KCJ10_HUMAN
ID KCJ10_HUMAN Reviewed; 379 AA.
AC P78508; A3KME7; Q5VUT9; Q8N4I7; Q92808;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 10;
DE AltName: Full=ATP-dependent inwardly rectifying potassium channel Kir4.1;
DE AltName: Full=Inward rectifier K(+) channel Kir1.2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 10;
GN Name=KCNJ10;
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 [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 143-379.
RC TISSUE=Kidney;
RX PubMed=8995301; DOI=10.1074/jbc.272.1.586;
RA Shuck M.E., Piser T.M., Bock J.H., Slightom J.L., Lee K.S.,
RA Bienkowski M.J.;
RT "Cloning and characterization of two K+ inward rectifier (Kir) 1.1
RT potassium channel homologs from human kidney (Kir1.2 and Kir1.3).";
RL J. Biol. Chem. 272:586-593(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-271.
RC TISSUE=Cerebellum;
RX PubMed=10659995; DOI=10.1016/s0898-6568(99)00059-5;
RA Schoots O., Wilson J.M., Ethier N., Bigras E., Hebert T.E., Van Tol H.H.M.;
RT "Co-expression of human Kir3 subunits can yield channels with different
RT functional properties.";
RL Cell. Signal. 11:871-883(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, CHARACTERIZATION OF VARIANTS SESAMES PRO-65; ARG-77; ARG-140;
RP ILE-164; VAL-167 AND CYS-297, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH KCNJ16 AND MAGI1.
RX PubMed=24561201; DOI=10.1016/j.febslet.2014.02.024;
RA Tanemoto M., Abe T., Uchida S., Kawahara K.;
RT "Mislocalization of K+ channels causes the renal salt wasting in
RT EAST/SeSAME syndrome.";
RL FEBS Lett. 588:899-905(2014).
RN [7]
RP VARIANTS SESAMES PRO-65 AND ARG-77.
RX PubMed=19420365; DOI=10.1056/nejmoa0810276;
RA Bockenhauer D., Feather S., Stanescu H.C., Bandulik S., Zdebik A.A.,
RA Reichold M., Tobin J., Lieberer E., Sterner C., Landoure G., Arora R.,
RA Sirimanna T., Thompson D., Cross J.H., van't Hoff W., Al Masri O.,
RA Tullus K., Yeung S., Anikster Y., Klootwijk E., Hubank M., Dillon M.J.,
RA Heitzmann D., Arcos-Burgos M., Knepper M.A., Dobbie A., Gahl W.A.,
RA Warth R., Sheridan E., Kleta R.;
RT "Epilepsy, ataxia, sensorineural deafness, tubulopathy, and KCNJ10
RT mutations.";
RL N. Engl. J. Med. 360:1960-1970(2009).
RN [8]
RP VARIANTS SESAMES PRO-65; ARG-140; ILE-164; VAL-167 AND CYS-297.
RX PubMed=19289823; DOI=10.1073/pnas.0901749106;
RA Scholl U.I., Choi M., Liu T., Ramaekers V.T., Hausler M.G., Grimmer J.,
RA Tobe S.W., Farhi A., Nelson-Williams C., Lifton R.P.;
RT "Seizures, sensorineural deafness, ataxia, mental retardation, and
RT electrolyte imbalance (SeSAME syndrome) caused by mutations in KCNJ10.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5842-5847(2009).
RN [9]
RP VARIANTS SESAMES PRO-68 AND VAL-129.
RX PubMed=22612257; DOI=10.1111/j.1528-1167.2012.03516.x;
RA Lemke J.R., Riesch E., Scheurenbrand T., Schubach M., Wilhelm C.,
RA Steiner I., Hansen J., Courage C., Gallati S., Buerki S., Strozzi S.,
RA Simonetti B.G., Grunt S., Steinlin M., Alber M., Wolff M., Klopstock T.,
RA Prott E.C., Lorenz R., Spaich C., Rona S., Lakshminarasimhan M., Kroell J.,
RA Dorn T., Kraemer G., Synofzik M., Becker F., Weber Y.G., Lerche H.,
RA Boehm D., Biskup S.;
RT "Targeted next generation sequencing as a diagnostic tool in epileptic
RT disorders.";
RL Epilepsia 53:1387-1398(2012).
