CBPC1_HUMAN
ID CBPC1_HUMAN Reviewed; 1226 AA.
AC Q9UPW5; B4DIT6; B4DRZ8; Q5VV80; Q63HM7; Q658P5; Q6P9D6; Q9H8U6; Q9H9W8;
AC Q9NVK1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytosolic carboxypeptidase 1 {ECO:0000303|PubMed:22170066};
DE EC=3.4.17.- {ECO:0000269|PubMed:22170066, ECO:0000269|PubMed:24022482, ECO:0000269|PubMed:30420557};
DE EC=3.4.17.24 {ECO:0000269|PubMed:22170066};
DE AltName: Full=ATP/GTP-binding protein 1 {ECO:0000250|UniProtKB:Q641K1};
DE AltName: Full=Nervous system nuclear protein induced by axotomy protein 1 homolog {ECO:0000250|UniProtKB:Q641K1};
DE AltName: Full=Protein deglutamylase CCP1 {ECO:0000305};
GN Name=AGTPBP1 {ECO:0000312|HGNC:HGNC:17258};
GN Synonyms=CCP1 {ECO:0000303|PubMed:22170066}, KIAA1035, NNA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 396-1226.
RC TISSUE=Esophageal carcinoma, and Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17244818; DOI=10.1096/fj.06-7329com;
RA Kalinina E., Biswas R., Berezniuk I., Hermoso A., Aviles F.X.,
RA Fricker L.D.;
RT "A novel subfamily of mouse cytosolic carboxypeptidases.";
RL FASEB J. 21:836-850(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22170066; DOI=10.1074/jbc.m111.309138;
RA Berezniuk I., Vu H.T., Lyons P.J., Sironi J.J., Xiao H., Burd B., Setou M.,
RA Angeletti R.H., Ikegami K., Fricker L.D.;
RT "Cytosolic carboxypeptidase 1 is involved in processing alpha- and beta-
RT tubulin.";
RL J. Biol. Chem. 287:6503-6517(2012).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24022482; DOI=10.1074/jbc.m113.497917;
RA Berezniuk I., Lyons P.J., Sironi J.J., Xiao H., Setou M., Angeletti R.H.,
RA Ikegami K., Fricker L.D.;
RT "Cytosolic carboxypeptidase 5 removes alpha- and gamma-linked glutamates
RT from tubulin.";
RL J. Biol. Chem. 288:30445-30453(2013).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=23085998; DOI=10.1096/fj.12-209080;
RA Rodriguez de la Vega Otazo M., Lorenzo J., Tort O., Aviles F.X.,
RA Bautista J.M.;
RT "Functional segregation and emerging role of cilia-related cytosolic
RT carboxypeptidases (CCPs).";
RL FASEB J. 27:424-431(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION.
RX PubMed=29593216; DOI=10.1038/s41467-018-03008-2;
RA Ye B., Liu B., Hao L., Zhu X., Yang L., Wang S., Xia P., Du Y., Meng S.,
RA Huang G., Qin X., Wang Y., Yan X., Li C., Hao J., Zhu P., He L., Tian Y.,
RA Fan Z.;
RT "Klf4 glutamylation is required for cell reprogramming and early embryonic
RT development in mice.";
RL Nat. Commun. 9:1261-1261(2018).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-423.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [19]
RP VARIANTS CONDCA 330-ARG--PRO-1226 DEL; ASP-694; 788-GLN--PRO-1226 DEL;
RP CYS-799; MET-851; 856-GLN--PRO-1226 DEL; CYS-910; TRP-918 AND LEU-990,
RP CHARACTERIZATION OF VARIANTS CONDCA ASP-694; MET-851; 856-GLN--PRO-1226
RP DEL; TRP-918 AND LEU-990, INVOLVEMENT IN CONDCA, AND FUNCTION.
RX PubMed=30420557; DOI=10.15252/embj.2018100540;
RG Undiagnosed Diseases Network;
RA Shashi V., Magiera M.M., Klein D., Zaki M., Schoch K.,
RA Rudnik-Schoeneborn S., Norman A., Lopes Abath Neto O., Dusl M., Yuan X.,
RA Bartesaghi L., De Marco P., Alfares A.A., Marom R., Arold S.T.,
RA Guzman-Vega F.J., Pena L.D., Smith E.C., Steinlin M., Babiker M.O.,
RA Mohassel P., Foley A.R., Donkervoort S., Kaur R., Ghosh P.S., Stanley V.,
RA Musaev D., Nava C., Mignot C., Keren B., Scala M., Tassano E., Picco P.,
RA Doneda P., Fiorillo C., Issa M.Y., Alassiri A., Alahmad A., Gerard A.,
RA Liu P., Yang Y., Ertl-Wagner B., Kranz P.G., Wentzensen I.M., Stucka R.,
RA Stong N., Allen A.S., Goldstein D.B., Schoser B., Roesler K.M.,
RA Alfadhel M., Capra V., Chrast R., Strom T.M., Kamsteeg E.J.,
RA Boennemann C.G., Gleeson J.G., Martini R., Janke C., Senderek J.;
RT "Loss of tubulin deglutamylase CCP1 causes infantile-onset
RT neurodegeneration.";
RL EMBO J. 37:0-0(2018).
