S4A7_HUMAN
ID S4A7_HUMAN Reviewed; 1214 AA.
AC Q9Y6M7; A6NIA8; B2CI53; B5M449; B5M451; B5M452; B5M453; B6DY52; B6DY53;
AC C9JST9; D3K174; D3K175; O60350; Q6AHZ9; Q9HC88; Q9UIB9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Sodium bicarbonate cotransporter 3;
DE AltName: Full=Electroneutral Na/HCO(3) cotransporter;
DE AltName: Full=Sodium bicarbonate cotransporter 2;
DE AltName: Full=Sodium bicarbonate cotransporter 2b;
DE Short=Bicarbonate transporter;
DE AltName: Full=Solute carrier family 4 member 7;
GN Name=SLC4A7; Synonyms=BT, NBC2, NBC2B, NBC3, NBCn1, SBC2, SLC4A6;
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 3), AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9610397; DOI=10.1006/bbrc.1998.8658;
RA Ishibashi K., Sasaki S., Marumo F.;
RT "Molecular cloning of a new sodium bicarbonate cotransporter cDNA from
RT human retina.";
RL Biochem. Biophys. Res. Commun. 246:535-538(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, REGULATION, AND VARIANT LYS-326.
RC TISSUE=Kidney, and Skeletal muscle;
RX PubMed=10347222; DOI=10.1074/jbc.274.23.16569;
RA Pushkin A., Abuladze N., Lee I., Newman D., Hwang J., Kurtz I.;
RT "Cloning, tissue distribution, genomic organization, and functional
RT characterization of NBC3, a new member of the sodium bicarbonate
RT cotransporter family.";
RL J. Biol. Chem. 274:16569-16575(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Neuroepithelium;
RA Romero M.F.;
RT "Cloning of a HCO3 transporter, NT2-NBC, from human brain, similar to both
RT the Anion exchangers (AEs) and the Na/Bicarbonate Cotransporters (NBCs).";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7; 8; 9; 10; 11 AND 12),
RP ALTERNATIVE SPLICING, AND VARIANT LYS-326.
RC TISSUE=Brain, Heart, Liver, and Skeletal muscle;
RA Liu Y., Chen L.-M., Parker M.D., Boron W.F.;
RT "Cloning and identification of novel human NBCn1 splice variants.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 13 AND 14).
RC TISSUE=Brain;
RA Liu Y., Chen L., Parker M.D., Boron W.F.;
RT "Cloning and identification of two novel human NBCn1 splice variants.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
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 [9]
RP FUNCTION, INTERACTION WITH CFTR AND SLC9A3R1, AND DOMAIN.
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 [10]
RP INTERACTION WITH ATP6V1B1 AND SLC9A3R1, AND MUTAGENESIS OF LEU-1214.
RX PubMed=12444018; DOI=10.1152/ajpcell.00225.2002;
RA Pushkin A., Abuladze N., Newman D., Muronets V., Sassani P., Tatishchev S.,
RA Kurtz I.;
RT "The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs
RT involved in their interaction.";
RL Am. J. Physiol. 284:C667-C673(2003).
RN [11]
RP INTERACTION WITH CA2, REGULATION, AND MUTAGENESIS OF 1135-ASP-ASP-1136 AND
RP 1163-ASP--ASP-1165.
RX PubMed=14736710; DOI=10.1152/ajpcell.00382.2003;
RA Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.;
RT "Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase
RT II and PKA.";
RL Am. J. Physiol. 286:C1423-C1433(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [13]
RP INTERACTION WITH USH1C.
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1167 AND SER-1176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-1213,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORMS 11; 6 AND 9),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1109 AND SER-1115 (ISOFORM
RP 13), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 (ISOFORMS 13 AND
RP 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010 AND SER-1016 (ISOFORM
RP 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORMS 3 AND 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774 AND SER-780 (ISOFORM 5),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105 AND SER-1111 (ISOFORM
RP 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1233 AND SER-1239
RP (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220 AND
RP SER-1226 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP REVIEW, AND ALTERNATIVE SPLICING.
