CBPC5_MOUSE
ID CBPC5_MOUSE Reviewed; 886 AA.
AC Q09M02; D3Z6S8; Q09M01; Q09M03; Q09M04; Q6PFZ3; Q8BLL9; Q8BM52; Q8BZD8;
AC Q8C0W4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0000303|PubMed:21074048};
DE EC=3.4.17.- {ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:24022482, ECO:0000269|PubMed:26829768};
DE EC=3.4.17.24 {ECO:0000269|PubMed:24022482, ECO:0000269|PubMed:26829768};
DE AltName: Full=ATP/GTP-binding protein-like 5;
DE AltName: Full=Protein deglutamylase CCP5 {ECO:0000305};
GN Name=Agbl5 {ECO:0000312|MGI:MGI:2441745};
GN Synonyms=Ccp5 {ECO:0000303|PubMed:21074048};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 7), TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=C57BLKS/J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 5 AND 6).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Embryoid bodies, Testis, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-841, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-252 AND GLU-255.
RX PubMed=21074048; DOI=10.1016/j.cell.2010.10.014;
RA Rogowski K., van Dijk J., Magiera M.M., Bosc C., Deloulme J.C., Bosson A.,
RA Peris L., Gold N.D., Lacroix B., Grau M.B., Bec N., Larroque C.,
RA Desagher S., Holzer M., Andrieux A., Moutin M.J., Janke C.;
RT "A family of protein-deglutamylating enzymes associated with
RT neurodegeneration.";
RL Cell 143:564-578(2010).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [8]
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=25103237; DOI=10.1091/mbc.e14-06-1072;
RA Tort O., Tanco S., Rocha C., Bieche I., Seixas C., Bosc C., Andrieux A.,
RA Moutin M.J., Aviles F.X., Lorenzo J., Janke C.;
RT "The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational
RT removal of acidic amino acids.";
RL Mol. Biol. Cell 25:3017-3027(2014).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP HIS-252 AND GLU-255.
RX PubMed=26829768; DOI=10.1038/ni.3356;
RA Xia P., Ye B., Wang S., Zhu X., Du Y., Xiong Z., Tian Y., Fan Z.;
RT "Glutamylation of the DNA sensor cGAS regulates its binding and synthase
RT activity in antiviral immunity.";
RL Nat. Immunol. 17:369-378(2016).
CC -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
CC tubulin and non-tubulin target proteins (PubMed:21074048,
CC PubMed:20519502, PubMed:24022482, PubMed:26829768). Catalyzes the
CC removal of polyglutamate side chains present on the gamma-carboxyl
CC group of glutamate residues within the C-terminal tail of alpha- and
CC beta-tubulin (PubMed:21074048, PubMed:20519502, PubMed:24022482).
CC Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as
CC well as the branching point glutamate (PubMed:21074048,
CC PubMed:24022482). Also catalyzes the removal of alpha-linked glutamate
CC residues from the carboxy-terminus of alpha-tubulin (PubMed:24022482).
CC Mediates deglutamylation of nucleotidyltransferase CGAS, leading to
CC CGAS antiviral defense response activation (PubMed:26829768).
CC {ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:21074048,
CC ECO:0000269|PubMed:24022482, ECO:0000269|PubMed:26829768}.
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:0000269|PubMed:20519502, ECO:0000269|PubMed:21074048};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153;
CC Evidence={ECO:0000305|PubMed:20519502, ECO:0000305|PubMed:21074048};
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:24022482, ECO:0000269|PubMed:26829768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000269|PubMed:26829768, ECO:0000305|PubMed:24022482};
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:0000269|PubMed:24022482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797;
CC Evidence={ECO:0000305|PubMed:24022482};
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:24022482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000305|PubMed:24022482};
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 {ECO:0000269|PubMed:17244818,
CC ECO:0000269|PubMed:24022482}. Nucleus {ECO:0000269|PubMed:17244818}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}.