CC -!- FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation
CC of tubulin and non-tubulin target proteins (PubMed:22170066,
CC PubMed:24022482, PubMed:30420557). 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 (PubMed:22170066, PubMed:24022482, PubMed:30420557).
CC Specifically cleaves tubulin long-side-chains, while it is not able to
CC remove the branching point glutamate (PubMed:24022482). Also catalyzes
CC the removal of polyglutamate residues from the carboxy-terminus of
CC alpha-tubulin as well as non-tubulin proteins such as MYLK
CC (PubMed:22170066). Involved in KLF4 deglutamylation which promotes KLF4
CC proteasome-mediated degradation, thereby negatively regulating cell
CC pluripotency maintenance and embryogenesis (PubMed:29593216).
CC {ECO:0000269|PubMed:22170066, ECO:0000269|PubMed:24022482,
CC ECO:0000269|PubMed:29593216, ECO:0000269|PubMed:30420557}.
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:0000269|PubMed:22170066, ECO:0000269|PubMed:24022482,
CC ECO:0000269|PubMed:30420557};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000305|PubMed:22170066, ECO:0000305|PubMed:24022482,
CC ECO:0000305|PubMed:30420557};
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:0000269|PubMed:22170066};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000305|PubMed:22170066};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with MYLK. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17244818,
CC ECO:0000269|PubMed:23085998}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q641K1}. Nucleus {ECO:0000269|PubMed:23085998}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q641K1}. Note=Localizes in both
CC the cytoplasm and nuclei of interphase and dividing cells.
CC {ECO:0000269|PubMed:23085998}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPW5-2; Sequence=VSP_029044;
CC Name=3;
CC IsoId=Q9UPW5-3; Sequence=VSP_040422, VSP_029044;
CC -!- DISEASE: Neurodegeneration, childhood-onset, with cerebellar atrophy
CC (CONDCA) [MIM:618276]: An autosomal recessive disorder characterized by
CC early onset of progressive neurodegeneration affecting the central and
CC peripheral nervous systems. Clinical features include global
CC developmental delay, impaired intellectual development, poor or absent
CC speech, and motor abnormalities. Brain imaging shows cerebellar
CC atrophy. Death in childhood may occur. {ECO:0000269|PubMed:30420557}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82987.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14100.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14505.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG61460.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH56222.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW62697.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB028958; BAA82987.2; ALT_FRAME; mRNA.
DR EMBL; AK001544; BAA91749.1; -; mRNA.
DR EMBL; AK022562; BAB14100.1; ALT_INIT; mRNA.
DR EMBL; AK023280; BAB14505.1; ALT_INIT; mRNA.
DR EMBL; AK295774; BAG58598.1; -; mRNA.
DR EMBL; AK299506; BAG61460.1; ALT_INIT; mRNA.
DR EMBL; AL157882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62694.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62698.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62697.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC060815; AAH60815.1; -; mRNA.
DR EMBL; BX648366; CAH56158.1; -; mRNA.
DR EMBL; AL833359; CAH56222.1; ALT_INIT; mRNA.
DR CCDS; CCDS6672.1; -. [Q9UPW5-2]
DR CCDS; CCDS69615.1; -. [Q9UPW5-3]
DR CCDS; CCDS83382.1; -. [Q9UPW5-1]
DR RefSeq; NP_001273644.1; NM_001286715.1.
DR RefSeq; NP_001273646.1; NM_001286717.1. [Q9UPW5-3]
DR RefSeq; NP_001317630.1; NM_001330701.1. [Q9UPW5-1]
DR RefSeq; NP_056054.2; NM_015239.2. [Q9UPW5-2]
DR RefSeq; XP_005251905.1; XM_005251848.2. [Q9UPW5-1]
DR RefSeq; XP_016870033.1; XM_017014544.1.
DR RefSeq; XP_016870035.1; XM_017014546.1.
DR AlphaFoldDB; Q9UPW5; -.
DR SMR; Q9UPW5; -.
DR BioGRID; 116885; 45.
DR IntAct; Q9UPW5; 18.
DR MINT; Q9UPW5; -.
DR STRING; 9606.ENSP00000338512; -.
DR ChEMBL; CHEMBL4523495; -.
DR MEROPS; M14.028; -.
