ID   ASIC3_HUMAN             Reviewed;         531 AA.
AC   Q9UHC3; B2R9V0; O60263; O75906; Q59FN9; Q9UER8; Q9UHC4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Acid-sensing ion channel 3;
DE            Short=ASIC3;
DE            Short=hASIC3;
DE   AltName: Full=Amiloride-sensitive cation channel 3;
DE   AltName: Full=Neuronal amiloride-sensitive cation channel 3;
DE   AltName: Full=Testis sodium channel 1;
DE            Short=hTNaC1;
GN   Name=ASIC3; Synonyms=ACCN3, SLNAC1, TNAC1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=9571199; DOI=10.1006/bbrc.1998.8483;
RA   Ishibashi K., Marumo F.;
RT   "Molecular cloning of a DEG/ENaC sodium channel cDNA from human testis.";
RL   Biochem. Biophys. Res. Commun. 245:589-593(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC   TISSUE=Embryo;
RX   PubMed=9744806; DOI=10.1016/s0014-5793(98)00916-8;
RA   de Weille J.R., Bassilana F., Lazdunski M., Waldmann R.;
RT   "Identification, functional expression and chromosomal localisation of a
RT   sustained human proton-gated cation channel.";
RL   FEBS Lett. 433:257-260(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND FUNCTION.
RC   TISSUE=Fetal brain;
RX   PubMed=9886053; DOI=10.1046/j.1471-4159.1999.0720051.x;
RA   Babinski K., Le K.-T., Seguela P.;
RT   "Molecular cloning and regional distribution of a human proton receptor
RT   subunit with biphasic functional properties.";
RL   J. Neurochem. 72:51-57(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA   Renard S., Besnard F., Partiseti M., Graham D.;
RT   "ASIC3b and ASIC3c, new modulatory subunits of the acid sensing ion channel
RT   family.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   INTERACTION WITH ASIC1.
RX   PubMed=10842183; DOI=10.1074/jbc.m004114200;
RA   Babinski K., Catarsi S., Biagini G., Seguela P.;
RT   "Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric proton-
RT   gated channels sensitive to Gd3+.";
RL   J. Biol. Chem. 275:28519-28525(2000).
RN   [9]
RP   REGULATION BY NPFF.
RX   PubMed=11587714; DOI=10.1016/s0028-3908(01)00107-1;
RA   Catarsi S., Babinski K., Seguela P.;
RT   "Selective modulation of heteromeric ASIC proton-gated channels by
RT   neuropeptide FF.";
RL   Neuropharmacology 41:592-600(2001).
RN   [10]
RP   PHOSPHORYLATION BY PKA.
RX   PubMed=12578970; DOI=10.1073/pnas.252782799;
RA   Leonard A.S., Yermolaieva O., Hruska-Hageman A., Askwith C.C., Price M.P.,
RA   Wemmie J.A., Welsh M.J.;
RT   "cAMP-dependent protein kinase phosphorylation of the acid-sensing ion
RT   channel-1 regulates its binding to the protein interacting with C-
RT   kinase-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2029-2034(2003).
RN   [11]
RP   INTERACTION WITH LIN7B; MAGI1 AND GOPC, AND MUTAGENESIS OF VAL-528;
RP   THR-529; GLN-530 AND LEU-531.
RX   PubMed=15317815; DOI=10.1074/jbc.m405874200;
RA   Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.;
RT   "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
RT   opposite effects on H+- gated current.";
RL   J. Biol. Chem. 279:46962-46968(2004).
CC   -!- FUNCTION: Cation channel with high affinity for sodium, which is gated
CC       by extracellular protons and inhibited by the diuretic amiloride.
CC       Generates a biphasic current with a fast inactivating and a slow
CC       sustained phase. In sensory neurons is proposed to mediate the pain
CC       induced by acidosis that occurs in ischemic, damaged or inflamed
CC       tissue. May be involved in hyperalgesia. May play a role in
CC       mechanoreception. Heteromeric channel assembly seems to modulate
CC       channel properties. {ECO:0000269|PubMed:9744806,
CC       ECO:0000269|PubMed:9886053}.
CC   -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
CC       similarity). Interacts with STOM; this regulates channel activity.
