SCN7A_HUMAN
ID SCN7A_HUMAN Reviewed; 1682 AA.
AC Q01118;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Sodium channel protein type 7 subunit alpha;
DE AltName: Full=Putative voltage-gated sodium channel subunit alpha Nax;
DE AltName: Full=Sodium channel protein cardiac and skeletal muscle subunit alpha;
DE AltName: Full=Sodium channel protein type VII subunit alpha;
GN Name=SCN7A; Synonyms=SCN6A;
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], TISSUE SPECIFICITY, AND VARIANTS ASN-41 AND
RP ILE-958.
RC TISSUE=Fetal skeletal muscle, and Heart;
RX PubMed=1317577; DOI=10.1073/pnas.89.11.4893;
RA George A.L. Jr., Knittle T.J., Tamkun M.M.;
RT "Molecular cloning of an atypical voltage-gated sodium channel expressed in
RT human heart and uterus: evidence for a distinct gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4893-4897(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC -!- TISSUE SPECIFICITY: Heart and uterus. {ECO:0000269|PubMed:1317577}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ.
CC This cysteine (position 656) is speculated in other sodium channel
CC subunits alpha to be implied in covalent binding with the sodium
CC channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family. SCN7A
CC subfamily. {ECO:0000305}.
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DR EMBL; M91556; AAA59899.1; -; mRNA.
DR EMBL; AC074101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46442.1; -.
DR PIR; A45380; A45380.
DR RefSeq; NP_002967.2; NM_002976.3.
DR RefSeq; XP_006712743.1; XM_006712680.2.
DR RefSeq; XP_006712744.1; XM_006712681.3.
DR RefSeq; XP_006712745.1; XM_006712682.3.
DR RefSeq; XP_011509917.1; XM_011511615.2.
DR RefSeq; XP_016860156.1; XM_017004667.1.
DR PDB; 7TJ8; EM; 3.20 A; A=1-1682.
DR PDB; 7TJ9; EM; 2.90 A; A=1-1682.
DR PDBsum; 7TJ8; -.
DR PDBsum; 7TJ9; -.
DR AlphaFoldDB; Q01118; -.
DR SMR; Q01118; -.
DR STRING; 9606.ENSP00000386796; -.
DR BindingDB; Q01118; -.
DR ChEMBL; CHEMBL3585; -.
DR DrugBank; DB09088; Amylocaine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB05541; Brivaracetam.
DR DrugBank; DB00564; Carbamazepine.
DR DrugBank; DB00907; Cocaine.
DR DrugBank; DB13269; Dichlorobenzyl alcohol.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB00776; Oxcarbazepine.
DR DrugBank; DB11186; Pentoxyverine.
DR DrugBank; DB09345; Pramocaine.
DR DrugBank; DB01069; Promethazine.
DR DrugBank; DB09342; Propoxycaine.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB09085; Tetracaine.
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB00313; Valproic acid.
DR DrugCentral; Q01118; -.
DR GlyConnect; 1753; 1 N-Linked glycan (1 site).
DR GlyGen; Q01118; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q01118; -.
DR PhosphoSitePlus; Q01118; -.
DR BioMuta; SCN7A; -.
DR DMDM; 296452902; -.
DR jPOST; Q01118; -.
DR MassIVE; Q01118; -.
DR PaxDb; Q01118; -.
DR PeptideAtlas; Q01118; -.
DR PRIDE; Q01118; -.
DR ProteomicsDB; 57921; -.
DR Antibodypedia; 1383; 138 antibodies from 24 providers.
DR DNASU; 6332; -.
DR Ensembl; ENST00000441411.2; ENSP00000403846.2; ENSG00000136546.17.
DR Ensembl; ENST00000643258.1; ENSP00000496114.1; ENSG00000136546.17.
DR GeneID; 6332; -.
DR KEGG; hsa:6332; -.
DR MANE-Select; ENST00000643258.1; ENSP00000496114.1; NM_002976.4; NP_002967.2.
DR UCSC; uc002udu.3; human.
