CBPC3_MOUSE
ID CBPC3_MOUSE Reviewed; 1006 AA.
AC Q8CDP0; B2RSY8; Q09M06; Q09M07; Q8BSW4; Q8R036;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytosolic carboxypeptidase 3 {ECO:0000303|PubMed:25103237};
DE EC=3.4.17.- {ECO:0000269|PubMed:25103237};
DE AltName: Full=ATP/GTP-binding protein-like 3;
DE AltName: Full=Protein deglutamylase CCP3 {ECO:0000305};
GN Name=Agbl3 {ECO:0000312|MGI:MGI:1923473};
GN Synonyms=Ccp3 {ECO:0000303|PubMed:17244818};
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 AND 3), TISSUE SPECIFICITY, AND
RP 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 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Pituitary, and Testis;
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 MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Brain, Mammary gland, and Testis;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-540.
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).
CC -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
CC tubulin and non-tubulin target proteins (PubMed:25103237). Catalyzes
CC the removal of polyglutamate side chains present on the gamma-carboxyl
CC group of glutamate residues within the C-terminal tail of tubulin
CC protein (PubMed:25103237). Specifically cleaves tubulin long-side-
CC chains, while it is not able to remove the branching point glutamate
CC (PubMed:25103237). Also catalyzes the removal of polyglutamate residues
CC from the carboxy-terminus of non-tubulin proteins such as MYLK
CC (PubMed:25103237). May catalyze the hydrolysis of aspartate from the
CC carboxy-terminus of target proteins (PubMed:25103237). Does not show
CC detyrosinase or deglycylase activities from the carboxy-terminus of
CC target proteins (PubMed:25103237). {ECO:0000269|PubMed:25103237}.
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:25103237};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000305|PubMed:25103237};
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, cytosol {ECO:0000269|PubMed:17244818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8CDP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CDP0-2; Sequence=VSP_024376, VSP_024379;
CC Name=3;
CC IsoId=Q8CDP0-3; Sequence=VSP_024376;
CC Name=4;
CC IsoId=Q8CDP0-4; Sequence=VSP_024376, VSP_024377, VSP_024378;
CC Name=5;
CC IsoId=Q8CDP0-5; Sequence=VSP_024374, VSP_024375;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed abundantly in tissues
CC with m otile cilia such as testis, lung and trachea. Abundantly
CC expressed in pituitary and kidney, moderately expressed in brain, eye,
CC fat, pancreas, stomach, and adrenal. {ECO:0000269|PubMed:17244818,
CC ECO:0000269|PubMed:25103237}.
CC -!- INDUCTION: Up-regulated during ciliogenesis.
CC {ECO:0000269|PubMed:25103237}.
CC -!- DISRUPTION PHENOTYPE: AGBL2 and AGBL3 double knockout mutant mice are
CC viable and display no obvious phenotypic alterations. Show an increase
CC in tubulin and MYLK polyglutamylation in sperm.
CC {ECO:0000269|PubMed:25103237}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; DQ867031; ABI51950.1; -; mRNA.
DR EMBL; DQ867032; ABI51951.1; -; mRNA.
DR EMBL; AK029793; BAC26620.1; -; mRNA.
DR EMBL; AK030378; BAC26932.1; -; mRNA.
DR EMBL; BC028521; AAH28521.1; -; mRNA.
DR EMBL; BC087897; AAH87897.1; -; mRNA.
DR EMBL; BC139065; AAI39066.1; -; mRNA.
DR CCDS; CCDS19995.2; -. [Q8CDP0-3]
DR CCDS; CCDS80515.1; -. [Q8CDP0-1]
DR CCDS; CCDS80516.1; -. [Q8CDP0-5]
DR RefSeq; NP_001276585.1; NM_001289656.1. [Q8CDP0-1]
DR RefSeq; NP_001276586.1; NM_001289657.1.
DR RefSeq; NP_001276587.1; NM_001289658.1. [Q8CDP0-5]
DR RefSeq; NP_848745.2; NM_178630.4. [Q8CDP0-3]
DR AlphaFoldDB; Q8CDP0; -.
DR SMR; Q8CDP0; -.
DR STRING; 10090.ENSMUSP00000110669; -.
DR MEROPS; M14.026; -.
DR iPTMnet; Q8CDP0; -.
DR PhosphoSitePlus; Q8CDP0; -.
DR PaxDb; Q8CDP0; -.
DR PRIDE; Q8CDP0; -.
DR ProteomicsDB; 265349; -. [Q8CDP0-1]
DR ProteomicsDB; 265350; -. [Q8CDP0-2]
DR ProteomicsDB; 265351; -. [Q8CDP0-3]
DR ProteomicsDB; 265352; -. [Q8CDP0-4]
DR ProteomicsDB; 265353; -. [Q8CDP0-5]
DR Antibodypedia; 9809; 65 antibodies from 21 providers.
DR DNASU; 76223; -.
