CTS12_CAEEL
ID CTS12_CAEEL Reviewed; 454 AA.
AC P52715;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine carboxypeptidase ctsa-1.2 {ECO:0000305};
DE EC=3.4.16.- {ECO:0000250|UniProtKB:P52719};
DE Flags: Precursor;
GN Name=ctsa-1.2 {ECO:0000312|WormBase:F13D12.6};
GN ORFNames=F13D12.6 {ECO:0000312|WormBase:F13D12.6};
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 -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; BX284602; CAA88947.1; -; Genomic_DNA.
DR PIR; T20829; T20829.
DR RefSeq; NP_496507.1; NM_064106.5.
DR AlphaFoldDB; P52715; -.
DR SMR; P52715; -.
DR BioGRID; 40107; 32.
DR DIP; DIP-27155N; -.
DR IntAct; P52715; 3.
DR MINT; P52715; -.
DR STRING; 6239.F13D12.6.1; -.
DR ESTHER; caeel-f13d12.6; Carboxypeptidase_S10.
DR MEROPS; S10.A55; -.
DR iPTMnet; P52715; -.
DR EPD; P52715; -.
DR PaxDb; P52715; -.
DR PeptideAtlas; P52715; -.
DR EnsemblMetazoa; F13D12.6.1; F13D12.6.1; WBGene00008741.
DR GeneID; 174802; -.
DR KEGG; cel:CELE_F13D12.6; -.
DR UCSC; F13D12.6.1; c. elegans.
DR CTD; 174802; -.
DR WormBase; F13D12.6; CE02185; WBGene00008741; ctsa-1.2.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_3_1; -.
DR InParanoid; P52715; -.
DR OMA; CCHNDTD; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; P52715; -.
DR Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:P52715; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008741; Expressed in adult organism 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 Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..454
FT /note="Serine carboxypeptidase ctsa-1.2"
FT /id="PRO_0000004337"
FT ACT_SITE 168
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT ACT_SITE 377
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT ACT_SITE 431
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 454 AA; 50115 MW; A95EEA7D39594DC9 CRC64;
MVMSRTLVLV ALLGFAYVCE SALITNLPGA PISNFKQYSG YYNVGTKKNH MLHYWFVESQ
SNPSTDPVLL WLTGGPGCSG LSALLTEWGP WNVNTDGATL RTNPYSWNKN ASILTLEAPA
GVGYSYATDN NIATGDDQTA SENWEALVAF FNEFPQYKGN DFYVTGESYG GIYVPTLVQT
ILDRQSQSHI NIKGLAIGNG CVSANEGVDS LVNFLYHHGV VDQAKWEHMK TSCCHNDTDA
CPWHSFSEFS ACGEFVEATQ QTAWNGGLNP YNMYADCIST SASFRFGMEY ERRFNKKYTP
EVLGTVPCLD ESPVTNYLNR QDVRKALGIP SSLPAWSICS NAISYGYKRQ YGDMTSRVLN
AVNNNNLKMM LYNGDVDLAC NALMGQRFTD KLGLTLSKKK THFTVKGQIG GYVTQYKGSQ
VTFATVRGAG HMVPTDKPAV AEHIIQSFLF NKAF
