ID A0A3Q3EMS7_9LABR Unreviewed; 724 AA.
AC A0A3Q3EMS7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0000256|ARBA:ARBA00024141};
DE EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
DE AltName: Full=ATP/GTP-binding protein-like 5 {ECO:0000256|ARBA:ARBA00032928};
DE AltName: Full=Protein deglutamylase CCP5 {ECO:0000256|ARBA:ARBA00032753};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000008791.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000008791.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] +
CC H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-
CC glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-
CC COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555,
CC ChEBI:CHEBI:149556; EC=3.4.17.24;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-
CC terminal L-alpha-aminoacyl-[tubulin] + L-glutamate;
CC Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782,
CC ChEBI:CHEBI:149556; EC=3.4.17.24;
CC Evidence={ECO:0000256|ARBA:ARBA00024627};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797;
CC Evidence={ECO:0000256|ARBA:ARBA00024627};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-
CC glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208,
CC Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:143622;
CC Evidence={ECO:0000256|ARBA:ARBA00029299};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153;
CC Evidence={ECO:0000256|ARBA:ARBA00029299};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Midbody
CC {ECO:0000256|ARBA:ARBA00004214}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR AlphaFoldDB; A0A3Q3EMS7; -.
DR Ensembl; ENSLBET00000009261.1; ENSLBEP00000008791.1; ENSLBEG00000006727.1.
DR GeneTree; ENSGT00940000158032; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; 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; cd06236; M14_AGBL5_like; 1.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR034286; M14_AGBL5-like.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF12; CYTOSOLIC CARBOXYPEPTIDASE-LIKE PROTEIN 5; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT DOMAIN 10..147
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 199..325
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 23..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 80560 MW; F0315B7F557A1C8C CRC64;
MESRFGNIVF SSKFDSGNLA RVEKVEKGSS SPSGDVAQGG SAPSGSNITP DYEFNVWTQP
DCAGTEHENG NRSWFYFSVR GAAPGKLLKI NVMNMNNQRK LYSQGMAPLV RTLPGKNRWE
RVRDRPSTEI VDNQFILSFT HRLSEVRGAT TFFSFCFPFS YTECQEMLQQ FDKSYPNAAQ
LSPSSAPGTV YYHRELLCES LDGNRVDLLT VTNCSGMQEE REPRLPKLFP DTNTPRPHRF
PGKRVFFLSS RVHPGETPSS FVFNGFLHFI LRRDDPRAHV LRNMFVFKLI PMLNPDGVVR
GHYRTDSRGV NLNRQYLNPS PELHPSIYAA KALLLYHHTH NRLHSTQSTT HCNSTPHTQT
PPLNMKPSNK LQSPPFTALE VSLNQRNAEK DAIPAMPEVP MNSLSSSSET VAPETIPPHE
GGVAYYVDLH GHASKRGCFM YGNSLPDESQ QVENMLYPRL IAVNSAHFDF LGCNFSEKNM
YARDKRDGQS KEGSGRVAMH KAIGLLHSYT LECNYNTGKT MNTIPPACHD NGRATPPPPP
SFPPKYTPEI FEQVGRAVAV SALDMAECNP WPRLVLSEHS CLTNLRAWIL KHVRNTKGLN
THIHAHPPIR IHHNGSRASP PKSFNNCLSG SASENTLSRV RCNSHSSSSQ TPSPKMHNSP
SFTFGCPPPR SHAQHNNTHT SGRGGNKTLG PVRGKSISHP PACVAGRHYP SPLLGCTSFF
SFAH
//