DR CTD; 6332; -.
DR DisGeNET; 6332; -.
DR GeneCards; SCN7A; -.
DR HGNC; HGNC:10594; SCN7A.
DR HPA; ENSG00000136546; Tissue enhanced (ovary).
DR MIM; 182392; gene.
DR neXtProt; NX_Q01118; -.
DR OpenTargets; ENSG00000136546; -.
DR PharmGKB; PA35008; -.
DR VEuPathDB; HostDB:ENSG00000136546; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000162042; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; Q01118; -.
DR OMA; VFGMKLF; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; Q01118; -.
DR TreeFam; TF323985; -.
DR PathwayCommons; Q01118; -.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR SignaLink; Q01118; -.
DR BioGRID-ORCS; 6332; 8 hits in 1061 CRISPR screens.
DR ChiTaRS; SCN7A; human.
DR GeneWiki; SCN7A; -.
DR GenomeRNAi; 6332; -.
DR Pharos; Q01118; Tclin.
DR PRO; PR:Q01118; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q01118; protein.
DR Bgee; ENSG00000136546; Expressed in trigeminal ganglion and 158 other tissues.
DR ExpressionAtlas; Q01118; baseline and differential.
DR Genevisible; Q01118; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0055078; P:sodium ion homeostasis; IEA:Ensembl.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; TAS:ProtInc.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028812; Na_channel_a7su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF14; PTHR10037:SF14; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1682
FT /note="Sodium channel protein type 7 subunit alpha"
FT /id="PRO_0000048499"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..137
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 138..144
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 166..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..197
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 198..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..220
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 221..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..259
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 260..338
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 339..363
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 364..370
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 392..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 506..524
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 525..535
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 536..555
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 556..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 570..589
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 590..591
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 592..609
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 610..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 626..644
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 645..673
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 674..694
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 695..707
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 708..727
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 728..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 936..953
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 954..966
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 967..985
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 986..999
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1000..1018
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1019..1021
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1022..1040
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1041..1057
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1058..1077
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1078..1128
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1129..1150
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1151..1167
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1168..1189
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1190..1252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1253..1270
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1271..1281
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1282..1300
