CUTA_HUMAN
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 03-AUG-2022, entry version 175.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 acetylcholinesterase:
RT amino acid sequence, genomic organization, and 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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 project:
RT 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 acetylcholinesterase
RT 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., Buerckstuemmer T.,
RA 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 structures
RT 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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., Ayoub D.,
RA 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 to
CC acetylcholinesterase (AChE).
CC -!- SUBUNIT: Homotrimer.
CC -!- INTERACTION:
CC O60888; Q8WUP2: FBLIM1; NbExp=4; IntAct=EBI-1051556, EBI-3864120;
CC O60888; P22736: NR4A1; NbExp=2; IntAct=EBI-1051556, EBI-721550;
CC O60888-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10979071, EBI-3867333;
CC O60888-3; Q8WUP2: FBLIM1; NbExp=3; IntAct=EBI-10979071, EBI-3864120;
CC O60888-3; P49639: HOXA1; NbExp=3; IntAct=EBI-10979071, EBI-740785;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=O60888-1; Sequence=Displayed;
CC Name=A;
CC IsoId=O60888-2; Sequence=VSP_013225;
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};
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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; -. [O60888-3]
DR CCDS; CCDS34433.1; -. [O60888-1]
DR CCDS; CCDS4779.1; -. [O60888-3]
DR RefSeq; NP_001014433.1; NM_001014433.2. [O60888-3]
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 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 AlphaFoldDB; O60888; -.
DR SMR; O60888; -.
DR BioGRID; 119628; 41.
DR IntAct; O60888; 24.
DR STRING; 9606.ENSP00000363624; -.
DR GlyGen; O60888; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; O60888; -.
DR PhosphoSitePlus; O60888; -.
DR SwissPalm; O60888; -.
DR BioMuta; CUTA; -.
DR EPD; O60888; -.
DR jPOST; O60888; -.
DR MassIVE; O60888; -.
DR MaxQB; O60888; -.
DR PaxDb; O60888; -.
DR PeptideAtlas; O60888; -.
DR PRIDE; O60888; -.
DR ProteomicsDB; 49653; -. [O60888-1]
DR ProteomicsDB; 49654; -. [O60888-2]
DR ProteomicsDB; 49655; -. [O60888-3]
DR Antibodypedia; 29177; 181 antibodies from 26 providers.
DR DNASU; 51596; -.
DR Ensembl; ENST00000374496.3; ENSP00000363620.3; ENSG00000112514.18. [O60888-3]
DR Ensembl; ENST00000374500.10; ENSP00000363624.6; ENSG00000112514.18. [O60888-3]
DR Ensembl; ENST00000435267.6; ENSP00000391509.2; ENSG00000226492.7. [O60888-2]
DR Ensembl; ENST00000440279.7; ENSP00000403268.2; ENSG00000112514.18. [O60888-3]
DR Ensembl; ENST00000440930.6; ENSP00000400114.2; ENSG00000226492.7. [O60888-1]
DR Ensembl; ENST00000487148.5; ENSP00000432744.1; ENSG00000226492.7. [O60888-3]
DR Ensembl; ENST00000488034.6; ENSP00000417544.1; ENSG00000112514.18. [O60888-1]
DR Ensembl; ENST00000607266.5; ENSP00000475963.1; ENSG00000112514.18. [O60888-3]
DR GeneID; 51596; -.
DR KEGG; hsa:51596; -.
DR MANE-Select; ENST00000488034.6; ENSP00000417544.1; NM_001014840.2; NP_001014840.1.
DR UCSC; uc003oej.2; human. [O60888-1]
DR CTD; 51596; -.
DR GeneCards; CUTA; -.
DR HGNC; HGNC:21101; CUTA.
DR HPA; ENSG00000112514; Low tissue specificity.
DR neXtProt; NX_O60888; -.
DR OpenTargets; ENSG00000112514; -.
DR PharmGKB; PA134928220; -.
DR VEuPathDB; HostDB:ENSG00000112514; -.
DR eggNOG; KOG3338; Eukaryota.
DR GeneTree; ENSGT00390000017030; -.
DR HOGENOM; CLU_098807_1_1_1; -.
DR InParanoid; O60888; -.
DR OMA; HPYEVVE; -.
DR OrthoDB; 1589955at2759; -.
DR PhylomeDB; O60888; -.
DR TreeFam; TF313269; -.
DR PathwayCommons; O60888; -.
DR SignaLink; O60888; -.
DR BioGRID-ORCS; 51596; 10 hits in 1081 CRISPR screens.
DR ChiTaRS; CUTA; human.
DR EvolutionaryTrace; O60888; -.
DR GenomeRNAi; 51596; -.
DR Pharos; O60888; Tbio.
DR PRO; PR:O60888; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60888; protein.
DR Bgee; ENSG00000112514; Expressed in pituitary gland and 94 other tissues.
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 DisProt; DP00846; -.
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; Direct protein sequencing;
KW Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..179
FT /note="Protein CutA"
FT /id="PRO_0000006379"
FT REGION 168..176
FT /note="O-glycosylated at one site"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10800960,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_013226"
FT VAR_SEQ 1..14
FT /note="MSGGRAPAVLLGGV -> MIGSGLAGSGGAGGPSSTVTWCALFSNHVAATQ
FT (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_013225"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:2ZFH"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:2ZFH"
FT STRAND 95..109
FT /evidence="ECO:0007829|PDB:2ZFH"
FT STRAND 112..126
FT /evidence="ECO:0007829|PDB:2ZFH"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2ZFH"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2ZFH"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2ZFH"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2ZFH"
FT HELIX 158..166
FT /evidence="ECO:0007829|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
