KCNJ1_HUMAN
ID KCNJ1_HUMAN Reviewed; 391 AA.
AC P48048; B2RMR4; Q6LD67;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 1;
DE AltName: Full=ATP-regulated potassium channel ROM-K;
DE AltName: Full=Inward rectifier K(+) channel Kir1.1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 1;
GN Name=KCNJ1; Synonyms=ROMK1;
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], FUNCTION, AND ALTERNATIVE SPLICING.
RC TISSUE=Kidney;
RX PubMed=7929082; DOI=10.1016/s0021-9258(19)51076-6;
RA Shuck M.E., Bock J.H., Benjamin C.W., Tsai T.-D., Lee K.S., Slightom J.L.,
RA Bienkowski M.J.;
RT "Cloning and characterization of multiple forms of the human kidney ROM-K
RT potassium channel.";
RL J. Biol. Chem. 269:24261-24270(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Kidney;
RX PubMed=8190102;
RA Yano H., Philipson L.H., Kugler J.L., Tokuyama Y., Davis E.M.,
RA le Beau M.M., Nelson D.J., Bell G.I., Takeda J.;
RT "Alternative splicing of human inwardly rectifying K+ channel ROMK1 mRNA.";
RL Mol. Pharmacol. 45:854-860(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=9099852; DOI=10.1016/s0378-1119(96)00759-7;
RA Bock J.H., Shuck M.E., Benjamin C.W., Chee M., Bienkowski M.J.,
RA Slightom J.L.;
RT "Nucleotide sequence analysis of the human KCNJ1 potassium channel locus.";
RL Gene 188:9-16(1997).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-177, AND TISSUE SPECIFICITY.
RC TISSUE=Brain cortex;
RX PubMed=7635463; DOI=10.1007/bf00207372;
RA Krishnan S.N., Desai T., Ward D.C., Haddad G.G.;
RT "Isolation and chromosomal localization of a human ATP-regulated potassium
RT channel.";
RL Hum. Genet. 96:155-160(1995).
RN [7]
RP GLYCOSYLATION AT ASN-117.
RX PubMed=10889209; DOI=10.1074/jbc.m005338200;
RA Pabon A., Chan K.W., Sui J.L., Wu X., Logothetis D.E., Thornhill W.B.;
RT "Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different
RT consequences in potassium channel function.";
RL J. Biol. Chem. 275:30677-30682(2000).
RN [8]
RP INTERACTION WITH SGK1 AND SLC9A3R2/NHERF2.
RX PubMed=14623317; DOI=10.1016/j.bbrc.2003.10.037;
RA Palmada M., Embark H.M., Yun C., Bohmer C., Lang F.;
RT "Molecular requirements for the regulation of the renal outer medullary
RT K(+) channel ROMK1 by the serum- and glucocorticoid-inducible kinase
RT SGK1.";
RL Biochem. Biophys. Res. Commun. 311:629-634(2003).
RN [9]
RP PHOSPHORYLATION AT SER-44 BY SGK1, AND SUBCELLULAR LOCATION.
RX PubMed=12684516; DOI=10.1074/jbc.m212301200;
RA Yoo D., Kim B.Y., Campo C., Nance L., King A., Maouyo D., Welling P.A.;
RT "Cell surface expression of the ROMK (Kir 1.1) channel is regulated by the
RT aldosterone-induced kinase, SGK-1, and protein kinase A.";
RL J. Biol. Chem. 278:23066-23075(2003).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=16357011; DOI=10.1113/jphysiol.2005.102202;
RA Leng Q., Kahle K.T., Rinehart J., MacGregor G.G., Wilson F.H.,
RA Canessa C.M., Lifton R.P., Hebert S.C.;
RT "WNK3, a kinase related to genes mutated in hereditary hypertension with
RT hyperkalaemia, regulates the K+ channel ROMK1 (Kir1.1).";
RL J. Physiol. (Lond.) 571:275-286(2006).
RN [11]
RP VARIANTS BARTS2 VAL-214; ARG-219 AND THR-357.
RX PubMed=8841184; DOI=10.1038/ng1096-152;
RA Simon D.B., Karet F.E., Rodriguez-Soriano J., Hamdan J.H., DiPietro A.,
RA Trachtman H., Sanjad S.A., Lifton R.P.;
RT "Genetic heterogeneity of Bartter's syndrome revealed by mutations in the
RT K+ channel, ROMK.";
RL Nat. Genet. 14:152-156(1996).
