CBPC1_CAEEL
ID CBPC1_CAEEL Reviewed; 1015 AA.
AC O76373;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytosolic carboxypeptidase 1;
DE EC=3.4.17.- {ECO:0000305|PubMed:21982591, ECO:0000305|PubMed:29129530};
GN Name=ccpp-1 {ECO:0000312|WormBase:F56H1.5};
GN ORFNames=F56H1.5 {ECO:0000312|WormBase:F56H1.5};
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 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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF GLY-596.
RX PubMed=21982591; DOI=10.1016/j.cub.2011.08.049;
RA O'Hagan R., Piasecki B.P., Silva M., Phirke P., Nguyen K.C., Hall D.H.,
RA Swoboda P., Barr M.M.;
RT "The tubulin deglutamylase CCPP-1 regulates the function and stability of
RT sensory cilia in C. elegans.";
RL Curr. Biol. 21:1685-1694(2011).
RN [4]
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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29129530; DOI=10.1016/j.cub.2017.09.066;
RA O'Hagan R., Silva M., Nguyen K.C.Q., Zhang W., Bellotti S., Ramadan Y.H.,
RA Hall D.H., Barr M.M.;
RT "Glutamylation Regulates Transport, Specializes Function, and Sculpts the
RT Structure of Cilia.";
RL Curr. Biol. 27:3430-3441.E6(2017).
CC -!- FUNCTION: Catalyzes the deglutamylation of polyglutamate side chains
CC generated by post-translational polyglutamylation of proteins such as
CC tubulins (Probable). Via the deglutamylation of tubulin, regulates the
CC localization and velocity of kinesin motors and the structural
CC integrity of microtubules in sensory cilia (PubMed:21982591,
CC PubMed:29129530). In male CEM sensory neurons, regulates the cilia
CC release of bioactive extracellular vesicles (PubMed:29129530). Also
CC regulates microtubule dynamics in uterine muscle cells
CC (PubMed:24780738). {ECO:0000269|PubMed:21982591,
CC ECO:0000269|PubMed:24780738, ECO:0000269|PubMed:29129530,
CC ECO:0000305|PubMed:21982591, ECO:0000305|PubMed:29129530}.
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: Perikaryon {ECO:0000269|PubMed:21982591}. Cell
CC projection, cilium {ECO:0000269|PubMed:21982591}. Cell projection,
CC dendrite {ECO:0000269|PubMed:21982591}.
CC -!- TISSUE SPECIFICITY: In hermaphrodites and males, expressed in amphid
CC and IL2 ciliated sensory neurons (PubMed:20519502, PubMed:21982591). In
CC males, expressed in CEM head neurons, RnB and HOB tail neurons, and in
CC gubernacular erector and retractor muscles (PubMed:21982591).
CC {ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:21982591}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the L1 or L4 larval
CC stages causes a defect in egg-laying without affecting uterine and
CC vulva muscle function. {ECO:0000269|PubMed:24780738}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BX284601; CCD62967.1; -; Genomic_DNA.
DR RefSeq; NP_491674.2; NM_059273.5.
DR AlphaFoldDB; O76373; -.
DR SMR; O76373; -.
DR BioGRID; 37696; 1.
DR STRING; 6239.F56H1.5; -.
DR MEROPS; M14.A36; -.
DR EPD; O76373; -.
DR PaxDb; O76373; -.
DR PeptideAtlas; O76373; -.
DR EnsemblMetazoa; F56H1.5.1; F56H1.5.1; WBGene00018995.
DR GeneID; 172241; -.
DR KEGG; cel:CELE_F56H1.5; -.
DR UCSC; F56H1.5; c. elegans.
DR CTD; 172241; -.
DR WormBase; F56H1.5; CE41324; WBGene00018995; ccpp-1.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000173340; -.
DR HOGENOM; CLU_297036_0_0_1; -.
DR InParanoid; O76373; -.
DR OMA; FCGFHKG; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; O76373; -.
DR BRENDA; 3.4.17.24; 1045.
DR PRO; PR:O76373; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00018995; Expressed in embryo and 4 other tissues.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035609; P:C-terminal protein deglutamylation; IBA:GO_Central.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0035610; P:protein side chain deglutamylation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell projection; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..1015
FT /note="Cytosolic carboxypeptidase 1"
FT /id="PRO_0000403764"
FT REGION 384..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 843
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 792
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT MUTAGEN 596
FT /note="G->R: In my22; abnormal accumulation of pkd-2 and
FT klp-6 in cilia and dendrites of male CEM, HOB and RnB
FT neurons. Age-dependent defects in cilia structure
FT associated with impaired osmolarity responses. Microtubule
FT polyglutamylation levels are increased in CEM neuron cilia
FT but reduced in the middle segment of amphid neuron cilia.
FT Impaired male mating behavior."
FT /evidence="ECO:0000269|PubMed:21982591"
SQ SEQUENCE 1015 AA; 116056 MW; BB183B3EC5BB9B3D CRC64;
MPSDSDDVAA VKQPWSQLIV DISNFLSEHP QSKTSQALLP SCNGVWSDEE KLELIEAFGH
KKQSHLTKSG VKAVLAAFEG DRTQPDVIFL CRLLHLIFSH FSSENDRKKE KYIVKCDVIA
TLTRITRKRI IMTLDVTDES SIDHNLDEVL WKLLHKIGLK DPRVSLKVRM GGLISPMCKL
FIQKDTLPEL FLPFFIKISR SPRNGQAIGR YEGFMTRLLV KIKALDASDQ TSQVLLLDKH
LQLLFFTMKN KRTRTQLLRE NICKYLLEVL RRHLASSSNS RPTRLLSSLF GTFDKSLSAA
HTEVVIGTIA ILRLLSNFKK ARDELKNLQV LDICSRELKE FWSDEWKTGP KSRIVDSLSA
LCLRCMSPLP YPLETRRFPI DFPLPTATPS TPGGHGRIRN SSSINISFDN GRSSDEDGMD
EEDEAFVRDD DDEGKDDRGS DDDDGKDDDE INGALPKTTR LNPQQLAKYA PFFVENEQGT
LQPTFSMIYQ TNQESWRSIC EKTRHVMPIH HHLPIEMFNT PTRIREKTAK TSNNMKKMII
EELDKPERSA TSNQVIYDLD TAAFDGLPSP ELPFVTGGGK LDTSKDLQFD SRFESGNLRM
VIQVAPTHYE LFLSPDVNQL RDHYQWFFFQ VSNMRKSVKY TFEIVNCLKS TSLYSQGMQP
VMYSMMESAN GWRRVGENVC YFRNLYINEN EEKKNVEEQK KKKYYYSIRF NVTFQNTGDI
CYIAYHYPYT YSFLNSSLSM LKKRKQENVY CREDVIGHSL AGNPIKMLTI TTPASAAEIA
AREVIVLSAR VHPGETNASW IMQGILENLL CRQSNEMYRL RESFIFKIVP MINPDGVTNG
SHRCSLAGID LNRMWDRPNE ALHPEVFATK AIIQYLCEVA NKKPFAYVDI HGHSKKWDYF
VYGNNASESW RADDVLDVGA AQLEEELHLA LPKALEATCP SRFNASECRF NITRAKESSA
RVNVWRQFGV STAYTLESTF CGFHKGQNSG YQINTSDLKE IGRDLLHSFL EMTKT
