B3A2_HUMAN
ID B3A2_HUMAN Reviewed; 1241 AA.
AC P04920; B2R6T0; B4DIT0; D3DX05; F8W682; Q45EY5; Q969L3;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 4.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Anion exchange protein 2;
DE Short=AE 2;
DE Short=Anion exchanger 2;
DE AltName: Full=Non-erythroid band 3-like protein;
DE Short=BND3L;
DE AltName: Full=Solute carrier family 4 member 2;
GN Name=SLC4A2; Synonyms=AE2, EPB3L1, HKB3, MPB3L;
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 A).
RX PubMed=1562608; DOI=10.1016/0167-4781(92)90446-7;
RA Gehrig H., Mueller W., Appelhans H.;
RT "Complete nucleotide sequence of band 3 related anion transport protein AE2
RT from human kidney.";
RL Biochim. Biophys. Acta 1130:326-328(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-26; VAL-202; TRP-311
RP AND PHE-1204.
RG NIEHS SNPs program;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND 3).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 375-1241.
RX PubMed=3015590; DOI=10.1002/j.1460-2075.1986.tb04348.x;
RA Demuth D.R., Showe L.C., Ballantine M., Palumbo A., Fraser P.J., Cioe L.,
RA Rovera G., Curtis P.J.;
RT "Cloning and structural characterization of a human non-erythroid band 3-
RT like protein.";
RL EMBO J. 5:1205-1214(1986).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-132; SER-173 AND
RP THR-183, AND 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [15]
RP IDENTIFICATION BY 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 [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-274, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [17]
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: Plasma membrane anion exchange protein of wide distribution.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=A;
CC IsoId=P04920-1; Sequence=Displayed;
CC Name=B1;
CC IsoId=P04920-2; Sequence=VSP_000456;
CC Name=3;
CC IsoId=P04920-3; Sequence=VSP_045953;
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/slc4a2/";
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DR EMBL; X62137; CAA44067.1; -; mRNA.
DR EMBL; DQ149844; AAZ38724.1; -; Genomic_DNA.
DR EMBL; AK295767; BAG58592.1; -; mRNA.
DR EMBL; AK312699; BAG35577.1; -; mRNA.
DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471173; EAW54046.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54047.1; -; Genomic_DNA.
DR EMBL; BC009386; AAH09386.1; -; mRNA.
DR EMBL; BC009434; AAH09434.1; -; mRNA.
DR EMBL; X03918; CAA27556.1; -; mRNA.
DR CCDS; CCDS56520.1; -. [P04920-3]
DR CCDS; CCDS56521.1; -. [P04920-2]
DR CCDS; CCDS5917.1; -. [P04920-1]
DR PIR; S21086; S21086.
DR RefSeq; NP_001186621.1; NM_001199692.2. [P04920-1]
DR RefSeq; NP_001186622.1; NM_001199693.1. [P04920-3]
DR RefSeq; NP_001186623.1; NM_001199694.2. [P04920-2]
DR RefSeq; NP_003031.3; NM_003040.3. [P04920-1]
DR AlphaFoldDB; P04920; -.
DR SMR; P04920; -.
DR BioGRID; 112413; 149.
DR IntAct; P04920; 40.
DR MINT; P04920; -.
DR STRING; 9606.ENSP00000419412; -.
DR TCDB; 2.A.31.1.2; the anion exchanger (ae) family.
DR GlyGen; P04920; 3 sites.
DR iPTMnet; P04920; -.
DR MetOSite; P04920; -.
DR PhosphoSitePlus; P04920; -.
DR SwissPalm; P04920; -.
DR BioMuta; SLC4A2; -.
DR DMDM; 85687559; -.
DR EPD; P04920; -.
DR jPOST; P04920; -.
DR MassIVE; P04920; -.
DR MaxQB; P04920; -.
DR PaxDb; P04920; -.
DR PeptideAtlas; P04920; -.
DR PRIDE; P04920; -.
DR ProteomicsDB; 29739; -.
