ID   S4A8_HUMAN              Reviewed;        1093 AA.
AC   Q2Y0W8; A0MMZ1; B4DHY0; E7EML0; F5GZ31; F5H7F5; O94843; O95233; Q004B4;
AC   Q8N3U2; Q8TC60; Q9UKX8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Electroneutral sodium bicarbonate exchanger 1;
DE   AltName: Full=Electroneutral Na(+)-driven Cl-HCO3 exchanger;
DE   AltName: Full=Solute carrier family 4 member 8;
DE   AltName: Full=k-NBC3;
GN   Name=SLC4A8 {ECO:0000312|EMBL:AAY79176.1,
GN   ECO:0000312|HGNC:HGNC:11034};
GN   Synonyms=KIAA0739, NBC {ECO:0000312|EMBL:AAC82380.1}, NBC3
GN   {ECO:0000303|PubMed:10362779}, NDCBE1 {ECO:0000303|PubMed:11133997};
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] {ECO:0000305, ECO:0000312|EMBL:AAC82380.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, ACTIVITY
RP   REGULATION (ISOFORM 3), AND TRANSPORTER ACTIVITY (ISOFORM 3).
RC   TISSUE=Frontal cortex {ECO:0000312|EMBL:AAC82380.1};
RX   PubMed=11133997; DOI=10.1074/jbc.c000716200;
RA   Grichtchenko I.I., Choi I., Zhong X., Bray-Ward P., Russell J.M.,
RA   Boron W.F.;
RT   "Cloning, characterization, and chromosomal mapping of a human
RT   electroneutral Na(+)-driven Cl-HCO3 exchanger.";
RL   J. Biol. Chem. 276:8358-8363(2001).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAY79176.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 5), ALTERNATIVE SPLICING
RP   (ISOFORM 3), FUNCTION, TRANSPORTER ACTIVITY (ISOFORMS 1; 3; 4 AND 5),
RP   ACTIVITY REGULATION (ISOFORMS 1; 3; 4 AND 5), SUBCELLULAR LOCATION
RP   (ISOFORMS 1; 3; 4 AND 5), AND TISSUE SPECIFICITY (ISOFORMS 1; 4 AND 5).
RC   TISSUE=Brain {ECO:0000312|EMBL:AAY79176.1}, and Heart
RC   {ECO:0000312|EMBL:ABJ91577.1};
RX   PubMed=18577713; DOI=10.1152/physiolgenomics.90259.2008;
RA   Parker M.D., Bouyer P., Daly C.M., Boron W.F.;
RT   "Cloning and characterization of novel human SLC4A8 gene products encoding
RT   Na+-driven Cl-/HCO3(-) exchanger variants NDCBE-A, -C, and -D.";
RL   Physiol. Genomics 34:265-276(2008).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:BAA34459.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain {ECO:0000312|EMBL:BAA34459.1};
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC   TISSUE=Caudate nucleus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   TISSUE=Amygdala;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [7] {ECO:0000305, ECO:0000312|EMBL:AAY79176.1}
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   [8] {ECO:0000305, ECO:0000312|EMBL:AAH25994.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Testis {ECO:0000312|EMBL:AAH25994.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9] {ECO:0000305, ECO:0000312|EMBL:AAD52981.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-670 (ISOFORMS 1/3/6), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Testis carcinoma {ECO:0000269|PubMed:10362779};
RX   PubMed=10362779; DOI=10.1152/ajprenal.1999.276.6.f903;
RA   Amlal H., Burnham C.E., Soleimani M.;
RT   "Characterization of Na+/HCO-3 cotransporter isoform NBC-3.";
RL   Am. J. Physiol. 276:F903-F913(1999).
RN   [10]
RP   ERRATUM OF PUBMED:10362779.
RA   Amlal H., Burnham C.E., Soleimani M.;
RL   Am. J. Physiol. 277:F477-F477(1999).
RN   [11] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17715183; DOI=10.1152/ajpregu.00356.2007;
RA   Damkier H.H., Nielsen S., Praetorius J.;
RT   "Molecular expression of SLC4-derived Na+-dependent anion transporters in
RT   selected human tissues.";
RL   Am. J. Physiol. 293:R2136-R2146(2007).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-344 (ISOFORM 4), SUBUNIT
RP   (ISOFORM 4), MUTAGENESIS OF TRP-80; HIS-167 AND HIS-169 (ISOFORM 4),
RP   ZINC-BINDING (ISOFORM 4), AND ACTIVITY REGULATION (ISOFORM 4).
