CTS11_CAEEL
ID CTS11_CAEEL Reviewed; 469 AA.
AC P52717;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Serine carboxypeptidase ctsa-1.1 {ECO:0000305};
DE EC=3.4.16.- {ECO:0000250|UniProtKB:P52719};
DE Flags: Precursor;
GN Name=ctsa-1.1 {ECO:0000312|WormBase:F41C3.5};
GN ORFNames=F41C3.5 {ECO:0000312|WormBase:F41C3.5};
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-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-328, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125 AND ASN-328, 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}.
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; CCD65861.1; -; Genomic_DNA.
DR PIR; T16316; T16316.
DR RefSeq; NP_494846.1; NM_062445.4.
DR AlphaFoldDB; P52717; -.
DR SMR; P52717; -.
DR BioGRID; 39172; 14.
DR DIP; DIP-26467N; -.
DR STRING; 6239.F41C3.5.2; -.
DR ESTHER; caeel-f41c3.5; Carboxypeptidase_S10.
DR MEROPS; S10.A59; -.
DR iPTMnet; P52717; -.
DR EPD; P52717; -.
DR PaxDb; P52717; -.
DR PeptideAtlas; P52717; -.
DR PRIDE; P52717; -.
DR EnsemblMetazoa; F41C3.5.1; F41C3.5.1; WBGene00018271.
DR GeneID; 173818; -.
DR KEGG; cel:CELE_F41C3.5; -.
DR UCSC; F41C3.5.1; c. elegans.
DR CTD; 173818; -.
DR WormBase; F41C3.5; CE02733; WBGene00018271; ctsa-1.1.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_3_1; -.
DR InParanoid; P52717; -.
DR OMA; AIHAQPV; -.
DR OrthoDB; 607679at2759; -.
DR PhylomeDB; P52717; -.
DR Reactome; R-CEL-2132295; MHC class II antigen presentation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:P52717; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00018271; Expressed in larva and 5 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; -; 2.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..469
FT /note="Serine carboxypeptidase ctsa-1.1"
FT /id="PRO_0000004339"
FT ACT_SITE 162
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT ACT_SITE 394
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT ACT_SITE 446
FT /evidence="ECO:0000250|UniProtKB:P52719"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
SQ SEQUENCE 469 AA; 53646 MW; C8B3503D9577CB74 CRC64;
MKTLLLLAFF VGVTCGEEIK DLPGLDFEPN FKHYSGFFQV SDNHVLHYWF VESQNEPSND
PLIFWFNGGP GCSSLDGLLN EMGPYVANED GKTLRENEYS WNKMASVVYI ESPAGVGYSY
ATDGNITTND DLTSLENYEA VKQFFTEFPQ FRHHQTFIMG ESYGGVYVPT LTARIVDGQK
DFPINLKGMA LGNGYVNEKL NIDTSVRFAY GHGLIDEKIW NTLERDCCRG CIDSCDLTQV
TGHCATLVED IFQFLWFGGL NPYDLYRDCD PNPSVNSKRM KHMLRGVAPA MAHFDELLKN
QTKTSLYQFL KNKSQSQKPL KADVPCLNDT EMLSYMNNPK VRKAIHIPFN LGKWDICSDK
VTTTYQKQYT DMTPFIKKIV KNHVRVLLYY GDTDMACNFM MGQQFSDQLG LRRTLKKTPW
KYDRQIAGFK TLFDGLSFIT IRGAGHMAPQ WRAPQMYYAV QQFLNNHPL
