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Anion exchange protein 2 (AE 2) (Anion exchanger 2) (Non-erythroid band 3-like protein) (BND3L) (Solute carrier family 4 member 2)

 B3A2_HUMAN              Reviewed;        1241 AA.
P04920; B2R6T0; B4DIT0; D3DX05; F8W682; Q45EY5; Q969L3;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 4.
25-OCT-2017, entry version 190.
RecName: Full=Anion exchange protein 2;
Short=AE 2;
Short=Anion exchanger 2;
AltName: Full=Non-erythroid band 3-like protein;
Short=BND3L;
AltName: Full=Solute carrier family 4 member 2;
Name=SLC4A2; Synonyms=AE2, EPB3L1, HKB3, MPB3L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=1562608; DOI=10.1016/0167-4781(92)90446-7;
Gehrig H., Mueller W., Appelhans H.;
"Complete nucleotide sequence of band 3 related anion transport
protein AE2 from human kidney.";
Biochim. Biophys. Acta 1130:326-328(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-26; VAL-202;
TRP-311 AND PHE-1204.
NIEHS SNPs program;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND 3).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 375-1241.
PubMed=3015590;
Demuth D.R., Showe L.C., Ballantine M., Palumbo A., Fraser P.J.,
Cioe L., Rovera G., Curtis P.J.;
"Cloning and structural characterization of a human non-erythroid band
3-like protein.";
EMBO J. 5:1205-1214(1986).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-132; SER-173
AND THR-183, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-243, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-274, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Plasma membrane anion exchange protein of wide
distribution.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=A;
IsoId=P04920-1; Sequence=Displayed;
Name=B1;
IsoId=P04920-2; Sequence=VSP_000456;
Name=3;
IsoId=P04920-3; Sequence=VSP_045953;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/slc4a2/";
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EMBL; X62137; CAA44067.1; -; mRNA.
EMBL; DQ149844; AAZ38724.1; -; Genomic_DNA.
EMBL; AK295767; BAG58592.1; -; mRNA.
EMBL; AK312699; BAG35577.1; -; mRNA.
EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471173; EAW54046.1; -; Genomic_DNA.
EMBL; CH471173; EAW54047.1; -; Genomic_DNA.
EMBL; BC009386; AAH09386.1; -; mRNA.
EMBL; BC009434; AAH09434.1; -; mRNA.
EMBL; X03918; CAA27556.1; -; mRNA.
CCDS; CCDS56520.1; -. [P04920-3]
CCDS; CCDS56521.1; -. [P04920-2]
CCDS; CCDS5917.1; -. [P04920-1]
PIR; S21086; S21086.
RefSeq; NP_001186621.1; NM_001199692.2. [P04920-1]
RefSeq; NP_001186622.1; NM_001199693.1. [P04920-3]
RefSeq; NP_001186623.1; NM_001199694.2. [P04920-2]
RefSeq; NP_003031.3; NM_003040.3. [P04920-1]
UniGene; Hs.647069; -.
ProteinModelPortal; P04920; -.
SMR; P04920; -.
BioGrid; 112413; 38.
IntAct; P04920; 17.
STRING; 9606.ENSP00000405600; -.
TCDB; 2.A.31.1.2; the anion exchanger (ae) family.
iPTMnet; P04920; -.
PhosphoSitePlus; P04920; -.
SwissPalm; P04920; -.
BioMuta; SLC4A2; -.
DMDM; 85687559; -.
EPD; P04920; -.
MaxQB; P04920; -.
PaxDb; P04920; -.
PeptideAtlas; P04920; -.
PRIDE; P04920; -.
DNASU; 6522; -.
Ensembl; ENST00000392826; ENSP00000376571; ENSG00000164889. [P04920-3]
Ensembl; ENST00000413384; ENSP00000405600; ENSG00000164889. [P04920-1]
Ensembl; ENST00000461735; ENSP00000419164; ENSG00000164889. [P04920-2]
Ensembl; ENST00000485713; ENSP00000419412; ENSG00000164889. [P04920-1]
GeneID; 6522; -.
KEGG; hsa:6522; -.
UCSC; uc003wit.4; human. [P04920-1]
CTD; 6522; -.
DisGeNET; 6522; -.
EuPathDB; HostDB:ENSG00000164889.12; -.
GeneCards; SLC4A2; -.
HGNC; HGNC:11028; SLC4A2.
HPA; HPA019339; -.
MIM; 109280; gene.
neXtProt; NX_P04920; -.
OpenTargets; ENSG00000164889; -.
PharmGKB; PA35896; -.
eggNOG; KOG1172; Eukaryota.
eggNOG; ENOG410XPHD; LUCA.
GeneTree; ENSGT00760000119021; -.
HOGENOM; HOG000280683; -.
HOVERGEN; HBG004326; -.
InParanoid; P04920; -.
KO; K13855; -.
OMA; PHKPHEV; -.
OrthoDB; EOG091G01FT; -.
PhylomeDB; P04920; -.
TreeFam; TF313630; -.
Reactome; R-HSA-425381; Bicarbonate transporters.
SIGNOR; P04920; -.
ChiTaRS; SLC4A2; human.
GeneWiki; SLC4A2; -.
GenomeRNAi; 6522; -.
PRO; PR:P04920; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000164889; -.
