GCP2_CAEBR
ID GCP2_CAEBR Reviewed; 770 AA.
AC Q5WN23; A8X602;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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:CBG08178};
GN ORFNames=CBG08178 {ECO:0000312|WormBase:CBG08178};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; HE600971; CAP28063.3; -; Genomic_DNA.
DR RefSeq; XP_002643302.1; XM_002643256.1.
DR AlphaFoldDB; Q5WN23; -.
DR SMR; Q5WN23; -.
DR STRING; 6238.CBG08178; -.
DR MEROPS; M28.A19; -.
DR EnsemblMetazoa; CBG08178.1; CBG08178.1; WBGene00030030.
DR GeneID; 8585296; -.
DR KEGG; cbr:CBG_08178; -.
DR CTD; 8585296; -.
DR WormBase; CBG08178; CBP01974; WBGene00030030; Cbr-gcp-2.1.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_3_2_1; -.
DR InParanoid; Q5WN23; -.
DR OMA; VFAPGIW; -.
DR OrthoDB; 804230at2759; -.
DR Proteomes; UP000008549; Chromosome X.
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 3: Inferred from homology;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..770
FT /note="Glutamate carboxypeptidase 2 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000174127"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..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:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 551
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"
SQ SEQUENCE 770 AA; 85603 MW; F5AF8158F41BC19C CRC64;
MPYVGVGAQK ASTNLTGGPM MKAYAFVLAF FLLGLGVLAL GKHHSGRRFN QYSKVSIDDI
HETDAKTIQD NIKSENIKKY LRIFTQEPHI AGTDANKKVA YAIASAWTEA GLEDVHTLPY
EVLLSYPDFE NPNSVVIQNS AGKEIFRSKG VSPVIIPDEQ SGKYAGHQWL AYGGNGTVSA
DVVYINRGNA NDFKNLKLMG VDVKGKIALM RYGHGFRGDK VYKAQQAGAI GAILFSDTSD
VAQDGVDSEH VYPKTIWMPN EGVQRGSLMH GDGDPLSPFY PSKKELFKGR TIEEAKDDGT
LPSIPVLPVS YTTALQLLKR MSGRAVPSDW QGFVGGNLTY KLGPGFVNGE KLTINVHSEL
KTKRIRNVIG YIRGAEEPDR YIMLGNHFDA WVYGSIDPNS GTAVLAEVAR AMMQTINETS
WRPARTIVFN AWDAEEFGLI GSTEFVEEFV DVLQKRAVVY INMDCIQGNA SLHVDTVPTL
EHIAIEAAKH VPNPSKRERS RGRNTVYDTW MKVFPEKKAG RPKIRVPGGG SDHAPFLNFA
GVPVINFNYK NYTTFDTYPL YHSMYETPFT NIHLMDTEDL AVHRAIGQYW AELAKTFADE
VVLPMNTTNL ASVMIKSYLP QLKASISGIN VSRIDFESIR TQYALLSKSS QDLLVMSKKF
QETMQFTFHS FSQNPYDAKH VNAVNERLIS TERCFINPRG VSKHNPSARH VLFSVSDSDS
YSNSLMAGIQ NAIHSYETSP SKKNLREIIN QISTVQYSVI CVVNTLRDVI
