CBPC5_HUMAN
ID CBPC5_HUMAN Reviewed; 886 AA.
AC Q8NDL9; A2VDI7; B7WPG9; B7Z7I7; D6W548; Q53SW0; Q53SZ0; Q96IK8; Q9H6V0;
AC Q9H8P8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cytosolic carboxypeptidase-like protein 5 {ECO:0000250|UniProtKB:Q09M02};
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q09M02};
DE EC=3.4.17.24 {ECO:0000250|UniProtKB:Q09M02};
DE AltName: Full=ATP/GTP-binding protein-like 5;
DE AltName: Full=Protein deglutamylase CCP5 {ECO:0000305};
GN Name=AGBL5 {ECO:0000312|HGNC:HGNC:26147};
GN Synonyms=CCP5 {ECO:0000250|UniProtKB:Q09M02};
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=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Ovary, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Skin;
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 [6]
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 [7]
RP INVOLVEMENT IN RP75, AND VARIANT RP75 ASN-295.
RX PubMed=26720455; DOI=10.1167/iovs.15-17473;
RA Kastner S., Thiemann I.J., Dekomien G., Petrasch-Parwez E., Schreiber S.,
RA Akkad D.A., Gerding W.M., Hoffjan S., Guenes S., Guenes S., Bagci H.,
RA Epplen J.T.;
RT "Exome Sequencing Reveals AGBL5 as Novel Candidate Gene and Additional
RT Variants for Retinitis Pigmentosa in Five Turkish Families.";
RL Invest. Ophthalmol. Vis. Sci. 56:8045-8053(2015).
RN [8]
RP INVOLVEMENT IN RP75, AND VARIANT RP75 TRP-276.
RX PubMed=26355662; DOI=10.1038/gim.2015.127;
RA Patel N., Aldahmesh M.A., Alkuraya H., Anazi S., Alsharif H., Khan A.O.,
RA Sunker A., Al-Mohsen S., Abboud E.B., Nowilaty S.R., Alowain M.,
RA Al-Zaidan H., Al-Saud B., Alasmari A., Abdel-Salam G.M., Abouelhoda M.,
RA Abdulwahab F.M., Ibrahim N., Naim E., Al-Younes B., E AlMostafa A.,
RA AlIssa A., Hashem M., Buzovetsky O., Xiong Y., Monies D., Altassan N.,
RA Shaheen R., Al-Hazzaa S.A., Alkuraya F.S.;
RT "Expanding the clinical, allelic, and locus heterogeneity of retinal
RT dystrophies.";
RL Genet. Med. 18:554-562(2016).
RN [9]
RP VARIANTS RP75 ARG-108; GLY-251 AND 592-TRP--VAL-886 DEL.
RX PubMed=27842159; DOI=10.1167/iovs.16-20148;
RA Astuti G.D., Arno G., Hull S., Pierrache L., Venselaar H., Carss K.,
RA Raymond F.L., Collin R.W., Faradz S.M., van den Born L.I., Webster A.R.,
RA Cremers F.P.;
RT "Mutations in AGBL5, Encoding alpha-Tubulin Deglutamylase, Are Associated
RT With Autosomal Recessive Retinitis Pigmentosa.";
RL Invest. Ophthalmol. Vis. Sci. 57:6180-6187(2016).
RN [10]
RP VARIANTS RP75 CYS-281 AND 487-ARG--VAL-886 DEL.
RX PubMed=27764769; DOI=10.1152/physiolgenomics.00101.2016;
RA Branham K., Matsui H., Biswas P., Guru A.A., Hicks M., Suk J.J., Li H.,
RA Jakubosky D., Long T., Telenti A., Nariai N., Heckenlively J.R.,
RA Frazer K.A., Sieving P.A., Ayyagari R.;
RT "Establishing the involvement of the novel gene AGBL5 in retinitis
RT pigmentosa by whole genome sequencing.";
RL Physiol. Genomics 48:922-927(2016).
CC -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
CC 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. Cleaves alpha- and gamma-linked polyglutamate tubulin side-
CC chain, as well as the branching point glutamate. Also catalyzes the
CC removal of alpha-linked glutamate residues from the carboxy-terminus of
CC alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS,
CC leading to CGAS antiviral defense response activation.
CC {ECO:0000250|UniProtKB:Q09M02}.
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:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:0000250|UniProtKB:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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:Q09M02};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000250|UniProtKB:Q09M02};
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
CC {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000269|PubMed:23085998}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23085998}. Midbody
CC {ECO:0000269|PubMed:23085998}. Note=Mainly cytoplasmic. Slight
CC accumulation in the nucleus is observed (By similarity). Colocalizes
CC with alpha-tubulin in the mitotic spindle and with midbody microtubules
CC in the intercellular bridges formed during cytokinesis.
CC {ECO:0000250|UniProtKB:Q09M02, ECO:0000269|PubMed:23085998}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NDL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDL9-2; Sequence=VSP_028361, VSP_028362;
CC Name=3;
CC IsoId=Q8NDL9-3; Sequence=VSP_028359, VSP_028360;
CC -!- TISSUE SPECIFICITY: Expressed in brain.
