CBPC5_RAT
ID CBPC5_RAT Reviewed; 832 AA.
AC B2GV17;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC166490; AAI66490.1; -; mRNA.
DR RefSeq; NP_001119844.1; NM_001126372.1.
DR AlphaFoldDB; B2GV17; -.
DR SMR; B2GV17; -.
DR STRING; 10116.ENSRNOP00000011635; -.
DR MEROPS; M14.036; -.
DR PaxDb; B2GV17; -.
DR PRIDE; B2GV17; -.
DR GeneID; 362710; -.
DR KEGG; rno:362710; -.
DR CTD; 60509; -.
DR RGD; 1598311; Agbl5.
DR VEuPathDB; HostDB:ENSRNOG00000008612; -.
DR eggNOG; KOG3641; Eukaryota.
DR HOGENOM; CLU_007523_3_2_1; -.
DR InParanoid; B2GV17; -.
DR OMA; NCAHFDF; -.
DR OrthoDB; 481670at2759; -.
DR PRO; PR:B2GV17; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008612; Expressed in testis and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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 Carboxypeptidase; Cytoplasm; Cytoskeleton; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Protease; Reference proteome; Zinc.
FT CHAIN 1..832
FT /note="Cytosolic carboxypeptidase-like protein 5"
FT /id="PRO_0000403762"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..752
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 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 832 AA; 92554 MW; D9977530F97FA44A CRC64;
MELRCGGLLF SSRFDSGNLA HVEKVETVPS DGEGVGGAAT APTSGSASSP DYEFNVWTRP
DCAETEYENG NRSWFYFSVR GGTPGKLIKI NIMNMNKQSK LYSQGMAPFV RTLPSRPRWE
RIRERPTFEM TETQFVLSFV HRFVEGRGAT TFFAFCYPFS YSDCQDLLSQ LDQRFPENYS
AHSSPLDSIY YHRELLCYSL DGLRVDLLTI TSCHGLRDDR EPRLEQLFPD VGTPRPFRFT
GKRIFFLSSR VHPGETPSSF VFNGFLDFIL RPDDPRAQTL RRLFVFKLIP MLNPDGVVRG
HYRTDSRGVN LNRQYLKPDA VLHPAIYGAK AVLLYHHVHS RLNSKNPSNQ QPSSLHLPPE
VPLSDLEKAN NLHNELHLGQ SPDGENHDRW TETEPTEEKT DPVWIMPQPI PELEEPAPDA
IPPKESGVAY YVDLHGHASK RGCFMYGNSF SDESTQVENM LYPKLISLNS AHFDFQGCNF
SEKNMYARDR RDGQSKEGSG RVAIYKASGI IHSYTLECNY NTGRSVNSIP AACHDNGRAS
PPPPPTFPSR YTVELFEQVG RALAIAALDM AECNPWPRIV LSEHSSLTNL RAWMLKHVRN
SRGLTSTANV GLNKKRGSRT PPKSNNGLPV SCSENALSRA RSFSTGTSTG GSSSQQNSPQ
MKNSPSFPFH GSRPAGLPGL GSSTQKVSHR VLGPVREPRC PDRRRRQQQQ QQQQQQQQQQ
QQQPLNQRST TSSLAPSPTL ASASPTSSRN MGSCLLPNSL SLSGSSCPFS SSGDKPEAVM
VIGKSLLGAG ARIPCIRTRL QTCQRRVSAR RGPGFPRLGP GWAGAHRRLA EG
