NACHO_HUMAN
ID NACHO_HUMAN Reviewed; 167 AA.
AC Q53FP2; Q9H7Y3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Novel acetylcholine receptor chaperone {ECO:0000303|PubMed:26875622, ECO:0000303|PubMed:28445721, ECO:0000303|PubMed:32676916, ECO:0000303|PubMed:32783947};
GN Name=TMEM35A {ECO:0000312|HGNC:HGNC:25864};
GN Synonyms=NACHO {ECO:0000303|PubMed:26875622, ECO:0000303|PubMed:28445721,
GN ECO:0000303|PubMed:32676916, ECO:0000303|PubMed:32783947}, TMEM35;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=26875622; DOI=10.1016/j.neuron.2016.01.018;
RA Gu S., Matta J.A., Lord B., Harrington A.W., Sutton S.W., Davini W.B.,
RA Bredt D.S.;
RT "Brain alpha7 Nicotinic Acetylcholine Receptor Assembly Requires NACHO.";
RL Neuron 89:948-955(2016).
RN [6]
RP FUNCTION.
RX PubMed=27789755; DOI=10.1177/1087057116676086;
RA Rex E.B., Shukla N., Gu S., Bredt D., DiSepio D.;
RT "A Genome-Wide Arrayed cDNA Screen to Identify Functional Modulators of
RT alpha7 Nicotinic Acetylcholine Receptors.";
RL SLAS Discovery 22:155-165(2017).
RN [7]
RP FUNCTION.
RX PubMed=28445721; DOI=10.1016/j.celrep.2017.04.008;
RA Matta J.A., Gu S., Davini W.B., Lord B., Siuda E.R., Harrington A.W.,
RA Bredt D.S.;
RT "NACHO Mediates Nicotinic Acetylcholine Receptor Function throughout the
RT Brain.";
RL Cell Rep. 19:688-696(2017).
RN [8]
RP FUNCTION.
RX PubMed=32204458; DOI=10.3390/biom10030470;
RA Deshpande A., Vinayakamoorthy R.M., Garg B.K., Thummapudi J.P., Oza G.,
RA Adhikari K., Agarwal A., Dalvi P., Iyer S., Thulasi Raman S., Ramesh V.,
RA Rameshbabu A., Rezvaya A., Sukumaran S., Swaminathan S., Tilak B., Wang Z.,
RA Tran P.V., Loring R.H.;
RT "Why Does Knocking Out NACHO, But Not RIC3, Completely Block Expression of
RT alpha7 Nicotinic Receptors in Mouse Brain?";
RL Biomolecules 10:0-0(2020).
RN [9]
RP FUNCTION.
RX PubMed=32676916; DOI=10.1007/s00018-020-03592-x;
RA Mazzaferro S., Whiteman S.T., Alcaino C., Beyder A., Sine S.M.;
RT "NACHO and 14-3-3 promote expression of distinct subunit stoichiometries of
RT the alpha4beta2 acetylcholine receptor.";
RL Cell. Mol. Life Sci. 78:1565-1575(2021).
RN [10]
RP FUNCTION.
RX PubMed=32783947; DOI=10.1016/j.celrep.2020.108025;
RA Kweon H.J., Gu S., Witham E., Dhara M., Yu H., Mandon E.D., Jawhari A.,
RA Bredt D.S.;
RT "NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic
RT Receptor Assembly.";
RL Cell Rep. 32:108025-108025(2020).
CC -!- FUNCTION: Molecular chaperone which mediates the proper assembly and
CC functional expression of the nicotinic acetylcholine receptors (nAChRs)
CC throughout the brain (PubMed:26875622, PubMed:27789755,
CC PubMed:28445721, PubMed:32204458, PubMed:32783947). Essential for the
CC proper folding, assembly, function and surface trafficking of alpha-7
CC (CHRNA7), alpha-4-beta-2, alpha-3-beta-2 and alpha-3-beta-4 receptors
CC (PubMed:26875622, PubMed:27789755, PubMed:28445721, PubMed:32204458,
CC PubMed:32783947). Stably associates with ribophorin-1 (RPN1) and
CC ribophorin-2 (RPN2) (components of the oligosaccharyl transferase (OST)
CC complex) and with calnexin (CANX), both of which are critical for
CC NACHO-mediated effects on CHRNA7 assembly and function (By similarity).
CC Facilitates the proper folding and assembly of alpha-6-beta-2 and
CC alpha-6-beta-2-beta-3 receptors and acts at early stages of the nAChRs
CC subunit assembly (PubMed:28445721). Promotes the expression of the
CC alpha-4(2):beta-2(3) stoichiometric form over the alpha-4(3):beta-2(2)
CC form (PubMed:32676916). {ECO:0000250|UniProtKB:Q9D328,
CC ECO:0000269|PubMed:26875622, ECO:0000269|PubMed:27789755,
CC ECO:0000269|PubMed:28445721, ECO:0000269|PubMed:32204458,
CC ECO:0000269|PubMed:32676916, ECO:0000269|PubMed:32783947}.