DR ProteomicsDB; 51757; -. [P04920-1]
DR ProteomicsDB; 51758; -. [P04920-2]
DR Antibodypedia; 18690; 161 antibodies from 29 providers.
DR DNASU; 6522; -.
DR Ensembl; ENST00000392826.6; ENSP00000376571.2; ENSG00000164889.15. [P04920-3]
DR Ensembl; ENST00000413384.7; ENSP00000405600.2; ENSG00000164889.15. [P04920-1]
DR Ensembl; ENST00000461735.1; ENSP00000419164.1; ENSG00000164889.15. [P04920-2]
DR Ensembl; ENST00000485713.5; ENSP00000419412.1; ENSG00000164889.15. [P04920-1]
DR GeneID; 6522; -.
DR KEGG; hsa:6522; -.
DR MANE-Select; ENST00000413384.7; ENSP00000405600.2; NM_003040.4; NP_003031.3.
DR UCSC; uc003wit.4; human. [P04920-1]
DR CTD; 6522; -.
DR DisGeNET; 6522; -.
DR GeneCards; SLC4A2; -.
DR HGNC; HGNC:11028; SLC4A2.
DR HPA; ENSG00000164889; Tissue enriched (choroid).
DR MIM; 109280; gene.
DR neXtProt; NX_P04920; -.
DR OpenTargets; ENSG00000164889; -.
DR PharmGKB; PA35896; -.
DR VEuPathDB; HostDB:ENSG00000164889; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000158259; -.
DR InParanoid; P04920; -.
DR OMA; GFHLDIV; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; P04920; -.
DR TreeFam; TF313630; -.
DR PathwayCommons; P04920; -.
DR Reactome; R-HSA-425381; Bicarbonate transporters.
DR SignaLink; P04920; -.
DR SIGNOR; P04920; -.
DR BioGRID-ORCS; 6522; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; SLC4A2; human.
DR GeneWiki; SLC4A2; -.
DR GenomeRNAi; 6522; -.
DR Pharos; P04920; Tbio.
DR PRO; PR:P04920; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P04920; protein.
DR Bgee; ENSG00000164889; Expressed in body of stomach and 179 other tissues.
DR ExpressionAtlas; P04920; baseline and differential.
DR Genevisible; P04920; HS.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008509; F:anion transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0005452; F:inorganic anion exchanger activity; TAS:Reactome.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0097186; P:amelogenesis; ISS:ARUK-UCL.
DR GO; GO:0006820; P:anion transport; TAS:ProtInc.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0070175; P:positive regulation of enamel mineralization; ISS:ARUK-UCL.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR001717; Anion_exchange.
DR InterPro; IPR002978; Anion_exchange_2.
DR InterPro; IPR018241; Anion_exchange_CS.
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 PANTHER; PTHR11453:SF14; PTHR11453:SF14; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01188; ANIONEXHNGR2.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Anion exchange; Antiport; Glycoprotein;
KW Ion transport; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1241
FT /note="Anion exchange protein 2"
FT /id="PRO_0000079215"
FT TOPO_DOM 1..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 784..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..900
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 901..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..933
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1010
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1036..1059
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1091..1136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1163..1199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..1241
FT /note="Membrane (anion exchange)"
FT COMPBIAS 32..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 274
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT LIPID 1173