RX PubMed=19448079; DOI=10.1242/jeb.028563;
RA Boron W.F., Chen L., Parker M.D.;
RT "Modular structure of sodium-coupled bicarbonate transporters.";
RL J. Exp. Biol. 212:1697-1706(2009).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-776; ASN-786 AND ASN-791.
RC TISSUE=Leukemic T-cell;
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1167 AND SER-1176,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORMS 11; 6 AND 9),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1077 (ISOFORM 13),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 (ISOFORMS 13 AND 14),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORMS 3 AND 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742 (ISOFORM 5),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1073 (ISOFORM 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1201 (ISOFORM 7),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1188 (ISOFORM 8), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1176, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-260 AND SER-263 (ISOFORMS 11; 6 AND 9),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106 AND SER-1109 (ISOFORM
RP 13), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-267
RP (ISOFORMS 13 AND 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND
RP SER-258 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1007 AND
RP SER-1010 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND
RP SER-168 (ISOFORMS 3 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-771 AND SER-774 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-1102 AND SER-1105 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS]
RP AT SER-1230 AND SER-1233 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-1217 AND SER-1220 (ISOFORM 8), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-403,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORMS 11; 6 AND 9),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106 (ISOFORM 13),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 (ISOFORMS 13 AND 14),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1007 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORMS 3 AND 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771 (ISOFORM 5),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102 (ISOFORM 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1230 (ISOFORM 7),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217 (ISOFORM 8), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-242; SER-403;
RP SER-407; SER-556 AND THR-557, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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:10347222, ECO:0000269|PubMed:12403779}.
CC -!- ACTIVITY REGULATION: Transporter activity is regulated by CA2/carbonic
CC anhydrase 2, cAMP and PKA. Insensitive to stilbene derivatives.
CC PubMed:10347222 states it is inhibited by 5-(N-ethyl-N-isopropyl)-
CC amiloride (EIPA).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 mM for external sodium {ECO:0000269|PubMed:10347222};
CC -!- SUBUNIT: Interacts with CFTR through SLC9A3R1/EBP50. Interacts with
CC USH1C. Forms a complex with ATP6V1B1 and SLC9A3R1/EBP50. Interacts in a
CC pH dependent-manner with CA2/carbonic anhydrase 2.
CC {ECO:0000269|PubMed:12403779, ECO:0000269|PubMed:12444018,
CC ECO:0000269|PubMed:14736710, ECO:0000269|PubMed:16301216}.
CC -!- INTERACTION:
CC Q9Y6M7; O76071: CIAO1; NbExp=3; IntAct=EBI-1044546, EBI-725145;
CC Q9Y6M7; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-1044546, EBI-11993254;
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=14;
CC Name=1; Synonyms=mNBC3, NBCn1-A;
CC IsoId=Q9Y6M7-1; Sequence=Displayed;
CC Name=2; Synonyms=NBCn1-F;
CC IsoId=Q9Y6M7-2; Sequence=VSP_047844;
CC Name=3;
CC IsoId=Q9Y6M7-3; Sequence=VSP_047839, VSP_047842, VSP_047844,
CC VSP_047849;
CC Name=4;
CC IsoId=Q9Y6M7-4; Sequence=VSP_047839, VSP_047842, VSP_047844;
CC Name=5;
CC IsoId=Q9Y6M7-5; Sequence=VSP_047838, VSP_047845, VSP_047848;
CC Name=6; Synonyms=NBCn1-G;
CC IsoId=Q9Y6M7-6; Sequence=VSP_047840, VSP_047844, VSP_047848;
CC Name=7; Synonyms=NBCn1-D;
CC IsoId=Q9Y6M7-7; Sequence=VSP_047841, VSP_047848;
CC Name=8; Synonyms=NBCn1-C;
CC IsoId=Q9Y6M7-8; Sequence=VSP_047841, VSP_047843, VSP_047848;
CC Name=9; Synonyms=NBCn1-E;
CC IsoId=Q9Y6M7-9; Sequence=VSP_047840, VSP_047844;
CC Name=10;
CC IsoId=Q9Y6M7-10; Sequence=VSP_047840, VSP_047843, VSP_047846,
CC VSP_047847;
CC Name=11;
CC IsoId=Q9Y6M7-11; Sequence=VSP_047840, VSP_047844, VSP_047846,
CC VSP_047847;
CC Name=12; Synonyms=NBCn1-H;
CC IsoId=Q9Y6M7-12; Sequence=VSP_047840, VSP_047843;
CC Name=13;
CC IsoId=Q9Y6M7-13; Sequence=VSP_047841, VSP_047844, VSP_047848;
CC Name=14;
CC IsoId=Q9Y6M7-14; Sequence=VSP_047841, VSP_047844, VSP_047846,
CC VSP_047847;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and spleen. Also
CC expressed in retina, colon, small intestine, ovary, thymus, prostate,
CC muscle, heart and kidney. Isoform 1 is expressed in skeletal muscle and
CC heart muscle. {ECO:0000269|PubMed:9610397}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with the CFTR,
CC SLC9A3R1/EBP50 complex and probably with USH1C.
