ID A0A060W8B9_ONCMY Unreviewed; 1002 AA.
AC A0A060W8B9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cytosolic carboxypeptidase 2 {ECO:0000256|ARBA:ARBA00041046};
DE AltName: Full=ATP/GTP-binding protein-like 2 {ECO:0000256|ARBA:ARBA00043107};
DE AltName: Full=Protein deglutamylase CCP2 {ECO:0000256|ARBA:ARBA00043071};
GN ORFNames=GSONMT00068719001 {ECO:0000313|EMBL:CDQ63226.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ63226.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ63226.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ63226.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O
CC = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-
CC glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-
CC COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623;
CC Evidence={ECO:0000256|ARBA:ARBA00029302};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000256|ARBA:ARBA00029302};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000256|ARBA:ARBA00004114}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; FR904433; CDQ63226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060W8B9; -.
DR STRING; 8022.A0A060W8B9; -.
DR MEROPS; M14.026; -.
DR PaxDb; 8022-A0A060W8B9; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06907; M14_AGBL2-3_like; 1.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF41; CYTOSOLIC CARBOXYPEPTIDASE 2; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380}.
FT DOMAIN 214..297
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 375..590
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 49..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 114440 MW; 2E9AE657F88D8A05 CRC64;
MKFTHTFLAS QDVFFIQSSN QDVPSIEDRH RDTGTDNYFQ GNLLRQRWRD SHHPGSSHPG
THSSDSNNSN MEDEEQEPGR RAFTLHLGQA LRTRQLVIDF DGERPIPRLR EPLDLFAIPS
TPFQGVRWPI EYEVFKEAIH HIEWDPPDPE PFYQPTGHER APMPVGEEKG NVVYCIDPGT
KTSYFTYSRV GGSRGPIKSS TSCAMHQDKS TLAFESRFES GNLQKAVQVG VHDYELTLRT
DMYTTKHTQW FYFRVRNMKA GVTYRFTIVN LMKASSLYCL GMRPLLYSER AAWEKGEGWR
RTGSNIRYYR NQHHQAEQDN NTTTNTKSLH SLTWTGQFPY DFDTCYLAHC YPYTYSHLQR
YLSRLTSNSA TGAYCKLRVL CRSLAGNAVH VLTVTSPGGG WMDRSAKRAV VVTARVHPGE
TNSSWMMQGF LDFLLGESDD ARLLRETFVF KVVPMLNPDG VVVGNYRCSL AGRDLNRNYN
TLLRDSFPCV WHTRNMVKRL MAERDVVLYC DFHGHSRKNN VFMYGCTNSD DATQRLHERV
FPLMMSKNAN DKFSFRSCKF RVHQSKEGTG RVVMWRLGIR NSYTMESTFG GSTLGNRKGT
HFSTRDLKSL GYYLCDTLLD YCDPDPTKTS HCLAELRAML RQELRERLGQ EVDSDGSLSV
SISDIESSTS GSNSTESDGL PVHLLNRIDE QSQVKKKHLR SGKERNRLRQ ERVRNVDPKV
LHRNIKNIDP VLPTEDMVKV RIQEKTVAVV REKKKREVPF VVKVSRQTGR SWIPHPTTRI
GVIGHVTLWQ EEESEKNEYL DAVRAAYLRT QPPVTAVQQR GFSVPVPTSK IRVHTTPIQQ
QPMPFSPDHR SHAGMRERMP ALHTSSPPVV PGMQCRVVPE FIPPQGLEPC RSSNVYRAKS
HHQCPRPEKQ GHAARVSKRY YMPEAPTSNT DALEPLWRSP ERDCTAGLSD AMPVGEQDQS
GPQAAFEKPP SKPGTDGNSY LPDLRHIDFR GKRLLSSPRQ AF
//
