GCP2_CAEEL
ID GCP2_CAEEL Reviewed; 770 AA.
AC P91406; Q65ZG3; Q65ZG4; Q86FL5;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glutamate carboxypeptidase 2 homolog {ECO:0000250|UniProtKB:Q04609};
DE EC=3.4.17.21 {ECO:0000250|UniProtKB:Q04609};
DE AltName: Full=Glutamate carboxypeptidase II homolog {ECO:0000250|UniProtKB:Q04609};
GN Name=gcp-2.1 {ECO:0000312|WormBase:R57.1a};
GN ORFNames=R57.1 {ECO:0000312|WormBase:R57.1a};
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], AND ALTERNATIVE SPLICING.
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-175 AND ASN-337, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
CC typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
CC EC=3.4.17.21; Evidence={ECO:0000250|UniProtKB:Q04609};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q04609};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:R57.1a};
CC IsoId=P91406-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:R57.1b};
CC IsoId=P91406-2; Sequence=VSP_009602, VSP_009603;
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {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; FO081648; CCD73106.1; -; Genomic_DNA.
DR EMBL; FO081648; CCD73107.1; -; Genomic_DNA.
DR PIR; T30154; T30154.
DR RefSeq; NP_508085.2; NM_075684.5. [P91406-1]
DR RefSeq; NP_872248.2; NM_182448.4. [P91406-2]
DR AlphaFoldDB; P91406; -.
DR SMR; P91406; -.
DR STRING; 6239.R57.1a; -.
DR MEROPS; M28.A19; -.
DR iPTMnet; P91406; -.
DR EPD; P91406; -.
DR PaxDb; P91406; -.
DR PeptideAtlas; P91406; -.
DR EnsemblMetazoa; R57.1a.1; R57.1a.1; WBGene00020082. [P91406-1]
DR EnsemblMetazoa; R57.1b.1; R57.1b.1; WBGene00020082. [P91406-2]
DR GeneID; 180386; -.
DR KEGG; cel:CELE_R57.1; -.
DR UCSC; R57.1c.2; c. elegans. [P91406-1]
DR CTD; 180386; -.
DR WormBase; R57.1a; CE30114; WBGene00020082; gcp-2.1. [P91406-1]
DR WormBase; R57.1b; CE37270; WBGene00020082; gcp-2.1. [P91406-2]
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT01030000234598; -.
DR InParanoid; P91406; -.
DR OMA; VFAPGIW; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; P91406; -.
DR Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CEL-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR PRO; PR:P91406; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00020082; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; P91406; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..770
FT /note="Glutamate carboxypeptidase 2 homolog"
FT /id="PRO_0000174128"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..770
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 282..597
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT ACT_SITE 435
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_009602"
FT VAR_SEQ 596..770
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_009603"
SQ SEQUENCE 770 AA; 85501 MW; 3411C4D612095190 CRC64;
MPYVGVGAQT VSTSLTGAPM VKAYIAIAAS LIFVFCIAAL GVHHSERKFN KFNKVSIDDI
HKSDAGVIQD NIKTENIKKY LRIFTKDPHV AGTEANKKVA YEIANAWSEA GLEDVHTLPY
EVLLSYPDFE NPNSVIIKSS AGKEVFKSKG VSPVIIPDEQ SGKYAGHQWL AYAGNGSASA
DVVYINHGTA NDFKNLKLMG VDIKGKIALM RYGHGFRGDK IHKAQQAGAI GAILFSDTQD
VAQDGVESEN VYPKKIWMPN EGVQRGSLMH GDGDALSPYY PSKKELFKGR TIEEAKEDGV
LPSIPVLPVS YTTGYEILKR LSGRPAPSDW QGFVGGNLTY KLGPGFVNGE KLSINVHSEL
RTKRIRNVIG YIRGSEEPDS YIMLGNHFDA WVYGSIDPNS GTAVLAEVAR AMMQTINETS
WKPARTIVFN AWDAEEFGLI GSTEFVEEFV NILQKRAVVY INMDCIQGNI SLHVDTVPIL
EHAVIEASKQ VENPSKRERS RGRKTLYDTW MKVFPDKKAG VPKIRVPGGG SDHAPFLNFA
GVPVINFTFK NYTTWDTYPL YHTMYETPFS NIHLLDTDNL SVHKAIGQYW AELAKTFADD
VILPMNTTHF ASVMLKTYLP QLKTTISGIN VSRSDFEDIR TQYALLSKSA QDLLTMSKKF
QETIHFTQHS FSQNPYDPKH VNAVNERLKS TERCFINPRG VSMHNPSARH VLFSVSDSDS
YSSSLMAGVQ NAINSYDLNP TKKGLREIIN QISIVQYSVI CVVNTLRDVI