RX   PubMed=28935959; DOI=10.1038/s41598-017-12409-0;
RA   Alvadia C.M., Sommer T., Bjerregaard-Andersen K., Damkier H.H.,
RA   Montrasio M., Aalkjaer C., Morth J.P.;
RT   "The crystal structure of the regulatory domain of the human sodium-driven
RT   chloride/bicarbonate exchanger.";
RL   Sci. Rep. 7:12131-12131(2017).
CC   -!- FUNCTION: Mediates electroneutral sodium- and carbonate-dependent
CC       chloride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of 2:1
CC       (PubMed:18577713). Plays a major role in pH regulation in neurons (By
CC       similarity). Mediates sodium reabsorption in the renal cortical
CC       collecting ducts (By similarity). {ECO:0000250|UniProtKB:Q8JZR6,
CC       ECO:0000269|PubMed:18577713}.
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) =
CC         chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:72739, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:18577713};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
CC       Reaction=chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) =
CC         chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:72739, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:11133997,
CC         ECO:0000269|PubMed:18577713};
CC   -!- CATALYTIC ACTIVITY: [Isoform 4]:
CC       Reaction=chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) =
CC         chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:72739, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:18577713};
CC   -!- CATALYTIC ACTIVITY: [Isoform 5]:
CC       Reaction=chloride(in) + 2 hydrogencarbonate(out) + Na(+)(out) =
CC         chloride(out) + 2 hydrogencarbonate(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:72739, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:18577713};
CC   -!- ACTIVITY REGULATION: [Isoform 1]: Activity is inhibited by 4,4'-Di-
CC       isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of
CC       several anion channels and transporters).
CC       {ECO:0000269|PubMed:18577713}.
CC   -!- ACTIVITY REGULATION: [Isoform 3]: Activity is inhibited by 4,4'-Di-
CC       isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of
CC       several anion channels and transporters). {ECO:0000269|PubMed:11133997,
CC       ECO:0000269|PubMed:18577713}.
CC   -!- ACTIVITY REGULATION: [Isoform 4]: Activity is inhibited by 4,4'-Di-
CC       isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of
CC       several anion channels and transporters) (PubMed:18577713). Zinc-
CC       binding negatively regulates its activity (Probable).
CC       {ECO:0000269|PubMed:18577713, ECO:0000305|PubMed:28935959}.
CC   -!- ACTIVITY REGULATION: [Isoform 5]: Activity is inhibited by 4,4'-Di-
CC       isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of
CC       several anion channels and transporters).
CC       {ECO:0000269|PubMed:18577713}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6RVG2}.
CC   -!- SUBUNIT: [Isoform 4]: Homodimer. {ECO:0000269|PubMed:15489334}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:17715183}; Multi-pass membrane protein
CC       {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q6RVG2}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC       membrane {ECO:0000250|UniProtKB:Q6RVG2}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC       {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane
CC       {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane
CC       {ECO:0000269|PubMed:18577713}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1 {ECO:0000269|PubMed:18577713}; Synonyms=NDCBE-A
CC       {ECO:0000303|PubMed:18577713};
CC         IsoId=Q2Y0W8-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:9872452};
CC         IsoId=Q2Y0W8-2; Sequence=VSP_052760, VSP_052765;
CC       Name=3 {ECO:0000269|PubMed:11133997}; Synonyms=NDCBE-B
CC       {ECO:0000303|PubMed:18577713};
CC         IsoId=Q2Y0W8-3; Sequence=VSP_052765;
CC       Name=4 {ECO:0000269|PubMed:11133997}; Synonyms=NDCBE-D
CC       {ECO:0000303|PubMed:18577713};
CC         IsoId=Q2Y0W8-4; Sequence=VSP_052759, VSP_052765;
CC       Name=5 {ECO:0000269|PubMed:18577713}; Synonyms=NDCBE-C
CC       {ECO:0000303|PubMed:18577713};
CC         IsoId=Q2Y0W8-5; Sequence=VSP_052759;
CC       Name=6 {ECO:0000269|PubMed:15489334};
CC         IsoId=Q2Y0W8-6; Sequence=VSP_052761, VSP_052762;
CC       Name=7;
CC         IsoId=Q2Y0W8-7; Sequence=VSP_052759, VSP_052763, VSP_052764;
CC       Name=8;
CC         IsoId=Q2Y0W8-8; Sequence=VSP_052759, VSP_052761, VSP_052762;
CC   -!- TISSUE SPECIFICITY: Expressed in the pyramidal cells of the hippocampus
CC       (at protein level). Highly expressed in all major regions of the brain,
CC       spinal column and in testis, and moderate levels in trachea, thyroid
CC       and medulla region of kidney. Low expression levels observed in
CC       pancreas and kidney cortex. {ECO:0000269|PubMed:10362779,
CC       ECO:0000269|PubMed:11133997, ECO:0000269|PubMed:17715183}.
