CBPC6_CAEEL
ID CBPC6_CAEEL Reviewed; 459 AA.
AC Q09296;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cytosolic carboxypeptidase 6;
DE EC=3.4.17.- {ECO:0000269|PubMed:17244817, ECO:0000305|PubMed:20519502};
DE AltName: Full=ATP/GTP-binding protein-like 4 homolog;
DE Short=CeAGBL4;
GN Name=ccpp-6 {ECO:0000312|WormBase:EEED8.6};
GN Synonyms=Nnac2 {ECO:0000303|PubMed:17244817};
GN ORFNames=EEED8.6 {ECO:0000312|WormBase:EEED8.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17244817; DOI=10.1096/fj.06-7330com;
RA Rodriguez de la Vega M., Sevilla R.G., Hermoso A., Lorenzo J., Tanco S.,
RA Diez A., Fricker L.D., Bautista J.M., Aviles F.X.;
RT "Nna1-like proteins are active metallocarboxypeptidases of a new and
RT diverse M14 subfamily.";
RL FASEB J. 21:851-865(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=20519502; DOI=10.1074/jbc.c110.128280;
RA Kimura Y., Kurabe N., Ikegami K., Tsutsumi K., Konishi Y., Kaplan O.I.,
RA Kunitomo H., Iino Y., Blacque O.E., Setou M.;
RT "Identification of tubulin deglutamylase among Caenorhabditis elegans and
RT mammalian cytosolic carboxypeptidases (CCPs).";
RL J. Biol. Chem. 285:22936-22941(2010).
RN [4]
RP FUNCTION.
RX PubMed=23000142; DOI=10.1016/j.devcel.2012.08.010;
RA Ghosh-Roy A., Goncharov A., Jin Y., Chisholm A.D.;
RT "Kinesin-13 and tubulin posttranslational modifications regulate
RT microtubule growth in axon regeneration.";
RL Dev. Cell 23:716-728(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24780738; DOI=10.1016/j.devcel.2014.03.007;
RA Lacroix B., Bourdages K.G., Dorn J.F., Ihara S., Sherwood D.R.,
RA Maddox P.S., Maddox A.S.;
RT "In situ imaging in C. elegans reveals developmental regulation of
RT microtubule dynamics.";
RL Dev. Cell 29:203-216(2014).
CC -!- FUNCTION: Metallocarboxypeptidase that catalyzes the removing of
CC polyglutamate side chains that are present on the gamma-carboxyl group
CC of glutamate residues of tubulin in sensory cilia (PubMed:17244817,
CC PubMed:20519502). Probably via the deglutamylation of tubulin, promotes
CC microtubule stability required for axon regrowth after injury
CC (PubMed:23000142). Also regulates microtubule dynamics in uterine
CC muscle cells (PubMed:24780738). {ECO:0000269|PubMed:17244817,
CC ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:23000142,
CC ECO:0000269|PubMed:24780738}.
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:0000305|PubMed:20519502};
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 {ECO:0000250|UniProtKB:Q09LZ8}.
CC -!- TISSUE SPECIFICITY: Expressed in labial and amphid neurons.
CC {ECO:0000269|PubMed:20519502}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L1 or L4 larval
CC stages or in the egg-laying apparatus causes a reduction in egg-laying
CC due to a defect in the egg-laying apparatus muscles.
CC {ECO:0000269|PubMed:24780738}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BX284602; CCD68733.1; -; Genomic_DNA.
DR PIR; T15916; T15916.
DR RefSeq; NP_495012.2; NM_062611.2.
DR AlphaFoldDB; Q09296; -.
DR SMR; Q09296; -.
DR BioGRID; 48845; 2.
DR DIP; DIP-26727N; -.
DR STRING; 6239.EEED8.6; -.
DR MEROPS; M14.A31; -.
DR PaxDb; Q09296; -.
DR PRIDE; Q09296; -.
DR EnsemblMetazoa; EEED8.6.1; EEED8.6.1; WBGene00017136.
DR GeneID; 184043; -.
DR KEGG; cel:CELE_EEED8.6; -.
DR UCSC; EEED8.6; c. elegans.
DR CTD; 184043; -.
DR WormBase; EEED8.6; CE40199; WBGene00017136; ccpp-6.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000155042; -.
DR HOGENOM; CLU_007523_6_1_1; -.
DR InParanoid; Q09296; -.
DR OMA; PYTEEAX; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; Q09296; -.
DR BRENDA; 3.4.17.24; 1045.
DR PRO; PR:Q09296; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017136; Expressed in larva.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0035608; P:protein deglutamylation; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:WormBase.
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 1: Evidence at protein level;
KW Carboxypeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..459
FT /note="Cytosolic carboxypeptidase 6"
FT /id="PRO_0000065272"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 459 AA; 53241 MW; 493371030E293619 CRC64;
MGYVGNVSYP DTIPGQGNLV FEASFESGNL GRVDKVSCSE YDLFIRPDTL NNKYRVWFYF
ECKNASENQR AIFNIVNFSK QRTLFEMGIA APVVKSNAQN SWARIPSRHI YYYRSSQHND
RWILSFAFIF ESPDPVQFAY CIPYTYGQMQ IWLNELESRK YPFFHRDLLV QTVQKRRVDL
ITIDATPDTF QGSKKMIFLT ARVHPGESPS SHVMHGIIEF LVSKDDRAQK LRKVYCFKII
PMLNPDGVFL GNYRCSLMGH DLNRMWRTPS DWAHPSIYAV KNLLTQYDNN PQAQTVIYVD
LHAHSQKPNC FLYGNVNMSA VEEKSTFRQL WLPHLLADLS EDYSLEFTQF NTDVEKAGTG
RRTMGDLLSC LCYTLEVSFF SYRHTDSSGN GIQHCTPYLQ YKYEALGEAF CRALLNFYEA
DCGLREIVLE RPFKTFLPAR AQKTLKKQAR KVIQTVMMK
