ID CUTA_HUMAN Reviewed; 179 AA. AC O60888; A2AB26; A2BEL4; Q3B784; Q5JXM9; Q5SU05; Q9NYQ9; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 13-FEB-2019, entry version 156. DE RecName: Full=Protein CutA; DE AltName: Full=Acetylcholinesterase-associated protein; DE AltName: Full=Brain acetylcholinesterase putative membrane anchor; DE Flags: Precursor; GN Name=CUTA; Synonyms=ACHAP, C6orf82; 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 [MRNA] (ISOFORM C), PROTEIN SEQUENCE OF 70-74 AND RP 84-178, TISSUE SPECIFICITY, AND PUTATIVE FUNCTION. RX PubMed=10800960; DOI=10.1046/j.1471-4159.2000.0742146.x; RA Navaratnam D.S., Fernando F.S., Priddle J.D., Giles K., Clegg S.M., RA Pappin D.J.C., Craig I., Smith A.D.; RT "Hydrophobic protein that copurifies with human brain RT acetylcholinesterase: amino acid sequence, genomic organization, and RT chromosomal localization."; RL J. Neurochem. 74:2146-2153(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). RA Luo W.Q., Chen J.H., Huan X.W., Zhou Y., Yuan J.G., Qiang B.Q.; RT "Cloning and isolating human CUTA cDNA."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C). RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP ALTERNATIVE SPLICING (ISOFORMS A; B AND C). RX PubMed=10954708; DOI=10.1074/jbc.M004289200; RA Perrier A.L., Cousin X., Boschetti N., Haas R., Chatel J.-M., Bon S., RA Roberts W.L., Pickett S.R., Massoulie J., Rosenberry T.L., Krejci E.; RT "Two distinct proteins are associated with tetrameric RT acetylcholinesterase on the cell surface."; RL J. Biol. Chem. 275:34260-34265(2000). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23234360; DOI=10.1021/pr300963h; RA Halim A., Ruetschi U., Larson G., Nilsson J.; RT "LC-MS/MS characterization of O-glycosylation sites and glycan RT structures of human cerebrospinal fluid glycoproteins."; RL J. Proteome Res. 12:573-584(2013). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 44-179. RG Southeast collaboratory for structural genomics (SECSG); RT "Divalent cation tolerant protein CUTA from Homo sapiens O60888."; RL Submitted (SEP-2004) to the PDB data bank. CC -!- FUNCTION: May form part of a complex of membrane proteins attached CC to acetylcholinesterase (AChE). CC -!- SUBUNIT: Homotrimer. CC -!- INTERACTION: CC Q8WUP2:FBLIM1; NbExp=3; IntAct=EBI-1051556, EBI-3864120; CC P22736:NR4A1; NbExp=2; IntAct=EBI-1051556, EBI-721550; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; CC IsoId=O60888-1; Sequence=Displayed; CC Note=No experimental confirmation available.; CC Name=A; CC IsoId=O60888-2; Sequence=VSP_013225; CC Note=No experimental confirmation available.; CC Name=C; CC IsoId=O60888-3; Sequence=VSP_013226; CC -!- TISSUE SPECIFICITY: Ubiquitous. Widely expressed in brain. CC {ECO:0000269|PubMed:10800960}. CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}. CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF61220.1; Type=Erroneous initiation; 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; AF230924; AAF61220.1; ALT_INIT; mRNA. DR EMBL; AF106943; AAD21026.1; -; mRNA. DR EMBL; AL050332; CAB63779.1; -; Genomic_DNA. DR EMBL; AL021366; CAA16160.1; -; Genomic_DNA. DR EMBL; AL662799; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX088650; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005890; AAH05890.1; -; mRNA. DR EMBL; BC107751; AAI07752.1; -; mRNA. DR CCDS; CCDS34432.1; -. [O60888-2] DR CCDS; CCDS34433.1; -. [O60888-1] DR CCDS; CCDS4779.1; -. [O60888-3] DR RefSeq; NP_001014433.1; NM_001014433.2. [O60888-2] DR RefSeq; NP_001014837.1; NM_001014837.1. [O60888-3] DR RefSeq; NP_001014838.1; NM_001014838.1. [O60888-3] DR RefSeq; NP_001014840.1; NM_001014840.1. [O60888-1] DR RefSeq; NP_057005.1; NM_015921.2. [O60888-3] DR UniGene; Hs.520070; -. DR PDB; 