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in the brain.
CC       {ECO:0000269|PubMed:18577713}.
CC   -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in the brain, heart and
CC       kidney. {ECO:0000269|PubMed:18577713}.
CC   -!- TISSUE SPECIFICITY: [Isoform 5]: Expressed in the brain, heart and
CC       kidney. {ECO:0000269|PubMed:18577713}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34459.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD38576.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF069512; AAC82380.1; -; mRNA.
DR   EMBL; DQ063579; AAY79176.1; -; mRNA.
DR   EMBL; DQ975204; ABJ09587.1; -; mRNA.
DR   EMBL; DQ996537; ABJ91576.1; -; mRNA.
DR   EMBL; DQ996398; ABJ91577.1; -; mRNA.
DR   EMBL; AB018282; BAA34459.1; ALT_INIT; mRNA.
DR   EMBL; AK295315; BAG58292.1; -; mRNA.
DR   EMBL; AL831915; CAD38576.2; ALT_INIT; mRNA.
DR   EMBL; AC025097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC046135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471111; EAW58192.1; -; Genomic_DNA.
DR   EMBL; BC025994; AAH25994.1; -; mRNA.
DR   EMBL; AF107099; AAD52981.1; -; mRNA.
DR   CCDS; CCDS44890.1; -. [Q2Y0W8-1]
DR   CCDS; CCDS58232.1; -. [Q2Y0W8-7]
DR   CCDS; CCDS58233.1; -. [Q2Y0W8-8]
DR   CCDS; CCDS73470.1; -. [Q2Y0W8-5]
DR   RefSeq; NP_001035049.1; NM_001039960.2. [Q2Y0W8-1]
DR   RefSeq; NP_001245330.1; NM_001258401.2. [Q2Y0W8-5]
DR   RefSeq; NP_001245331.1; NM_001258402.1. [Q2Y0W8-6]
DR   RefSeq; NP_001245332.1; NM_001258403.1. [Q2Y0W8-7]
DR   RefSeq; NP_001254544.1; NM_001267615.1. [Q2Y0W8-8]
DR   RefSeq; XP_016875730.1; XM_017020241.1.
DR   PDB; 5JHO; X-ray; 2.80 A; A/B=54-397.
DR   PDBsum; 5JHO; -.
DR   AlphaFoldDB; Q2Y0W8; -.
DR   SMR; Q2Y0W8; -.
DR   BioGRID; 114877; 35.
DR   IntAct; Q2Y0W8; 30.
DR   STRING; 9606.ENSP00000405812; -.
DR   DrugBank; DB01390; Sodium bicarbonate.
DR   TCDB; 2.A.31.2.4; the anion exchanger (ae) family.
DR   GlyGen; Q2Y0W8; 1 site.
DR   iPTMnet; Q2Y0W8; -.
DR   PhosphoSitePlus; Q2Y0W8; -.
DR   SwissPalm; Q2Y0W8; -.
DR   BioMuta; SLC4A8; -.
DR   DMDM; 121942008; -.
DR   EPD; Q2Y0W8; -.
DR   jPOST; Q2Y0W8; -.
DR   MassIVE; Q2Y0W8; -.
DR   MaxQB; Q2Y0W8; -.
