S4A7_MOUSE
ID S4A7_MOUSE Reviewed; 1034 AA.
AC Q8BTY2; Q3U5H7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Sodium bicarbonate cotransporter 3;
DE AltName: Full=Solute carrier family 4 member 7;
GN Name=Slc4a7; Synonyms=Nbc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-932 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1034 (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [3]
RP INTERACTION WITH CFTR AND SLC9A3R1.
RX PubMed=12403779; DOI=10.1074/jbc.m201862200;
RA Park M., Ko S.B.H., Choi J.Y., Muallem G., Thomas P.J., Pushkin A.,
RA Lee M.-S., Kim J.Y., Lee M.G., Muallem S., Kurtz I.;
RT "The cystic fibrosis transmembrane conductance regulator interacts with and
RT regulates the activity of the HCO3- salvage transporter human Na+-HCO3-
RT cotransport isoform 3.";
RL J. Biol. Chem. 277:50503-50509(2002).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12808454; DOI=10.1038/ng1176;
RA Bok D., Galbraith G., Lopez I., Woodruff M., Nusinowitz S.,
RA BeltrandelRio H., Huang W., Zhao S., Geske R., Montgomery C.,
RA van Sligtenhorst I., Friddle C., Platt K., Sparks M.J., Pushkin A.,
RA Abuladze N., Ishiyama A., Dukkipati R., Liu W., Kurtz I.;
RT "Blindness and auditory impairment caused by loss of the sodium bicarbonate
RT cotransporter NBC3.";
RL Nat. Genet. 34:313-319(2003).
RN [5]
RP INTERACTION WITH USH1C, AND TISSUE SPECIFICITY.
RX PubMed=16301216; DOI=10.1093/hmg/ddi417;
RA Reiners J., van Wijk E., Maerker T., Zimmermann U., Juergens K.,
RA te Brinke H., Overlack N., Roepman R., Knipper M., Kremer H., Wolfrum U.;
RT "Scaffold protein harmonin (USH1C) provides molecular links between Usher
RT syndrome type 1 and type 2.";
RL Hum. Mol. Genet. 14:3933-3943(2005).
RN [6]
RP REPRESSION BY HYPOXIA.
RX PubMed=17928512; DOI=10.1152/ajpregu.00497.2007;
RA Chen L.M., Choi I., Haddad G.G., Boron W.F.;
RT "Chronic continuous hypoxia decreases the expression of SLC4A7 (NBCn1) and
RT SLC4A10 (NCBE) in mouse brain.";
RL Am. J. Physiol. 293:R2412-R2420(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-238 AND SER-960,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-654 AND ASN-664.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; SER-250; SER-271;
RP SER-275; THR-951 AND SER-960, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-260 AND SER-263 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Electroneutral sodium- and bicarbonate-dependent
CC cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Regulates
CC intracellular pH and may play a role in bicarbonate salvage in
CC secretory epithelia. May also have an associated sodium channel
CC activity. {ECO:0000269|PubMed:12808454}.
CC -!- ACTIVITY REGULATION: Transporter activity is regulated by CA2/carbonic
CC anhydrase 2, cAMP and PKA. Insensitive to stilbene derivatives. May be
CC inhibited by 5-(N-ethyl-N-isopropyl)-amiloride (EIPA) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with ATP6V1B1 and SLC9A3R1/EBP50. Interacts in
CC a pH dependent-manner with CA2/carbonic anhydrase 2 (By similarity).
CC Interacts with CFTR through SLC9A3R1/EBP50. Interacts with USH1C.
CC {ECO:0000250, ECO:0000269|PubMed:12403779,
CC ECO:0000269|PubMed:16301216}.
CC -!- INTERACTION:
CC Q8BTY2; Q9ES64-3: Ush1c; NbExp=2; IntAct=EBI-11621670, EBI-7418919;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Apical cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell projection, stereocilium {ECO:0000250}.
CC Note=Also described at the apical cell membrane. Localizes to the
CC stereocilia of cochlear outer hair cells and to the lateral membrane of
CC cochlear inner hair cells (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BTY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BTY2-2; Sequence=VSP_017166, VSP_017167, VSP_017168;
CC -!- TISSUE SPECIFICITY: Expressed in the spiral ligament throughout the
CC cochlea and in photoreceptors of the outer plexiform layer of the
CC retina (at protein level). {ECO:0000269|PubMed:12808454,
CC ECO:0000269|PubMed:16301216}.
CC -!- INDUCTION: Repressed in the brain by chronic continuous hypoxia (at
CC protein level). {ECO:0000269|PubMed:17928512}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with the CFTR,
CC SLC9A3R1/EBP50 complex and probably with USH1C. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deafness and blindness due to degeneration of
CC sensory receptors in internal ear and retina.
CC {ECO:0000269|PubMed:12808454}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; AK088400; BAC40330.1; -; mRNA.
DR EMBL; AK152233; BAE31059.1; -; mRNA.
DR EMBL; AK153567; BAE32101.1; -; mRNA.
DR EMBL; CN532915; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q8BTY2; -.
