NACHO_XENTR
ID NACHO_XENTR Reviewed; 162 AA.
AC A4IGI5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
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;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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 {ECO:0000250|UniProtKB:Q53FP2}.
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; BC135118; AAI35119.1; -; mRNA.
DR RefSeq; NP_001090850.1; NM_001097381.1.
DR AlphaFoldDB; A4IGI5; -.
DR STRING; 8364.ENSXETP00000061631; -.
DR PaxDb; A4IGI5; -.
DR DNASU; 100038262; -.
DR GeneID; 100038262; -.
DR KEGG; xtr:100038262; -.
DR CTD; 59353; -.
DR Xenbase; XB-GENE-957194; tmem35a.
DR eggNOG; ENOG502RXPR; Eukaryota.
DR HOGENOM; CLU_121618_0_0_1; -.
DR InParanoid; A4IGI5; -.
DR OMA; ICGIIMT; -.
DR OrthoDB; 1615454at2759; -.
DR PhylomeDB; A4IGI5; -.
DR TreeFam; TF300206; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000031136; Expressed in brain and 4 other tissues.
DR ExpressionAtlas; A4IGI5; differential.
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; IBA:GO_Central.
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; IPR032808; DoxX.
DR InterPro; IPR029693; TMEM35A.
DR InterPro; IPR040399; TMEM35A/B.
DR PANTHER; PTHR13163; PTHR13163; 1.
DR PANTHER; PTHR13163:SF0; PTHR13163:SF0; 1.
DR Pfam; PF13564; DoxX_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..162
FT /note="Novel acetylcholine receptor chaperone"
FT /id="PRO_0000359758"
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..131
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 141..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 162 AA; 17953 MW; 4611734C9962E3C4 CRC64;
MASPRTVTIV ALSVTLGLFF VFMGTIKLTP RLSKDAYSEM KRAYKSYVKA LPALKKIGIS
SVFLRKAIGS LELACGIVLT LVPGRPKDVA NFILLLLVLI VLFFHQLVGD PLKRYAHALV
FGILLTCRLL VSRQPEEEFP EKKLSRGNNG AHSREPIKMK VS