RN [10]
RP VARIANT HIS-271.
RX PubMed=28887846; DOI=10.1002/humu.23335;
RA Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
RT "Mutations in KARS cause early-onset hearing loss and leukoencephalopathy:
RT Potential pathogenic mechanism.";
RL Hum. Mutat. 38:1740-1750(2017).
CC -!- FUNCTION: May be responsible for potassium buffering action of glial
CC cells in the brain. Inward rectifier potassium channels are
CC characterized by a greater tendency to allow potassium to flow into the
CC cell rather than out of it. Their voltage dependence is regulated by
CC the concentration of extracellular potassium; as external potassium is
CC raised, the voltage range of the channel opening shifts to more
CC positive voltages. The inward rectification is mainly due to the
CC blockage of outward current by internal magnesium. Can be blocked by
CC extracellular barium and cesium (By similarity). In the kidney,
CC together with KCNJ16, mediates basolateral K(+) recycling in distal
CC tubules; this process is critical for Na(+) reabsorption at the
CC tubules. {ECO:0000250, ECO:0000305|PubMed:24561201}.
CC -!- SUBUNIT: Heterodimer with Kir5.1/KCNJ16; this interaction is required
CC for KCNJ16 localization to the basolateral membrane in kidney cells.
CC Interacts with MAGI1, alone and possibly as a heterodimer with KCNJ16;
CC this interaction may facilitate KCNJ10/KCNJ16 potassium channel
CC expression at the basolateral membrane in kidney cells
CC (PubMed:24561201). Interacts with PATJ (By similarity).
CC {ECO:0000250|UniProtKB:Q9JM63, ECO:0000269|PubMed:24561201}.
CC -!- INTERACTION:
CC P78508; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-9117877, EBI-747107;
CC P78508; F1PK57: MAGI1; Xeno; NbExp=2; IntAct=EBI-9117877, EBI-9118227;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:24561201}; Multi-
CC pass membrane protein. Basolateral cell membrane
CC {ECO:0000269|PubMed:24561201}. Note=In kidney distal convoluted
CC tubules, located in the basolateral membrane where it colocalizes with
CC KCNJ16. {ECO:0000269|PubMed:24561201}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
CC {ECO:0000269|PubMed:24561201}.
CC -!- DISEASE: Seizures, sensorineural deafness, ataxia, intellectual
CC disability, and electrolyte imbalance (SESAMES) [MIM:612780]: A complex
CC disorder characterized by generalized seizures with onset in infancy,
CC delayed psychomotor development, ataxia, sensorineural hearing loss,
CC hypokalemia, metabolic alkalosis, and hypomagnesemia.
CC {ECO:0000269|PubMed:19289823, ECO:0000269|PubMed:19420365,
CC ECO:0000269|PubMed:22612257, ECO:0000269|PubMed:24561201}. 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. KCNJ10 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34036.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73192; AAC50923.1; -; Genomic_DNA.
DR EMBL; U73193; AAC50924.1; -; mRNA.
DR EMBL; U52155; AAB07046.1; -; mRNA.
DR EMBL; AL513302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52749.1; -; Genomic_DNA.
DR EMBL; BC034036; AAH34036.2; ALT_INIT; mRNA.
DR EMBL; BC131627; AAI31628.1; -; mRNA.
DR CCDS; CCDS1193.1; -.
DR RefSeq; NP_002232.2; NM_002241.4.
DR AlphaFoldDB; P78508; -.
DR SMR; P78508; -.
DR BioGRID; 109968; 35.
DR CORUM; P78508; -.
DR IntAct; P78508; 14.
DR MINT; P78508; -.
DR STRING; 9606.ENSP00000357068; -.
