CBPC1_XENLA
ID CBPC1_XENLA Reviewed; 1225 AA.
AC Q6DD21;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, 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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) 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; BC077808; AAH77808.1; -; mRNA.
DR RefSeq; NP_001087104.1; NM_001093635.1.
DR AlphaFoldDB; Q6DD21; -.
DR SMR; Q6DD21; -.
DR BioGRID; 103853; 1.
DR IntAct; Q6DD21; 1.
DR MaxQB; Q6DD21; -.
DR DNASU; 446993; -.
DR GeneID; 446993; -.
DR KEGG; xla:446993; -.
DR CTD; 446993; -.
DR Xenbase; XB-GENE-5932611; agtpbp1.L.
DR OMA; HVATCGN; -.
DR OrthoDB; 481670at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446993; Expressed in lung and 19 other tissues.
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..1225
FT /note="Cytosolic carboxypeptidase 1"
FT /id="PRO_0000308693"
FT REGION 366..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1225
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 COMPBIAS 1181..1208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 964
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 914
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 1011
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 1225 AA; 138782 MW; 9D560A9F5D0513B3 CRC64;
MSKVKATAEK CQLNISRIQS LLSQLEKVNA ESLLFDTDNT RYVTAKIFHL AQTQEKTRKE
MTAKGSTGIE VILCTLENTR DLQTILNILN ILNELASTAG GRRINALISK GGARILLQLL
LSASKESPSN EELMIVLHSL LAKLGPKDKK FGVKARVSGA LNISLNLVKQ NLQNPRLILP
CLQVLRVCCM NSVNSAYLGK NGAVEILFKI IGPFTRRNTG LIKVSLDTLA ALLKSRTNAR
KAVDRAYVQT LISTYMDWHR HDTRHRHMLI RKGILQCLKS ITNIKIGRKA FIDANGMKTL
YNTSQECQAV RTLDPLVNTS SLIMRKCFPK NRLPLPTIKS AFQFQLPFMP TSGPVALLYS
MPPEVDDVVD ESDDNEDTDA ETEAEAENED SDQICKNDDI ETDITKLIPG QELGRTLEDL
KMYERFFPEL TEDFQEFDLV SNEPKPGAKL GPIIVPTAGE EQPEVPNNFM KNLARRSCNI
SLEDESNQRP TFLDMSKNVT NKGNSLDQKV HVDKDGSCYY YSNDIVRDLE KLSLHKASGN
HPCRNGCVSA KDKPNFLPHP CNKSTSSSIS CSNSLFEKHS MHLGPLCCSG IAPDDDESSP
LDEQVMREMT DFDSILPLHD PDLYIEIVKN TKSVPEYTEV AYPDYFGHVP PFFKERLLER
PYGVQRSKIF QDIERMIHPN DIIDRVIYDL DNPSCSAHDE IDILKFNSKF ESGNLRKVIQ
IRKNEYDLIL NSDINSNHYH QWFYFEVSGM RTGVAYRFNI INCEKSNSQF NYGMQPLMYS
VQEALASRPW WYRVGTDICY YKNHFSRSSL ATGGQKGKSY YTITFTVTFP HKDDVCYFAY
HYPYTYSTLK MHLQKLESLH SPQQIYFRQE VLCETLGGNG CPVITITAMP ESNYYEHVYQ
FRNRPYIFLT SRVHPGETNA SWVMKGTLEF LMGSSATAQS LRESYIFKIV PMLNPDGVIN
GNHRCSLSGE DLNRQWQNPN SDLHPTIYHT KGLLQYLSAI KRVPLVYCDY HGHSRKKNVF
MYGCSIKETV WHTNANAASC DMVEESGYKT LPKVLNQIAP AFSMSSCSFV VEKSKESTAR
VVVWKEIGVQ RSYTMESTLC GCDQGKYKDL QIGTKELEEM GAKFCVGLLR LKRLTSPMEL
TLPPSLIDIE NELIESSCKV ASPTTYVLED DEPRFIEEVD YSAESNDDVD PDLPENIGDF
ETSTLEEESF SDSEITRTHM SGQST
