ID CBPC6_HUMAN Reviewed; 503 AA. AC Q5VU57; B3KT26; B4DG37; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 21-SEP-2011, entry version 57. DE RecName: Full=Cytosolic carboxypeptidase 6; DE EC=3.4.17.-; DE AltName: Full=ATP/GTP-binding protein-like 4; GN Name=AGBL4; Synonyms=CCP6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Brain; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). CC -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of CC target proteins. Catalyzes the deglutamylation of polyglutamate CC side chains generated by post-translational polyglutamylation in CC proteins such as tubulins. Also removes gene-encoded CC polyglutamates from the carboxy-terminus of target proteins such CC as MYLK. Acts as a long-chain deglutamylase and specifically CC shortens long polyglutamate chains, while it is not able to remove CC the branching point glutamate, a process catalyzed by AGBL5/CCP5 CC (By similarity). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Interacts with MYLK (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5VU57-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5VU57-2; Sequence=VSP_040435, VSP_040436; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the peptidase M14 family. CC -!- SEQUENCE CAUTION: CC Sequence=BAG52938.1; Type=Frameshift; Positions=501; CC Sequence=BAG57648.1; Type=Frameshift; Positions=501; 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; AK094826; BAG52938.1; ALT_FRAME; mRNA. DR EMBL; AK294394; BAG57648.1; ALT_FRAME; mRNA. DR EMBL; AL590432; CAH70510.1; -; Genomic_DNA. DR EMBL; AC099788; CAH70510.1; JOINED; Genomic_DNA. DR EMBL; AL355809; CAH70510.1; JOINED; Genomic_DNA. DR EMBL; AL390023; CAH70510.1; JOINED; Genomic_DNA. DR EMBL; AL391844; CAH70510.1; JOINED; Genomic_DNA. DR EMBL; AL591602; CAH70510.1; JOINED; Genomic_DNA. DR EMBL; AL645507; CAH70510.1; JOINED; Genomic_DNA. DR EMBL; AL645730; CAH70510.1; JOINED; Genomic_DNA. DR EMBL; AL391844; CAI13521.1; -; Genomic_DNA. DR EMBL; AC099788; CAI13521.1; JOINED; Genomic_DNA. DR EMBL; AL355809; CAI13521.1; JOINED; Genomic_DNA. DR EMBL; AL390023; CAI13521.1; JOINED; Genomic_DNA. DR EMBL; AL590432; CAI13521.1; JOINED; Genomic_DNA. DR EMBL; AL591602; CAI13521.1; JOINED; Genomic_DNA. DR EMBL; AL645507; CAI13521.1; JOINED; Genomic_DNA. DR EMBL; AL645730; CAI13521.1; JOINED; Genomic_DNA. DR EMBL; AL645507; CAI14372.1; -; Genomic_DNA. DR EMBL; AC099788; CAI14372.1; JOINED; Genomic_DNA. DR EMBL; AL355809; CAI14372.1; JOINED; Genomic_DNA. DR EMBL; AL390023; CAI14372.1; JOINED; Genomic_DNA. DR EMBL; AL391844; CAI14372.1; JOINED; Genomic_DNA. DR EMBL; AL590432; CAI14372.1; JOINED; Genomic_DNA. DR EMBL; AL591602; CAI14372.1; JOINED; Genomic_DNA. DR EMBL; AL645730; CAI14372.1; JOINED; Genomic_DNA. DR EMBL; AL645730; CAI17069.1; -; Genomic_DNA. DR EMBL; AC099788; CAI17069.1; JOINED; Genomic_DNA. DR EMBL; AL355809; CAI17069.1; JOINED; Genomic_DNA. DR EMBL; AL390023; CAI17069.1; JOINED; Genomic_DNA. DR EMBL; AL391844; CAI17069.1; JOINED; Genomic_DNA. DR EMBL; AL590432; CAI17069.1; JOINED; Genomic_DNA. DR EMBL; AL591602; CAI17069.1; JOINED; Genomic_DNA. DR EMBL; AL645507; CAI17069.1; JOINED; Genomic_DNA. DR EMBL; AL591602; CAI19137.1; -; Genomic_DNA. DR EMBL; AC099788; CAI19137.1; JOINED; Genomic_DNA. DR EMBL; AL355809; CAI19137.1; JOINED; Genomic_DNA. DR EMBL; AL390023; CAI19137.1; JOINED; Genomic_DNA. DR EMBL; AL391844; CAI19137.1; JOINED; Genomic_DNA. DR