CBPC1_CHICK
ID CBPC1_CHICK Reviewed; 1224 AA.
AC E1C3P4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Cytosolic carboxypeptidase 1 {ECO:0000250|UniProtKB:Q641K1};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q641K1};
DE EC=3.4.17.24 {ECO:0000250|UniProtKB:Q641K1};
DE AltName: Full=ATP/GTP-binding protein 1 {ECO:0000250|UniProtKB:Q641K1};
DE AltName: Full=Protein deglutamylase CCP1 {ECO:0000305};
GN Name=AGTPBP1; Synonyms=CCP1K;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation
CC of 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. Specifically cleaves tubulin long-side-chains, while it is not
CC able to remove the branching point glutamate. Also catalyzes the
CC removal of polyglutamate residues from the carboxy-terminus of alpha-
CC tubulin as well as non-tubulin proteins.
CC {ECO:0000250|UniProtKB:Q641K1}.
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:Q641K1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000250|UniProtKB:Q641K1};
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:Q641K1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000250|UniProtKB:Q641K1};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus
CC {ECO:0000250|UniProtKB:Q641K1}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q641K1}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AADN02064844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02064845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02064846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02064847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02064848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02064849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02064850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02064851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C3P4; -.
DR SMR; E1C3P4; -.
DR STRING; 9031.ENSGALP00000020540; -.
DR PaxDb; E1C3P4; -.
DR PRIDE; E1C3P4; -.
DR VEuPathDB; HostDB:geneid_427460; -.
DR eggNOG; KOG3641; Eukaryota.
DR InParanoid; E1C3P4; -.
DR PhylomeDB; E1C3P4; -.
DR TreeFam; TF313794; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; 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:0021702; P:cerebellar Purkinje cell differentiation; ISS:UniProtKB.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0050905; P:neuromuscular process; ISS:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:0035610; P:protein side chain deglutamylation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06906; M14_Nna1; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033852; CBPC1/4.
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 SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Mitochondrion; Nucleus; Protease; Reference proteome; Zinc.
FT CHAIN 1..1224
FT /note="Cytosolic carboxypeptidase 1"
FT /id="PRO_0000403756"
FT REGION 361..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 968
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 921
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 1015
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
SQ SEQUENCE 1224 AA; 137742 MW; 6A4AFE6AFBBAF01A CRC64;
MKVKKNLTCS VSTSSRTMSL LSQLEKINLD SVLGEADNAR YVTAKILHLV QSQEKTKKEM
TSKGSSAIEV ILSTLENTRD PQTILNILSI LIELVSVGGG RRASVLVTKG GTQILLQLLL
NASKESPPNE ELMVLLHTLL AKIGPKDKKI GMKARINGAL NISLNLVKQN LQNHRLILPC
LQVLRVYSTN SVNAVSLGKN GVVELMFKII GPFSKKNTSL MKVALDTLAA LLKSKTNARR
AVDRGYVHML LTIYVDWHRH DSRHRYMLIR KGVLQCIKSV TNIKLGRKAF IDANGMKILY
NTSQECLAVR TLDPLVNTSS LIMRKCFPKN RLPLPTIKSA FHFQLPVIPA SGPVAQMYNL
PPDVDDVVDE SDDNDDAETE SEIETEDDKD QNFKNDDIET DINKLKPRQE LGRPLEELKM
YEQFFPELTE NFQECDLVSK EPKPFVSNAN LGGPIVVPTA GEEFSAETNP SVIGISLKEG
NPLLTEEYNR RPAFLGLPKK DSIKASSLLQ QNVQRNLLPS CQCLSQEIVT GLDRISLQNT
SENDQYYATG CVIKKDNKTS LTPLACSKTC EHVSPCGSSL FEGSSVHLGK FCCTGVESEE
EDSKSSSSGE QVVLEVSDVS PVHDCDLYIE MVKTTKSIPE YSEVAYPDYF GHIPPPFKEP
ILERPYGVQR TKISQDIERL IHQNDIIDRV VYDLDNSICS APEEVDVLKF NSKFESGNLR
KVIQIRKNEY DLILNSDINS NHYHQWFYFE VSGMKTGIGY RFNIINCEKS NSQFNYGMQP
LMYSVQEALN SRPSWTRVGT DICYYKNHFS RSSIAAGGQK GKSYYTITFT VTFQHKDDVC
YFAYHYPYTY STLKMHLQKL ESMHNPQQIY FRQDALCETL GGNICPIVTI TAMPESNYYE
HICQFRNRPY IFLSARVHPG ETNASWVMKG TLEYLMSSNP SAQSLRESYI FKIIPMLNPD
GVINGNHRCS LSGEDLNRQW QNPNPDLHPT IYHAKGLLQY LAAIKRLPLV YCDYHGHSRK
KNVFMYGCSI KETMWHTNVN TASCDLMEDP GYRVLPKILS QTAPAFCMGS CSFVVEKSKE
STARVVVWRE IGVQRSYTME STLCGCDQGK YKGLQIGTKE LEEMGAKFCV GLLRLKRMAS
PLEYNLPSGL LDIENELIES SCKVTSPTTY VLDEDEPRFL EEVDYSAESN DDQDAELADN
VGDYEANNQE DGLSDSDSTR ILLS
