SL9B2_HUMAN
ID SL9B2_HUMAN Reviewed; 537 AA.
AC Q86UD5; B5ME52; Q6ZMD8; Q96D95;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sodium/hydrogen exchanger 9B2;
DE AltName: Full=Na(+)/H(+) exchanger NHA2;
DE AltName: Full=Na(+)/H(+) exchanger-like domain-containing protein 2;
DE Short=NHE domain-containing protein 2;
DE AltName: Full=Sodium/hydrogen exchanger-like domain-containing protein 2;
DE AltName: Full=Solute carrier family 9 subfamily B member 2;
GN Name=SLC9B2; Synonyms=NHA2, NHEDC2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Testis;
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 [5]
RP FUNCTION, MUTAGENESIS OF 278-ASP-ASP-279, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18000046; DOI=10.1073/pnas.0707120104;
RA Xiang M., Feng M., Muend S., Rao R.;
RT "A human Na+/H+ antiporter sharing evolutionary origins with bacterial NhaA
RT may be a candidate gene for essential hypertension.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18677-18681(2007).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18508966; DOI=10.1681/asn.2007111245;
RA Fuster D.G., Zhang J., Shi M., Bobulescu I.A., Andersson S., Moe O.W.;
RT "Characterization of the sodium/hydrogen exchanger NHA2.";
RL J. Am. Soc. Nephrol. 19:1547-1556(2008).
RN [7]
RP FUNCTION.
RX PubMed=22948142; DOI=10.1074/jbc.m112.403550;
RA Kondapalli K.C., Kallay L.M., Muszelik M., Rao R.;
RT "Unconventional chemiosmotic coupling of NHA2, a mammalian Na+/H+
RT antiporter, to a plasma membrane H+ gradient.";
RL J. Biol. Chem. 287:36239-36250(2012).
RN [8]
RP MUTAGENESIS OF 278-ASP-ASP-279.
RX PubMed=23720317; DOI=10.1073/pnas.1220009110;
RA Deisl C., Simonin A., Anderegg M., Albano G., Kovacs G., Ackermann D.,
RA Moch H., Dolci W., Thorens B., Hediger M.A., Fuster D.G.;
RT "Sodium/hydrogen exchanger NHA2 is critical for insulin secretion in beta-
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10004-10009(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=28071645; DOI=10.1038/ncomms13993;
RA Landreh M., Marklund E.G., Uzdavinys P., Degiacomi M.T., Coincon M.,
RA Gault J., Gupta K., Liko I., Benesch J.L., Drew D., Robinson C.V.;
RT "Integrating mass spectrometry with MD simulations reveals the role of
RT lipids in Na(+)/H(+) antiporters.";
RL Nat. Commun. 8:13993-13993(2017).
RN [11]
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND MUTAGENESIS OF ARG-432.
RX PubMed=28154142; DOI=10.1073/pnas.1614521114;
RA Uzdavinys P., Coincon M., Nji E., Ndi M., Winkelmann I., von Ballmoos C.,
RA Drew D.;
RT "Dissecting the proton transport pathway in electrogenic Na(+)/H(+)
RT antiporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1101-E1110(2017).
CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes Na(+) or Li(+) in
CC exchange for external protons across the membrane (PubMed:18000046,
CC PubMed:28154142, PubMed:22948142, PubMed:18508966). Contributes to the
CC regulation of intracellular pH, sodium homeostasis, and cell volume.
CC Plays an important role for insulin secretion and clathrin-mediated
CC endocytosis in beta-cells (By similarity). Involved in sperm motility
CC and fertility (By similarity). It is controversial whether SLC9B2 plays
CC a role in osteoclast differentiation or not (By similarity).
CC {ECO:0000250|UniProtKB:Q5BKR2, ECO:0000269|PubMed:18000046,
CC ECO:0000269|PubMed:18508966, ECO:0000269|PubMed:22948142,
CC ECO:0000269|PubMed:28154142}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 mM for Na(+) {ECO:0000269|PubMed:28154142};
CC KM=67 mM for Li(+) {ECO:0000269|PubMed:28154142};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:28154142};
CC -!- SUBUNIT: Homodimer (PubMed:28071645). {ECO:0000269|PubMed:28071645}.
