CBPC1_XENTR
ID CBPC1_XENTR Reviewed; 1226 AA.
AC A9JRL3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Cytosolic carboxypeptidase 1 {ECO:0000250|UniProtKB:Q641K1};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q641K1};
DE EC=3.4.17.24 {ECO:0000250|UniProtKB:Q641K1};
DE AltName: Full=ATP/GTP-binding protein 1 {ECO:0000250|UniProtKB:Q641K1};
DE AltName: Full=Protein deglutamylase CCP1 {ECO:0000305};
GN Name=agtpbp1; Synonyms=ccp1;
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 (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation
CC of 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. Specifically cleaves tubulin long-side-chains, while it is not
CC able to remove the branching point glutamate. Also catalyzes the
CC removal of polyglutamate residues from the carboxy-terminus of alpha-
CC tubulin as well as non-tubulin proteins.
CC {ECO:0000250|UniProtKB:Q641K1}.
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:Q641K1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000250|UniProtKB:Q641K1};
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:Q641K1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000250|UniProtKB:Q641K1};
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 {ECO:0000250|UniProtKB:Q9UPW5}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus
CC {ECO:0000250|UniProtKB:Q641K1}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q641K1}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BC155703; AAI55704.1; -; mRNA.
DR RefSeq; NP_001107308.1; NM_001113836.1.
DR RefSeq; XP_012808696.1; XM_012953242.2.
DR AlphaFoldDB; A9JRL3; -.
DR SMR; A9JRL3; -.
DR STRING; 8364.ENSXETP00000059516; -.
DR MEROPS; M14.028; -.
DR PaxDb; A9JRL3; -.
DR PRIDE; A9JRL3; -.
DR Ensembl; ENSXETT00000061259; ENSXETP00000059516; ENSXETG00000011732.
DR GeneID; 100135097; -.
DR KEGG; xtr:100135097; -.
DR CTD; 23287; -.
DR Xenbase; XB-GENE-5932583; agtpbp1.
DR eggNOG; KOG3641; Eukaryota.
DR HOGENOM; CLU_007391_0_0_1; -.
DR InParanoid; A9JRL3; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; A9JRL3; -.
DR TreeFam; TF313794; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000011732; Expressed in testis and 15 other tissues.
DR ExpressionAtlas; A9JRL3; differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; 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:0021702; P:cerebellar Purkinje cell differentiation; ISS:UniProtKB.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0050905; P:neuromuscular process; ISS:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:0035610; P:protein side chain deglutamylation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06906; M14_Nna1; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033852; CBPC1/4.
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 SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Mitochondrion; Nucleus; Protease; Reference proteome; Zinc.
FT CHAIN 1..1226
FT /note="Cytosolic carboxypeptidase 1"
FT /id="PRO_0000403757"
FT REGION 366..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 965
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 1012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 1226 AA; 138681 MW; 35FBCC8EFCF40BD6 CRC64;
MSKAKATADK CLSNNSRIQS LLSQLEKVNA EPLLFDSDNT RYVTAKILHL AQTQEKTRKE
IAAKGSTGME VILCTLENTR DLQTILNILN ILNELASTAG GRRINALISK GGSRILLQLL
LSASKESSSN EELMMVLHSL LAKVGPKDKK FGIKARVSGA LNISLNLVKQ NLQNPRLILP
CLQVLRVCCM NSVNSVYLGK NGAVEILFKL IGPFTRRNTG LIKVSLDTFA ALLKSKTNAR
KAVDRGYVQA LLSIYTDWHR HDTRHRHMLI RKGILQCLKS ITNIKIGRKA FIDANGMKTL
YNTSQECQAV RTLDPLVNTS SLIMRKCFPK NRLPLPTIKS AFQFQLPIMP TSGPVALLYS
MPPEVDDVVD ESDDNDDTEA ETEAEAENEE SDQLCKNDDI ETDITKLIPG QELGRTLEDL
KMYERFFPEL TEDFQEFDLV SNEPKPGAKL GPIIVPTAGE EQPEVPNNFM KDLEKRSCNI
SLEDECNKRP TFLDMPKNVT NKGNDGLGQQ VHGDIDRSCY YFSSDIVKDL EKLSLRKPSG
NHPCRNGCVS AKDKPIFLPH PCNKSTSNSG SCSNNLFEKH SMHLSPLCCS GITPDDDESS
PLDELAMREI TDFDNLLPLH DPDLYIEIVK NTKSVPEYSE VAYPDYFGHV PPFFKERLLE
RPYGVQRSKI FQDIERMIHP NDIIDRVVYD LDNSSCSAQD ESEVLKFNSK FESGNLRKVI
QIRKNEYDLI LNSDINSNHY HQWFYFEVSG MRTGVAYRFN IINCEKSNSQ FNYGMQPLMY
SVQEALASRP WWYRVGMDIC YYKNHFSRSS IATGGQKGKS YYTITFTVTF PHRDDVCYFA
YHYPYTYSTL KMHLKKLESL HNPQQVYFRQ EVLCETLGGN GCPVITITAM PESNYYEHVY
QFRNRPYIFL SSRVHPGETN ASWVMKGTLE FLMGSSTSAQ SLRESYIFKI VPMLNPDGVI
NGNHRCSLSG EDLNRQWQNP NVDLHPTIYH TKGLLQYLAA IRRTPLVYCD YHGHSRKKNV
FMYGCSIKET VWHTNANAAS CDMVEDSGYR TLPKVLNQLA PAFSMSSCSF VVEKSKESTA
RVVVWREIGV QRSYTMESTL CGCDQGKYKD LQIGTKELEE MGAKFCVGLL RLKRLTSPME
LTLPPSLIDI ENELIESSCK VASPTTYVLE DDEPRFLEEV DYSAESNDDA DPDLPDTIGD
FENTALEEEG FSDSEITRTH TSGQST