CC {ECO:0000269|PubMed:12403779}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB012130; BAA25898.1; -; mRNA.
DR EMBL; AF047033; AAD38322.1; -; mRNA.
DR EMBL; AF089726; AAG16773.1; -; mRNA.
DR EMBL; AF053755; AAF21720.1; -; mRNA.
DR EMBL; EU499349; ACB47400.1; -; mRNA.
DR EMBL; EU934246; ACH61958.1; -; mRNA.
DR EMBL; EU934248; ACH61960.1; -; mRNA.
DR EMBL; EU934249; ACH61961.1; -; mRNA.
DR EMBL; EU934250; ACH61962.1; -; mRNA.
DR EMBL; FJ178574; ACI24740.1; -; mRNA.
DR EMBL; FJ178575; ACI24741.1; -; mRNA.
DR EMBL; FJ178576; ACI24742.1; -; mRNA.
DR EMBL; GU354307; ADC32649.1; -; mRNA.
DR EMBL; GU354308; ADC32650.1; -; mRNA.
DR EMBL; GU354309; ADC32651.1; -; mRNA.
DR EMBL; GU354310; ADC32652.1; -; mRNA.
DR EMBL; CR627428; CAH10515.1; -; mRNA.
DR EMBL; AC099535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64382.1; -; Genomic_DNA.
DR CCDS; CCDS33721.1; -. [Q9Y6M7-1]
DR CCDS; CCDS58819.1; -. [Q9Y6M7-2]
DR CCDS; CCDS58820.1; -. [Q9Y6M7-6]
DR CCDS; CCDS82747.1; -. [Q9Y6M7-7]
DR CCDS; CCDS82749.1; -. [Q9Y6M7-8]
DR CCDS; CCDS82750.1; -. [Q9Y6M7-9]
DR CCDS; CCDS82751.1; -. [Q9Y6M7-12]
DR PIR; JE0160; JE0160.
DR RefSeq; NP_001245308.1; NM_001258379.1. [Q9Y6M7-6]
DR RefSeq; NP_001245309.1; NM_001258380.1. [Q9Y6M7-2]
DR RefSeq; NP_001308032.1; NM_001321103.1. [Q9Y6M7-7]
DR RefSeq; NP_001308033.1; NM_001321104.1. [Q9Y6M7-8]
DR RefSeq; NP_001308034.1; NM_001321105.1.
DR RefSeq; NP_001308035.1; NM_001321106.1. [Q9Y6M7-12]
DR RefSeq; NP_001308036.1; NM_001321107.1. [Q9Y6M7-9]
DR RefSeq; NP_001308037.1; NM_001321108.1. [Q9Y6M7-13]
DR RefSeq; NP_003606.3; NM_003615.4. [Q9Y6M7-1]
DR RefSeq; XP_016863017.1; XM_017007528.1. [Q9Y6M7-5]
DR RefSeq; XP_016863018.1; XM_017007529.1. [Q9Y6M7-5]
DR AlphaFoldDB; Q9Y6M7; -.
DR SMR; Q9Y6M7; -.
DR BioGRID; 114876; 167.