RN [12]
RP VARIANTS BARTS2 GLU-72; TYR-74; CYS-99; HIS-108; LEU-110; GLU-122; GLU-167;
RP THR-198 AND GLY-315.
RX PubMed=9002665; DOI=10.1093/hmg/6.1.17;
RA Karolyi L., Konrad M., Koeckerling A., Ziegler A., Zimmermann D.K.,
RA Roth B., Wieg C., Grzeschik K.-H., Koch M.C., Seyberth H.W., Vargas R.,
RA Forestier L., Jean G., Deschaux M., Rizzoni G.F., Niaudet P., Antignac C.,
RA Feldmann D., Lorridon F., Cougoureux E., Laroze F., Alessandri J.-L.,
RA David L., Saunier P., Deschenes G., Hildebrandt F., Vollmer M.,
RA Proesmans W., Brandis M., van den Heuvel L.P.W.J., Lemmink H.H.,
RA Nillesen W., Monnens L.A.H., Knoers N.V.A.M., Guay-Woodford L.M.,
RA Wright C.J., Madrigal G., Hebert S.C.;
RT "Mutations in the gene encoding the inwardly-rectifying renal potassium
RT channel, ROMK, cause the antenatal variant of Bartter syndrome: evidence
RT for genetic heterogeneity.";
RL Hum. Mol. Genet. 6:17-26(1997).
RN [13]
RP VARIANT BARTS2 LYS-124.
RX PubMed=9727001; DOI=10.1074/jbc.273.37.23884;
RA Derst C., Wischmeyer E., Preisig-Mueller R., Spauschus A., Konrad M.,
RA Hensen P., Jeck N., Seyberth H.W., Daut J., Karschin A.;
RT "A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary
RT potassium) channels reveals a crucial residue for channel function in
RT Kir1.3 channels.";
RL J. Biol. Chem. 273:23884-23891(1998).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-115.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: In the kidney, probably plays a major role in potassium
CC homeostasis. Inward rectifier potassium channels are characterized by a
CC greater tendency to allow potassium to flow into the cell rather than
CC out of it. Their voltage dependence is regulated by the concentration
CC of extracellular potassium; as external potassium is raised, the
CC voltage range of the channel opening shifts to more positive voltages.
CC The inward rectification is mainly due to the blockage of outward
CC current by internal magnesium. This channel is activated by internal
CC ATP and can be blocked by external barium.
CC {ECO:0000269|PubMed:7929082}.
CC -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000269|PubMed:16357011}.
CC -!- SUBUNIT: Interacts with SGK1 and SLC9A3R2/NHERF2.
CC {ECO:0000269|PubMed:14623317}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12684516};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12684516}.
CC Note=Phosphorylation at Ser-44 by SGK1 is necessary for its expression
CC at the cell membrane. {ECO:0000269|PubMed:12684516}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ROM-K1;
CC IsoId=P48048-1; Sequence=Displayed;
CC Name=2; Synonyms=2-4-5, ROM-K2, ROM-K4, ROM-K5, ROM-K6;
CC IsoId=P48048-2; Sequence=VSP_002797;
CC Name=3; Synonyms=ROM-K3;
CC IsoId=P48048-3; Sequence=VSP_002798;
CC -!- TISSUE SPECIFICITY: In the kidney and pancreatic islets. Lower levels
CC in skeletal muscle, pancreas, spleen, brain, heart and liver.
CC {ECO:0000269|PubMed:7635463}.
CC -!- PTM: Phosphorylation at Ser-44 by SGK1 is necessary for its expression
CC at the cell membrane. {ECO:0000269|PubMed:12684516}.
CC -!- DISEASE: Bartter syndrome 2, antenatal (BARTS2) [MIM:241200]: A form of
CC Bartter syndrome, an autosomal recessive disorder characterized by
CC impaired salt reabsorption in the thick ascending loop of Henle with
CC pronounced salt wasting, hypokalemic metabolic alkalosis, and varying
CC degrees of hypercalciuria. BARTS2 is a life-threatening condition
CC beginning in utero, with marked fetal polyuria that leads to
CC polyhydramnios and premature delivery. Another hallmark is a marked
CC hypercalciuria and, as a secondary consequence, the development of
CC nephrocalcinosis and osteopenia. {ECO:0000269|PubMed:8841184,
CC ECO:0000269|PubMed:9002665, ECO:0000269|PubMed:9727001}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ1 subfamily. {ECO:0000305}.
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DR EMBL; U12541; AAA61712.1; -; mRNA.
DR EMBL; U12542; AAA61713.1; -; mRNA.