CC -!- INTERACTION:
CC Q86UD5; O15173: PGRMC2; NbExp=3; IntAct=EBI-9916342, EBI-1050125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18000046};
CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:18508966}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-
CC pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5BKR2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5BKR2}. Cell
CC projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q5BKR2};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q5BKR2};
CC Multi-pass membrane protein {ECO:0000255}. Note=Strong colocalization
CC with LAMP1 and TCIRG1 in osteoclasts. In beta-cells colocalizes with
CC RAB4A and SYP. Localizes to the basolateral membrane of polarized
CC osteoclasts. {ECO:0000250|UniProtKB:Q5BKR2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86UD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UD5-2; Sequence=VSP_033152, VSP_033153;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:18508966). High levels
CC detected in the distal tubules of the kidney nephron (PubMed:18508966).
CC Detected in red blood cells (at protein level) (PubMed:18000046,
CC PubMed:18508966). {ECO:0000269|PubMed:18000046,
CC ECO:0000269|PubMed:18508966}.
CC -!- MISCELLANEOUS: Inhibited by phloretin but not by the classical SLC9A-
CC inhibitor amiloride (PubMed:18000046). {ECO:0000269|PubMed:18000046}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
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DR EMBL; AK172823; BAD18790.1; -; mRNA.
DR EMBL; AC097485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06159.1; -; Genomic_DNA.
DR EMBL; BC009732; AAH09732.1; -; mRNA.
DR EMBL; BC047447; AAH47447.2; -; mRNA.
DR CCDS; CCDS3662.1; -. [Q86UD5-1]
DR RefSeq; NP_001287685.1; NM_001300756.1.
DR RefSeq; NP_849155.2; NM_178833.5. [Q86UD5-1]
DR RefSeq; XP_006714148.1; XM_006714085.2.
DR PDB; 7B4L; EM; 3.10 A; A/B=1-537.
DR PDB; 7B4M; EM; 7.20 A; A/B=1-537.
DR PDBsum; 7B4L; -.
DR PDBsum; 7B4M; -.
DR AlphaFoldDB; Q86UD5; -.
DR SMR; Q86UD5; -.
DR BioGRID; 126354; 7.
DR IntAct; Q86UD5; 5.
DR STRING; 9606.ENSP00000378265; -.
DR TCDB; 2.A.36.2.2; the monovalent cation:proton antiporter-1 (cpa1) family.
DR iPTMnet; Q86UD5; -.
DR PhosphoSitePlus; Q86UD5; -.
DR BioMuta; SLC9B2; -.
DR DMDM; 121944426; -.
DR EPD; Q86UD5; -.
DR jPOST; Q86UD5; -.
DR MassIVE; Q86UD5; -.
DR MaxQB; Q86UD5; -.
DR PaxDb; Q86UD5; -.
DR PeptideAtlas; Q86UD5; -.
DR PRIDE; Q86UD5; -.
DR ProteomicsDB; 69803; -. [Q86UD5-1]
DR ProteomicsDB; 69804; -. [Q86UD5-2]
DR Antibodypedia; 26081; 162 antibodies from 24 providers.
DR DNASU; 133308; -.
DR Ensembl; ENST00000362026.7; ENSP00000354574.3; ENSG00000164038.16. [Q86UD5-1]
DR Ensembl; ENST00000394785.9; ENSP00000378265.3; ENSG00000164038.16. [Q86UD5-1]
DR GeneID; 133308; -.
DR KEGG; hsa:133308; -.
DR MANE-Select; ENST00000394785.9; ENSP00000378265.3; NM_178833.7; NP_849155.2.
DR UCSC; uc003hwx.5; human. [Q86UD5-1]
DR CTD; 133308; -.
DR DisGeNET; 133308; -.
DR GeneCards; SLC9B2; -.
DR HGNC; HGNC:25143; SLC9B2.
DR HPA; ENSG00000164038; Tissue enhanced (liver).
DR MIM; 611789; gene.
DR neXtProt; NX_Q86UD5; -.
DR OpenTargets; ENSG00000164038; -.
DR PharmGKB; PA162397515; -.
DR VEuPathDB; HostDB:ENSG00000164038; -.
DR eggNOG; KOG3826; Eukaryota.
DR GeneTree; ENSGT00390000013285; -.
DR HOGENOM; CLU_018415_4_1_1; -.
DR InParanoid; Q86UD5; -.
DR OMA; PAILMCF; -.
DR PhylomeDB; Q86UD5; -.
DR TreeFam; TF319087; -.
DR PathwayCommons; Q86UD5; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; Q86UD5; -.
DR BioGRID-ORCS; 133308; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; SLC9B2; human.
DR GenomeRNAi; 133308; -.
