NACHO_DANRE
ID NACHO_DANRE Reviewed; 160 AA.
AC Q58EL2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=zgc:110832;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-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 {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; BC091856; AAH91856.1; -; mRNA.
DR AlphaFoldDB; Q58EL2; -.
DR STRING; 7955.ENSDARP00000068937; -.
DR PaxDb; Q58EL2; -.
DR ZFIN; ZDB-GENE-030815-1; tmem35.
DR eggNOG; ENOG502RXPR; Eukaryota.
DR InParanoid; Q58EL2; -.
DR PhylomeDB; Q58EL2; -.
DR PRO; PR:Q58EL2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..160
FT /note="Novel acetylcholine receptor chaperone"
FT /id="PRO_0000359757"
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..113
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..131
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 137..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 160 AA; 17887 MW; F2716D67DFE87B06 CRC64;
MASPRTVTIV ALSFALGLFF VFMGTIKLTP RLSKDAYSEM KRAYKSYAKA LPALKKMGVS
SVLLRKIIGT LEVGCGIVLT LVPGRPKDVA NFILLLVMLA VLFFHQLVGD PLKRYAHALV
FGILLTCRLL IARQAEDRPE REERREEQIN AQEKNKVKVS