CC -!- DISEASE: Retinitis pigmentosa 75 (RP75) [MIM:617023]: A form of
CC retinitis pigmentosa, a retinal dystrophy belonging to the group of
CC pigmentary retinopathies. Retinitis pigmentosa is characterized by
CC retinal pigment deposits visible on fundus examination and primary loss
CC of rod photoreceptor cells followed by secondary loss of cone
CC photoreceptors. Patients typically have night vision blindness and loss
CC of midperipheral visual field. As their condition progresses, they lose
CC their far peripheral visual field and eventually central vision as
CC well. RP75 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:26355662, ECO:0000269|PubMed:26720455,
CC ECO:0000269|PubMed:27764769, ECO:0000269|PubMed:27842159}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX93164.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAY14655.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB15151.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL833844; CAD38704.1; -; mRNA.
DR EMBL; AK302091; BAH13623.1; -; mRNA.
DR EMBL; AC013403; AAX93164.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013472; AAY14655.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471053; EAX00649.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00651.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00652.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00653.1; -; Genomic_DNA.
DR EMBL; BC007415; AAH07415.2; -; mRNA.
DR EMBL; BC018584; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC131498; AAI31499.1; -; mRNA.
DR EMBL; AK023398; BAB14560.1; -; mRNA.
DR EMBL; AK025492; BAB15151.1; ALT_INIT; mRNA.
DR CCDS; CCDS1732.3; -. [Q8NDL9-1]
DR CCDS; CCDS42665.1; -. [Q8NDL9-3]
DR RefSeq; NP_001030584.1; NM_001035507.2. [Q8NDL9-3]
DR RefSeq; NP_068603.4; NM_021831.5. [Q8NDL9-1]
DR RefSeq; XP_011531313.1; XM_011533011.2. [Q8NDL9-1]
DR RefSeq; XP_011531314.1; XM_011533012.2. [Q8NDL9-1]
DR RefSeq; XP_011531315.1; XM_011533013.2. [Q8NDL9-1]
DR AlphaFoldDB; Q8NDL9; -.
DR SMR; Q8NDL9; -.
DR BioGRID; 121935; 23.
DR IntAct; Q8NDL9; 8.
DR MINT; Q8NDL9; -.
DR STRING; 9606.ENSP00000353249; -.
DR MEROPS; M14.025; -.
DR iPTMnet; Q8NDL9; -.
DR PhosphoSitePlus; Q8NDL9; -.
DR BioMuta; AGBL5; -.
DR DMDM; 74715354; -.
DR EPD; Q8NDL9; -.
DR jPOST; Q8NDL9; -.
DR MassIVE; Q8NDL9; -.
DR MaxQB; Q8NDL9; -.
DR PaxDb; Q8NDL9; -.
DR PeptideAtlas; Q8NDL9; -.
DR PRIDE; Q8NDL9; -.
DR ProteomicsDB; 73036; -. [Q8NDL9-1]
DR ProteomicsDB; 73037; -. [Q8NDL9-2]
DR ProteomicsDB; 73038; -. [Q8NDL9-3]
DR Antibodypedia; 28106; 156 antibodies from 25 providers.
DR DNASU; 60509; -.
DR Ensembl; ENST00000323064.12; ENSP00000323681.8; ENSG00000084693.16. [Q8NDL9-3]
DR Ensembl; ENST00000360131.5; ENSP00000353249.4; ENSG00000084693.16. [Q8NDL9-1]
DR Ensembl; ENST00000487078.5; ENSP00000433830.1; ENSG00000084693.16. [Q8NDL9-2]
DR GeneID; 60509; -.
DR KEGG; hsa:60509; -.
DR MANE-Select; ENST00000360131.5; ENSP00000353249.4; NM_021831.6; NP_068603.4.
DR UCSC; uc002rid.4; human. [Q8NDL9-1]
DR CTD; 60509; -.
DR DisGeNET; 60509; -.
DR GeneCards; AGBL5; -.
DR HGNC; HGNC:26147; AGBL5.
DR HPA; ENSG00000084693; Group enriched (parathyroid gland, testis).
DR MalaCards; AGBL5; -.
DR MIM; 615900; gene.
DR MIM; 617023; phenotype.
DR neXtProt; NX_Q8NDL9; -.
DR OpenTargets; ENSG00000084693; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA162375816; -.
DR VEuPathDB; HostDB:ENSG00000084693; -.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000158032; -.
DR HOGENOM; CLU_007523_3_2_1; -.
DR InParanoid; Q8NDL9; -.
DR OMA; NCAHFDF; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; Q8NDL9; -.
DR TreeFam; TF324301; -.
DR BRENDA; 3.4.17.24; 2681.
DR PathwayCommons; Q8NDL9; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q8NDL9; -.
DR BioGRID-ORCS; 60509; 19 hits in 1085 CRISPR screens.
DR ChiTaRS; AGBL5; human.
DR GenomeRNAi; 60509; -.
DR Pharos; Q8NDL9; Tbio.
DR PRO; PR:Q8NDL9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NDL9; protein.
DR Bgee; ENSG00000084693; Expressed in left testis and 174 other tissues.