DR BindingDB; P78508; -.
DR ChEMBL; CHEMBL2146348; -.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB01392; Yohimbine.
DR DrugCentral; P78508; -.
DR GuidetoPHARMACOLOGY; 438; -.
DR TCDB; 1.A.2.1.16; the inward rectifier k(+) channel (irk-c) family.
DR iPTMnet; P78508; -.
DR PhosphoSitePlus; P78508; -.
DR BioMuta; KCNJ10; -.
DR DMDM; 2493605; -.
DR MassIVE; P78508; -.
DR PaxDb; P78508; -.
DR PeptideAtlas; P78508; -.
DR PRIDE; P78508; -.
DR ProteomicsDB; 57627; -.
DR TopDownProteomics; P78508; -.
DR Antibodypedia; 1679; 288 antibodies from 27 providers.
DR DNASU; 3766; -.
DR Ensembl; ENST00000638728.1; ENSP00000492619.1; ENSG00000177807.10.
DR Ensembl; ENST00000638868.1; ENSP00000491250.1; ENSG00000177807.10.
DR Ensembl; ENST00000644903.1; ENSP00000495557.1; ENSG00000177807.10.
DR GeneID; 3766; -.
DR KEGG; hsa:3766; -.
DR MANE-Select; ENST00000644903.1; ENSP00000495557.1; NM_002241.5; NP_002232.2.
DR UCSC; uc001fuw.3; human.
DR CTD; 3766; -.
DR DisGeNET; 3766; -.
DR GeneCards; KCNJ10; -.
DR GeneReviews; KCNJ10; -.
DR HGNC; HGNC:6256; KCNJ10.
DR HPA; ENSG00000177807; Group enriched (brain, kidney, retina).
DR MalaCards; KCNJ10; -.
DR MIM; 602208; gene.
DR MIM; 612780; phenotype.
DR neXtProt; NX_P78508; -.
DR OpenTargets; ENSG00000177807; -.
DR Orphanet; 199343; EAST syndrome.
DR Orphanet; 705; Pendred syndrome.
DR PharmGKB; PA30043; -.
DR VEuPathDB; HostDB:ENSG00000177807; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_3_3_1; -.
DR InParanoid; P78508; -.
DR OMA; QVNVAFQ; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P78508; -.
DR TreeFam; TF313676; -.
DR PathwayCommons; P78508; -.
DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-HSA-1296067; Potassium transport channels.
DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR SignaLink; P78508; -.
DR BioGRID-ORCS; 3766; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; KCNJ10; human.
DR GeneWiki; KCNJ10; -.
DR GenomeRNAi; 3766; -.
DR Pharos; P78508; Tbio.
DR PRO; PR:P78508; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P78508; protein.
DR Bgee; ENSG00000177807; Expressed in C1 segment of cervical spinal cord and 127 other tissues.
DR ExpressionAtlas; P78508; baseline and differential.
DR Genevisible; P78508; HS.
DR GO; GO:0097449; C:astrocyte projection; ISS:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044297; C:cell body; ISS:ARUK-UCL.
