CBPC2_MACFA
ID CBPC2_MACFA Reviewed; 840 AA.
AC Q4R632;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 {ECO:0000250|UniProtKB:Q8CDK2};
GN ORFNames=QtsA-19251;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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 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 such as MYLK. {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 -!- ACTIVITY REGULATION: Inhibited by RARRES1. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RARRES1, KIF11 AND MAPRE1.
CC {ECO:0000250|UniProtKB:Q5U5Z8}.
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; AB169358; BAE01443.1; -; mRNA.
DR RefSeq; NP_001306283.1; NM_001319354.1.
DR AlphaFoldDB; Q4R632; -.
DR SMR; Q4R632; -.
DR STRING; 9541.XP_005577978.1; -.
DR MEROPS; M14.029; -.
DR GeneID; 101864761; -.
DR CTD; 79841; -.
DR eggNOG; KOG3641; Eukaryota.
DR Proteomes; UP000233100; 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..840
FT /note="Cytosolic carboxypeptidase 2"
FT /id="PRO_0000283749"
FT REGION 706..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 474
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 840 AA; 97606 MW; 4566DCCC7F1CA52B CRC64;
MFPALETHLK QTIPDPYEDF MYRHLQYYGY FKAQRGSLPN SATHQHVRKN NPQYLLHGSL
GGKDDLIPDT LQKEKLLWPT SLSSAVHRQI EAINRDSHML SLPHLRSRQL LYDELDEVNP
RLREPQELFS ILSTKRPLLA PRWPIECEVI KESIHHIEWA PPQPEYFYQP KGNEKVPEIV
GEKKGTVVYQ LDSVPTEGSY FTSSRVGGKQ GIIKELAVTL QGPEDNTLLF ESRFECGNLQ
KAVRVDTYEY ELTLRTDLYT NRHTQWFYFR VQNTRKDATY RFTIVNLLKP KSLYTVGMKP
LLYSQMDANT RNIGWRREGN EIKYCKNNMD DGQQPFYCLT WTIQFPYDQD TCFFAHFYPY
TYTDLQCYLL SVANNPIQSQ FCKLQTLCRS LAGNTVYLLT ITNPSQTPQE AAAKKAVVLS
ARVHPGESNG SWVMKGFLDF ILSNSPDAQL LRDIFVFKVL PMLNPDGVIV GNYRCSLAGR
DLNRHYKTIL KESFPCIWYT RNMIKRLLEE REVLLYCDFH GHSRKNNTFL YGCNNNNRKY
WLHERVFPLM LSKNAPDRFS FHSCNFKVQK CKEGTGRVVM WRMGILNSYT MESTFGGSTL
GSKRDTHFTI EDLKSLGYHV CDTLLDFCDP DQTKFTQCLA ELKELLRQEI HKKFHELGQD
VDLEESWSDI SLSDIESSTS GSDSSLSDGL PVHLANIADE LTQKKMFKKK KKKSLQTRKQ
RNEQYQKKNL MWKLKLTEDT SEFASTLQKH PAFFKNSESS SFLPMRNENP RLNETNLNRR
DKDTSLDPSM TTLILPKNKG RMQTNLNRRD KDTSLDPSMT TLILPKNKGR MQVLHLIYCI
