CBPC3_BOVIN
ID CBPC3_BOVIN Reviewed; 1003 AA.
AC E1B9D8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Cytosolic carboxypeptidase 3 {ECO:0000250|UniProtKB:Q8CDP0};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q8CDP0};
DE AltName: Full=ATP/GTP-binding protein-like 3;
DE AltName: Full=Protein deglutamylase CCP3 {ECO:0000305};
GN Name=AGBL3; Synonyms=CCP3 {ECO:0000250|UniProtKB:Q8CDP0};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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. May catalyze the hydrolysis of aspartate from
CC the carboxy-terminus of target proteins. Does not show detyrosinase or
CC deglycylase activities from the carboxy-terminus of target proteins.
CC {ECO:0000250|UniProtKB:Q8CDP0}.
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:Q8CDP0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000250|UniProtKB:Q8CDP0};
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:Q8CDP0}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AAFC03005324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03061398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03061399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03061400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03061401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1B9D8; -.
DR SMR; E1B9D8; -.
DR STRING; 9913.ENSBTAP00000033443; -.
DR PaxDb; E1B9D8; -.
DR PRIDE; E1B9D8; -.
DR eggNOG; KOG1814; Eukaryota.
DR eggNOG; KOG3641; Eukaryota.
DR InParanoid; E1B9D8; -.
DR OrthoDB; 481670at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Carboxypeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..1003
FT /note="Cytosolic carboxypeptidase 3"
FT /id="PRO_0000403760"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 1003 AA; 116561 MW; 082FA2A4E3360A89 CRC64;
MSEDSEKEDY SDRTISDEDE SDEDNFMKFV NEDIHQCALL TADSISDPFF PRTTQILLEY
QLGRWVPRLR KPRDLYGVSS SGPLSPTRWP YHCEVIDEKI EHIDWTPSNP EPMYIPTGLE
VEPLYANSKE ETVVYLAEDA YKEPCFVYSR VGGNRTPLKQ PVDNCDDTLM FEARFESGNL
QKVVKVGEYE YQLTVRPDLF TNKHTQWYYF QVTNTQAGIV YRFTITNFTK PASLYNRGMR
PLFYSEKEAS AHNIGWQRIG DQIKYYRNNQ GQDRHHHFSL TWTFQFPHSK DTCYFAHCYP
YTYTNLQEYL SGINNDPVRS KFCKIRVLCH TIARNMVYIL TITTPLKNSE SRKRKAVILT
ARVHPGETNS SWIMKGFLDY ILGNSSDAKL LRDTFVFKVV PMLNPDGVIV GNYRCSLAGR
DLNRNYTSLL KESFPSVWYT RNMIRRLMEK REVILYCDLH GHSKKENIFM YGCDGSDRCK
ALYLQQRIFP LMLSKNCPDK FSFSSCKFNI QKSKEGTGRV VMWKMGIRNS FTMEATFCGS
TLGNKRGTHF NTKDLESMGY HFCDSLLDYC DPDRTKYYQC LKELDEMEKH INLEKVIDDS
DTSLKEITLD LETSSHASDS SESNDSQTDL LKLNSQIKTK KKQLKTKKER NSTIERHQNI
REEEQEVCDK GHLVQRHKES DSDVTDTRPS ISDDCIFDYF RRQLPNQGFF KILGLKFYCG
YTHMISQTVI QKLSRDQQRC VLGTDKKNQE TVQPRNNDLY GNCIKVTSLK CPLNKQTPIW
TEKTRIPTED LHHNLKSNMK ECPSFQSKKA DINWTDDEKR IYRDKNIAQT QEILQYLLPI
MRSTKNVQTT QIKEVFNPRT SFQIQHQQKP SSNINIRKCS TSWTPPRNLP LISQRTLIVS
TSKWLQPLDW KSSESSLPLG GPKKRRKYSR VKATKTKDMK AASSKWEMTP SSSEKDADKS
LQAEGSSQQG TMQTAPHPTK TKGEQPKKKH GQPAFHLKLQ RDT