CC Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Colocalizes with alpha-
CC tubulin in the mitotic spindle and with midbody microtubules in the
CC intercellular bridges formed during cytokinesis (By similarity). Mainly
CC cytoplasmic. Slight accumulation in the nucleus is observed
CC (PubMed:17244818). {ECO:0000250|UniProtKB:Q8NDL9,
CC ECO:0000269|PubMed:17244818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q09M02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q09M02-2; Sequence=VSP_040433;
CC Name=3;
CC IsoId=Q09M02-3; Sequence=VSP_040432;
CC Name=4;
CC IsoId=Q09M02-4; Sequence=VSP_040434;
CC Name=5;
CC IsoId=Q09M02-5; Sequence=VSP_040427, VSP_040428, VSP_040429,
CC VSP_040430;
CC Name=6;
CC IsoId=Q09M02-6; Sequence=VSP_040431;
CC Name=7;
CC IsoId=Q09M02-7; Sequence=VSP_040428, VSP_040433;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis, and
CC moderately in pituitary, brain, eye and kidney.
CC {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:25103237}.
CC -!- DISRUPTION PHENOTYPE: Mice are more vulnerable to DNA virus infection
CC due to impaired immune response. {ECO:0000269|PubMed:26829768}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57349.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ867034; ABI51953.1; -; mRNA.
DR EMBL; DQ867035; ABI51954.1; -; mRNA.
DR EMBL; DQ867036; ABI51955.1; -; mRNA.
DR EMBL; DQ867037; ABI51956.1; -; mRNA.
DR EMBL; DQ867038; ABI51957.1; -; mRNA.
DR EMBL; AK029676; BAC26559.1; -; mRNA.
DR EMBL; AK035680; BAC29150.1; -; mRNA.
DR EMBL; AK034894; BAC28871.1; -; mRNA.
DR EMBL; AK044195; BAC31813.1; -; mRNA.
DR EMBL; AC109606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057349; AAH57349.1; ALT_INIT; mRNA.
DR CCDS; CCDS19165.1; -. [Q09M02-6]
DR CCDS; CCDS39048.1; -. [Q09M02-7]
DR CCDS; CCDS80242.1; -. [Q09M02-3]
DR CCDS; CCDS89898.1; -. [Q09M02-2]
DR RefSeq; NP_001041657.1; NM_001048192.2. [Q09M02-7]
DR RefSeq; NP_001281191.1; NM_001294262.1. [Q09M02-3]
DR RefSeq; NP_777274.1; NM_174849.3. [Q09M02-6]
DR RefSeq; XP_006503936.1; XM_006503873.3. [Q09M02-2]
DR RefSeq; XP_006503937.1; XM_006503874.3. [Q09M02-4]
DR RefSeq; XP_006503938.1; XM_006503875.1. [Q09M02-1]
DR RefSeq; XP_006503939.1; XM_006503876.1. [Q09M02-1]
DR RefSeq; XP_006503940.1; XM_006503877.1. [Q09M02-1]
DR AlphaFoldDB; Q09M02; -.
DR SMR; Q09M02; -.
DR STRING; 10090.ENSMUSP00000110348; -.
DR MEROPS; M14.036; -.
DR iPTMnet; Q09M02; -.
DR PhosphoSitePlus; Q09M02; -.
DR PaxDb; Q09M02; -.
DR PRIDE; Q09M02; -.
DR ProteomicsDB; 283697; -. [Q09M02-1]
DR ProteomicsDB; 283698; -. [Q09M02-2]
DR ProteomicsDB; 283699; -. [Q09M02-3]
DR ProteomicsDB; 283700; -. [Q09M02-4]
DR ProteomicsDB; 283701; -. [Q09M02-5]
DR ProteomicsDB; 283702; -. [Q09M02-6]
DR ProteomicsDB; 283703; -. [Q09M02-7]
DR Antibodypedia; 28106; 156 antibodies from 25 providers.
