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 27-MAR-2024, entry version 150. 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}; 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; 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; 25. DR IntAct; Q8NDL9; 8. DR MINT; Q8NDL9; -. DR STRING; 9606.ENSP00000353249; -. DR MEROPS; M14.025; -. DR GlyGen; Q8NDL9; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000353249; -. DR PeptideAtlas; Q8NDL9; -. DR ProteomicsDB; 73036; -. [Q8NDL9-1] DR ProteomicsDB; 73037; -. [Q8NDL9-2] DR ProteomicsDB; 73038; -. [Q8NDL9-3] DR Antibodypedia; 28106; 169 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 AGR; HGNC:26147; -. 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; CAHFDFL; -. DR OrthoDB; 168164at2759; -. 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; 21 hits in 1161 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 176 other cell types or tissues. DR ExpressionAtlas; Q8NDL9; baseline and differential. 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 Gene3D; 2.60.40.3120; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 2. DR InterPro; IPR034286; M14_AGBL5-like. DR InterPro; IPR040626; Pepdidase_M14_N. DR InterPro; IPR000834; Peptidase_M14. DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1. DR PANTHER; PTHR12756:SF12; CYTOSOLIC CARBOXYPEPTIDASE-LIKE PROTEIN 5; 1. DR Pfam; PF18027; Pepdidase_M14_N; 1. DR Pfam; PF00246; Peptidase_M14; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS52035; PEPTIDASE_M14; 1. DR Genevisible; Q8NDL9; HS. 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 DOMAIN 157..570 FT /note="Peptidase M14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" 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 516 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT BINDING 434 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27842159" FT /id="VAR_079522" FT VARIANT 251 FT /note="V -> G (in RP75; uncertain 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; uncertain 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 //