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 -!- INTERACTION:
CC Q53FP2; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-11722971, EBI-10827839;
CC Q53FP2; O15155: BET1; NbExp=3; IntAct=EBI-11722971, EBI-749204;
CC Q53FP2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-11722971, EBI-11522780;
CC Q53FP2; Q5RI15: COX20; NbExp=3; IntAct=EBI-11722971, EBI-2834035;
CC Q53FP2; O43169: CYB5B; NbExp=3; IntAct=EBI-11722971, EBI-1058710;
CC Q53FP2; Q08426: EHHADH; NbExp=3; IntAct=EBI-11722971, EBI-2339219;
CC Q53FP2; Q96LL3: FIMP; NbExp=3; IntAct=EBI-11722971, EBI-12887376;
CC Q53FP2; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-11722971, EBI-713304;
CC Q53FP2; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-11722971, EBI-11991950;
CC Q53FP2; O14653: GOSR2; NbExp=3; IntAct=EBI-11722971, EBI-4401517;
CC Q53FP2; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-11722971, EBI-12133176;
CC Q53FP2; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-11722971, EBI-12866138;
CC Q53FP2; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-11722971, EBI-1054848;
CC Q53FP2; Q59EV6: PPGB; NbExp=3; IntAct=EBI-11722971, EBI-14210385;
CC Q53FP2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-11722971, EBI-10244780;
CC Q53FP2; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-11722971, EBI-8636004;
CC Q53FP2; P07204: THBD; NbExp=3; IntAct=EBI-11722971, EBI-941422;
CC Q53FP2; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-11722971, EBI-2821497;
CC Q53FP2; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-11722971, EBI-727322;
CC Q53FP2; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-11722971, EBI-2339195;
CC Q53FP2; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-11722971, EBI-11994282;
CC Q53FP2; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-11722971, EBI-347385;
CC Q53FP2; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-11722971, EBI-12195227;
CC Q53FP2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-11722971, EBI-12887458;
CC Q53FP2; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-11722971, EBI-12038591;
CC Q53FP2; P23763-3: VAMP1; NbExp=3; IntAct=EBI-11722971, EBI-12097582;
CC Q53FP2; Q15836: VAMP3; NbExp=3; IntAct=EBI-11722971, EBI-722343;
CC Q53FP2; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-11722971, EBI-1059156;
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; AK024146; BAB14840.1; -; mRNA.
DR EMBL; AK223240; BAD96960.1; -; mRNA.
DR EMBL; AL109952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050273; AAH50273.1; -; mRNA.
DR EMBL; BC078658; AAH78658.1; -; mRNA.
DR CCDS; CCDS14478.1; -.
DR RefSeq; NP_067650.1; NM_021637.2.
DR AlphaFoldDB; Q53FP2; -.
DR BioGRID; 121894; 34.
DR IntAct; Q53FP2; 31.
DR MINT; Q53FP2; -.
DR STRING; 9606.ENSP00000362021; -.
DR TCDB; 8.A.179.1.1; the novel acetylcholine receptor chaperone (nacho) family.
DR iPTMnet; Q53FP2; -.
DR PhosphoSitePlus; Q53FP2; -.
DR BioMuta; TMEM35A; -.
DR DMDM; 121957117; -.
DR EPD; Q53FP2; -.
DR jPOST; Q53FP2; -.
DR MassIVE; Q53FP2; -.
DR PaxDb; Q53FP2; -.
DR PeptideAtlas; Q53FP2; -.
DR PRIDE; Q53FP2; -.
DR ProteomicsDB; 62467; -.
DR TopDownProteomics; Q53FP2; -.
DR Antibodypedia; 28590; 32 antibodies from 15 providers.
DR DNASU; 59353; -.
DR Ensembl; ENST00000372930.5; ENSP00000362021.4; ENSG00000126950.8.
DR GeneID; 59353; -.
DR KEGG; hsa:59353; -.
DR MANE-Select; ENST00000372930.5; ENSP00000362021.4; NM_021637.3; NP_067650.1.
DR UCSC; uc004egw.4; human.
DR CTD; 59353; -.
DR GeneCards; TMEM35A; -.
DR HGNC; HGNC:25864; TMEM35A.
DR HPA; ENSG00000126950; Tissue enhanced (brain, seminal vesicle).
DR neXtProt; NX_Q53FP2; -.
DR OpenTargets; ENSG00000126950; -.
DR PharmGKB; PA134905238; -.
DR VEuPathDB; HostDB:ENSG00000126950; -.
DR eggNOG; ENOG502RXPR; Eukaryota.
DR GeneTree; ENSGT00940000154325; -.
DR HOGENOM; CLU_121618_0_0_1; -.
DR InParanoid; Q53FP2; -.
DR OMA; ICGIIMT; -.
DR OrthoDB; 1615454at2759; -.
DR PhylomeDB; Q53FP2; -.
DR TreeFam; TF300206; -.
DR PathwayCommons; Q53FP2; -.
DR SignaLink; Q53FP2; -.
DR BioGRID-ORCS; 59353; 9 hits in 694 CRISPR screens.
DR ChiTaRS; TMEM35A; human.
DR GenomeRNAi; 59353; -.
DR Pharos; Q53FP2; Tdark.
DR PRO; PR:Q53FP2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q53FP2; protein.
DR Bgee; ENSG00000126950; Expressed in cortical plate and 139 other tissues.
DR Genevisible; Q53FP2; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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; IDA:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:UniProtKB.
DR InterPro; IPR029693; TMEM35A.
DR InterPro; IPR040399; TMEM35A/B.
DR PANTHER; PTHR13163; PTHR13163; 1.
DR PANTHER; PTHR13163:SF0; PTHR13163:SF0; 1.
PE 1: Evidence at protein 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_0000271607"
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"
FT CONFLICT 50
FT /note="A -> T (in Ref. 2; BAD96960)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="N -> S (in Ref. 2; BAD96960)"
FT /evidence="ECO:0000305"
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