1XK8; X-ray; 2.70 A; A/B/C/D/E/F=44-179. DR PDB; 2ZFH; X-ray; 2.05 A; A/B/C/D/E/F=1-179. DR PDBsum; 1XK8; -. DR PDBsum; 2ZFH; -. DR DisProt; DP00846; -. DR ProteinModelPortal; O60888; -. DR SMR; O60888; -. DR BioGrid; 119628; 26. DR IntAct; O60888; 12. DR STRING; 9606.ENSP00000363624; -. DR iPTMnet; O60888; -. DR PhosphoSitePlus; O60888; -. DR SwissPalm; O60888; -. DR BioMuta; CUTA; -. DR EPD; O60888; -. DR jPOST; O60888; -. DR MaxQB; O60888; -. DR PaxDb; O60888; -. DR PeptideAtlas; O60888; -. DR PRIDE; O60888; -. DR ProteomicsDB; 49653; -. DR ProteomicsDB; 49654; -. [O60888-2] DR ProteomicsDB; 49655; -. [O60888-3] DR Ensembl; ENST00000374496; ENSP00000363620; ENSG00000112514. [O60888-3] DR Ensembl; ENST00000374500; ENSP00000363624; ENSG00000112514. [O60888-2] DR Ensembl; ENST00000435267; ENSP00000391509; ENSG00000226492. [O60888-2] DR Ensembl; ENST00000440279; ENSP00000403268; ENSG00000112514. [O60888-3] DR Ensembl; ENST00000440930; ENSP00000400114; ENSG00000226492. [O60888-1] DR Ensembl; ENST00000487148; ENSP00000432744; ENSG00000226492. [O60888-3] DR Ensembl; ENST00000488034; ENSP00000417544; ENSG00000112514. [O60888-1] DR Ensembl; ENST00000607266; ENSP00000475963; ENSG00000112514. [O60888-3] DR Ensembl; ENST00000611509; ENSP00000480360; ENSG00000112514. [O60888-3] DR GeneID; 51596; -. DR KEGG; hsa:51596; -. DR UCSC; uc003oej.2; human. [O60888-1] DR CTD; 51596; -. DR DisGeNET; 51596; -. DR EuPathDB; HostDB:ENSG00000112514.15; -. DR GeneCards; CUTA; -. DR HGNC; HGNC:21101; CUTA. DR HPA; CAB016787; -. DR HPA; HPA064369; -. DR neXtProt; NX_O60888; -. DR OpenTargets; ENSG00000112514; -. DR PharmGKB; PA134928220; -. DR eggNOG; KOG3338; Eukaryota. DR eggNOG; COG1324; LUCA. DR GeneTree; ENSGT00390000017030; -. DR HOVERGEN; HBG051265; -. DR InParanoid; O60888; -. DR KO; K03926; -. DR OMA; SPYLHWV; -. DR OrthoDB; 1589955at2759; -. DR PhylomeDB; O60888; -. DR TreeFam; TF313269; -. DR ChiTaRS; CUTA; human. DR EvolutionaryTrace; O60888; -. DR GenomeRNAi; 51596; -. DR PRO; PR:O60888; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000112514; Expressed in 223 organ(s), highest expression level in adenohypophysis. DR ExpressionAtlas; O60888; baseline and differential. DR Genevisible; O60888; HS. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0008104; P:protein localization; IDA:UniProtKB. DR GO; GO:0010038; P:response to metal ion; IEA:InterPro. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR004323; Ion_tolerance_CutA. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR PANTHER; PTHR23419; PTHR23419; 1. DR Pfam; PF03091; CutA1; 1. DR SUPFAM; SSF54913; SSF54913; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Glycoprotein; Reference proteome; Signal. FT SIGNAL 1 32 {ECO:0000255}. FT CHAIN 33 179 Protein CutA. FT /FTId=PRO_0000006379. FT REGION 168 176 O-glycosylated at one site. FT COMPBIAS 34 37 Poly-Leu. FT VAR_SEQ 1 23 Missing (in isoform C). FT {ECO:0000303|PubMed:10800960, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.2}. FT /FTId=VSP_013226. FT VAR_SEQ 1 14 MSGGRAPAVLLGGV -> MIGSGLAGSGGAGGPSSTVTWCA FT LFSNHVAATQ (in isoform A). {ECO:0000305}. FT /FTId=VSP_013225. FT STRAND 67 77 {ECO:0000244|PDB:2ZFH}. FT HELIX 78 90 {ECO:0000244|PDB:2ZFH}. FT STRAND 95 109 {ECO:0000244|PDB:2ZFH}. FT STRAND 112 126 {ECO:0000244|PDB:2ZFH}. FT HELIX 127 129 {ECO:0000244|PDB:2ZFH}. FT HELIX 130 140 {ECO:0000244|PDB:2ZFH}. FT STRAND 142 145 {ECO:0000244|PDB:2ZFH}. FT STRAND 148 153 {ECO:0000244|PDB:2ZFH}. FT HELIX 158 166 {ECO:0000244|PDB:2ZFH}. SQ SEQUENCE 179 AA; 19116 MW; B8EBD7F8C069862A CRC64; MSGGRAPAVL LGGVASLLLS FVWMPALLPV ASRLLLLPRV LLTMASGSPP TQPSPASDSG SGYVPGSVSA AFVTCPNEKV AKEIARAVVE KRLAACVNLI PQITSIYEWK GKIEEDSEVL MMIKTQSSLV PALTDFVRSV HPYEVAEVIA LPVEQGNFPY LQWVRQVTES VSDSITVLP //