CC       Interacts with DLG4 (By similarity). Interacts with LIN7B,
CC       MAGI1/BAIAP1, GOPC and ASIC2. {ECO:0000250,
CC       ECO:0000269|PubMed:10842183, ECO:0000269|PubMed:15317815}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Cell surface
CC       expression may be stabilized by interaction with LIN7B and cytoplasmic
CC       retention by interaction with DLG4. In part cytoplasmic in cochlea
CC       cells (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9UHC3-1; Sequence=Displayed;
CC       Name=2; Synonyms=ASIC3b;
CC         IsoId=Q9UHC3-2; Sequence=VSP_015602;
CC       Name=3; Synonyms=ASIC3c;
CC         IsoId=Q9UHC3-3; Sequence=VSP_015603;
CC       Name=4; Synonyms=c;
CC         IsoId=Q9UHC3-4; Sequence=VSP_015600, VSP_015601;
CC   -!- TISSUE SPECIFICITY: Expressed by sensory neurons. Strongly expressed in
CC       brain, spinal chord, lung, lymph nodes, kidney, pituitary, heart and
CC       testis. {ECO:0000269|PubMed:9571199, ECO:0000269|PubMed:9886053}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues, expression increases
CC       in lung and kidney adult tissues. {ECO:0000269|PubMed:9886053}.
CC   -!- DOMAIN: The PDZ domain-binding motif is involved in interaction with
CC       LIN7A, GOPC and MAGI1.
CC   -!- PTM: Phosphorylated by PKA. Phosphorylated by PKC. In vitro,
CC       PRKCABP/PICK-1 is necessary for PKC phosphorylation and activation of a
CC       ASIC3/ACCN3-ASIC2/ASIC2b channel, but does not activate a homomeric
CC       ASIC3 channel (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Potentiated by FMRFamide-related neuropeptides.
CC       Sensitized and potentiated by NPSF. Regulated by lactate and Ca(2+).
CC       Inhibited by anti-inflammatory drugs, like salicylic acid (By
CC       similarity). Sensitized and potentiated by NPFF. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel
CC       (TC 1.A.6) family. ASIC3 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25897.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAD92658.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB010575; BAA25897.1; ALT_FRAME; mRNA.
DR   EMBL; AF095897; AAC64188.1; -; mRNA.
DR   EMBL; AF057711; AAC62935.1; -; mRNA.
DR   EMBL; AF195024; AAF19817.1; -; mRNA.
DR   EMBL; AF195025; AAF19818.1; -; mRNA.
DR   EMBL; AK313926; BAG36647.1; -; mRNA.
DR   EMBL; AB209421; BAD92658.1; ALT_INIT; mRNA.
DR   EMBL; CH471173; EAW54052.1; -; Genomic_DNA.
DR   CCDS; CCDS5914.1; -. [Q9UHC3-2]
DR   CCDS; CCDS5915.1; -. [Q9UHC3-3]
DR   CCDS; CCDS5916.1; -. [Q9UHC3-1]
DR   PIR; JE0091; JE0091.
DR   RefSeq; NP_004760.1; NM_004769.3. [Q9UHC3-1]
DR   RefSeq; NP_064717.1; NM_020321.3. [Q9UHC3-3]
DR   RefSeq; NP_064718.1; NM_020322.3. [Q9UHC3-2]
DR   AlphaFoldDB; Q9UHC3; -.
DR   SMR; Q9UHC3; -.
DR   BioGRID; 114723; 7.
DR   STRING; 9606.ENSP00000297512; -.
DR   BindingDB; Q9UHC3; -.
DR   ChEMBL; CHEMBL5368; -.
DR   DrugBank; DB08838; Agmatine.
DR   DrugCentral; Q9UHC3; -.
DR   GuidetoPHARMACOLOGY; 686; -.
DR   GlyCosmos; Q9UHC3; 2 sites, No reported glycans.
DR   GlyGen; Q9UHC3; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UHC3; -.
DR   PhosphoSitePlus; Q9UHC3; -.
DR   BioMuta; ASIC3; -.
DR   DMDM; 82582992; -.
DR   MassIVE; Q9UHC3; -.
DR   PaxDb; 9606-ENSP00000297512; -.
DR   PeptideAtlas; Q9UHC3; -.
DR   ProteomicsDB; 84310; -. [Q9UHC3-4]
DR   Antibodypedia; 18677; 218 antibodies from 28 providers.
DR   DNASU; 9311; -.