DR IntAct; Q9Y6M7; 50.
DR MINT; Q9Y6M7; -.
DR STRING; 9606.ENSP00000295736; -.
DR ChEMBL; CHEMBL3774290; -.
DR DrugBank; DB01390; Sodium bicarbonate.
DR TCDB; 2.A.31.2.11; the anion exchanger (ae) family.
DR GlyGen; Q9Y6M7; 9 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6M7; -.
DR PhosphoSitePlus; Q9Y6M7; -.
DR SwissPalm; Q9Y6M7; -.
DR BioMuta; SLC4A7; -.
DR DMDM; 229462789; -.
DR EPD; Q9Y6M7; -.
DR jPOST; Q9Y6M7; -.
DR MassIVE; Q9Y6M7; -.
DR MaxQB; Q9Y6M7; -.
DR PaxDb; Q9Y6M7; -.
DR PeptideAtlas; Q9Y6M7; -.
DR PRIDE; Q9Y6M7; -.
DR ProteomicsDB; 12778; -.
DR ProteomicsDB; 3404; -.
DR ProteomicsDB; 5941; -.
DR ProteomicsDB; 5942; -.
DR ProteomicsDB; 6243; -.
DR ProteomicsDB; 6244; -.
DR ProteomicsDB; 86734; -. [Q9Y6M7-1]
DR ProteomicsDB; 86735; -. [Q9Y6M7-2]
DR ProteomicsDB; 86736; -. [Q9Y6M7-3]
DR ProteomicsDB; 86737; -. [Q9Y6M7-4]
DR ProteomicsDB; 86738; -. [Q9Y6M7-5]
DR Antibodypedia; 45253; 181 antibodies from 24 providers.
DR DNASU; 9497; -.
DR Ensembl; ENST00000295736.9; ENSP00000295736.5; ENSG00000033867.17. [Q9Y6M7-1]
DR Ensembl; ENST00000428386.5; ENSP00000416368.1; ENSG00000033867.17. [Q9Y6M7-2]
DR Ensembl; ENST00000437179.5; ENSP00000394252.1; ENSG00000033867.17. [Q9Y6M7-9]
DR Ensembl; ENST00000437266.5; ENSP00000409418.1; ENSG00000033867.17. [Q9Y6M7-11]
DR Ensembl; ENST00000438530.5; ENSP00000407304.1; ENSG00000033867.17. [Q9Y6M7-10]
DR Ensembl; ENST00000440156.5; ENSP00000414797.1; ENSG00000033867.17. [Q9Y6M7-8]
DR Ensembl; ENST00000446700.5; ENSP00000406605.1; ENSG00000033867.17. [Q9Y6M7-12]
DR Ensembl; ENST00000454389.6; ENSP00000390394.1; ENSG00000033867.17. [Q9Y6M7-7]
DR Ensembl; ENST00000455077.5; ENSP00000407382.1; ENSG00000033867.17. [Q9Y6M7-6]
DR Ensembl; ENST00000457377.5; ENSP00000408323.1; ENSG00000033867.17. [Q9Y6M7-11]
DR GeneID; 9497; -.
DR KEGG; hsa:9497; -.
DR MANE-Select; ENST00000454389.6; ENSP00000390394.1; NM_001321103.2; NP_001308032.1. [Q9Y6M7-7]
DR UCSC; uc003cdu.6; human. [Q9Y6M7-1]
DR CTD; 9497; -.
DR DisGeNET; 9497; -.
DR GeneCards; SLC4A7; -.
DR HGNC; HGNC:11033; SLC4A7.
DR HPA; ENSG00000033867; Tissue enhanced (intestine, retina).
DR MIM; 603353; gene.
DR neXtProt; NX_Q9Y6M7; -.
DR OpenTargets; ENSG00000033867; -.
DR PharmGKB; PA35899; -.
DR VEuPathDB; HostDB:ENSG00000033867; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000157045; -.
DR HOGENOM; CLU_002289_0_0_1; -.
DR InParanoid; Q9Y6M7; -.
DR OMA; TEENFAC; -.
DR OrthoDB; 863978at2759; -.