DR Ensembl; ENSMUST00000115014; ENSMUSP00000110666; ENSMUSG00000038836. [Q8CDP0-5]
DR Ensembl; ENSMUST00000115016; ENSMUSP00000110668; ENSMUSG00000038836. [Q8CDP0-1]
DR Ensembl; ENSMUST00000115017; ENSMUSP00000110669; ENSMUSG00000038836. [Q8CDP0-3]
DR GeneID; 76223; -.
DR KEGG; mmu:76223; -.
DR UCSC; uc009bhm.2; mouse. [Q8CDP0-5]
DR UCSC; uc009bhp.1; mouse. [Q8CDP0-4]
DR UCSC; uc009bhq.1; mouse. [Q8CDP0-2]
DR UCSC; uc009bhr.2; mouse. [Q8CDP0-3]
DR UCSC; uc009bhs.2; mouse. [Q8CDP0-1]
DR CTD; 340351; -.
DR MGI; MGI:1923473; Agbl3.
DR VEuPathDB; HostDB:ENSMUSG00000038836; -.
DR eggNOG; KOG1814; Eukaryota.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000160916; -.
DR HOGENOM; CLU_318835_0_0_1; -.
DR InParanoid; Q8CDP0; -.
DR OMA; NCDNTLM; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; Q8CDP0; -.
DR TreeFam; TF313794; -.
DR BioGRID-ORCS; 76223; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8CDP0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CDP0; protein.
DR Bgee; ENSMUSG00000038836; Expressed in spermatid and 133 other tissues.
DR ExpressionAtlas; Q8CDP0; baseline and differential.
DR Genevisible; Q8CDP0; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035610; P:protein side chain deglutamylation; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..1006
FT /note="Cytosolic carboxypeptidase 3"
FT /id="PRO_0000283752"
FT REGION 790..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT VAR_SEQ 104..129
FT /note="EWTPFVPEPVYVPTGLEIEPVYPNSK -> GMFLEVLGIQTLANLSILMLMR
FT TLMM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024374"
FT VAR_SEQ 130..1006
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024375"
FT VAR_SEQ 140..144
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:17244818"
FT /id="VSP_024376"
FT VAR_SEQ 507..516
FT /note="FSFSACKFNV -> VRTFKTLTSL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024377"
FT VAR_SEQ 517..1006
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024378"
FT VAR_SEQ 867..1006
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17244818"
FT /id="VSP_024379"
FT MUTAGEN 540
FT /note="E->A: Abolishes deglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25103237"
SQ SEQUENCE 1006 AA; 116378 MW; A7E0C781E00CDCBF CRC64;
MSEDSEEEDY SDRSISDDDD LDEDSFMKFV SDDIHPCTLL AADSIGDPFF PRTTQILLEY
QLGRWVPRLR GPRDLYGVSS SGPLSPTRWP YHCEVIDEKV QHIEWTPFVP EPVYVPTGLE
IEPVYPNSKE DTVVYLAEDD HLCKAYKEPC FVYSRVGGNR TSLKQPVDNC DNTLVFEARF
ESGNLQKVVK VADHEYELTV RPDLFTNKHT QWYYFQVTNT QAEIVYRFTI VNFTKPASLY
NRGMKPLFYS EKEAKTHNIG WQRIGDQIKY YKNNLGQDGR HFFSLTWTFQ FPHSQDTCYF
AHCYPYTYSN LQEYLSGINS DPVRSKFCKI RVLCHTLARN MVYVLTITTP LKTSDSKRKA
VILTARVHPG ETNSSWIMKG FLDYILGDSS DARLLRDTFI FKVVPMLNPD GVIVGNYRCS
LAGRDLNRNY TSLLKESFPS VWYTRNMINR LMEKREVILY CDLHGHSRKQ NIFMYGCDGS
SRSKTKGLYL QQRIFPLMLS KNCPNIFSFS ACKFNVQKSK EGTGRVVMWK MGIRNSFTLE
ATFCGSTLGN KRGTHFGTKD LESMGYHFCD SLLDYCDPDR SKYYQCLKEL EEMEKHLSSE
RVSDNTDTSL VEISLDVESS SRGSDSSESN DTQTYLLKVT SQARNKKKYL KTKRERNAIL
ANCQNNMQEV YGKEHLLQRH DESNSDGNDP RIDAPDVYVA HCFRRPLPNQ GVVKIPGQRF
YPGKTWSSSQ RMIKSLNKDH RTCILETCKN PIQEVQSRGI NIHESCFKMA KCPMNKRPSH
WIEKTRIPTE SHHQLKSKAK RCSSFQSKRT GTNWTDDEKR IYRDKRIAQT QEILKYLLPI
VESSQNRKST QMNNLINPIA NLQQHQLIPT ACINRRRYSI PWTPTRNLPF KAQRNLMTDT
SEWLQSVPLG SFESLLPLCN LQKKTKHFEL WGKKAKDVQL ATSQWEAVPL SSNMDASIIR
GNSVLQPKEF TMRSSKQRIP YLTKTSKKPS ESDGLLTFQL KIHRNS
