CLCKB_HUMAN
ID CLCKB_HUMAN Reviewed; 687 AA.
AC P51801; B3KUY3; Q5T5Q7; Q5T5Q8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Chloride channel protein ClC-Kb;
DE Short=Chloride channel Kb;
DE AltName: Full=ClC-K2;
GN Name=CLCNKB;
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 VARIANTS LEU-27; GLY-214;
RP VAL-287; THR-562 AND GLU-578.
RC TISSUE=Kidney;
RX PubMed=8041726; DOI=10.1073/pnas.91.15.6943;
RA Kieferle S., Fong P., Bens M., Vandewalle A., Jentsch T.;
RT "Two highly homologous members of the ClC chloride channel family in both
RT rat and human kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6943-6947(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LEU-27; GLY-214;
RP VAL-287; THR-562 AND GLU-578.
RC TISSUE=Kidney;
RX PubMed=8544406; DOI=10.1038/ki.1995.439;
RA Takeuchi Y., Uchida S., Marumo F., Sasaki S.;
RT "Cloning, tissue distribution, and intrarenal localization of ClC chloride
RT channels in human kidney.";
RL Kidney Int. 48:1497-1503(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-287.
RC TISSUE=Uterus;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-203.
RA Schutte B.C., Malik M.I., Fingert J., Barna T.J., Stone E., Lamb F.S.;
RT "Refined chromosomal localization of six human CLCN chloride ion channel
RT genes.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTIONAL CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=11734858; DOI=10.1038/35107099;
RA Estevez R., Boettger T., Stein V., Birkenhaeger R., Otto E.,
RA Hildebrandt F., Jentsch T.J.;
RT "Barttin is a Cl- channel beta-subunit crucial for renal Cl-reabsorption
RT and inner ear K+ secretion.";
RL Nature 414:558-561(2001).
RN [7]
RP INVOLVEMENT IN BARTS4B.
RX PubMed=15044642; DOI=10.1056/nejmoa032843;
RA Schlingmann K.P., Konrad M., Jeck N., Waldegger P., Reinalter S.C.,
RA Holder M., Seyberth H.W., Waldegger S.;
RT "Salt wasting and deafness resulting from mutations in two chloride
RT channels.";
RL N. Engl. J. Med. 350:1314-1319(2004).
RN [8]
RP INVOLVEMENT IN BARTS4B.
RX PubMed=18310267; DOI=10.1136/jmg.2007.052944;
RA Nozu K., Inagaki T., Fu X.J., Nozu Y., Kaito H., Kanda K., Sekine T.,
RA Igarashi T., Nakanishi K., Yoshikawa N., Iijima K., Matsuo M.;
RT "Molecular analysis of digenic inheritance in Bartter syndrome with
RT sensorineural deafness.";
RL J. Med. Genet. 45:182-186(2008).
RN [9]
RP VARIANTS BARTS3 LEU-124; THR-204; ASP-349; HIS-432 AND CYS-438.
RX PubMed=9326936; DOI=10.1038/ng1097-171;
RA Simon D.B., Bindra R.S., Mansfield T.A., Nelson-Williams C., Mendonca E.,
RA Stone R., Schurman S., Nayir A., Alpay H., Bakkaloglu A.,
RA Rodriguez-Soriano J., Morales J.M., Sanjad S.A., Taylor C.M., Pilz D.,
RA Brem A., Trachtman H., Griswold W., Richard G.A., John E., Lifton R.P.;
RT "Mutations in the chloride channel gene, CLCNKB, cause Bartter's syndrome
RT type III.";
RL Nat. Genet. 17:171-178(1997).
CC -!- FUNCTION: Voltage-gated chloride channel. Chloride channels have
CC several functions including the regulation of cell volume; membrane
CC potential stabilization, signal transduction and transepithelial
CC transport. May be important in urinary concentrating mechanisms.
CC {ECO:0000269|PubMed:11734858}.