DR PhylomeDB; Q9Y6M7; -.
DR TreeFam; TF313630; -.
DR PathwayCommons; Q9Y6M7; -.
DR Reactome; R-HSA-425381; Bicarbonate transporters.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9Y6M7; -.
DR BioGRID-ORCS; 9497; 243 hits in 1085 CRISPR screens.
DR ChiTaRS; SLC4A7; human.
DR GeneWiki; SLC4A7; -.
DR GenomeRNAi; 9497; -.
DR Pharos; Q9Y6M7; Tbio.
DR PRO; PR:Q9Y6M7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6M7; protein.
DR Bgee; ENSG00000033867; Expressed in oocyte and 195 other tissues.
DR ExpressionAtlas; Q9Y6M7; baseline and differential.
DR Genevisible; Q9Y6M7; HS.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
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:0055085; P:transmembrane transport; IBA:GO_Central.
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; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR Pfam; PF07565; Band_3_cyto; 2.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; SSF55804; 2.
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..1214
FT /note="Sodium bicarbonate cotransporter 3"
FT /id="PRO_0000079233"
FT TOPO_DOM 1..608
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..695
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..817
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 839..861
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 883..908
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 930..954
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..1011
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1033..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1035..1055
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1056..1092
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1093..1113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1114..1214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1136
FT /note="CA2-binding"
FT REGION 1144..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1211..1214
FT /note="PDZ-binding"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTY2"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1N3"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1N3"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTY2"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTY2"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1N3"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 1213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 766..768
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 802..814
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT VAR_SEQ 1..450
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_047838"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9610397, ECO:0000303|Ref.3"
FT /id="VSP_047839"
FT VAR_SEQ 1..11
FT /note="MERFRLEKKLP -> MEADGAGEQMRPLLTR (in isoform 6,
FT isoform 9, isoform 10, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047840"
FT VAR_SEQ 1..11
FT /note="MERFRLEKKLP -> MEADGAGEQMRPLLTRVTSR (in isoform 7,
FT isoform 8, isoform 13 and isoform 14)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_047841"
FT VAR_SEQ 91..118
FT /note="SQRVQFILGTEDDDEEHIPHDLFTEMDE -> MAVTQFIHFREEIMGNMFFI
FT IIFSTKDK (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9610397, ECO:0000303|Ref.3"
FT /id="VSP_047842"
FT VAR_SEQ 238..250
FT /note="Missing (in isoform 8, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047843"
FT VAR_SEQ 251..374
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 6, isoform 9, isoform 11, isoform 13 and isoform 14)"
FT /evidence="ECO:0000303|PubMed:10347222,
FT ECO:0000303|PubMed:9610397, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_047844"
FT VAR_SEQ 451..465
FT /note="PAVLLTGLTEVPVPT -> MEVVEAEKIVLLTSA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_047845"
FT VAR_SEQ 581..582
FT /note="LF -> VQ (in isoform 10, isoform 11 and isoform 14)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_047846"
FT VAR_SEQ 583..1214
FT /note="Missing (in isoform 10, isoform 11 and isoform 14)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_047847"
FT VAR_SEQ 1188
FT /note="S -> SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS (in
FT isoform 5, isoform 6, isoform 7, isoform 8 and isoform 13)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.5"
FT /id="VSP_047848"
FT VAR_SEQ 1189..1214
FT /note="PDKPVSVKISFEDEPRKKYVDAETSL -> GDPSIGNISDEMAKTAQWKALS
FT MNTENAKVTRSNMSPDKPVSVK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9610397"
FT /id="VSP_047849"
FT VARIANT 326
FT /note="E -> K (in dbSNP:rs3755652)"
FT /evidence="ECO:0000269|PubMed:10347222, ECO:0000269|Ref.4"
FT /id="VAR_055317"
FT MUTAGEN 1135..1136
FT /note="DD->NN: Loss of interaction with CA2. Loss of
FT regulation by CA2."
FT /evidence="ECO:0000269|PubMed:14736710"
FT MUTAGEN 1163..1165
FT /note="DDD->NNN: No effect on interaction with CA2. No
FT effect on regulation by CA2."
