ID A0A2U4BZN6_TURTR Unreviewed; 885 AA.
AC A0A2U4BZN6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
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};
GN Name=AGBL5 {ECO:0000313|RefSeq:XP_019798629.2,
GN ECO:0000313|RefSeq:XP_033694776.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019798629.2};
RN [1] {ECO:0000313|RefSeq:XP_019798629.2, ECO:0000313|RefSeq:XP_033694776.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019798629.2,
RC ECO:0000313|RefSeq:XP_033694776.1};
RG RefSeq;
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 RefSeq; XP_019798629.2; XM_019943070.2.
DR RefSeq; XP_033694776.1; XM_033838885.1.
DR STRING; 9739.ENSTTRP00000004841; -.
DR Proteomes; UP000245320; Chromosome 14.
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 Carboxypeptidase {ECO:0000313|RefSeq:XP_019798629.2,
KW ECO:0000313|RefSeq:XP_033694776.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000313|RefSeq:XP_019798629.2,
KW ECO:0000313|RefSeq:XP_033694776.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000313|RefSeq:XP_019798629.2,
KW ECO:0000313|RefSeq:XP_033694776.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT DOMAIN 11..141
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 199..318
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 343..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 97587 MW; D30B3CDCCF7A55A6 CRC64;
MELRCGGLLF SSRFDSGNLA HVEKVESVSS DGEGVVGGAS ASTSSIASSP DYEFNVWTRP
DCAETEFENG NRSWFYFSVR GGTPGKLIKI NVMNMNKQSK LYSQGMAPFV RTLPTRPRWE
RIRDRPTFEM TETQFVLSFV HRFVESRGAT TFFAFCYPFS YSDCQDLLNQ LDQRFLENHP
THSSPLDTIY YHRETLCYSL DGLRVDLLTI SSCHGLREDR EPRLEQLFPD ASTPRPFRFT
GKRIFFLSSR VHPGETPSSF VFNGFLDFIL RPDDPRAQTL RRLFVFKLIP MLNPDGVVRG
HYRTDSRGVN LNRQYLKPDA VLHPAVYGAK AVLLYHHVHS RLNSQSPSEH QRSPHLPPNA
PLSDLEKANN LRNEARLGHS PDGGSPEAWT QTEPAEPKHH SVWIMPQRST EAEHPDPDTI
PPKESGVAYY VDLHGHASKR GCFMYGNSFS DENTQVENML YPKLISLNSA HFDFQGCNFS
EKNMYARDRR DGQSKEGSGR VAIYKASGII HSYTLECNYN TGRSVNSIPA ACHDNGRASP
PPLPAFPSRY TVEQFEQVGR AMAIAALDMA ECNPWPRIVL SEHNSLTNLR AWMLKHVRSS
RGLSTTVNTG VNKKRGSRTP PKSNNGLPVS CSENTLSCTR SFSTGTSAGG SSSSQQNSPQ
MKNSLSFPFH GSRPAGLPGL GSSTQKVSHR VLGPVREPRS QDRRRRQQPL THHPTSSSPA
PSPTPVSSNT ASLHMGSCLL PNSLGTSGSS CSFLPSGDKP EAVMVIGKGL LGAGPRIPCI
RTRLQARPRL GRGSPPTRRG MRGSSGPTSP TPRSRESSEP EPGPCSIPRL PQAGPPRPCS
APAFSPISRS LSDSQSRICY SGGPLGQTEV CFVPKSPPLT VSPRV
//