DR EMBL; U12543; AAA61714.1; -; mRNA.
DR EMBL; U12544; AAA61715.1; -; mRNA.
DR EMBL; U12545; AAA61716.1; -; mRNA.
DR EMBL; U03884; AAA20594.1; -; mRNA.
DR EMBL; U65406; AAC51220.1; -; Genomic_DNA.
DR EMBL; U65406; AAC51221.1; -; Genomic_DNA.
DR EMBL; U65406; AAC51222.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67724.1; -; Genomic_DNA.
DR EMBL; BC074752; AAH74752.1; -; mRNA.
DR EMBL; BC136360; AAI36361.1; -; mRNA.
DR EMBL; BC136361; AAI36362.1; -; mRNA.
DR EMBL; S78737; AAB35012.1; -; mRNA.
DR CCDS; CCDS8476.1; -. [P48048-1]
DR CCDS; CCDS8477.1; -. [P48048-2]
DR PIR; A55119; A55119.
DR RefSeq; NP_000211.1; NM_000220.4. [P48048-1]
DR RefSeq; NP_722448.1; NM_153764.2. [P48048-2]
DR RefSeq; NP_722449.3; NM_153765.2. [P48048-3]
DR RefSeq; NP_722450.1; NM_153766.2. [P48048-2]
DR RefSeq; NP_722451.1; NM_153767.3. [P48048-2]
DR AlphaFoldDB; P48048; -.
DR SMR; P48048; -.
DR BioGRID; 109960; 4.
DR ELM; P48048; -.
DR STRING; 9606.ENSP00000376432; -.
DR BindingDB; P48048; -.
DR ChEMBL; CHEMBL1293292; -.
DR DrugBank; DB00414; Acetohexamide.
DR DrugBank; DB08838; Agmatine.
DR DrugBank; DB00217; Bethanidine.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB00222; Glimepiride.
DR DrugBank; DB01382; Glymidine.
DR DrugBank; DB00350; Minoxidil.
DR DrugBank; DB01124; Tolbutamide.
DR DrugBank; DB01392; Yohimbine.
DR DrugCentral; P48048; -.
DR GuidetoPHARMACOLOGY; 429; -.
DR TCDB; 1.A.2.1.1; the inward rectifier k(+) channel (irk-c) family.
DR CarbonylDB; P48048; -.
DR GlyGen; P48048; 1 site.
DR iPTMnet; P48048; -.
DR PhosphoSitePlus; P48048; -.
DR BioMuta; KCNJ1; -.
DR DMDM; 1352479; -.
DR MassIVE; P48048; -.
DR PaxDb; P48048; -.
DR PeptideAtlas; P48048; -.
DR PRIDE; P48048; -.
DR ProteomicsDB; 55838; -. [P48048-1]
DR ProteomicsDB; 55839; -. [P48048-2]
DR ProteomicsDB; 55840; -. [P48048-3]
DR Antibodypedia; 33020; 289 antibodies from 31 providers.
DR DNASU; 3758; -.
DR Ensembl; ENST00000324036.7; ENSP00000316233.3; ENSG00000151704.16. [P48048-2]
DR Ensembl; ENST00000392664.2; ENSP00000376432.2; ENSG00000151704.16. [P48048-1]
DR Ensembl; ENST00000392665.6; ENSP00000376433.2; ENSG00000151704.16. [P48048-2]
DR Ensembl; ENST00000392666.6; ENSP00000376434.1; ENSG00000151704.16. [P48048-2]
DR Ensembl; ENST00000440599.6; ENSP00000406320.2; ENSG00000151704.16. [P48048-2]
DR GeneID; 3758; -.
DR KEGG; hsa:3758; -.
DR MANE-Select; ENST00000392666.6; ENSP00000376434.1; NM_153766.3; NP_722450.1. [P48048-2]
DR UCSC; uc001qeo.3; human. [P48048-1]
DR CTD; 3758; -.
DR DisGeNET; 3758; -.
DR GeneCards; KCNJ1; -.
DR HGNC; HGNC:6255; KCNJ1.
DR HPA; ENSG00000151704; Tissue enriched (kidney).
DR MalaCards; KCNJ1; -.
DR MIM; 241200; phenotype.
DR MIM; 600359; gene.
DR neXtProt; NX_P48048; -.
DR OpenTargets; ENSG00000151704; -.
DR Orphanet; 620220; Bartter syndrome type 2.
DR PharmGKB; PA213; -.
DR VEuPathDB; HostDB:ENSG00000151704; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_3_0_1; -.
DR InParanoid; P48048; -.