FT /evidence="ECO:0000269|PubMed:14736710"
FT MUTAGEN 1214
FT /note="L->G: Loss of interaction with ATP6V1B1."
FT /evidence="ECO:0000269|PubMed:12444018"
FT MOD_RES Q9Y6M7-2:255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-2:258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-3:165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-3:168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-3:1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-3:1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-3:1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9Y6M7-4:165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-4:168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-5:742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q9Y6M7-5:771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-5:774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-5:780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9Y6M7-6:260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-6:263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-6:1073
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q9Y6M7-6:1102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-6:1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-6:1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9Y6M7-7:1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q9Y6M7-7:1230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-7:1233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-7:1239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9Y6M7-8:1188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q9Y6M7-8:1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-8:1220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-8:1226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9Y6M7-9:260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-9:263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-11:260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-11:263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-13:264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-13:267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-13:1077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q9Y6M7-13:1106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES Q9Y6M7-13:1109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-13:1115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9Y6M7-14:264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q9Y6M7-14:267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
SQ SEQUENCE 1214 AA; 136044 MW; 7B4ADA1E3F26813C CRC64;
MERFRLEKKL PGPDEEAVVD LGKTSSTVNT KFEKEELESH RAVYIGVHVP FSKESRRRHR
HRGHKHHHRR RKDKESDKED GRESPSYDTP SQRVQFILGT EDDDEEHIPH DLFTEMDELC
YRDGEEYEWK ETARWLKFEE DVEDGGDRWS KPYVATLSLH SLFELRSCIL NGTVMLDMRA
STLDEIADMV LDNMIASGQL DESIRENVRE ALLKRHHHQN EKRFTSRIPL VRSFADIGKK
HSDPHLLERN GEGLSASRHS LRTGLSASNL SLRGESPLSL LLGHLLPSSR AGTPAGSRCT
TPVPTPQNSP PSSPSISRLT SRSSQESQRQ APELLVSPAS DDIPTVVIHP PEEDLEAALK
GEEQKNEENV DLTPGILASP QSAPGNLDNS KSGEIKGNGS GGSRENSTVD FSKVDMNFMR
KIPTGAEASN VLVGEVDFLE RPIIAFVRLA PAVLLTGLTE VPVPTRFLFL LLGPAGKAPQ
YHEIGRSIAT LMTDEIFHDV AYKAKDRNDL LSGIDEFLDQ VTVLPPGEWD PSIRIEPPKS
VPSQEKRKIP VFHNGSTPTL GETPKEAAHH AGPELQRTGR LFGGLILDIK RKAPFFLSDF
KDALSLQCLA SILFLYCACM SPVITFGGLL GEATEGRISA IESLFGASLT GIAYSLFAGQ
PLTILGSTGP VLVFEKILYK FCRDYQLSYL SLRTSIGLWT SFLCIVLVAT DASSLVCYIT
RFTEEAFAAL ICIIFIYEAL EKLFDLGETY AFNMHNNLDK LTSYSCVCTE PPNPSNETLA
QWKKDNITAH NISWRNLTVS ECKKLRGVFL GSACGHHGPY IPDVLFWCVI LFFTTFFLSS
FLKQFKTKRY FPTKVRSTIS DFAVFLTIVI MVTIDYLVGV PSPKLHVPEK FEPTHPERGW
IISPLGDNPW WTLLIAAIPA LLCTILIFMD QQITAVIINR KEHKLKKGAG YHLDLLMVGV
MLGVCSVMGL PWFVAATVLS ISHVNSLKVE SECSAPGEQP KFLGIREQRV TGLMIFILMG
LSVFMTSVLK FIPMPVLYGV FLYMGVSSLK GIQLFDRIKL FGMPAKHQPD LIYLRYVPLW
KVHIFTVIQL TCLVLLWVIK VSAAAVVFPM MVLALVFVRK LMDLCFTKRE LSWLDDLMPE
SKKKKEDDKK KKEKEEAERM LQDDDDTVHL PFEGGSLLQI PVKALKYSPD KPVSVKISFE
DEPRKKYVDA ETSL