CC -!- SUBUNIT: Interacts with BSND. Forms heteromers with BSND in the thick
CC ascending limb of Henle and more distal segments (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51801-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51801-2; Sequence=VSP_045965, VSP_045966, VSP_045967;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the kidney.
CC {ECO:0000269|PubMed:11734858}.
CC -!- DISEASE: Bartter syndrome 3 (BARTS3) [MIM:607364]: A form of Bartter
CC syndrome, an autosomal recessive disorder characterized by impaired
CC salt reabsorption in the thick ascending loop of Henle with pronounced
CC salt wasting, hypokalemic metabolic alkalosis, and varying degrees of
CC hypercalciuria. {ECO:0000269|PubMed:9326936}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Bartter syndrome 4B, neonatal, with sensorineural deafness
CC (BARTS4B) [MIM:613090]: A digenic form of Bartter syndrome, an
CC autosomal recessive disorder characterized by impaired salt
CC reabsorption in the thick ascending loop of Henle with pronounced salt
CC wasting, hypokalemic metabolic alkalosis, and varying degrees of
CC hypercalciuria. BARTS4B is associated with sensorineural deafness.
CC {ECO:0000269|PubMed:15044642, ECO:0000269|PubMed:18310267}. Note=The
CC disease is caused by variants affecting distinct genetic loci,
CC including the gene represented in this entry. Loss-of-function of both
CC CLCNKA and CLCNKB results in the disease phenotype (PubMed:18310267).
CC {ECO:0000269|PubMed:18310267}.
CC -!- MISCELLANEOUS: Compared with CLCNKA/BSND, CLCNKB/BSND is more sensitive
CC to pH and less responsive to Ca(2+).
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. CLCNKB
CC subfamily. {ECO:0000305}.
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DR EMBL; Z30644; CAA83121.1; -; mRNA.
DR EMBL; S80315; AAB35898.1; -; mRNA.
DR EMBL; AK098217; BAG53595.1; -; mRNA.
DR EMBL; AL355994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U93879; AAB65149.1; -; Genomic_DNA.
DR CCDS; CCDS168.1; -. [P51801-1]
DR CCDS; CCDS57974.1; -. [P51801-2]
DR PIR; D57713; D57713.
DR RefSeq; NP_000076.2; NM_000085.4. [P51801-1]
DR RefSeq; NP_001159417.2; NM_001165945.2. [P51801-2]
DR AlphaFoldDB; P51801; -.
DR SMR; P51801; -.
DR IntAct; P51801; 1.
DR MINT; P51801; -.
DR STRING; 9606.ENSP00000364831; -.
DR DrugCentral; P51801; -.
DR GuidetoPHARMACOLOGY; 701; -.
DR GlyGen; P51801; 1 site.
DR iPTMnet; P51801; -.
DR PhosphoSitePlus; P51801; -.
DR BioMuta; CLCNKB; -.
DR DMDM; 288558843; -.
DR jPOST; P51801; -.
DR MassIVE; P51801; -.
DR PaxDb; P51801; -.
DR PeptideAtlas; P51801; -.
DR PRIDE; P51801; -.
DR ProteomicsDB; 56400; -. [P51801-1]
DR ProteomicsDB; 64546; -.
DR Antibodypedia; 14485; 144 antibodies from 23 providers.
DR DNASU; 1188; -.
DR Ensembl; ENST00000375667.7; ENSP00000364819.3; ENSG00000184908.20. [P51801-2]
DR Ensembl; ENST00000375679.9; ENSP00000364831.5; ENSG00000184908.20. [P51801-1]
DR Ensembl; ENST00000682338.1; ENSP00000507062.1; ENSG00000184908.20. [P51801-1]
DR Ensembl; ENST00000682793.1; ENSP00000506910.1; ENSG00000184908.20. [P51801-1]
DR Ensembl; ENST00000684324.1; ENSP00000507937.1; ENSG00000184908.20. [P51801-1]
DR Ensembl; ENST00000684545.1; ENSP00000506733.1; ENSG00000184908.20. [P51801-1]
DR GeneID; 1188; -.
