CBPC5_BOVIN
ID CBPC5_BOVIN Reviewed; 885 AA.
AC Q58CX9; A1A4I0; E1B7H7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0000250|UniProtKB:Q09M02};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q09M02};
DE EC=3.4.17.24 {ECO:0000250|UniProtKB:Q09M02};
DE AltName: Full=ATP/GTP-binding protein-like 5;
DE AltName: Full=Protein deglutamylase CCP5 {ECO:0000305};
GN Name=AGBL5; Synonyms=CCP5 {ECO:0000250|UniProtKB:Q09M02};
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 MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-885 (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) 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 alpha- and beta-
CC tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-
CC chain, as well as the branching point glutamate. Also catalyzes the
CC removal of alpha-linked glutamate residues from the carboxy-terminus of
CC alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS,
CC leading to CGAS antiviral defense response activation.
CC {ECO:0000250|UniProtKB:Q09M02}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-
CC glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208,
CC Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:143622;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-
CC terminal L-alpha-aminoacyl-[tubulin] + L-glutamate;
CC Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782,
CC ChEBI:CHEBI:149556; EC=3.4.17.24;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}.
CC Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Mainly cytoplasmic. Slight
CC accumulation in the nucleus is observed. Colocalizes with alpha-tubulin
CC in the mitotic spindle and with midbody microtubules in the
CC intercellular bridges formed during cytokinesis.
CC {ECO:0000250|UniProtKB:Q09M02, ECO:0000250|UniProtKB:Q8NDL9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58CX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58CX9-2; Sequence=VSP_040426;
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BT021818; AAX46665.1; -; mRNA.
DR EMBL; AAFC03088657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126504; AAI26505.1; -; mRNA.
DR RefSeq; NP_001019735.1; NM_001024564.1.
DR RefSeq; XP_005213081.1; XM_005213024.3. [Q58CX9-1]
DR AlphaFoldDB; Q58CX9; -.
DR SMR; Q58CX9; -.
DR STRING; 9913.ENSBTAP00000017831; -.
DR MEROPS; M14.025; -.
DR MEROPS; M14.036; -.
DR PaxDb; Q58CX9; -.
DR PRIDE; Q58CX9; -.
DR Ensembl; ENSBTAT00000017831; ENSBTAP00000017831; ENSBTAG00000013403. [Q58CX9-2]
DR Ensembl; ENSBTAT00000079929; ENSBTAP00000067922; ENSBTAG00000013403. [Q58CX9-1]
DR GeneID; 538585; -.
DR KEGG; bta:538585; -.
DR CTD; 60509; -.
DR VEuPathDB; HostDB:ENSBTAG00000013403; -.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000158032; -.
DR HOGENOM; CLU_007523_3_2_1; -.
DR InParanoid; Q58CX9; -.
DR OMA; NCAHFDF; -.
DR OrthoDB; 481670at2759; -.
DR TreeFam; TF324301; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000013403; Expressed in spermatid and 110 other tissues.
DR ExpressionAtlas; Q58CX9; baseline.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; 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:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0035611; P:protein branching point deglutamylation; ISS:UniProtKB.
DR GO; GO:0035608; P:protein deglutamylation; ISS:UniProtKB.
DR GO; GO:0035610; P:protein side chain deglutamylation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06236; M14_AGBL5_like; 1.
DR InterPro; IPR034286; M14_AGBL5-like.
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 Alternative splicing; Carboxypeptidase; Cytoplasm; Cytoskeleton; Hydrolase;
KW Metal-binding; Metalloprotease; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..885
FT /note="Cytosolic carboxypeptidase-like protein 5"
FT /id="PRO_0000305920"
FT REGION 343..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT VAR_SEQ 697..885
FT /note="EPRSQDRRRRQQPVTHRPTSSSLAPSPTPASSNLASSHMGSCLLPNSLSISG
FT SSCSFLSSGDKTEAVMVIGKGLLGAGPRIPCIRTRLQARPRLAQGSPPTRRGMRGSPGP
FT TSPIPQTKKSSEPELGPRCTPRLPQAGPPRPCSAPAFSPISCSLSDSQSRICYSGGPLG
FT QTEVCFVPKSPPFTVSPRV -> GKLVWEPLQQVFGCLGHCWGK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16305752, ECO:0000303|Ref.3"
FT /id="VSP_040426"
FT CONFLICT 12..13
FT /note="SR -> CG (in Ref. 1; AAX46665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 885 AA; 97441 MW; 0112D3720F09B49A CRC64;
MELRCGGLLF SSRFDSGNLA HVEKVESVSN DGEGVAGGAS ASTSSIASSP DYEFNVWTRP
DCAETEFENG NRSWFYFSVR GGTPGKLIKI NIMNMNKQSK LYSQGMAPFV RTLPTRPRWE
RIRDRPTFEM TETQFVLSFI HRFVEGRGAT TFFAFCYPFS YSDCQDLLSQ LDQRFLENSP
THSSPLDTIY YHRETLCYSL DGLRVDLLTI SSCHGLREDR EPRLEQLFPD ASTPRPFRFT
GKRIFFLSSR VHPGETPSSF VFNGFLDFIL RPDDPRAQTL RRLFVFKLIP MLNPDGVVRG
HYRTDSRGVN LNRQYLKPDA VLHPAIYGAK AVLLYHHVHS RLNSQSPSEH QHSSHLPPDA
PLSDPEKADS LQNRAHLGRS SSGDKPEAWT QTEVAEQKPN SVWITPQESA EVEQLAPDAI
PPRESGVAYY VDLHGHASKR GCFMYGNSFS DENTQVENML YPKLISLNSA HFDFQGCNFS
EKNMYARDRR DGQSKEGSGR VAIYKASGII HSYTLECNYN TGRSVNSIPA ACHDNGRASP
PPPPAFPSRY TVELFEQVGR AMAIAALDMA ECNPWPRIVL SEHSSLTNLR AWMLKHVRSS
RGLSTTVNMS ISKKRGSRTP PRSNNGLPVS CSENTLSRAR SFSTGTSAGG SSSSQQNSPQ
MKNSPSFPFH GSRPAGLPGL GSSTQKVSHR VLGPVREPRS QDRRRRQQPV THRPTSSSLA
PSPTPASSNL ASSHMGSCLL PNSLSISGSS CSFLSSGDKT EAVMVIGKGL LGAGPRIPCI
RTRLQARPRL AQGSPPTRRG MRGSPGPTSP IPQTKKSSEP ELGPRCTPRL PQAGPPRPCS
APAFSPISCS LSDSQSRICY SGGPLGQTEV CFVPKSPPFT VSPRV
