2]
DR AlphaFoldDB; Q09991; -.
DR SMR; Q09991; -.
DR STRING; 6239.K10B2.2a; -.
DR ESTHER; caeel-k10b2.2; Carboxypeptidase_S10.
DR MEROPS; S10.A58; -.
DR EPD; Q09991; -.
DR PaxDb; Q09991; -.
DR PeptideAtlas; Q09991; -.
DR PRIDE; Q09991; -.
DR EnsemblMetazoa; K10B2.2a.1; K10B2.2a.1; WBGene00019605. [Q09991-1]
DR EnsemblMetazoa; K10B2.2b.1; K10B2.2b.1; WBGene00019605. [Q09991-2]
DR GeneID; 174057; -.
DR KEGG; cel:CELE_K10B2.2; -.
DR UCSC; K10B2.2a; c. elegans.
DR CTD; 174057; -.
DR WormBase; K10B2.2a; CE02009; WBGene00019605; ctsa-4.1. [Q09991-1]
DR WormBase; K10B2.2b; CE33418; WBGene00019605; ctsa-4.1. [Q09991-2]
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_3_1; -.
DR InParanoid; Q09991; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; Q09991; -.
DR Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q09991; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00019605; Expressed in larva and 3 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; IPR033124; Ser_caboxypep_his_AS.
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; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Carboxypeptidase; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..470
FT /note="Serine carboxypeptidase ctsa-4.1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000004340"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 380
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT ACT_SITE 441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10075"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..267
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060208"
SQ SEQUENCE 470 AA; 53158 MW; CCC2DACB75EF30FC CRC64;
MKLLSILFIF VSSYSFCLAA PATDKVNDLP GLTFTPDFFH YSGYLRAWTD KYLHYWLTES
SRAPTQDPLV LWLNGGPGCS SLDGLIEELG PFHVKDFGNS IYYNEYAWNK FANVLFLESP
AGVGYSYSTN FNLTVSDDEV SLHNYMALLD FLSKFPEYKG RDFWITGESY AGVYIPTLAV
RILNDKKNFP NFKGVAIGNG ALNFPNNYNT MVPFYYYHAL VRDDLYNDIA RNCCNNNIGT
CDIYSKFFDP NCRDKVINAL DGTNELNMYN LYDVCYYNPT TNLKKAFIER QMRIAVGLPA
RKHNAATTVP LCAQTNNTHV YLNRADVRKS LHIPSSLPAW EECSDQVGKN YVVTHFNVIP
EFQTMIAAGI KILVYNGDVD TACNSIMNQQ FLTSLNLTVL GEQEKVNEAW HYSGQTGTAV
AGFQTKFAGN VDFLTVRGSG HFVPEDKPKE SQQMIFNFIN NKDYSTPIQL