DR KEGG; hsa:1188; -.
DR MANE-Select; ENST00000375679.9; ENSP00000364831.5; NM_000085.5; NP_000076.2.
DR UCSC; uc001axx.6; human. [P51801-1]
DR CTD; 1188; -.
DR DisGeNET; 1188; -.
DR GeneCards; CLCNKB; -.
DR HGNC; HGNC:2027; CLCNKB.
DR HPA; ENSG00000184908; Tissue enriched (kidney).
DR MalaCards; CLCNKB; -.
DR MIM; 602023; gene.
DR MIM; 607364; phenotype.
DR MIM; 613090; phenotype.
DR neXtProt; NX_P51801; -.
DR OpenTargets; ENSG00000184908; -.
DR Orphanet; 93605; Bartter syndrome type 3.
DR Orphanet; 89938; Bartter syndrome type 4.
DR Orphanet; 358; Gitelman syndrome.
DR PharmGKB; PA26554; -.
DR VEuPathDB; HostDB:ENSG00000184908; -.
DR eggNOG; KOG0476; Eukaryota.
DR GeneTree; ENSGT00940000158748; -.
DR HOGENOM; CLU_006904_4_0_1; -.
DR InParanoid; P51801; -.
DR OMA; NYWRAFV; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P51801; -.
DR TreeFam; TF300522; -.
DR PathwayCommons; P51801; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; P51801; -.
DR BioGRID-ORCS; 1188; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; CLCNKB; human.
DR GeneWiki; CLCNKB; -.
DR GenomeRNAi; 1188; -.
DR Pharos; P51801; Tchem.
DR PRO; PR:P51801; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P51801; protein.
DR Bgee; ENSG00000184908; Expressed in renal medulla and 121 other tissues.
DR ExpressionAtlas; P51801; baseline and differential.
DR Genevisible; P51801; HS.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0070293; P:renal absorption; TAS:UniProtKB.
DR GO; GO:0070294; P:renal sodium ion absorption; IMP:UniProtKB.
DR GO; GO:0030321; P:transepithelial chloride transport; TAS:UniProtKB.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR002250; Cl_channel-K.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01119; CLCHANNELKDY.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Bartter syndrome; Calcium; CBS domain; Cell membrane;
KW Chloride; Chloride channel; Deafness; Disease variant; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..687
FT /note="Chloride channel protein ClC-Kb"
FT /id="PRO_0000094459"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 51..82
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 116..127
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 203..224
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 282..310
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 325..342
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 349..360
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 421..440
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 464..496
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 521..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT DOMAIN 551..609
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 626..684
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 121
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..49
FT /note="MEEFVGLREGSSGNPVTLQELWGPCPRIRRGIRGGLEWLKQKLFRLGED ->
FT MPCPPLLSVPVRAAGEQDRWVREEVTWGGGPTVTGGWGWRAHLRSVSPP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045965"
