NACHO_BOVIN
ID NACHO_BOVIN Reviewed; 177 AA.
AC Q5E9T5; Q5EAA9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BT020660; AAX08677.1; -; mRNA.
DR EMBL; BT020835; AAX08852.1; -; mRNA.
DR EMBL; BC122649; AAI22650.1; -; mRNA.
DR RefSeq; NP_001014940.1; NM_001014940.1.
DR AlphaFoldDB; Q5E9T5; -.
DR STRING; 9913.ENSBTAP00000028319; -.
DR PaxDb; Q5E9T5; -.
DR PRIDE; Q5E9T5; -.
DR Ensembl; ENSBTAT00000028319; ENSBTAP00000028319; ENSBTAG00000021252.
DR GeneID; 533337; -.
DR KEGG; bta:533337; -.
DR CTD; 59353; -.
DR VEuPathDB; HostDB:ENSBTAG00000021252; -.
DR VGNC; VGNC:36077; TMEM35A.
DR eggNOG; ENOG502RXPR; Eukaryota.
DR GeneTree; ENSGT00940000154325; -.
DR HOGENOM; CLU_121618_0_0_1; -.
DR InParanoid; Q5E9T5; -.
DR OMA; ICGIIMT; -.
DR OrthoDB; 1615454at2759; -.
DR TreeFam; TF300206; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000021252; Expressed in Ammon's horn and 95 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; 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; 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..177
FT /note="Novel acetylcholine receptor chaperone"
FT /id="PRO_0000271606"
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..177
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..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 5
FT /note="R -> I (in Ref. 1; AAX08677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 177 AA; 19307 MW; 539355781EB9D52F CRC64;
MASPRTVTVV ALSVALGLFF VFMGTIKLTP RLSKDAYSEM KRAYKSYVRA LPLLKKMGIN
SILLRKSIGA LEVACGIVMT LVPGRPKDVA NFFLLLLVLA VLFFHQLVGD PLKRYAHALV
FGILLTCRLL IARKPEDRSS EKKSSPPGNA GSDGNAGNTE EQPSLYEKAP QGKMKLS
