ASIC3_HUMAN
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 03-AUG-2022, entry version 165.
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-kinase-
RT 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 (TC
CC 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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; Q9UHC3; -.
DR PeptideAtlas; Q9UHC3; -.
DR PRIDE; Q9UHC3; -.
DR ProteomicsDB; 84310; -. [Q9UHC3-4]
DR Antibodypedia; 18677; 180 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 CTD; 9311; -.
DR DisGeNET; 9311; -.
DR GeneCards; ASIC3; -.
DR HGNC; HGNC:101; ASIC3.
DR HPA; ENSG00000213199; Tissue enhanced (testis).
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; SDICVFA; -.
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 1076 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 106 other tissues.
DR ExpressionAtlas; Q9UHC3; baseline and differential.
DR Genevisible; Q9UHC3; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0005261; F:cation channel activity; TAS:ProtInc.
DR GO; GO:0042931; F:enterobactin transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IBA:GO_Central.
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:0051649; P:establishment of localization in cell; 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 InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
DR PROSITE; PS01206; ASC; 1.
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