DR GlyGen; Q9UPW5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPW5; -.
DR PhosphoSitePlus; Q9UPW5; -.
DR BioMuta; AGTPBP1; -.
DR DMDM; 160019039; -.
DR EPD; Q9UPW5; -.
DR jPOST; Q9UPW5; -.
DR MassIVE; Q9UPW5; -.
DR MaxQB; Q9UPW5; -.
DR PaxDb; Q9UPW5; -.
DR PeptideAtlas; Q9UPW5; -.
DR PRIDE; Q9UPW5; -.
DR ProteomicsDB; 85460; -. [Q9UPW5-1]
DR ProteomicsDB; 85461; -. [Q9UPW5-2]
DR ProteomicsDB; 85462; -. [Q9UPW5-3]
DR Antibodypedia; 27717; 347 antibodies from 31 providers.
DR DNASU; 23287; -.
DR Ensembl; ENST00000357081.8; ENSP00000349592.3; ENSG00000135049.16. [Q9UPW5-1]
DR Ensembl; ENST00000376083.7; ENSP00000365251.3; ENSG00000135049.16. [Q9UPW5-2]
DR Ensembl; ENST00000628899.1; ENSP00000487074.1; ENSG00000135049.16. [Q9UPW5-3]
DR GeneID; 23287; -.
DR KEGG; hsa:23287; -.
DR MANE-Select; ENST00000357081.8; ENSP00000349592.3; NM_001330701.2; NP_001317630.1.
DR UCSC; uc010mqc.4; human. [Q9UPW5-1]
DR CTD; 23287; -.
DR DisGeNET; 23287; -.
DR GeneCards; AGTPBP1; -.
DR HGNC; HGNC:17258; AGTPBP1.
DR HPA; ENSG00000135049; Tissue enhanced (bone marrow, brain, retina).
DR MalaCards; AGTPBP1; -.
DR MIM; 606830; gene.
DR MIM; 618276; phenotype.
DR neXtProt; NX_Q9UPW5; -.
DR OpenTargets; ENSG00000135049; -.
DR Orphanet; 2254; Pontocerebellar hypoplasia type 1.
DR PharmGKB; PA24630; -.
DR VEuPathDB; HostDB:ENSG00000135049; -.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000157707; -.
DR HOGENOM; CLU_007391_0_0_1; -.
DR InParanoid; Q9UPW5; -.
DR OMA; HVATCGN; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; Q9UPW5; -.
DR TreeFam; TF313794; -.
DR BRENDA; 3.4.17.24; 2681.
DR PathwayCommons; Q9UPW5; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q9UPW5; -.
DR BioGRID-ORCS; 23287; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; AGTPBP1; human.
DR GenomeRNAi; 23287; -.
DR Pharos; Q9UPW5; Tbio.
DR PRO; PR:Q9UPW5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UPW5; protein.
DR Bgee; ENSG00000135049; Expressed in cortical plate and 197 other tissues.
DR ExpressionAtlas; Q9UPW5; baseline and differential.
DR Genevisible; Q9UPW5; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0098957; P:anterograde axonal transport of mitochondrion; IEA:Ensembl.
DR GO; GO:0035609; P:C-terminal protein deglutamylation; IDA:UniProtKB.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
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:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; ISS:UniProtKB.
DR GO; GO:0042133; P:neurotransmitter metabolic process; IEA:Ensembl.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0035608; P:protein deglutamylation; IMP:UniProtKB.