DR PhylomeDB; P48048; -.
DR TreeFam; TF313676; -.
DR PathwayCommons; P48048; -.
DR Reactome; R-HSA-1296067; Potassium transport channels.
DR SignaLink; P48048; -.
DR SIGNOR; P48048; -.
DR BioGRID-ORCS; 3758; 10 hits in 1075 CRISPR screens.
DR GeneWiki; ROMK; -.
DR GenomeRNAi; 3758; -.
DR Pharos; P48048; Tchem.
DR PRO; PR:P48048; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P48048; protein.
DR Bgee; ENSG00000151704; Expressed in renal medulla and 93 other tissues.
DR ExpressionAtlas; P48048; baseline and differential.
DR Genevisible; P48048; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:ARUK-UCL.
DR GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 2.60.40.1400; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR041647; IRK_C.
DR InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR InterPro; IPR003268; K_chnl_inward-rec_Kir1.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF6; PTHR11767:SF6; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Bartter syndrome; Cell membrane;
KW Disease variant; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..391
FT /note="ATP-sensitive inward rectifier potassium channel 1"
FT /id="PRO_0000154917"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 78..102
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 103..127
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT INTRAMEM 128..139
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 140..146
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 147..155
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 156..177
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 178..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT MOTIF 141..146
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 171
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000269|PubMed:12684516"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10889209"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002797"
FT VAR_SEQ 1..12
FT /note="MNASSRNVFDTL -> MPTVYLCSEQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002798"
FT VARIANT 6
FT /note="R -> W (in dbSNP:rs34191956)"
FT /id="VAR_049668"
FT VARIANT 72
FT /note="V -> E (in BARTS2)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001548"
FT VARIANT 74
FT /note="D -> Y (in BARTS2)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001549"
FT VARIANT 99
FT /note="W -> C (in BARTS2; dbSNP:rs1213764655)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001550"
FT VARIANT 108
FT /note="D -> H (in BARTS2; dbSNP:rs104894250)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001551"
FT VARIANT 110
FT /note="P -> L (in BARTS2; dbSNP:rs373745258)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001552"
FT VARIANT 115
FT /note="S -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036426"
FT VARIANT 122
FT /note="V -> E (in BARTS2; dbSNP:rs766131330)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001553"
FT VARIANT 124
FT /note="N -> K (in BARTS2; dbSNP:rs104894251)"
FT /evidence="ECO:0000269|PubMed:9727001"
FT /id="VAR_019724"
FT VARIANT 167
FT /note="G -> E (in BARTS2; dbSNP:rs104894254)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001554"
FT VARIANT 198
FT /note="A -> T (in BARTS2; dbSNP:rs104894253)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001555"
FT VARIANT 214
FT /note="A -> V (in BARTS2; dbSNP:rs104894246)"
FT /evidence="ECO:0000269|PubMed:8841184"
FT /id="VAR_019725"
FT VARIANT 219
FT /note="S -> R (in BARTS2; dbSNP:rs104894245)"
FT /evidence="ECO:0000269|PubMed:8841184"
FT /id="VAR_019726"
FT VARIANT 315
FT /note="V -> G (in BARTS2; dbSNP:rs753949204)"
FT /evidence="ECO:0000269|PubMed:9002665"
FT /id="VAR_001556"
FT VARIANT 357
FT /note="M -> T (in BARTS2; dbSNP:rs59172778)"
FT /evidence="ECO:0000269|PubMed:8841184"
FT /id="VAR_019727"
SQ SEQUENCE 391 AA; 44795 MW; DF01C89B16BE6205 CRC64;
MNASSRNVFD TLIRVLTESM FKHLRKWVVT RFFGHSRQRA RLVSKDGRCN IEFGNVEAQS
RFIFFVDIWT TVLDLKWRYK MTIFITAFLG SWFFFGLLWY AVAYIHKDLP EFHPSANHTP
CVENINGLTS AFLFSLETQV TIGYGFRCVT EQCATAIFLL IFQSILGVII NSFMCGAILA
KISRPKKRAK TITFSKNAVI SKRGGKLCLL IRVANLRKSL LIGSHIYGKL LKTTVTPEGE
TIILDQININ FVVDAGNENL FFISPLTIYH VIDHNSPFFH MAAETLLQQD FELVVFLDGT
VESTSATCQV RTSYVPEEVL WGYRFAPIVS KTKEGKYRVD FHNFSKTVEV ETPHCAMCLY
NEKDVRARMK RGYDNPNFIL SEVNETDDTK M
