Full text data of CUTA
CUTA
(ACHAP, C6orf82)
[Confidence: low (only semi-automatic identification from reviews)]
Protein CutA (Acetylcholinesterase-associated protein; Brain acetylcholinesterase putative membrane anchor; Flags: Precursor)
Protein CutA (Acetylcholinesterase-associated protein; Brain acetylcholinesterase putative membrane anchor; Flags: Precursor)
UniProt
O60888
ID CUTA_HUMAN Reviewed; 179 AA.
AC O60888; A2AB26; A2BEL4; Q3B784; Q5JXM9; Q5SU05; Q9NYQ9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 111.
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 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 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 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 -!- PTM: O-glycosylated.
CC -!- SIMILARITY: Belongs to the CutA family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61220.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; CAI18273.2; -; Genomic_DNA.
DR EMBL; AL662799; CAM25571.1; -; Genomic_DNA.
DR EMBL; BX088650; CAM26302.1; -; Genomic_DNA.
DR EMBL; BX088650; CAM26303.1; -; Genomic_DNA.
DR EMBL; BC005890; AAH05890.1; -; mRNA.
DR EMBL; BC107751; AAI07752.1; -; mRNA.
DR RefSeq; NP_001014433.1; NM_001014433.2.
DR RefSeq; NP_001014837.1; NM_001014837.1.
DR RefSeq; NP_001014838.1; NM_001014838.1.
DR RefSeq; NP_001014840.1; NM_001014840.1.
DR RefSeq; NP_057005.1; NM_015921.2.
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 ProteinModelPortal; O60888; -.
DR SMR; O60888; 61-169.
DR IntAct; O60888; 7.
DR STRING; 9606.ENSP00000363624; -.
DR PhosphoSite; O60888; -.
DR PaxDb; O60888; -.
DR PRIDE; O60888; -.
DR Ensembl; ENST00000374496; ENSP00000363620; ENSG00000112514.
DR Ensembl; ENST00000374500; ENSP00000363624; ENSG00000112514.
DR Ensembl; ENST00000435267; ENSP00000391509; ENSG00000226492.
DR Ensembl; ENST00000440279; ENSP00000403268; ENSG00000112514.
DR Ensembl; ENST00000440930; ENSP00000400114; ENSG00000226492.
DR Ensembl; ENST00000487148; ENSP00000432744; ENSG00000226492.
DR Ensembl; ENST00000488034; ENSP00000417544; ENSG00000112514.
DR Ensembl; ENST00000607266; ENSP00000475963; ENSG00000112514.
DR GeneID; 51596; -.
DR KEGG; hsa:51596; -.
DR UCSC; uc003oej.1; human.
DR CTD; 51596; -.
DR GeneCards; GC06M033384; -.
DR GeneCards; GC06Mo33523; -.
DR HGNC; HGNC:21101; CUTA.
DR HPA; CAB016787; -.
DR neXtProt; NX_O60888; -.
DR PharmGKB; PA134928220; -.
DR eggNOG; COG1324; -.
DR HOVERGEN; HBG051265; -.
DR KO; K03926; -.
DR OMA; PVEQGNS; -.
DR ChiTaRS; CUTA; human.
DR EvolutionaryTrace; O60888; -.
DR GenomeRNAi; 51596; -.
DR NextBio; 55447; -.
DR PRO; PR:O60888; -.
DR ArrayExpress; O60888; -.
DR Bgee; O60888; -.
DR CleanEx; HS_CUTA; -.
DR Genevestigator; O60888; -.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0010038; P:response to metal ion; IEA:InterPro.
DR InterPro; IPR004323; Ion_tolerance_CutA.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
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 Potential.
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 /FTId=VSP_013226.
FT VAR_SEQ 1 14 MSGGRAPAVLLGGV -> MIGSGLAGSGGAGGPSSTVTWCA
FT LFSNHVAATQ (in isoform A).
FT /FTId=VSP_013225.