FT VAR_SEQ 50..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045966"
FT VAR_SEQ 616
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045967"
FT VARIANT 4
FT /note="F -> L (in dbSNP:rs34851419)"
FT /id="VAR_033770"
FT VARIANT 27
FT /note="R -> L (in dbSNP:rs2015352)"
FT /evidence="ECO:0000269|PubMed:8041726,
FT ECO:0000269|PubMed:8544406"
FT /id="VAR_046797"
FT VARIANT 88
FT /note="S -> R (in dbSNP:rs5256)"
FT /id="VAR_014466"
FT VARIANT 104
FT /note="V -> I (in dbSNP:rs35530360)"
FT /id="VAR_033771"
FT VARIANT 124
FT /note="P -> L (in BARTS3; dbSNP:rs121909131)"
FT /evidence="ECO:0000269|PubMed:9326936"
FT /id="VAR_001624"
FT VARIANT 143
FT /note="N -> H (in dbSNP:rs5259)"
FT /id="VAR_014467"
FT VARIANT 204
FT /note="A -> T (in BARTS3; dbSNP:rs121909132)"
FT /evidence="ECO:0000269|PubMed:9326936"
FT /id="VAR_001625"
FT VARIANT 214
FT /note="A -> G (in dbSNP:rs1889789)"
FT /evidence="ECO:0000269|PubMed:8041726,
FT ECO:0000269|PubMed:8544406"
FT /id="VAR_033772"
FT VARIANT 287
FT /note="A -> V (in dbSNP:rs7367494)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8041726, ECO:0000269|PubMed:8544406"
FT /id="VAR_069104"
FT VARIANT 334
FT /note="V -> L (in dbSNP:rs5251)"
FT /id="VAR_014468"
FT VARIANT 349
FT /note="A -> D (in BARTS3; dbSNP:rs121909134)"
FT /evidence="ECO:0000269|PubMed:9326936"
FT /id="VAR_001626"
FT VARIANT 395
FT /note="R -> W (in dbSNP:rs34255952)"
FT /id="VAR_046799"
FT VARIANT 419
FT /note="I -> V (in dbSNP:rs6650119)"
FT /id="VAR_033773"
FT VARIANT 432
FT /note="Y -> H (in BARTS3; dbSNP:rs121909135)"
FT /evidence="ECO:0000269|PubMed:9326936"
FT /id="VAR_001627"
FT VARIANT 438
FT /note="R -> C (in BARTS3; dbSNP:rs121909133)"
FT /evidence="ECO:0000269|PubMed:9326936"
FT /id="VAR_001628"
FT VARIANT 481
FT /note="T -> S (in dbSNP:rs12140311)"
FT /id="VAR_046800"
FT VARIANT 562
FT /note="M -> T (in dbSNP:rs5253)"
FT /evidence="ECO:0000269|PubMed:8041726,
FT ECO:0000269|PubMed:8544406"
FT /id="VAR_014469"
FT VARIANT 578
FT /note="K -> E (in dbSNP:rs2275166)"
FT /evidence="ECO:0000269|PubMed:8041726,
FT ECO:0000269|PubMed:8544406"
FT /id="VAR_024409"
FT VARIANT 660
FT /note="S -> L (in dbSNP:rs5255)"
FT /id="VAR_046801"
FT CONFLICT 609
FT /note="S -> P (in Ref. 3; BAG53595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 75446 MW; 4D28BC19DDD5D412 CRC64;
MEEFVGLREG SSGNPVTLQE LWGPCPRIRR GIRGGLEWLK QKLFRLGEDW YFLMTLGVLM
ALVSCAMDLA VESVVRAHQW LYREIGDSHL LRYLSWTVYP VALVSFSSGF SQSITPSSGG
SGIPEVKTML AGVVLEDYLD IKNFGAKVVG LSCTLACGST LFLGKVGPFV HLSVMMAAYL
GRVRTTTIGE PENKSKQNEM LVAAAAVGVA TVFAAPFSGV LFSIEVMSSH FSVWDYWRGF
FAATCGAFMF RLLAVFNSEQ ETITSLYKTS FRVDVPFDLP EIFFFVALGG LCGILGSAYL
FCQRIFFGFI RNNRFSSKLL ATSKPVYSAL ATLVLASITY PPSAGRFLAS RLSMKQHLDS
LFDNHSWALM TQNSSPPWPE ELDPQHLWWE WYHPRFTIFG TLAFFLVMKF WMLILATTIP
MPAGYFMPIF VYGAAIGRLF GETLSFIFPE GIVAGGITNP IMPGGYALAG AAAFSGAVTH
TISTALLAFE VTGQIVHALP VLMAVLAANA IAQSCQPSFY DGTVIVKKLP YLPRILGRNI
GSHRVRVEHF MNHSITTLAK DMPLEEVVKV VTSTDVAKYP LVESTESQIL VGIVRRAQLV
QALKAEPPSW APGHQQCLQD ILAAGCPTEP VTLKLSPETS LHEAHNLFEL LNLHSLFVTS
RGRAVGCVSW VEMKKAISNL TNPPAPK