DR GO; GO:0035610; P:protein side chain deglutamylation; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0098958; P:retrograde axonal transport of mitochondrion; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Cytoplasm; Disease variant;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion;
KW Neurodegeneration; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..1226
FT /note="Cytosolic carboxypeptidase 1"
FT /id="PRO_0000308690"
FT REGION 599..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 970
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 920
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 923
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 1017
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..11
FT /note="MSKLKVIPEKS -> MRTGSAASSAAAAAAAAAASASPATGVCMKTPGGGRR
FT GIRRDPGAEPGAAALRGPRQRPILSR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040422"
FT VAR_SEQ 304..343
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029044"
FT VARIANT 330..1226
FT /note="Missing (in CONDCA)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081908"
FT VARIANT 423
FT /note="E -> K (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036884"
FT VARIANT 694
FT /note="Y -> D (in CONDCA; decreased tubulin deglutamylation
FT shown by in vitro functional expression of the homologous
FT murine variant; dbSNP:rs1564071824)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081909"
FT VARIANT 788..1226
FT /note="Missing (in CONDCA)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081910"
FT VARIANT 799
FT /note="R -> C (in CONDCA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081911"
FT VARIANT 851
FT /note="T -> M (in CONDCA; decreased tubulin deglutamylation
FT asshown by in vitro functional expression of the homologous
FT murine variant; dbSNP:rs760300826)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081912"
FT VARIANT 856..1226
FT /note="Missing (in CONDCA; loss of tubulin deglutamylation;
FT patient cells show lack of protein and excess of tubulin
FT polyglutamylation)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081913"
FT VARIANT 910
FT /note="R -> C (in CONDCA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081914"
FT VARIANT 918
FT /note="R -> W (in CONDCA; decreased tubulin deglutamylation
FT shown by in vitro functional expression of the homologous
FT murine variant; dbSNP:rs1564035967)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081915"
FT VARIANT 990
FT /note="H -> L (in CONDCA; decreased tubulin deglutamylation
FT shown by in vitro functional expression of the homologous
FT murine variant; dbSNP:rs1564034077)"
FT /evidence="ECO:0000269|PubMed:30420557"
FT /id="VAR_081916"
FT CONFLICT 274
FT /note="Q -> R (in Ref. 3; BAA91749)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..399
FT /note="DI -> KK (in Ref. 7; CAH56222)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="E -> G (in Ref. 3; BAA91749)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="M -> V (in Ref. 3; BAB14505)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="M -> V (in Ref. 3; BAB14100)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="E -> G (in Ref. 3; BAA91749)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="F -> I (in Ref. 7; CAH56222)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="M -> T (in Ref. 3; BAB14100)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="S -> P (in Ref. 3; BAB14505)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="T -> A (in Ref. 7; CAH56158)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="N -> D (in Ref. 3; BAB14505)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="G -> R (in Ref. 3; BAG58598)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="Y -> F (in Ref. 3; BAB14505)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="L -> P (in Ref. 7; CAH56158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1226 AA; 138448 MW; A6D598D11D2BD1F8 CRC64;
MSKLKVIPEK SLTNNSRIVG LLAQLEKINA EPSESDTARY VTSKILHLAQ SQEKTRREMT
AKGSTGMEIL LSTLENTKDL QTTLNILSIL VELVSAGGGR RVSFLVTKGG SQILLQLLMN
ASKESPPHED LMVQIHSILA KIGPKDKKFG VKARINGALN ITLNLVKQNL QNHRLVLPCL
QLLRVYSANS VNSVSLGKNG VVELMFKIIG PFSKKNSSLI KVALDTLAAL LKSKTNARRA
VDRGYVQVLL TIYVDWHRHD NRHRNMLIRK GILQSLKSVT NIKLGRKAFI DANGMKILYN
TSQECLAVRT LDPLVNTSSL IMRKCFPKNR LPLPTIKSSF HFQLPVIPVT GPVAQLYSLP
PEVDDVVDES DDNDDIDVEA ENETENEDDL DQNFKNDDIE TDINKLKPQQ EPGRTIEDLK
MYEHLFPELV DDFQDYDLIS KEPKPFVFEG KVRGPIVVPT AGEETSGNSG NLRKVVMKEN
ISSKGDEGEK KSTFMDLAKE DIKDNDRTLQ QQPGDQNRTI SSVHGLNNDI VKALDRITLQ
NIPSQTAPGF TAEMKKDCSL PLTVLTCAKA CPHMATCGNV LFEGRTVQLG KLCCTGVETE
DDEDTESNSS VEQASVEVPD GPTLHDPDLY IEIVKNTKSV PEYSEVAYPD YFGHIPPPFK
EPILERPYGV QRTKIAQDIE RLIHQSDIID RVVYDLDNPN YTIPEEGDIL KFNSKFESGN
LRKVIQIRKN EYDLILNSDI NSNHYHQWFY FEVSGMRPGV AYRFNIINCE KSNSQFNYGM
QPLMYSVQEA LNARPWWIRM GTDICYYKNH FSRSSVAAGG QKGKSYYTIT FTVNFPHKDD
VCYFAYHYPY TYSTLQMHLQ KLESAHNPQQ IYFRKDVLCE TLSGNSCPLV TITAMPESNY
YEHICHFRNR PYVFLSARVH PGETNASWVM KGTLEYLMSN NPTAQSLRES YIFKIVPMLN
PDGVINGNHR CSLSGEDLNR QWQSPSPDLH PTIYHAKGLL QYLAAVKRLP LVYCDYHGHS
RKKNVFMYGC SIKETVWHTN DNATSCDVVE DTGYRTLPKI LSHIAPAFCM SSCSFVVEKS
KESTARVVVW REIGVQRSYT MESTLCGCDQ GKYKGLQIGT RELEEMGAKF CVGLLRLKRL
TSPLEYNLPS SLLDFENDLI ESSCKVTSPT TYVLDEDEPR FLEEVDYSAE SNDELDIELA
ENVGDYEPSA QEEVLSDSEL SRTYLP