DR   PaxDb; 9606-ENSP00000405812; -.
DR   PeptideAtlas; Q2Y0W8; -.
DR   ProteomicsDB; 16963; -.
DR   ProteomicsDB; 24921; -.
DR   ProteomicsDB; 61540; -. [Q2Y0W8-1]
DR   ProteomicsDB; 61541; -. [Q2Y0W8-2]
DR   ProteomicsDB; 61542; -. [Q2Y0W8-3]
DR   ProteomicsDB; 61543; -. [Q2Y0W8-4]
DR   ProteomicsDB; 61544; -. [Q2Y0W8-5]
DR   ProteomicsDB; 61545; -. [Q2Y0W8-6]
DR   ProteomicsDB; 61546; -. [Q2Y0W8-7]
DR   Antibodypedia; 26410; 193 antibodies from 25 providers.
DR   DNASU; 9498; -.
DR   Ensembl; ENST00000358657.7; ENSP00000351483.4; ENSG00000050438.17. [Q2Y0W8-5]
DR   Ensembl; ENST00000453097.7; ENSP00000405812.2; ENSG00000050438.17. [Q2Y0W8-1]
DR   Ensembl; ENST00000514353.7; ENSP00000442561.2; ENSG00000050438.17. [Q2Y0W8-7]
DR   Ensembl; ENST00000535225.6; ENSP00000441520.1; ENSG00000050438.17. [Q2Y0W8-8]
DR   GeneID; 9498; -.
DR   KEGG; hsa:9498; -.
DR   MANE-Select; ENST00000453097.7; ENSP00000405812.2; NM_001039960.3; NP_001035049.1.
DR   UCSC; uc001rys.3; human. [Q2Y0W8-1]
DR   AGR; HGNC:11034; -.
DR   CTD; 9498; -.
DR   DisGeNET; 9498; -.
DR   GeneCards; SLC4A8; -.
DR   HGNC; HGNC:11034; SLC4A8.
DR   HPA; ENSG00000050438; Group enriched (brain, pituitary gland, retina, testis).
DR   MIM; 605024; gene.
DR   neXtProt; NX_Q2Y0W8; -.
DR   OpenTargets; ENSG00000050438; -.
DR   PharmGKB; PA35900; -.
DR   VEuPathDB; HostDB:ENSG00000050438; -.
DR   eggNOG; KOG1172; Eukaryota.
DR   GeneTree; ENSGT00940000157422; -.
DR   HOGENOM; CLU_002289_5_3_1; -.
DR   InParanoid; Q2Y0W8; -.
DR   OMA; VCHIEAE; -.
DR   OrthoDB; 1013180at2759; -.
DR   PhylomeDB; Q2Y0W8; -.
DR   TreeFam; TF313630; -.
DR   PathwayCommons; Q2Y0W8; -.
DR   Reactome; R-HSA-425381; Bicarbonate transporters.
DR   SignaLink; Q2Y0W8; -.
DR   SIGNOR; Q2Y0W8; -.
DR   BioGRID-ORCS; 9498; 17 hits in 1150 CRISPR screens.
DR   ChiTaRS; SLC4A8; human.
DR   GeneWiki; SLC4A8; -.
DR   GenomeRNAi; 9498; -.
DR   Pharos; Q2Y0W8; Tbio.
DR   PRO; PR:Q2Y0W8; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q2Y0W8; Protein.
DR   Bgee; ENSG00000050438; Expressed in pons and 168 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032279; C:asymmetric synapse; ISS:ARUK-UCL.
DR   GO; GO:0043679; C:axon terminus; ISS:ARUK-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR   GO; GO:0097386; C:glial cell projection; ISS:ARUK-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; ISS:ARUK-UCL.
DR   GO; GO:0097457; C:hippocampal mossy fiber; ISS:ARUK-UCL.
DR   GO; GO:0016020; C:membrane; ISS:ARUK-UCL.
DR   GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISS:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; ISS:ARUK-UCL.
DR   GO; GO:0042734; C:presynaptic membrane; ISS:ARUK-UCL.