DR   Ensembl; ENST00000297512.12; ENSP00000297512.8; ENSG00000213199.8. [Q9UHC3-3]
DR   Ensembl; ENST00000349064.10; ENSP00000344838.5; ENSG00000213199.8. [Q9UHC3-1]
DR   Ensembl; ENST00000357922.8; ENSP00000350600.4; ENSG00000213199.8. [Q9UHC3-2]
DR   Ensembl; ENST00000377904.8; ENSP00000367136.4; ENSG00000213199.8. [Q9UHC3-4]
DR   Ensembl; ENST00000468325.5; ENSP00000418605.1; ENSG00000213199.8. [Q9UHC3-4]
DR   GeneID; 9311; -.
DR   KEGG; hsa:9311; -.
DR   MANE-Select; ENST00000349064.10; ENSP00000344838.5; NM_004769.4; NP_004760.1.
DR   UCSC; uc003win.4; human. [Q9UHC3-1]
DR   AGR; HGNC:101; -.
DR   CTD; 9311; -.
DR   DisGeNET; 9311; -.
DR   GeneCards; ASIC3; -.
DR   HGNC; HGNC:101; ASIC3.
DR   HPA; ENSG00000213199; Tissue enhanced (brain).
DR   MIM; 611741; gene.
DR   neXtProt; NX_Q9UHC3; -.
DR   OpenTargets; ENSG00000213199; -.
DR   PharmGKB; PA24435; -.
DR   VEuPathDB; HostDB:ENSG00000213199; -.
DR   eggNOG; KOG4294; Eukaryota.
DR   GeneTree; ENSGT00940000162081; -.
DR   HOGENOM; CLU_020415_1_3_1; -.
DR   InParanoid; Q9UHC3; -.
DR   OMA; GQFHHVT; -.
DR   OrthoDB; 3415680at2759; -.
DR   PhylomeDB; Q9UHC3; -.
DR   TreeFam; TF330663; -.
DR   PathwayCommons; Q9UHC3; -.
DR   Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR   SignaLink; Q9UHC3; -.
DR   BioGRID-ORCS; 9311; 10 hits in 1156 CRISPR screens.
DR   ChiTaRS; ASIC3; human.
DR   GeneWiki; ACCN3; -.
DR   GenomeRNAi; 9311; -.
DR   Pharos; Q9UHC3; Tchem.
DR   PRO; PR:Q9UHC3; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9UHC3; Protein.
DR   Bgee; ENSG00000213199; Expressed in right hemisphere of cerebellum and 108 other cell types or tissues.
DR   ExpressionAtlas; Q9UHC3; baseline and differential.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0044736; F:acid-sensing ion channel activity; IBA:GO_Central.
DR   GO; GO:0042931; F:enterobactin transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0015280; F:ligand-gated sodium channel activity; IEA:Ensembl.
DR   GO; GO:0005261; F:monoatomic cation channel activity; TAS:ProtInc.
DR   GO; GO:0005272; F:sodium channel activity; TAS:ProtInc.
DR   GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0007600; P:sensory perception; TAS:ProtInc.
DR   GO; GO:0050915; P:sensory perception of sour taste; IMP:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.3590.10; acid-sensing ion channel 1 domain; 2.
DR   Gene3D; 1.10.287.820; Acid-sensing ion channel domain; 1.
DR   Gene3D; 1.10.287.770; YojJ-like; 1.
DR   InterPro; IPR001873; ENaC.
DR   InterPro; IPR004724; ENaC_chordates.
DR   InterPro; IPR020903; ENaC_CS.
DR   NCBIfam; TIGR00859; ENaC; 1.
DR   PANTHER; PTHR11690:SF228; ACID-SENSING ION CHANNEL 3; 1.
DR   PANTHER; PTHR11690; AMILORIDE-SENSITIVE SODIUM CHANNEL-RELATED; 1.
DR   Pfam; PF00858; ASC; 1.
DR   PRINTS; PR01078; AMINACHANNEL.
DR   PROSITE; PS01206; ASC; 1.