DR SMR; Q8BTY2; -.
DR IntAct; Q8BTY2; 1.
DR STRING; 10090.ENSMUSP00000058313; -.
DR ChEMBL; CHEMBL3774291; -.
DR GlyGen; Q8BTY2; 5 sites.
DR iPTMnet; Q8BTY2; -.
DR PhosphoSitePlus; Q8BTY2; -.
DR SwissPalm; Q8BTY2; -.
DR EPD; Q8BTY2; -.
DR jPOST; Q8BTY2; -.
DR MaxQB; Q8BTY2; -.
DR PaxDb; Q8BTY2; -.
DR PeptideAtlas; Q8BTY2; -.
DR PRIDE; Q8BTY2; -.
DR ProteomicsDB; 260797; -. [Q8BTY2-1]
DR ProteomicsDB; 260798; -. [Q8BTY2-2]
DR MGI; MGI:2443878; Slc4a7.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q8BTY2; -.
DR PhylomeDB; Q8BTY2; -.
DR Reactome; R-MMU-425381; Bicarbonate transporters.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR ChiTaRS; Slc4a7; mouse.
DR PRO; PR:Q8BTY2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BTY2; protein.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0060117; P:auditory receptor cell development; IMP:MGI.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IMP:MGI.
DR GO; GO:0021747; P:cochlear nucleus development; IMP:MGI.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0046666; P:retinal cell programmed cell death; IMP:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 3.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1034
FT /note="Sodium bicarbonate cotransporter 3"
FT /id="PRO_0000079234"
FT TOPO_DOM 1..476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..563
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..750
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 751..776
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..812
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..920
FT /note="CA2-binding"
FT /evidence="ECO:0000250"
FT REGION 926..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1031..1034
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 58..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1N3"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1N3"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1N3"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT MOD_RES 951
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 634..636
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 670..682
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT VAR_SEQ 243
FT /note="G -> GKKHSDPHLLERNG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017166"
FT VAR_SEQ 815
FT /note="F -> KGAGYHLDLLMVGVMLGVCSIMGLPWFVAATVLSISHVNSLKVESEC
FT SAPGEQPKFLGIREQRVTGLMIFILMGLSVFMTSVLKVKPLWQCSTILFTLTFILSCKE
FT IKH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017167"
FT VAR_SEQ 816..1034
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017168"
FT CONFLICT 430
FT /note="G -> D (in Ref. 1; BAC40330)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="G -> R (in Ref. 1; BAC40330)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8BTY2-2:260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8BTY2-2:263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1034 AA; 116514 MW; 92B080274D206097 CRC64;
MEADGAGEQM RPLLTRGPDE EAVVDLGKTS STVNTKFEKE ELESHRAVYV GVHVPFSKES
RRRHKHRGHK HHHRRRKDKD SDKEDGRESP SYDTPSQRVQ FILGTEDDDE EHIPHDLFTE
MDELCYRDGE EYEWKETARW LKFEEDVEDG GDRWSKPYVA TLSLHSLFEL RSCILNGTVM
LDMRASTLDE IADMVLDNMI ASGQLDDSIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA
DIGILASPQS APGNLDNSKS GEMKGNGSGG SRENSTVDFS KVDMNFMRKI PTGAEASNVL
VGEVDFLERP IIAFVRLAPA VLLSGLTEVP VPTRFLFLLL GPAGKAPQYH EIGRSIATLM
TDEIFHDVAY KAKDRNDLLS GIDEFLDQVT VLPPGEWDPS IRIEPPKSVP SQEKRKIPVF
PNGSAAMSVG PPKEDDHHAG PELQRTGRLF GGLILDIKRK APFFLSDFKD ALSLQCLASI
LFLYCACMSP VITFGGLLGE ATEGRISAIE SLFGASLTGI AYSLFAGQPL TILGSTGPVL
VFEKILFKFC RDYHLSYLSL RTSIGLWTSF LCIVLVATDA SSLVCYITRF TEEAFAALIC
IIFIYEALEK LFHLGEIYAF NMHNNLDELT SYTCVCAEPS NPSNETLELW KRKNITAYSV
SWGNLTVSEC KTFHGMFVGS ACGPHGPYVP DVLFWCVVLF FTTFFLSSFL KQFKTKGYFP
TKVRSTISDF AVFLTIVIMV AIDYLVGIPS PKLHVPEKFE PTDPSRGWII SPLGDNPWWT
LLIAAVPALL CTILIFMDQQ ITAVIINRKE HKLKFIPMPV LYGVFLYMGV SSLKGIQFFD
RIKLFGMPAK HQPDLIYLRY VPLWKVHVFT VVQLTCLVLL WVIKASAAAV VFPMMVLALV
FVRKLMDLCF TKRELSWLDD LMPESKKKKE DDKKKKEKEE AERMLQDDED TVHLPFERGS
LLQIPVKTLK YSIDPSVVNI SDEMAKTAQW KALSMNTENA KVTRPNTSPE KPVSVTINFE
DEPSKKYMDA ETSL
