CBPC5_AILME
ID CBPC5_AILME Reviewed; 884 AA.
AC D2GXM8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
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};
GN ORFNames=PANDA_001668;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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 -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; GL192369; EFB20547.1; -; Genomic_DNA.
DR RefSeq; XP_019663924.1; XM_019808365.1.
DR RefSeq; XP_019663929.1; XM_019808370.1.
DR AlphaFoldDB; D2GXM8; -.
DR SMR; D2GXM8; -.
DR STRING; 9646.ENSAMEP00000002036; -.
DR MEROPS; M14.025; -.
DR GeneID; 100467720; -.
DR KEGG; aml:100467720; -.
DR CTD; 60509; -.
DR eggNOG; KOG3641; Eukaryota.
DR HOGENOM; CLU_007523_3_2_1; -.
DR InParanoid; D2GXM8; -.
DR OMA; NCAHFDF; -.
DR OrthoDB; 481670at2759; -.
DR TreeFam; TF324301; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Carboxypeptidase; Cytoplasm; Cytoskeleton; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..884
FT /note="Cytosolic carboxypeptidase-like protein 5"
FT /id="PRO_0000403761"
FT REGION 343..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..670
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..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..859
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 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
SQ SEQUENCE 884 AA; 96914 MW; 0217A5C6E56BB2B2 CRC64;
MELRCGGLLF SSRFDSGNLA HVEKVDSVSG DGEGGAAGAS APFSSIASSP DYEFNVWTRP
DCAETEFENG NRSWFYFSVR GGTPGKLIKI NIMNMNKQSK LYSQGMAPFV RTLPTRPRWE
RIRDRPTFEM TETQFVLSFV HRFVEGRGAT TFFAFCYPFS YSDCQDLLNQ LDQRFLENHP
THSSPLDTIY YHREILCYSL DGLRVDLLTI TSCHGLREDR EPRLQQLFPD TGTPRPFCFT
GKRIFFLSSR VHPGETPSSF VFNGFLDFIL RPDDPRAQTL RRLFVFKLIP MLNPDGVVRG
HYRTDSRGVN LNRQYLKPDA ALHPAIYGAK AVLLYHHVHS RLHPQSPSEH QHSPCLPPDA
PLSDLEKANH LRNEAHLGHT SDGDSPEDWT QTRPAEQKAS GVWLMPQQCA DAEQPAPDTI
PPKESGVAYY VDLHGHASKR GCFMYGNSFS DESTQVENML YPKLISLNSA HFDFQGCNFS
EKNMYARDRR DGQSKEGSGR VAIYKASGII HSYTLECNYN TGRSVNSIPA ACHDNGRASP
PPPPAFPSRY TVELFEQVGR AMAIAALDMA ECNPWPRIVL SEHSSLTNLR AWMLKHVRSS
RGLSSTVSGA VNKKRGSRTP PRSNSGLPVS CSENPLSRAR SFSTGTSAGG SSSSQQNSPQ
MKNSPSFPFH GSRPTGLPGL GSSTQKVSHR VLGPVREPRS QDRRRRQQPL THRPTSSSLA
PSPNPTSSSP ASSHSTGPCL LPSAFSVSGS SCSLLSSGDK PEAVMVIGKG LLGPRIPCIR
TRLQVRPRLG QGSPPTCRGM SGSSGPTSPI PRTRESSEPE PGPHSAPGLP QAGPPRPRSA
PAFSPISCSL SDSQSRICYS GGPLGQPEVC FGPKSPPLTV SPRV
