CBPC5_DANRE
ID CBPC5_DANRE Reviewed; 885 AA.
AC Q68EI3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0000250|UniProtKB:Q09M02};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q09M02};
DE EC=3.4.17.24 {ECO:0000250|UniProtKB:Q09M02};
DE AltName: Full=ATP/GTP-binding protein-like 5;
DE AltName: Full=Protein deglutamylase CCP5 {ECO:0000305};
GN Name=agbl5; Synonyms=ccp5; ORFNames=zgc:91997;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
CC tubulin and non-tubulin target proteins. Catalyzes the removal of
CC polyglutamate side chains present on the gamma-carboxyl group of
CC glutamate residues within the C-terminal tail of alpha- and beta-
CC tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-
CC chain, as well as the branching point glutamate. Also catalyzes the
CC removal of alpha-linked glutamate residues from the carboxy-terminus of
CC alpha-tubulin. {ECO:0000250|UniProtKB:Q09M02}.
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:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}.
CC Midbody {ECO:0000250|UniProtKB:Q8NDL9}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BC080248; AAH80248.1; -; mRNA.
DR RefSeq; NP_001004113.1; NM_001004113.1.
DR AlphaFoldDB; Q68EI3; -.
DR STRING; 7955.ENSDARP00000094377; -.
DR MEROPS; M14.036; -.
DR PaxDb; Q68EI3; -.
DR GeneID; 445479; -.
DR KEGG; dre:445479; -.
DR CTD; 60509; -.
DR ZFIN; ZDB-GENE-040822-29; agbl5.
DR eggNOG; KOG3641; Eukaryota.
DR InParanoid; Q68EI3; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; Q68EI3; -.
DR BRENDA; 3.4.17.24; 928.
DR PRO; PR:Q68EI3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035609; P:C-terminal protein deglutamylation; ISS:UniProtKB.
DR GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0035611; P:protein branching point deglutamylation; ISS:UniProtKB.
DR GO; GO:0035608; P:protein deglutamylation; ISS:UniProtKB.
DR GO; GO:0035610; P:protein side chain deglutamylation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06236; M14_AGBL5_like; 1.
DR InterPro; IPR034286; M14_AGBL5-like.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Cytoplasm; Cytoskeleton; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Protease; Reference proteome; Zinc.
FT CHAIN 1..885
FT /note="Cytosolic carboxypeptidase-like protein 5"
FT /id="PRO_0000305923"
FT REGION 341..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 885 AA; 98709 MW; 4EB7F42104357E8D CRC64;
MEIRVGSAVF SSRFDSGNLA RVERVEASEA AGESSRSASV PQPDYEFNVW TRPDCASTEF
ENGNRSWFYF SVRGLLPGKL LKINMMNMNK QSKLYTQGMA PFVRTLPVKT RWERVRDRPT
FEMSDSQFIL SFVHRLLDVR GVTTYFSFCY PFSYAECQDM MLQLDHKFLS STSTHTACSP
PESIYYHREL LCHSLDGHRV DLITVSSCHG LLEEREPRLD KLFPDLSTAR SHRFTGKRVF
FVSSRVHPGE TPSSFVFNGF LNFILSQEDP RAQTLRRMFV FKLIPMLNPD GVVRGHYRTD
SRGVNLNRQY VNPSPDLHPS IYGAKSLLLY HHIHNRLGHA SGSALKTSNQ SNTSPPVATP
TERERCMNLR NEAERGEGPT FDLSEIPMQL EESWEKSGVQ REAEHSDENE SAQSRGETNS
APSEQVPPQE SGVAYYIDLH GHASKRGCFM YGNNLTEESQ QVENMLYAKL ISLNCAHFDF
LGCNFSEKNM YARDKRDGQS KEGSGRVAIH KAIGLVHSYT LECNYNTGRS VNTIPPACHD
NGRATPPPPP AFPPKYTPEV YEQVGRAVAV AALDMAECNP WPRLVLSEHS SLLNLRASIL
KHVRNSTGLT SNNRRNTHCK TSSSPPKPVS LSTSASENSL NRTRSTTNVQ GSRQTPQLKS
SPSFTFGTTA HRPSHRSLGP VRECKAQEKR RPPPPPLPHH HHQQHQRLSV RLSAPVRAPL
SPSSSSSSSS SSPSSSSSAP GPGSISLAGN SCPEFRPANQ IKELRGGRGK GGRSGPAYCH
SSQQRTALTT KEPLQDSLDI LTSIEYSRCE LQPRPSRIPV RRELQSSVIP LSSTETPTMR
VWKLIKPGLK KHLAGVSGKD RLSTKALLKN SSRQTDQHIH RSLPT