DR GO; GO:0097546; C:ciliary base; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; TAS:ProtInc.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
DR GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
DR GO; GO:0051935; P:glutamate reuptake; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0055075; P:potassium ion homeostasis; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0060075; P:regulation of resting membrane potential; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
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; IPR003269; K_chnl_inward-rec_Kir1.2.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF21; PTHR11767:SF21; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01322; KIR12CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Deafness; Disease variant; Epilepsy;
KW Intellectual disability; Ion channel; Ion transport; Membrane;
KW Nucleotide-binding; Potassium; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..379
FT /note="ATP-sensitive inward rectifier potassium channel 10"
FT /id="PRO_0000154953"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..89
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..114
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 115..126
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 127..133
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 134..142
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..164
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 165..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 128..133
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 158
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT VARIANT 65
FT /note="R -> P (in SESAMES; no effect on localization to the
FT basolateral membrane in kidney cells; dbSNP:rs137853066)"
FT /evidence="ECO:0000269|PubMed:19289823,
FT ECO:0000269|PubMed:19420365, ECO:0000269|PubMed:24561201"
FT /id="VAR_063059"
FT VARIANT 68
FT /note="L -> P (in SESAMES)"
FT /evidence="ECO:0000269|PubMed:22612257"
FT /id="VAR_072746"
FT VARIANT 77
FT /note="G -> R (in SESAMES; important loss of localization
FT to the basolateral membrane in kidney cells; in non-tubular
FT cells, does not form functional channels;
FT dbSNP:rs137853072)"
FT /evidence="ECO:0000269|PubMed:19420365,
FT ECO:0000269|PubMed:24561201"
FT /id="VAR_063060"
FT VARIANT 129
FT /note="I -> V (in SESAMES; dbSNP:rs751625111)"
FT /evidence="ECO:0000269|PubMed:22612257"
FT /id="VAR_072747"
FT VARIANT 140
FT /note="C -> R (in SESAMES; loss of localization to the
FT basolateral membrane in kidney cells; in non-tubular cells,
FT does not form functional channels; dbSNP:rs137853068)"
FT /evidence="ECO:0000269|PubMed:19289823,
FT ECO:0000269|PubMed:24561201"
FT /id="VAR_063061"
FT VARIANT 164
FT /note="T -> I (in SESAMES; no effect on localization to the
FT basolateral membrane in kidney cells; dbSNP:rs137853069)"
FT /evidence="ECO:0000269|PubMed:19289823,
FT ECO:0000269|PubMed:24561201"
FT /id="VAR_063062"
FT VARIANT 167
FT /note="A -> V (in SESAMES; loss of localization to the
FT basolateral membrane in kidney cells; in non-tubular cells,
FT forms functional channels; important loss of MAGI1-binding
FT when transfected in tubular MDCKII cells, but not in non-
FT tubular HEK293T cells; dbSNP:rs137853070)"
FT /evidence="ECO:0000269|PubMed:19289823,
FT ECO:0000269|PubMed:24561201"
FT /id="VAR_063063"
FT VARIANT 271
FT /note="R -> C (in dbSNP:rs1130183)"
FT /evidence="ECO:0000269|PubMed:10659995"
FT /id="VAR_034018"
FT VARIANT 271
FT /note="R -> H (in dbSNP:rs3795339)"
FT /evidence="ECO:0000269|PubMed:28887846"
FT /id="VAR_020339"
FT VARIANT 297
FT /note="R -> C (in SESAMES; no effect on localization to the
FT basolateral membrane in kidney cells; dbSNP:rs137853071)"
FT /evidence="ECO:0000269|PubMed:19289823,
FT ECO:0000269|PubMed:24561201"
FT /id="VAR_063064"
FT CONFLICT 50
FT /note="L -> P (in Ref. 2; AAB07046)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="G -> V (in Ref. 5; AAH34036)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="L -> Q (in Ref. 2; AAB07046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42508 MW; D9DA013FF4003533 CRC64;
MTSVAKVYYS QTTQTESRPL MGPGIRRRRV LTKDGRSNVR MEHIADKRFL YLKDLWTTFI
DMQWRYKLLL FSATFAGTWF LFGVVWYLVA VAHGDLLELD PPANHTPCVV QVHTLTGAFL
FSLESQTTIG YGFRYISEEC PLAIVLLIAQ LVLTTILEIF ITGTFLAKIA RPKKRAETIR
FSQHAVVASH NGKPCLMIRV ANMRKSLLIG CQVTGKLLQT HQTKEGENIR LNQVNVTFQV
DTASDSPFLI LPLTFYHVVD ETSPLKDLPL RSGEGDFELV LILSGTVEST SATCQVRTSY
LPEEILWGYE FTPAISLSAS GKYIADFSLF DQVVKVASPS GLRDSTVRYG DPEKLKLEES
LREQAEKEGS ALSVRISNV
