CBPC1_DANRE
ID CBPC1_DANRE Reviewed; 1153 AA.
AC Q4U2V3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 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 [MRNA].
RC STRAIN=SJD;
RA Yang C.-T., Johnson S.L.;
RT "Genetic analyses of larval melanocyte regeneration in zebrafish.";
RL Submitted (APR-2005) 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}.
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; DQ018111; AAY42353.1; -; mRNA.
DR RefSeq; NP_001019616.1; NM_001024445.2.
DR AlphaFoldDB; Q4U2V3; -.
DR SMR; Q4U2V3; -.
DR STRING; 7955.ENSDARP00000025120; -.
DR PaxDb; Q4U2V3; -.
DR PRIDE; Q4U2V3; -.
DR GeneID; 554164; -.
DR KEGG; dre:554164; -.
DR CTD; 23287; -.
DR ZFIN; ZDB-GENE-081104-267; agtpbp1.
DR eggNOG; KOG3641; Eukaryota.
DR InParanoid; Q4U2V3; -.
DR BRENDA; 3.4.17.24; 928.
DR PRO; PR:Q4U2V3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0043009; P:chordate embryonic development; IMP:ZFIN.
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 GO; GO:0033077; P:T cell differentiation in thymus; IMP:ZFIN.
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..1153
FT /note="Cytosolic carboxypeptidase 1"
FT /id="PRO_0000308692"
FT REGION 357..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..385
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 895
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 845
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 848
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 942
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 1153 AA; 129792 MW; DC910C842BD8D4B0 CRC64;
MNKPKMAAEK SASRVLMLLS QLERLNEESR VSDNDAIRQV TGKILHLIQT QEKTRKEVGS
KGSGGMEIIL SSLENTRDLQ TTLNILGILN ELLTVGGGRR TGLFVSKGGT AILLQLLVSS
SKDPPANEEL MLHIHSLLVK VGPKDRKFGV KARLNGALNV TLNLAKHNLQ NYKLLLPCLQ
VLRVYSSNSV NAVSLGKSGA LEILFEIVGP FSKKSTTLLK VALDTLAALL KSGMNARRAV
DRGYLPTLLA IYQDWHRNDT RHRHVIIRKS ILGCIKNITN IKLGRKAFIE ASGMRILYNT
STECLPVRTL DPLVNTSSLI MRKCFPKNRL PLPTIKSVFL YPLPHIPAGG PVAQLYNQPP
GVDDVVDESD ENEATEVDTE NDTENEEDDT GHKTQNDDIE TDINKLRPKQ MNTRPFEELR
VYEHFCREFT ETFQDIDFED SISAIPPSRV NSELHRPIII PTTQSSPGLQ NRRPLRESAL
PLKPEQSPLE LDSISIAKRP DGRADADLVC SLGHLILDAA VNGGSVDGCQ DDGGEQSVLE
VPDTAALLPL HDPELYLEMV KSTRSVPGYT EVAYPDYFGH VALNLREPIL ERVYGVQRTK
IFQDIERLIH SSDILDKVVY DLDNQSSPLT DNGESLKFNS KFESGNLRKA IQVRKFEYDL
ILNSDINSNH YHQWFYFEVG NMRPGVRYRF NIINCEKSNS QFNYGMQVIM YSVQEAINGS
PHWVRTGSDI CYYKNHFARS SIAAGGQKGK SYFTMTFTVT FQHKDDVCYF AYHYPYTYSM
LKMHLQKLSA LCTPEIYYRQ EDLCETLGGN GCPLLTITAM PESSSDEHIS QFRSRPVIFL
SARVHPGETN SSWVMKGSLE FLMSCSPQAQ SLRQSYIFKI MPMLNPDGVI NGNHRCSLSG
EDLNRQWQNP NAELHPTIYH AKSLLQYLRA TGRTPLVFCD YHGHSRKKNV FMYGCSIKET
MWQSSVNTST CDLNEDLGYR TLPKLLSQMA PAFSLSSCSF VVERSKEATA RVVVWREIGV
QRSYTMESTL CGCDQGKYKG LQIGTSELEE MGSQFCLALL RLRRFTSPLE LHNHNSHLLD
MENELIDTRH IPNITSPTTY VLDEDEPAFL EEVDYSAESN DENDPELEPD LRDNHALPDP
SSDSELSHQD SLT