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1301..1312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1313..1330
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1331..1343
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1344..1360
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1361..1379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1380..1397
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1398..1419
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1420..1442
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1443..1472
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1473..1495
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1496..1682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 100..401
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 487..758
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 916..1224
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1233..1531
FT /note="IV"
FT /evidence="ECO:0000305"
FT REGION 801..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 442
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 777
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 869
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 905
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 267..316
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 696..705
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT VARIANT 41
FT /note="T -> N (in dbSNP:rs7565062)"
FT /evidence="ECO:0000269|PubMed:1317577"
FT /id="VAR_063120"
FT VARIANT 407
FT /note="I -> V (in dbSNP:rs11888208)"
FT /id="VAR_024410"
FT VARIANT 600
FT /note="M -> L (in dbSNP:rs34183637)"
FT /id="VAR_055641"
FT VARIANT 958
FT /note="M -> I (in dbSNP:rs6738031)"
FT /evidence="ECO:0000269|PubMed:1317577"
FT /id="VAR_063121"
FT VARIANT 1313
FT /note="A -> V (in dbSNP:rs6760593)"
FT /id="VAR_055642"
FT VARIANT 1516
FT /note="R -> K (in dbSNP:rs34799257)"
FT /id="VAR_055643"
FT VARIANT 1596
FT /note="V -> L (in dbSNP:rs3791251)"
FT /id="VAR_055644"
FT VARIANT 1657
FT /note="D -> G (in dbSNP:rs35344714)"
FT /id="VAR_055645"
FT CONFLICT 361
FT /note="Q -> L (in Ref. 1; AAA59899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1682 AA; 193493 MW; 38CD8D41975BCE18 CRC64;
MLASPEPKGL VPFTKESFEL IKQHIAKTHN EDHEEEDLKP TPDLEVGKKL PFIYGNLSQG
MVSEPLEDVD PYYYKKKNTF IVLNKNRTIF RFNAASILCT LSPFNCIRRT TIKVLVHPFF
QLFILISVLI DCVFMSLTNL PKWRPVLENT LLGIYTFEIL VKLFARGVWA GSFSFLGDPW
NWLDFSVTVF EVIIRYSPLD FIPTLQTART LRILKIIPLN QGLKSLVGVL IHCLKQLIGV
IILTLFFLSI FSLIGMGLFM GNLKHKCFRW PQENENETLH NRTGNPYYIR ETENFYYLEG
ERYALLCGNR TDAGQCPEGY VCVKAGINPD QGFTNFDSFG WALFALFRLM AQDYPEVLYH
QILYASGKVY MIFFVVVSFL FSFYMASLFL GILAMAYEEE KQRVGEISKK IEPKFQQTGK
ELQEGNETDE AKTIQIEMKK RSPISTDTSL DVLEDATLRH KEELEKSKKI CPLYWYKFAK
TFLIWNCSPC WLKLKEFVHR IIMAPFTDLF LIICIILNVC FLTLEHYPMS KQTNTLLNIG
NLVFIGIFTA EMIFKIIAMH PYGYFQVGWN IFDSMIVFHG LIELCLANVA GMALLRLFRM
LRIFKLGKYW PTFQILMWSL SNSWVALKDL VLLLFTFIFF SAAFGMKLFG KNYEEFVCHI
DKDCQLPRWH MHDFFHSFLN VFRILCGEWV ETLWDCMEVA GQSWCIPFYL MVILIGNLLV
LYLFLALVSS FSSCKDVTAE ENNEAKNLQL AVARIKKGIN YVLLKILCKT QNVPKDTMDH
VNEVYVKEDI SDHTLSELSN TQDFLKDKEK SSGTEKNATE NESQSLIPSP SVSETVPIAS
GESDIENLDN KEIQSKSGDG GSKEKIKQSS SSECSTVDIA ISEEEEMFYG GERSKHLKNG
CRRGSSLGQI SGASKKGKIW QNIRKTCCKI VENNWFKCFI GLVTLLSTGT LAFEDIYMDQ
RKTIKILLEY ADMIFTYIFI LEMLLKWMAY GFKAYFSNGW YRLDFVVVIV FCLSLIGKTR
EELKPLISMK FLRPLRVLSQ FERMKVVVRA LIKTTLPTLN VFLVCLMIWL IFSIMGVDLF
AGRFYECIDP TSGERFPSSE VMNKSRCESL LFNESMLWEN AKMNFDNVGN GFLSLLQVAT
FNGWITIMNS AIDSVAVNIQ PHFEVNIYMY CYFINFIIFG VFLPLSMLIT VIIDNFNKHK
IKLGGSNIFI TVKQRKQYRR LKKLMYEDSQ RPVPRPLNKL QGFIFDVVTS QAFNVIVMVL
ICFQAIAMMI DTDVQSLQMS IALYWINSIF VMLYTMECIL KLIAFRCFYF TIAWNIFDFM
VVIFSITGLC LPMTVGSYLV PPSLVQLILL SRIIHMLRLG KGPKVFHNLM LPLMLSLPAL
LNIILLIFLV MFIYAVFGMY NFAYVKKEAG INDVSNFETF GNSMLCLFQV AIFAGWDGML
DAIFNSKWSD CDPDKINPGT QVRGDCGNPS VGIFYFVSYI LISWLIIVNM YIVVVMEFLN
IASKKKNKTL SEDDFRKFFQ VWKRFDPDRT QYIDSSKLSD FAAALDPPLF MAKPNKGQLI
ALDLPMAVGD RIHCLDILLA FTKRVMGQDV RMEKVVSEIE SGFLLANPFK ITCEPITTTL
KRKQEAVSAT IIQRAYKNYR LRRNDKNTSD IHMIDGDRDV HATKEGAYFD KAKEKSPIQS
QI