DR DNASU; 231093; -.
DR Ensembl; ENSMUST00000069705; ENSMUSP00000063228; ENSMUSG00000029165. [Q09M02-6]
DR Ensembl; ENSMUST00000114700; ENSMUSP00000110348; ENSMUSG00000029165. [Q09M02-7]
DR Ensembl; ENSMUST00000201168; ENSMUSP00000143808; ENSMUSG00000029165. [Q09M02-1]
DR Ensembl; ENSMUST00000201225; ENSMUSP00000143934; ENSMUSG00000029165. [Q09M02-3]
DR Ensembl; ENSMUST00000201817; ENSMUSP00000144304; ENSMUSG00000029165. [Q09M02-4]
DR Ensembl; ENSMUST00000201917; ENSMUSP00000144188; ENSMUSG00000029165. [Q09M02-2]
DR Ensembl; ENSMUST00000202060; ENSMUSP00000144018; ENSMUSG00000029165. [Q09M02-3]
DR GeneID; 231093; -.
DR KEGG; mmu:231093; -.
DR UCSC; uc008wwc.1; mouse. [Q09M02-6]
DR UCSC; uc008wwd.1; mouse. [Q09M02-5]
DR UCSC; uc008wwf.2; mouse. [Q09M02-3]
DR UCSC; uc008wwg.2; mouse. [Q09M02-7]
DR CTD; 60509; -.
DR MGI; MGI:2441745; Agbl5.
DR VEuPathDB; HostDB:ENSMUSG00000029165; -.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000158032; -.
DR HOGENOM; CLU_007523_3_2_1; -.
DR InParanoid; Q09M02; -.
DR OMA; NCAHFDF; -.
DR PhylomeDB; Q09M02; -.
DR TreeFam; TF324301; -.
DR BRENDA; 3.4.17.24; 3474.
DR BioGRID-ORCS; 231093; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Agbl5; mouse.
DR PRO; PR:Q09M02; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q09M02; protein.
DR Bgee; ENSMUSG00000029165; Expressed in spermatid and 192 other tissues.
DR ExpressionAtlas; Q09M02; baseline and differential.
DR Genevisible; Q09M02; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035609; P:C-terminal protein deglutamylation; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0035611; P:protein branching point deglutamylation; IDA:UniProtKB.
DR GO; GO:0035608; P:protein deglutamylation; IDA:UniProtKB.
DR GO; GO:0035610; P:protein side chain deglutamylation; IMP: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 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Cytoplasm; Cytoskeleton; Hydrolase;
KW Metal-binding; Metalloprotease; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..886
FT /note="Cytosolic carboxypeptidase-like protein 5"
FT /id="PRO_0000305922"
FT REGION 344..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..843
FT /note="Pro 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:0000305|PubMed:21074048"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:21074048"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040427"
FT VAR_SEQ 129
FT /note="E -> ELGSKLSPCFSKPEEAGSHVESVRGRELVK (in isoform 5
FT and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_040428"
FT VAR_SEQ 456..458
FT /note="VEN -> VGL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040429"
FT VAR_SEQ 459..886