EMBL; AL590432; CAI19137.1; JOINED; Genomic_DNA. DR EMBL; AL645507; CAI19137.1; JOINED; Genomic_DNA. DR EMBL; AL645730; CAI19137.1; JOINED; Genomic_DNA. DR EMBL; AL355809; CAI22167.1; -; Genomic_DNA. DR EMBL; AC099788; CAI22167.1; JOINED; Genomic_DNA. DR EMBL; AL390023; CAI22167.1; JOINED; Genomic_DNA. DR EMBL; AL391844; CAI22167.1; JOINED; Genomic_DNA. DR EMBL; AL590432; CAI22167.1; JOINED; Genomic_DNA. DR EMBL; AL591602; CAI22167.1; JOINED; Genomic_DNA. DR EMBL; AL645507; CAI22167.1; JOINED; Genomic_DNA. DR EMBL; AL645730; CAI22167.1; JOINED; Genomic_DNA. DR EMBL; AL390023; CAI23365.1; -; Genomic_DNA. DR EMBL; AC099788; CAI23365.1; JOINED; Genomic_DNA. DR EMBL; AL355809; CAI23365.1; JOINED; Genomic_DNA. DR EMBL; AL391844; CAI23365.1; JOINED; Genomic_DNA. DR EMBL; AL590432; CAI23365.1; JOINED; Genomic_DNA. DR EMBL; AL591602; CAI23365.1; JOINED; Genomic_DNA. DR EMBL; AL645507; CAI23365.1; JOINED; Genomic_DNA. DR EMBL; AL645730; CAI23365.1; JOINED; Genomic_DNA. DR IPI; IPI00973592; -. DR IPI; IPI01013035; -. DR RefSeq; NP_116174.3; NM_032785.3. DR UniGene; Hs.551844; -. DR UniGene; Hs.679809; -. DR ProteinModelPortal; Q5VU57; -. DR STRING; Q5VU57; -. DR PhosphoSite; Q5VU57; -. DR PRIDE; Q5VU57; -. DR Ensembl; ENST00000371839; ENSP00000360905; ENSG00000186094. DR GeneID; 84871; -. DR KEGG; hsa:84871; -. DR CTD; 84871; -. DR GeneCards; GC01M047116; -. DR HGNC; HGNC:25892; AGBL4. DR HPA; HPA037994; -. DR neXtProt; NX_Q5VU57; -. DR PharmGKB; PA142672636; -. DR GeneTree; ENSGT00550000074405; -. DR HOVERGEN; HBG107588; -. DR InParanoid; Q5VU57; -. DR OMA; VYRYERH; -. DR OrthoDB; EOG45X7X0; -. DR ArrayExpress; Q5VU57; -. DR Bgee; Q5VU57; -. DR CleanEx; HS_AGBL4; -. DR Genevestigator; Q5VU57; -. DR GO; GO:0005829; C:cytosol; ISS: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:0035610; P:protein side chain deglutamylation; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR000834; Peptidase_M14. DR Pfam; PF00246; Peptidase_M14; 1. DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; FALSE_NEG. DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; FALSE_NEG. PE 2: Evidence at transcript level; KW Alternative splicing; Carboxypeptidase; Complete proteome; Cytoplasm; KW Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; KW Reference proteome; Zinc. FT CHAIN 1 503 Cytosolic carboxypeptidase 6. FT /FTId=PRO_0000284835. FT ACT_SITE 280 280 Nucleophile (By similarity). FT METAL 230 230 Zinc (By similarity). FT METAL 233 233 Zinc (By similarity). FT METAL 328 328 Zinc (By similarity). FT VAR_SEQ 94 94 Q -> QVREIVDTFRVVL (in isoform 2). FT /FTId=VSP_040435. FT VAR_SEQ 455 463 Missing (in isoform 2). FT /FTId=VSP_040436. FT VARIANT 443 443 V -> M (in dbSNP:rs60977321). FT /FTId=VAR_061078. FT CONFLICT 237 237 S -> L (in Ref. 1; BAG57648). FT CONFLICT 490 490 K -> R (in Ref. 1; BAG57648). SQ SEQUENCE 503 AA; 58230 MW; 4D1AD20229664D90 CRC64; MAEGSQSAPE AGNDMGNDDA IGGNVSKYIV LPTGYCGQPK KGHLIFDACF ESGNLGRVDQ VSEFEYDLFI RPDTCNPRFR VWFNFTVENV KESQRVIFNI VNFSKTKSLY RDGMAPMVKS TSRPKWQRLP PKNVYYYRCP DHRKNYVMSF AFCFDREEDI YQFAYCYPYT YTRFQHYLDS LQKRNMDYFF REQLGQSVQQ RKLDLLTITS PDNLREGAEQ KVVFITGRVH PGETPSSFVC QGIIDFLVSQ HPIACVLREY LVFKIAPMLN PDGVYLGNYR CSLMGFDLNR HWLDPSPWVH PTLHGVKQLI VQMYNDPKTS LEFYIDIHAH STMMNGFMYG NIFEDEERFQ RQAIFPKLLC QNAEDFSYSS TSFNRDAVKA GTGRRFLGGL LDHTSYCYTL EVSFYSYIIS GTTAAVPYTE EAYMKLGRNV ARTFLDYYRL NPVVEKVAIP MPRLRNKEIE VQRRKEKSPP YKHPLLRGPA SNYPNSKGDK KSSVNHKDPS TPF //