DR   Genevisible; Q9UHC3; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..531
FT                   /note="Acid-sensing ion channel 3"
FT                   /id="PRO_0000181301"
FT   TOPO_DOM        1..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..441
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        461..531
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          285..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           528..531
FT                   /note="PDZ-binding"
FT   SITE            26
FT                   /note="Potassium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        92..186
FT                   /evidence="ECO:0000250"
FT   DISULFID        164..171
FT                   /evidence="ECO:0000250"
FT   DISULFID        282..370
FT                   /evidence="ECO:0000250"
FT   DISULFID        315..366
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..364
FT                   /evidence="ECO:0000250"
FT   DISULFID        328..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        330..342
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         356..407
FT                   /note="DAMLRKDSCACPNPCASTRYAKELSMVRIPSRAAARFLARKLNRSEAYIAEN
FT                   -> GRTCWPWTSSLRPSTMRPWSRRRPMRCQSCLVTLGARWGCSSGPACSPSSRS (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|Ref.6"
FT                   /id="VSP_015600"
FT   VAR_SEQ         408..531
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.6"
FT                   /id="VSP_015601"
FT   VAR_SEQ         487..531
FT                   /note="LQEGLGSHRTQVPHLSLGPRPPTPPCAVTKTLSASHRTCYLVTQL -> TSH
FT                   PSLCRHQDSLRLPPHLLPCHTALDLLSVSSEPRPDILDMPSLHVAFPSSPQIKS (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT                   /id="VSP_015602"
FT   VAR_SEQ         506..531
FT                   /note="RPPTPPCAVTKTLSASHRTCYLVTQL -> STLLCSEDLPPLPVPSPRLSPP
FT                   PTAPATLSHSSRPAVCVLGAPP (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_015603"
FT   VARIANT         228
FT                   /note="N -> S (in dbSNP:rs1864545)"
FT                   /id="VAR_052037"
FT   MUTAGEN         528
FT                   /note="V->A: No effect on interaction with LIN7B, MAGI1 and
FT                   GOPC."
FT                   /evidence="ECO:0000269|PubMed:15317815"
FT   MUTAGEN         529
FT                   /note="T->A: Loss of interaction with LIN7B, MAGI1."
FT                   /evidence="ECO:0000269|PubMed:15317815"
FT   MUTAGEN         530
FT                   /note="Q->A: Loss of interaction with GOPC. No effect on
FT                   interaction LIN7B and MAGI1."
FT                   /evidence="ECO:0000269|PubMed:15317815"
FT   MUTAGEN         531
FT                   /note="L->A: Loss of interaction with LIN7B, MAGI1 and
FT                   GOPC."
FT                   /evidence="ECO:0000269|PubMed:15317815"
FT   CONFLICT        13
FT                   /note="P -> Q (in Ref. 1; BAA25897 and 3; AAC62935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="A -> P (in Ref. 3; AAC62935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="I -> V (in Ref. 3; AAC62935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243..244
FT                   /note="SQ -> GH (in Ref. 1; BAA25897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="M -> I (in Ref. 3; AAC62935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        397
FT                   /note="L -> F (in Ref. 1; BAA25897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="S -> R (in Ref. 1; BAA25897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        518
FT                   /note="L -> F (in Ref. 1; BAA25897)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   531 AA;  58905 MW;  A46DD64590EC4871 CRC64;
     MKPTSGPEEA RRPASDIRVF ASNCSMHGLG HVFGPGSLSL RRGMWAAAVV LSVATFLYQV
     AERVRYYREF HHQTALDERE SHRLIFPAVT LCNINPLRRS RLTPNDLHWA GSALLGLDPA
     EHAAFLRALG RPPAPPGFMP SPTFDMAQLY ARAGHSLDDM LLDCRFRGQP CGPENFTTIF
     TRMGKCYTFN SGADGAELLT TTRGGMGNGL DIMLDVQQEE YLPVWRDNEE TPFEVGIRVQ
     IHSQEEPPII DQLGLGVSPG YQTFVSCQQQ QLSFLPPPWG DCSSASLNPN YEPEPSDPLG
     SPSPSPSPPY TLMGCRLACE TRYVARKCGC RMVYMPGDVP VCSPQQYKNC AHPAIDAMLR
     KDSCACPNPC ASTRYAKELS MVRIPSRAAA RFLARKLNRS EAYIAENVLA LDIFFEALNY
     ETVEQKKAYE MSELLGDIGG QMGLFIGASL LTILEILDYL CEVFRDKVLG YFWNRQHSQR
     HSSTNLLQEG LGSHRTQVPH LSLGPRPPTP PCAVTKTLSA SHRTCYLVTQ L
//