DR   GO; GO:0032280; C:symmetric synapse; ISS:ARUK-UCL.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:ARUK-UCL.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043195; C:terminal bouton; ISS:ARUK-UCL.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0140892; F:sodium,bicarbonate:chloride antiporter activity; IDA:UniProtKB.
DR   GO; GO:0008510; F:sodium:bicarbonate symporter activity; IDA:ARUK-UCL.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; TAS:Reactome.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0110010; P:basolateral protein secretion; IEA:Ensembl.
DR   GO; GO:0015701; P:bicarbonate transport; IDA:ARUK-UCL.
DR   GO; GO:1902476; P:chloride transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:ARUK-UCL.
DR   GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; ISS:ARUK-UCL.
DR   GO; GO:0051453; P:regulation of intracellular pH; IDA:ARUK-UCL.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:ARUK-UCL.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 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   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF37; ELECTRONEUTRAL SODIUM BICARBONATE EXCHANGER 1; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   Genevisible; Q2Y0W8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Anion exchange; Antiport;
KW   Cell membrane; Coiled coil; Cytoplasmic vesicle; Disulfide bond;
KW   Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW   Sodium transport; Synapse; Transmembrane; Transmembrane helix; Transport;
KW   Zinc.
FT   CHAIN           1..1093
FT                   /note="Electroneutral sodium bicarbonate exchanger 1"
FT                   /id="PRO_0000328922"
FT   TOPO_DOM        1..478
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        479..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        500..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..565
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        587..595
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        596..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        617..687
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        688..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        709..731
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        732..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        753..778
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        779..799
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        800..824
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        825..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        846..881
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        882..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        903..904
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        905..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        926..962
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        963..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        984..1093
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1010..1036
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        57..77
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        646
FT                   /note="N-linked (GlcNAc) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RVG2"
FT   DISULFID        636..684
FT                   /evidence="ECO:0000250|UniProtKB:Q6RVG2"
FT   DISULFID        638..672
FT                   /evidence="ECO:0000250|UniProtKB:Q6RVG2"
FT   VAR_SEQ         1..53
FT                   /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT                   isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:18577713"
FT                   /id="VSP_052759"
FT   VAR_SEQ         1..16
FT                   /note="MPAAGSNEPDGVLSYQ -> MFNKNNSNKLRSTPRYRRGDPGYLNFTELGPL
FT                   KPEQKDQWSQH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9872452"
FT                   /id="VSP_052760"
FT   VAR_SEQ         671..691
FT                   /note="ECQEMHGEFMGSACGHHGPYT -> VSLGAARCPSIVTTGLGGTSK (in
FT                   isoform 6 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052761"
FT   VAR_SEQ         692..1093
FT                   /note="Missing (in isoform 6 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052762"
FT   VAR_SEQ         725..800
FT                   /note="VRSMVSDFAVFLTIFTMVIIDFLIGVPSPKLQVPSVFKPTRDDRGWIINPIG
FT                   PNPWWTVIAAIIPALLCTILIFMD -> MESCSVAWLECGGVILAHCNLRLLPSSWDYR
FT                   HAPPQPANFCIFSRDGVSPCWPGWSQSLDLVICLPRPPKMLGLQA (in isoform
FT                   7)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_052763"
FT   VAR_SEQ         801..1093
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_052764"
FT   VAR_SEQ         1028..1093
FT                   /note="EAEKMLEIGGDKFPLESRKLLSSPGKNISCRCDPSEINISDEMPKTTVWKAL
FT                   SMNSGNAKEKSLFN -> VIVLAPTVYLGASNYRT (in isoform 2, isoform
FT                   3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11133997,
FT                   ECO:0000303|PubMed:18577713, ECO:0000303|PubMed:9872452"
FT                   /id="VSP_052765"
FT   VARIANT         312
FT                   /note="D -> A (in dbSNP:rs35966334)"
FT                   /id="VAR_048351"
FT   VARIANT         898
FT                   /note="I -> V (in dbSNP:rs12318785)"
FT                   /id="VAR_048352"
FT   CONFLICT        482
FT                   /note="F -> L (in Ref. 4; BAG58292)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1008
FT                   /note="M -> T (in Ref. 1; AAC82380)"
FT                   /evidence="ECO:0000305"
FT   HELIX           98..104
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          116..125
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          133..147
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           163..175
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          176..182
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           187..195
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   TURN            198..201
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           206..216
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          299..308
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          315..325
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   TURN            328..330
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          337..345
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           350..363
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           367..375
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   HELIX           379..392
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   STRAND          394..396
FT                   /evidence="ECO:0007829|PDB:5JHO"
FT   MOTIF           Q2Y0W8-4:340..344
FT                   /note="VTVLP; mediates dimerization"
FT                   /evidence="ECO:0000269|PubMed:28935959"
FT   BINDING         Q2Y0W8-4:167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305|PubMed:28935959"
FT   BINDING         Q2Y0W8-4:169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305|PubMed:28935959"
FT   MUTAGEN         Q2Y0W8-4:80
FT                   /note="W->F: Significant reduction in zinc binding."
