NACHO_MACFA
ID NACHO_MACFA Reviewed; 167 AA.
AC Q4R5F4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Novel acetylcholine receptor chaperone {ECO:0000250|UniProtKB:Q53FP2};
DE AltName: Full=Transmembrane protein 35A;
GN Name=TMEM35A; Synonyms=NACHO {ECO:0000250|UniProtKB:Q53FP2}, TMEM35;
GN ORFNames=QnpA-14372;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone which mediates the proper assembly and
CC functional expression of the nicotinic acetylcholine receptors (nAChRs)
CC throughout the brain (By similarity). Essential for the proper folding,
CC assembly, function and surface trafficking of alpha-7 (CHRNA7), alpha-
CC 4-beta-2, alpha-3-beta-2 and alpha-3-beta-4 receptors (By similarity).
CC Stably associates with ribophorin-1 (RPN1) and ribophorin-2 (RPN2)
CC (components of the oligosaccharyl transferase (OST) complex) and with
CC calnexin (CANX), both of which are critical for NACHO-mediated effects
CC on CHRNA7 assembly and function (By similarity). Facilitates the proper
CC folding and assembly of alpha-6-beta-2 and alpha-6-beta-2-beta-3
CC receptors and acts at early stages of the nAChRs subunit assembly (By
CC similarity). Promotes the expression of the alpha-4(2):beta-2(3)
CC stoichiometric form over the alpha-4(3):beta-2(2) form (By similarity).
CC {ECO:0000250|UniProtKB:Q53FP2, ECO:0000250|UniProtKB:Q9D328}.
CC -!- SUBUNIT: May interact with NGFR (By similarity). Interacts with RPN1,
CC RPN2 and CANX (By similarity). {ECO:0000250|UniProtKB:Q6JAM9,
CC ECO:0000250|UniProtKB:Q9D328}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q9D328}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q6JAM9}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9D328}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Shedding may lead to a
CC soluble peptide. {ECO:0000250|UniProtKB:Q6JAM9}.
CC -!- SIMILARITY: Belongs to the DoxX family. {ECO:0000305}.
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DR EMBL; AB169589; BAE01671.1; -; mRNA.
DR RefSeq; NP_001270235.1; NM_001283306.1.
DR AlphaFoldDB; Q4R5F4; -.
DR STRING; 9541.XP_005594191.1; -.
DR Ensembl; ENSMFAT00000001209; ENSMFAP00000027027; ENSMFAG00000044929.
DR GeneID; 101926690; -.
DR CTD; 59353; -.
DR VEuPathDB; HostDB:ENSMFAG00000044929; -.
DR eggNOG; ENOG502RXPR; Eukaryota.
DR GeneTree; ENSGT00940000154325; -.
DR OMA; ICGIIMT; -.
DR OrthoDB; 1615454at2759; -.
DR Proteomes; UP000233100; Chromosome X.
DR Bgee; ENSMFAG00000044929; Expressed in temporal lobe and 4 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030548; F:acetylcholine receptor regulator activity; IEA:Ensembl.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISS:UniProtKB.
DR InterPro; IPR029693; TMEM35A.
DR InterPro; IPR040399; TMEM35A/B.
DR PANTHER; PTHR13163; PTHR13163; 1.
DR PANTHER; PTHR13163:SF0; PTHR13163:SF0; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..167
FT /note="Novel acetylcholine receptor chaperone"
FT /id="PRO_0000271608"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..61
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 89..109
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..114
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..132
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 43..54
FT /note="Interaction with NGFR"
FT /evidence="ECO:0000250|UniProtKB:Q6JAM9"
FT REGION 136..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 167 AA; 18440 MW; 062A6E7700DB33B7 CRC64;
MASPRTVTIV ALSVALGLFF VFMGTIKLTP RLSKDAYSEM KRAYKSYVRA LPLLKKMGIN
SILLRKSIGA LEVACGIVMT LVPGRPKDVA NFFLLLLVLA VLFFHQLVGD PLKRYAHALV
FGILLTCRLL IARKPEDRSS EKKPLPGNAE EQPSLYEKAP QGKVKVS
