ID   CTS31_CAEEL             Reviewed;         574 AA.
AC   P52716;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Serine carboxypeptidase ctsa-3.1 {ECO:0000305};
DE            EC=3.4.16.- {ECO:0000250|UniProtKB:P52719};
DE   Flags: Precursor;
GN   Name=ctsa-3.1 {ECO:0000312|WormBase:F32A5.3};
GN   ORFNames=F32A5.3 {ECO:0000312|WormBase:F32A5.3};
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).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241 AND ASN-408, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; BX284602; CCD66273.1; -; Genomic_DNA.
DR   PIR; T16230; T16230.
DR   RefSeq; NP_495509.1; NM_063108.5.
DR   AlphaFoldDB; P52716; -.
DR   SMR; P52716; -.
DR   BioGRID; 39525; 8.
DR   STRING; 6239.F32A5.3; -.
DR   ESTHER; caeel-f32a5.3; Carboxypeptidase_S10.
DR   MEROPS; S10.A65; -.
DR   iPTMnet; P52716; -.
DR   EPD; P52716; -.
DR   PaxDb; P52716; -.
DR   PeptideAtlas; P52716; -.
DR   EnsemblMetazoa; F32A5.3.1; F32A5.3.1; WBGene00017969.
DR   GeneID; 174189; -.
DR   KEGG; cel:CELE_F32A5.3; -.
DR   UCSC; F32A5.3; c. elegans.
DR   CTD; 174189; -.
DR   WormBase; F32A5.3; CE01273; WBGene00017969; ctsa-3.1.
DR   eggNOG; KOG1282; Eukaryota.
DR   GeneTree; ENSGT00940000167871; -.
DR   HOGENOM; CLU_008523_13_3_1; -.
DR   InParanoid; P52716; -.
DR   OMA; MIPYHKT; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; P52716; -.
DR   Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   PRO; PR:P52716; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00017969; Expressed in larva and 3 other tissues.
DR   GO; GO:0045121; C:membrane raft; HDA:WormBase.
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   1: Evidence at protein level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..574
FT                   /note="Serine carboxypeptidase ctsa-3.1"
FT                   /id="PRO_0000004338"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   ACT_SITE        507
FT                   /evidence="ECO:0000250|UniProtKB:P52719"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   574 AA;  64087 MW;  507EE63C433FA216 CRC64;
     MCRTLLGVAF LVVTVLSQGE KDLIQNLPGL LFKANFKSYS GYVDANANGT WKMHYMLTES
     RSNPDTDPLL VWFNGGPGCS SLGGLFEELG PFYVNFDGQT LYENPYAWNA KANVLYLESP
     IGVGYSYDTT TPGYFQANDD QSAAQNYQAL TNFFNVAQPK YTNRTFYLSG ESYAGIYIPM
     LTDLIVQGIN NPNQPFPNKN FQGSAIGNGF MNVAGLLNAL TLWSAYHGRV SEQNWADIKA
     NCSKGADVDS FDFSQFTTSQ NKIDYVGDGS YCGNLIQPLI SQNALGNEGF DQYNFYQECY
     DKSVFQAPPP AGGKRHKRSA MQGVSSVQKN LQYQQLGNFQ GTSNLAKNTA TLVNRFSNDN
     QFGYFCWNED AVSKYLNSDN VQNALNIPQA WKDQKNTWED CRMSIYNNYT LKYNTTNRFF
     NNIITNLTTD FRFLIYNGDV DTVCNYLGDA KHILQVAKDN GLTSGPRTPW YYSNNQQLAG
     YVQTYSGKNK NNAMITIDLL TVKGAGHMVP YDRAGPSVQM ISNFVWAPKN VVINYTSQDN
     FNPNIQLSDL VDSGSSSTVA FFISMFAVLL NIVF