DR Pharos; Q86UD5; Tbio.
DR PRO; PR:Q86UD5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q86UD5; protein.
DR Bgee; ENSG00000164038; Expressed in sural nerve and 143 other tissues.
DR ExpressionAtlas; Q86UD5; baseline and differential.
DR Genevisible; Q86UD5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0010348; F:lithium:proton antiporter activity; IMP:UniProtKB.
DR GO; GO:0005451; F:monovalent cation:proton antiporter activity; TAS:Reactome.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IMP:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:2001206; P:positive regulation of osteoclast development; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR037072; SLC9B2.
DR PANTHER; PTHR31102:SF14; PTHR31102:SF14; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiport; Cell membrane;
KW Cell projection; Cilium; Cytoplasmic vesicle; Endosome; Flagellum;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..537
FT /note="Sodium/hydrogen exchanger 9B2"
FT /id="PRO_0000331270"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 278
FT /note="Important for cation transport"
FT /evidence="ECO:0000269|PubMed:18000046"
FT SITE 279
FT /note="Important for cation transport"
FT /evidence="ECO:0000269|PubMed:18000046"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 420..502
FT /note="LCVATVGIAVLIRILTTFLMVCFAGFNLKEKIFISFAWLPKATVQAAIGSVA
FT LDTARSHGEKQLEDYGMDVLTVAFLSILITA -> SADSITGNFGTERPKLLGPPSTQL
FT RFHFFHIQLST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033152"
FT VAR_SEQ 503..537
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033153"
FT VARIANT 159
FT /note="I -> T (in dbSNP:rs7672710)"
FT /id="VAR_042751"
FT VARIANT 161
FT /note="V -> A (in dbSNP:rs7672707)"
FT /id="VAR_042752"
FT VARIANT 357
FT /note="F -> C (in dbSNP:rs2276976)"
FT /id="VAR_042753"
FT MUTAGEN 278..279
FT /note="DD->CC: Loss of ion transport activity; Does not
FT rescue insulin secretion defect induced by knockdown of
FT SLC9B2 in Min6 cells."
FT /evidence="ECO:0000269|PubMed:18000046,
FT ECO:0000269|PubMed:23720317"
FT MUTAGEN 432
FT /note="R->K,H: Loss of ion transport activity;."
FT /evidence="ECO:0000269|PubMed:28154142"
FT HELIX 83..105
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 114..133
FT /evidence="ECO:0007829|PDB:7B4L"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7B4L"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 170..189
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 202..223
FT /evidence="ECO:0007829|PDB:7B4L"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:7B4L"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:7B4L"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 277..294
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 299..326
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 335..357
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 362..377
FT /evidence="ECO:0007829|PDB:7B4L"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 383..405
FT /evidence="ECO:0007829|PDB:7B4L"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 419..439
FT /evidence="ECO:0007829|PDB:7B4L"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 447..455
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 462..467
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 470..478
FT /evidence="ECO:0007829|PDB:7B4L"
FT HELIX 482..516
FT /evidence="ECO:0007829|PDB:7B4L"
SQ SEQUENCE 537 AA; 57564 MW; 85A8BDA60ABE2587 CRC64;
MGDEDKRITY EDSEPSTGMN YTPSMHQEAQ EETVMKLKGI DANEPTEGSI LLKSSEKKLQ
ETPTEANHVQ RLRQMLACPP HGLLDRVITN VTIIVLLWAV VWSITGSECL PGGNLFGIII
LFYCAIIGGK LLGLIKLPTL PPLPSLLGML LAGFLIRNIP VINDNVQIKH KWSSSLRSIA
LSIILVRAGL GLDSKALKKL KGVCVRLSMG PCIVEACTSA LLAHYLLGLP WQWGFILGFV
LGAVSPAVVV PSMLLLQGGG YGVEKGVPTL LMAAGSFDDI LAITGFNTCL GIAFSTGSTV
FNVLRGVLEV VIGVATGSVL GFFIQYFPSR DQDKLVCKRT FLVLGLSVLA VFSSVHFGFP
GSGGLCTLVM AFLAGMGWTS EKAEVEKIIA VAWDIFQPLL FGLIGAEVSI ASLRPETVGL
CVATVGIAVL IRILTTFLMV CFAGFNLKEK IFISFAWLPK ATVQAAIGSV ALDTARSHGE
KQLEDYGMDV LTVAFLSILI TAPIGSLLIG LLGPRLLQKV EHQNKDEEVQ GETSVQV