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..17
FT /note="MSSAPRRPAKGADSFCT -> MDFLLRPQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045953"
FT VAR_SEQ 1..17
FT /note="MSSAPRRPAKGADSFCT -> MTQ (in isoform B1)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000456"
FT VARIANT 26
FT /note="G -> E (in dbSNP:rs2303929)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025168"
FT VARIANT 202
FT /note="E -> V (in dbSNP:rs2229551)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025169"
FT VARIANT 311
FT /note="R -> W (in dbSNP:rs35016052)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025170"
FT VARIANT 1204
FT /note="L -> F (in dbSNP:rs34918764)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025171"
FT CONFLICT 7
FT /note="R -> L (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> M (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="H -> R (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="D -> G (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="E -> V (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="Q -> R (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="E -> R (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="Missing (in Ref. 7; CAA27556)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="L -> V (in Ref. 1; CAA44067)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..475
FT /note="LLGHHHGQGAESDPHVTEPLMGGVPE -> CWGITMVRGLRVTPTSPSLSWE
FT VFLR (in Ref. 7; CAA27556)"
FT /evidence="ECO:0000305"
FT CONFLICT 485..486
FT /note="EL -> DV (in Ref. 1; CAA44067 and 7; CAA27556)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="E -> K (in Ref. 3; BAG58592)"
FT /evidence="ECO:0000305"
FT CONFLICT 666..681
FT /note="AAGAAEDDPLRRTGRP -> RQGQLKMIPSADGAA (in Ref. 1;
FT CAA44067 and 7; CAA27556)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="Q -> R (in Ref. 1; CAA44067 and 7; CAA27556)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="L -> P (in Ref. 1; CAA44067 and 7; CAA27556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1241 AA; 137009 MW; 35E32D9FC34DFB61 CRC64;
MSSAPRRPAK GADSFCTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE
EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GPGRKPRRRP GASPTGETPT
IEEGEEDEDE ASEAEGARAL TQPSPVSTPS SVQFFLQEDD SADRKAERTS PSSPAPLPHQ
EATPRASKGA QAGTQVEEAE AEAVAVASGT AGGDDGGASG RPLPKAQPGH RSYNLQERRR
IGSMTGAEQA LLPRVPTDEI EAQTLATADL DLMKSHRFED VPGVRRHLVR KNAKGSTQSG
REGREPGPTP RARPRAPHKP HEVFVELNEL LLDKNQEPQW RETARWIKFE EDVEEETERW
GKPHVASLSF RSLLELRRTL AHGAVLLDLD QQTLPGVAHQ VVEQMVISDQ IKAEDRANVL
RALLLKHSHP SDEKDFSFPR NISAGSLGSL LGHHHGQGAE SDPHVTEPLM GGVPETRLEV
ERERELPPPA PPAGITRSKS KHELKLLEKI PENAEATVVL VGCVEFLSRP TMAFVRLREA
VELDAVLEVP VPVRFLFLLL GPSSANMDYH EIGRSISTLM SDKQFHEAAY LADEREDLLT
AINAFLDCSV VLPPSEVQGE ELLRSVAHFQ RQMLKKREEQ GRLLPTGAGL EPKSAQDKAL
LQMVEAAGAA EDDPLRRTGR PFGGLIRDVR RRYPHYLSDF RDALDPQCLA AVIFIYFAAL
SPAITFGGLL GEKTQDLIGV SELIMSTALQ GVVFCLLGAQ PLLVIGFSGP LLVFEEAFFS
FCSSNHLEYL VGRVWIGFWL VFLALLMVAL EGSFLVRFVS RFTQEIFAFL ISLIFIYETF
YKLVKIFQEH PLHGCSASNS SEVDGGENMT WAGARPTLGP GNRSLAGQSG QGKPRGQPNT
ALLSLVLMAG TFFIAFFLRK FKNSRFFPGR IRRVIGDFGV PIAILIMVLV DYSIEDTYTQ
KLSVPSGFSV TAPEKRGWVI NPLGEKSPFP VWMMVASLLP AILVFILIFM ETQITTLIIS
KKERMLQKGS GFHLDLLLIV AMGGICALFG LPWLAAATVR SVTHANALTV MSKAVAPGDK
PKIQEVKEQR VTGLLVALLV GLSIVIGDLL RQIPLAVLFG IFLYMGVTSL NGIQFYERLH
LLLMPPKHHP DVTYVKKVRT LRMHLFTALQ LLCLALLWAV MSTAASLAFP FILILTVPLR
MVVLTRIFTD REMKCLDANE AEPVFDEREG VDEYNEMPMP V
