CBPC2_XENTR
ID CBPC2_XENTR Reviewed; 967 AA.
AC Q0P4M4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, 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};
GN Name=agbl2; Synonyms=ccp2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) 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}.
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DR EMBL; BC121989; AAI21990.1; -; mRNA.
DR RefSeq; NP_001072531.1; NM_001079063.1.
DR AlphaFoldDB; Q0P4M4; -.
DR SMR; Q0P4M4; -.
DR MEROPS; M14.029; -.
DR PRIDE; Q0P4M4; -.
DR GeneID; 779986; -.
DR KEGG; xtr:779986; -.
DR CTD; 79841; -.
DR Xenbase; XB-GENE-997506; agbl2.
DR InParanoid; Q0P4M4; -.
DR OrthoDB; 481670at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; 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.
DR SMART; SM00631; Zn_pept; 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..967
FT /note="Cytosolic carboxypeptidase 2"
FT /id="PRO_0000403759"
FT REGION 679..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 446
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 967 AA; 110770 MW; 1F87B86878E1BDA1 CRC64;
MCPALSTDLK QEVLTDPYES FMHHHLQYYG YFRGLEPREQ FKLPVQRCRK VVTDSDSDMP
SSQEDQKKLV YSLLLDSPVF KSRQLVFEDQ EGKIIPRLRE PKDLYGSSSQ DGCWQQARWP
SECEVIKQDI SHIEWDPTDR EIFYKPTGNE PKPPVVSEGT GAVVYEISPA HKGSYFKGSR
TGGRKCSHRK NQKVQCNNDL QFESRFESGN LQKAMKVGMY EYELTLRTDL YTSKHTQWFY
FQVKNTRKGV PYRFTITNLM KTNSLYNEGL KPLLYSQQDA ALKGIGWRRE GKDIKYYKNT
RSLDGRSLYS LTWTFEFPHD DDICYFAHCY PYTYSDLQRD LKSKISDPAC SHYCKLRTLC
RSLAGNSIYL LTITSPSTNL TTGAKKKAIV VTARVHPGET NGSWMMKGFL DFILSDSPDA
QLLRDTFIFK VVPMLNPDGV IVGNYRCSLS GRDLNRNYKS MLKDAFPCIW HTRSMVKRLL
TEREVILYCD FHGHSRKNNV FMYGCNSKGH PLTKLHERIF PLMLSKNAPD KFLFKGCKFK
VQKSKEGTGR IDMWKQGIQN SYTMEATFGG STLGNRKDTH FTTQDLKSMG HHFCDTLLDY
CDPDSSKFKL CLSELQRLVE EDIREKMKQL GRDMDSDFTL SDITLSDLES STSGSNSSES
DGLPAHLVDI AEKFYQKKKR RLRSRKERNS LYQKRNARQK QKLHEAVEVS EPAAHIVRNE
LTKSSGKRKK EQKVAKIKFQ EDLVPQTEEN LTTAAPTEKS SMLYSRKPES VSMKTQMINS
LPTSCVRDFM DLDHVCERQM TIRPRPSANG NRLPLIITVV QQSTLPPVPK GISALKQHPP
PFHSILDQSG DQLTVADHVF RRDKSVAKRG FSSAGIRPYC SGISGEKQKV LDGSIVPLDL
HLSLSPEVHR QNKPRQEPLI TLGSTEYFEG FLPKPKTDPV RRFPGISSSE PHFPNSSEDI
TVRNTMK