CleanEx; HS_SLC4A2; -.
ExpressionAtlas; P04920; baseline and differential.
Genevisible; P04920; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008509; F:anion transmembrane transporter activity; TAS:ProtInc.
GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0005452; F:inorganic anion exchanger activity; TAS:Reactome.
GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
GO; GO:0006820; P:anion transport; TAS:ProtInc.
GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
Gene3D; 3.40.930.10; -; 1.
InterPro; IPR001717; Anion_exchange.
InterPro; IPR002978; Anion_exchange_2.
InterPro; IPR018241; Anion_exchange_CS.
InterPro; IPR013769; Band3_cytoplasmic_dom.
InterPro; IPR011531; HCO3_transpt_C.
InterPro; IPR003020; HCO3_transpt_euk.
InterPro; IPR016152; PTrfase/Anion_transptr.
PANTHER; PTHR11453; PTHR11453; 1.
PANTHER; PTHR11453:SF14; PTHR11453:SF14; 1.
Pfam; PF07565; Band_3_cyto; 1.
Pfam; PF00955; HCO3_cotransp; 1.
PRINTS; PR00165; ANIONEXCHNGR.
PRINTS; PR01188; ANIONEXHNGR2.
PRINTS; PR01231; HCO3TRNSPORT.
SUPFAM; SSF55804; SSF55804; 2.
TIGRFAMs; TIGR00834; ae; 1.
PROSITE; PS00219; ANION_EXCHANGER_1; 1.
PROSITE; PS00220; ANION_EXCHANGER_2; 1.
1: Evidence at protein level;
Alternative splicing; Anion exchange; Antiport; Complete proteome;
Glycoprotein; Ion transport; Lipoprotein; Membrane; Methylation;
Palmitate; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1241 Anion exchange protein 2.
/FTId=PRO_0000079215.
TOPO_DOM 1 707 Cytoplasmic. {ECO:0000255}.
TRANSMEM 708 731 Helical. {ECO:0000255}.
TRANSMEM 737 774 Helical. {ECO:0000255}.
TRANSMEM 784 816 Helical. {ECO:0000255}.
TRANSMEM 826 847 Helical. {ECO:0000255}.
TOPO_DOM 848 900 Extracellular. {ECO:0000255}.
TRANSMEM 901 918 Helical. {ECO:0000255}.
TOPO_DOM 919 933 Cytoplasmic. {ECO:0000255}.
TRANSMEM 934 954 Helical. {ECO:0000255}.
TRANSMEM 988 1010 Helical. {ECO:0000255}.
TRANSMEM 1036 1059 Helical. {ECO:0000255}.
TRANSMEM 1091 1136 Helical. {ECO:0000255}.
TRANSMEM 1163 1199 Helical. {ECO:0000255}.
REGION 708 1241 Membrane (anion exchange).
COMPBIAS 5 320 Pro-rich.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000250|UniProtKB:P13808}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000250|UniProtKB:P13808}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 183 183 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 257 257 Phosphothreonine.
{ECO:0000250|UniProtKB:P13808}.
MOD_RES 274 274 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 301 301 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P16283}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
LIPID 1173 1173 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 859 859 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 868 868 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 882 882 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 17 MSSAPRRPAKGADSFCT -> MDFLLRPQ (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_045953.
VAR_SEQ 1 17 MSSAPRRPAKGADSFCT -> MTQ (in isoform B1).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000456.
VARIANT 26 26 G -> E (in dbSNP:rs2303929).
{ECO:0000269|Ref.2}.
/FTId=VAR_025168.
VARIANT 202 202 E -> V (in dbSNP:rs2229551).
{ECO:0000269|Ref.2}.
/FTId=VAR_025169.
VARIANT 311 311 R -> W (in dbSNP:rs35016052).
{ECO:0000269|Ref.2}.
/FTId=VAR_025170.
VARIANT 1204 1204 L -> F (in dbSNP:rs34918764).
{ECO:0000269|Ref.2}.
/FTId=VAR_025171.
CONFLICT 7 7 R -> L (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 68 68 E -> M (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 74 74 H -> R (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 92 92 D -> G (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 122 122 E -> V (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 157 157 Q -> R (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 248 248 E -> R (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 399 399 Missing (in Ref. 7; CAA27556).
{ECO:0000305}.
CONFLICT 447 447 L -> V (in Ref. 1; CAA44067).
{ECO:0000305}.
CONFLICT 450 475 LLGHHHGQGAESDPHVTEPLMGGVPE -> CWGITMVRGLR
VTPTSPSLSWEVFLR (in Ref. 7; CAA27556).
{ECO:0000305}.
CONFLICT 485 486 EL -> DV (in Ref. 1; CAA44067 and 7;
CAA27556). {ECO:0000305}.
CONFLICT 571 571 E -> K (in Ref. 3; BAG58592).
{ECO:0000305}.
CONFLICT 666 681 AAGAAEDDPLRRTGRP -> RQGQLKMIPSADGAA (in
Ref. 1; CAA44067 and 7; CAA27556).
{ECO:0000305}.
CONFLICT 824 824 Q -> R (in Ref. 1; CAA44067 and 7;
CAA27556). {ECO:0000305}.
CONFLICT 902 902 L -> P (in Ref. 1; CAA44067 and 7;
CAA27556). {ECO:0000305}.
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


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