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040430"
FT VAR_SEQ 697..886
FT /note="EPRCSDRRRRQQPLNHRSTTSSLAPSPTLASSGPTSSRNMGSCLLPNSLSLS
FT GSSCSFSSSGDKPEAVMVIGKSLLGAGARIPCIRTRLQARPRLGRSSPPTRRGMRGSSP
FT TSPIPQTRESSELEPGPHSATPGLPQAGPPRPRSAPAFSPISCTLSDSPSRICYSRGLL
FT NQCEVCFVPKSPPLTISPRV -> GKPVWEPLQQVFGCLGHCWGERA (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040431"
FT VAR_SEQ 750..886
FT /note="SSCSFSSSGDKPEAVMVIGKSLLGAGARIPCIRTRLQARPRLGRSSPPTRRG
FT MRGSSPTSPIPQTRESSELEPGPHSATPGLPQAGPPRPRSAPAFSPISCTLSDSPSRIC
FT YSRGLLNQCEVCFVPKSPPLTISPRV -> RYPLPLKPELPTFFPFLPPRA (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_040432"
FT VAR_SEQ 787..886
FT /note="ARPRLGRSSPPTRRGMRGSSPTSPIPQTRESSELEPGPHSATPGLPQAGPPR
FT PRSAPAFSPISCTLSDSPSRICYSRGLLNQCEVCFVPKSPPLTISPRV -> TCQRRVS
FT ARRGPGFPRLGPGWAGAHRRLAEG (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_040433"
FT VAR_SEQ 787..886
FT /note="ARPRLGRSSPPTRRGMRGSSPTSPIPQTRESSELEPGPHSATPGLPQAGPPR
FT PRSAPAFSPISCTLSDSPSRICYSRGLLNQCEVCFVPKSPPLTISPRV -> TPLSLPD
FT APQPQPTSFGFPTRP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_040434"
FT MUTAGEN 252
FT /note="H->S: Abolishes deglutamylase activity; when
FT associated with Q-255."
FT /evidence="ECO:0000269|PubMed:21074048,
FT ECO:0000269|PubMed:26829768"
FT MUTAGEN 255
FT /note="E->Q: Abolishes deglutamylase activity; when
FT associated with S-252."
FT /evidence="ECO:0000269|PubMed:21074048,
FT ECO:0000269|PubMed:26829768"
FT CONFLICT 103
FT /note="S -> A (in Ref. 2; BAC29150)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="H -> R (in Ref. 2; BAC28871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 97607 MW; 58A971BD521890D6 CRC64;
MELRCGGLLF SSRFDSGNLA HVEKVETVSS DGEGVGGVAT APASGSAASP DYEFNVWTRP
DCAETEYENG NRSWFYFSVR GGTPGKLIKI NIMNMNKQSK LYSQGMAPFV RTLPSRPRWE
RIRERPTFEM TETQFVLSFV HRFVEGRGAT TFFAFCYPFS YSDCQDLLSQ LDQRFSENYS
THSSPLDSIY YHRELLCYSL DGLRVDLLTI TSCHGLRDDR EPRLEQLFPD LGTPRPFRFT
GKRIFFLSSR VHPGETPSSF VFNGFLDFIL RPDDPRAQTL RRLFVFKLIP MLNPDGVVRG
HYRTDSRGVN LNRQYLKPDA VLHPAIYGAK AVLLYHHVHS RLNAKSPTNQ QPTLHLPPEA
PLSDLEKANN LHNEAHLGQS PDGENPATWP ETEPAEEKTD PVWLMPQPIP ELEEPAPDTI
PPKESGVAYY VDLHGHASKR GCFMYGNSFS DESTQVENML YPKLISLNSA HFDFQGCNFS
EKNMYARDRR DGQSKEGSGR VAIYKASGII HSYTLECNYN TGRSVNSIPA ACHDNGRASP
PPPPAFPSRY TVELFEQVGR AMAIAALDMA ECNPWPRIVL SEHSSLTNLR AWMLRHVRNS
RGLTSAGNMG ASKKRGARTP PKSNNSLPVS CSENALSRVR SFSTGTSTGG SSSSQQNSPQ
MKNSPSFPFH GSRTAGLPGL GSSTQKVSHR VLGPVREPRC SDRRRRQQPL NHRSTTSSLA
PSPTLASSGP TSSRNMGSCL LPNSLSLSGS SCSFSSSGDK PEAVMVIGKS LLGAGARIPC
IRTRLQARPR LGRSSPPTRR GMRGSSPTSP IPQTRESSEL EPGPHSATPG LPQAGPPRPR
SAPAFSPISC TLSDSPSRIC YSRGLLNQCE VCFVPKSPPL TISPRV
