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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
 
 
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