CBPC2_DANRE
ID CBPC2_DANRE Reviewed; 721 AA.
AC A6H8T7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Cytosolic carboxypeptidase 2 {ECO:0000250|UniProtKB:Q8CDK2};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q8CDK2};
DE AltName: Full=ATP/GTP-binding protein-like 2;
DE AltName: Full=Protein deglutamylase CCP2 {ECO:0000305};
DE AltName: Full=Testis-expressed protein 25;
GN Name=zte25; Synonyms=agbl2, ccp2; ORFNames=zgc:165648;
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].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
CC target proteins. Catalyzes the deglutamylation of polyglutamate side
CC chains generated by post-translational polyglutamylation in proteins
CC such as tubulins. Also removes gene-encoded polyglutamates from the
CC carboxy-terminus of target proteins such as MYLK. Does not show
CC detyrosinase or deglycylase activities from the carboxy-terminus of
CC tubulin. {ECO:0000250|UniProtKB:Q8CDK2}.
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 tubulin protein.
CC Specifically cleaves tubulin long-side-chains, while it is not able to
CC remove the branching point glutamate. Also catalyzes the removal of
CC polyglutamate residues from the carboxy-terminus of non-tubulin
CC proteins. {ECO:0000250|UniProtKB:Q8CDK2}.
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:Q8CDK2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000250|UniProtKB:Q8CDK2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8CDK2}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q5U5Z8}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q5U5Z8}. Note=Colocalizes with gamma-
CC tubulin in the centrioles and with glutamylated tubulin in the basal
CC bodies of ciliated cells. {ECO:0000250|UniProtKB:Q5U5Z8}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- CAUTION: Was initially shown to catalyze the removal of carboxy-
CC terminus tyrosine from alpha-tubulin (By similarity). However, later
CC studies did not identified any detyrosinase or deglycylase activities
CC from the carboxy-terminus of tubulin (By similarity).
CC {ECO:0000250|UniProtKB:Q5U5Z8, ECO:0000250|UniProtKB:Q8CDK2}.
CC -!- CAUTION: Was originally thought to have detyrosinating activity from C-
CC terminal positions on tubulin. {ECO:0000250|UniProtKB:Q5U5Z8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC146747; AAI46748.1; -; mRNA.
DR AlphaFoldDB; A6H8T7; -.
DR SMR; A6H8T7; -.
DR STRING; 7955.ENSDARP00000116922; -.
DR MEROPS; M14.029; -.
DR PaxDb; A6H8T7; -.
DR PRIDE; A6H8T7; -.
DR ZFIN; ZDB-GENE-070719-6; agbl2.
DR eggNOG; KOG3641; Eukaryota.
DR InParanoid; A6H8T7; -.
DR PhylomeDB; A6H8T7; -.
DR PRO; PR:A6H8T7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035610; P:protein side chain deglutamylation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Cell projection; Cytoplasm; Cytoskeleton; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..721
FT /note="Cytosolic carboxypeptidase 2"
FT /id="PRO_0000403758"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 450
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 721 AA; 82236 MW; 35C5F5ED43CB8D6B CRC64;
MQKKSDDPYE RLLLLHLQHY GFLSDNSSGI PIKREWEGIQ DSTASDMINS SSPSESSDSN
LEEEQEESKP CSNFFSLNKA LRTRQLVFDF DGERPIPRLR DPLDLFTIPS TSCPFQGVRW
PIECDVICDK IQHIEWDPSE PETFYQPTGN EQTPMPVGEV RGNTVYCIDP ATKASSFTYS
RVGGSRGPIK SATSCANNQK EPTLAFESRF ECGNLQKAVQ VGQYDYGLTL RTDLYTTKHT
QWFYFRVRNM REGVTYRFTI INLMKSSSLY GAGMCPLLYS EKTAWLKGEG WKRTGSSIRY
YRNNIEQDGK ALYSLTWTLE FPYDGDTCYL AHCYPYTYSK LQHYLREVIS DPVRAAYCKL
RVLCRSLAGN AVYVLTITAP SSSLAERKAK RAVVVTARVH PGETNGSWMM QGFLEFLLSD
LPDAHLLRET FIFKVIPMLN PDGVVVGNYR CSLAGRDLNR NYRSMLRDSF PCIWYTRNMV
KRLLAEREVV VYCDFHGHSR KNNVFMYGCN ERKDASQCLQ ERVFPLMMSK NAKDKFSFRS
CKFKMHKSKE GTGRIVMWRL GIRNSYTMES TFGGSTLGDR KGTHFSTLDL KSMGYCFCDT
LLDFCDPDPA KMTRCLEELG VLLKQEIRRK LGREVDSLEN LSDIDIESST SGSNSTESDG
LPVHLLNVTN QGKKKLLRSR KERNRLRQGR VQSAGKTDAS KPYSCQTLNA TTQHGDTEDQ
S