FT                   /evidence="ECO:0000269|PubMed:28935959"
FT   MUTAGEN         Q2Y0W8-4:167
FT                   /note="H->A: Significant reduction in zinc binding."
FT                   /evidence="ECO:0000269|PubMed:28935959"
FT   MUTAGEN         Q2Y0W8-4:169
FT                   /note="H->A: Significant reduction in zinc binding."
FT                   /evidence="ECO:0000269|PubMed:28935959"
FT   CONFLICT        Q2Y0W8-7:707
FT                   /note="Q -> R (in Ref. 5; CAD38576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q2Y0W8-7:716
FT                   /note="R -> G (in Ref. 5; CAD38576)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1093 AA;  122938 MW;  DDF9D0BC3CBD1A06 CRC64;
     MPAAGSNEPD GVLSYQRPDE EAVVDQGGTS TILNIHYEKE ELEGHRTLYV GVRMPLGRQS
     HRHHRTHGQK HRRRGRGKGA SQGEEGLEAL AHDTPSQRVQ FILGTEEDEE HVPHELFTEL
     DEICMKEGED AEWKETARWL KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCLINGTVLL
     DMHANSIEEI SDLILDQQEL SSDLNDSMRV KVREALLKKH HHQNEKKRNN LIPIVRSFAE
     VGKKQSDPHL MDKHGQTVSP QSVPTTNLEV KNGVNCEHSP VDLSKVDLHF MKKIPTGAEA
     SNVLVGEVDI LDRPIVAFVR LSPAVLLSGL TEVPIPTRFL FILLGPVGKG QQYHEIGRSM
     ATIMTDEIFH DVAYKAKERD DLLAGIDEFL DQVTVLPPGE WDPSIRIEPP KNVPSQEKRK
     MPGVPNGNVC HIEQEPHGGH SGPELQRTGR LFGGLVLDIK RKAPWYWSDY RDALSLQCLA
     SFLFLYCACM SPVITFGGLL GEATEGRISA IESLFGASMT GIAYSLFAGQ ALTILGSTGP
     VLVFEKILFK FCKDYALSYL SLRACIGLWT AFLCIVLVAT DASSLVCYIT RFTEEAFASL
     ICIIFIYEAI EKLIHLAETY PIHMHSQLDH LSLYYCRCTL PENPNNHTLQ YWKDHNIVTA
     EVHWANLTVS ECQEMHGEFM GSACGHHGPY TPDVLFWSCI LFFTTFILSS TLKTFKTSRY
     FPTRVRSMVS DFAVFLTIFT MVIIDFLIGV PSPKLQVPSV FKPTRDDRGW IINPIGPNPW
     WTVIAAIIPA LLCTILIFMD QQITAVIINR KEHKLKKGCG YHLDLLMVAI MLGVCSIMGL
     PWFVAATVLS ITHVNSLKLE SECSAPGEQP KFLGIREQRV TGLMIFVLMG CSVFMTAILK
     FIPMPVLYGV FLYMGVSSLQ GIQFFDRLKL FGMPAKHQPD FIYLRHVPLR KVHLFTLIQL
     TCLVLLWVIK ASPAAIVFPM MVLALVFVRK VMDLCFSKRE LSWLDDLMPE SKKKKLDDAK
     KKAKEEEEAE KMLEIGGDKF PLESRKLLSS PGKNISCRCD PSEINISDEM PKTTVWKALS
     MNSGNAKEKS LFN
//