FT STRAND 67 77
FT HELIX 78 90
FT STRAND 95 109
FT STRAND 112 126
FT HELIX 127 129
FT HELIX 130 140
FT STRAND 142 145
FT STRAND 148 153
FT HELIX 158 166
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
//
ID CUTA_HUMAN Reviewed; 179 AA.
AC O60888; A2AB26; A2BEL4; Q3B784; Q5JXM9; Q5SU05; Q9NYQ9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 111.
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 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 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 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 -!- PTM: O-glycosylated.
CC -!- SIMILARITY: Belongs to the CutA family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61220.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; CAI18273.2; -; Genomic_DNA.
DR EMBL; AL662799; CAM25571.1; -; Genomic_DNA.
DR EMBL; BX088650; CAM26302.1; -; Genomic_DNA.
DR EMBL; BX088650; CAM26303.1; -; Genomic_DNA.
DR EMBL; BC005890; AAH05890.1; -; mRNA.
DR EMBL; BC107751; AAI07752.1; -; mRNA.
DR RefSeq; NP_001014433.1; NM_001014433.2.
DR RefSeq; NP_001014837.1; NM_001014837.1.
DR RefSeq; NP_001014838.1; NM_001014838.1.
DR RefSeq; NP_001014840.1; NM_001014840.1.
DR RefSeq; NP_057005.1; NM_015921.2.
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 ProteinModelPortal; O60888; -.
DR SMR; O60888; 61-169.
DR IntAct; O60888; 7.
DR STRING; 9606.ENSP00000363624; -.
DR PhosphoSite; O60888; -.
DR PaxDb; O60888; -.
DR PRIDE; O60888; -.
DR Ensembl; ENST00000374496; ENSP00000363620; ENSG00000112514.
DR Ensembl; ENST00000374500; ENSP00000363624; ENSG00000112514.
DR Ensembl; ENST00000435267; ENSP00000391509; ENSG00000226492.
DR Ensembl; ENST00000440279; ENSP00000403268; ENSG00000112514.
DR Ensembl; ENST00000440930; ENSP00000400114; ENSG00000226492.
DR Ensembl; ENST00000487148; ENSP00000432744; ENSG00000226492.
DR Ensembl; ENST00000488034; ENSP00000417544; ENSG00000112514.
DR Ensembl; ENST00000607266; ENSP00000475963; ENSG00000112514.
DR GeneID; 51596; -.
DR KEGG; hsa:51596; -.
DR UCSC; uc003oej.1; human.
DR CTD; 51596; -.
DR GeneCards; GC06M033384; -.
DR GeneCards; GC06Mo33523; -.
DR HGNC; HGNC:21101; CUTA.
DR HPA; CAB016787; -.
DR neXtProt; NX_O60888; -.
DR PharmGKB; PA134928220; -.
DR eggNOG; COG1324; -.
DR HOVERGEN; HBG051265; -.
DR KO; K03926; -.
DR OMA; PVEQGNS; -.
DR ChiTaRS; CUTA; human.
DR EvolutionaryTrace; O60888; -.
DR GenomeRNAi; 51596; -.
DR NextBio; 55447; -.
DR PRO; PR:O60888; -.
DR ArrayExpress; O60888; -.
DR Bgee; O60888; -.
DR CleanEx; HS_CUTA; -.
DR Genevestigator; O60888; -.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0010038; P:response to metal ion; IEA:InterPro.
DR InterPro; IPR004323; Ion_tolerance_CutA.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
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 Potential.
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 /FTId=VSP_013226.
FT VAR_SEQ 1 14 MSGGRAPAVLLGGV -> MIGSGLAGSGGAGGPSSTVTWCA
FT LFSNHVAATQ (in isoform A).
FT /FTId=VSP_013225.
FT STRAND 67 77
FT HELIX 78 90
FT STRAND 95 109
FT STRAND 112 126
FT HELIX 127 129
FT HELIX 130 140
FT STRAND 142 145
FT STRAND 148 153
FT HELIX 158 166
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
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