DR ExpressionAtlas; Q8NDL9; baseline and differential.
DR Genevisible; Q8NDL9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA: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:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0035611; P:protein branching point deglutamylation; ISS:UniProtKB.
DR GO; GO:0035608; P:protein deglutamylation; ISS:UniProtKB.
DR GO; GO:0035610; P:protein side chain deglutamylation; ISS: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;
KW Disease variant; Hydrolase; Metal-binding; Metalloprotease; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Retinitis pigmentosa; Zinc.
FT CHAIN 1..886
FT /note="Cytosolic carboxypeptidase-like protein 5"
FT /id="PRO_0000305921"
FT REGION 344..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..667
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 710..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..824
FT /note="Polar 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:0000250|UniProtKB:Q09M02"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
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:0000250|UniProtKB:Q09M02"
FT VAR_SEQ 697..717
FT /note="EPRSQDRRRQQQPLNHRPAGS -> GKPVWEPLQHVFGCLGHCWGK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028359"
FT VAR_SEQ 718..886
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028360"
FT VAR_SEQ 786..816
FT /note="ARPRLGRGSPPTRRGMKGSSGPTSPTPRTRE -> TCPRRVSARRGPGFPRL
FT GPGWAGAHRRLAEG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028361"
FT VAR_SEQ 817..886
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028362"
FT VARIANT 108
FT /note="P -> R (in RP75; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27842159"
FT /id="VAR_079522"
FT VARIANT 251
FT /note="V -> G (in RP75; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27842159"
FT /id="VAR_079523"
FT VARIANT 276
FT /note="R -> W (in RP75; dbSNP:rs879253769)"
FT /evidence="ECO:0000269|PubMed:26355662"
FT /id="VAR_077018"
FT VARIANT 281
FT /note="R -> C (in RP75; unknown pathological significance;
FT dbSNP:rs780394281)"
FT /evidence="ECO:0000269|PubMed:27764769"
FT /id="VAR_079524"
FT VARIANT 295
FT /note="D -> N (in RP75; dbSNP:rs879253768)"
FT /evidence="ECO:0000269|PubMed:26720455"
FT /id="VAR_077019"
FT VARIANT 487..886
FT /note="Missing (in RP75)"
FT /evidence="ECO:0000269|PubMed:27764769"
FT /id="VAR_079525"
FT VARIANT 592..886
FT /note="Missing (in RP75)"
FT /evidence="ECO:0000269|PubMed:27842159"
FT /id="VAR_079526"
FT VARIANT 649
FT /note="G -> D (in dbSNP:rs35804461)"
FT /id="VAR_035231"
FT CONFLICT 38..40
FT /note="GAS -> CLL (in Ref. 5; AAI31499)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="N -> S (in Ref. 2; BAH13623)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="I -> R (in Ref. 5; AAI31499)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="S -> G (in Ref. 2; BAB15151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 97534 MW; 0948AD0F37B0725A CRC64;
MELRCGGLLF SSRFDSGNLA HVEKVESLSS DGEGVGGGAS ALTSGIASSP DYEFNVWTRP
DCAETEFENG NRSWFYFSVR GGMPGKLIKI NIMNMNKQSK LYSQGMAPFV RTLPTRPRWE
RIRDRPTFEM TETQFVLSFV HRFVEGRGAT TFFAFCYPFS YSDCQELLNQ LDQRFPENHP
THSSPLDTIY YHRELLCYSL DGLRVDLLTI TSCHGLREDR EPRLEQLFPD TSTPRPFRFA
GKRIFFLSSR VHPGETPSSF VFNGFLDFIL RPDDPRAQTL RRLFVFKLIP MLNPDGVVRG
HYRTDSRGVN LNRQYLKPDA VLHPAIYGAK AVLLYHHVHS RLNSQSSSEH QPSSCLPPDA
PVSDLEKANN LQNEAQCGHS ADRHNAEAWK QTEPAEQKLN SVWIMPQQSA GLEESAPDTI
PPKESGVAYY VDLHGHASKR GCFMYGNSFS DESTQVENML YPKLISLNSA HFDFQGCNFS
EKNMYARDRR DGQSKEGSGR VAIYKASGII HSYTLECNYN TGRSVNSIPA ACHDNGRASP
PPPPAFPSRY TVELFEQVGR AMAIAALDMA ECNPWPRIVL SEHSSLTNLR AWMLKHVRNS
RGLSSTLNVG VNKKRGLRTP PKSHNGLPVS CSENTLSRAR SFSTGTSAGG SSSSQQNSPQ
MKNSPSFPFH GSRPAGLPGL GSSTQKVTHR VLGPVREPRS QDRRRQQQPL NHRPAGSLAP
SPAPTSSGPA SSHKLGSCLL PDSFNIPGSS CSLLSSGDKP EAVMVIGKGL LGTGARMPCI
KTRLQARPRL GRGSPPTRRG MKGSSGPTSP TPRTRESSEL ELGSCSATPG LPQARPPRPR
SAPAFSPISC SLSDSPSWNC YSRGPLGQPE VCFVPKSPPL TVSPRV
