CUTA_RAT
ID CUTA_RAT Reviewed; 177 AA.
AC Q6MGD0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein CutA;
DE AltName: Full=Brain acetylcholinesterase putative membrane anchor;
DE Flags: Precursor;
GN Name=Cuta;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 44-169.
RC STRAIN=LE392;
RX PubMed=12949080; DOI=10.1074/jbc.m304398200;
RA Arnesano F., Banci L., Benvenuti M., Bertini I., Calderone V., Mangani S.,
RA Viezzoli M.S.;
RT "The evolutionarily conserved trimeric structure of CutA1 proteins suggests
RT a role in signal transduction.";
RL J. Biol. Chem. 278:45999-46006(2003).
CC -!- FUNCTION: May form part of a complex of membrane proteins attached to
CC acetylcholinesterase (AChE).
CC -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE83916.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX883042; CAE83916.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001158178.1; NM_001164706.1.
DR RefSeq; NP_001158179.1; NM_001164707.1.
DR PDB; 1OSC; X-ray; 2.15 A; A/B/C/D/E/F=44-169.
DR PDBsum; 1OSC; -.
DR AlphaFoldDB; Q6MGD0; -.
DR SMR; Q6MGD0; -.
DR STRING; 10116.ENSRNOP00000000568; -.
DR iPTMnet; Q6MGD0; -.
DR PhosphoSitePlus; Q6MGD0; -.
DR jPOST; Q6MGD0; -.
DR PaxDb; Q6MGD0; -.
DR PRIDE; Q6MGD0; -.
DR GeneID; 294288; -.
DR KEGG; rno:294288; -.
DR UCSC; RGD:1303306; rat.
DR CTD; 51596; -.
DR RGD; 1303306; Cuta.
DR eggNOG; KOG3338; Eukaryota.
DR InParanoid; Q6MGD0; -.
DR PhylomeDB; Q6MGD0; -.
DR EvolutionaryTrace; Q6MGD0; -.
DR PRO; PR:Q6MGD0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP: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; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..177
FT /note="Protein CutA"
FT /id="PRO_0000006381"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:1OSC"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:1OSC"
FT STRAND 93..107
FT /evidence="ECO:0007829|PDB:1OSC"
FT STRAND 110..124
FT /evidence="ECO:0007829|PDB:1OSC"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1OSC"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:1OSC"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1OSC"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1OSC"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:1OSC"
SQ SEQUENCE 177 AA; 18659 MW; 208BF71CB48B945E CRC64;
MNWGGALGVL LGGGATLLLS FLCMPALLPV ASRLLLLPRA LLSMASGSPP SQPSPASGSG
YVPGSVSAAF VTCPNEKVAK EIARAVVEKR LAACVNLIPQ ITSIYEWKGK IEEDSEVLMM
IKTQSSLVPA LTEFVRSVHP YEVAEVIALP VEQGNPPYLH WVHQVTESVS GSGKALP