Band 3 anion transport protein

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• actin binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "alpha-cardiac actin (ACTC) binds to the band 3 (AE1) cardiac isoform."
    Moura Lima P.R., Salles T.S., Costa F.F., Saad S.T.
    J. Cell. Biochem. 89:1215-1221(2003) [PubMed] [Europe PMC] [Abstract]
• anion:anion antiporter activity Source: UniProtKB
• ankyrin binding Source: RGDInferred from sequence orthologyⁱ
  • "An 11-amino acid beta-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes."
    Stefanovic M., Markham N.O., Parry E.M., Garrett-Beal L.J., Cline A.P., Gallagher P.G., Low P.S., Bodine D.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:13972-13977(2007) [PubMed] [Europe PMC] [Abstract]
  • "The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes."
    Bennett V., Stenbuck P.J.
    Nature 280:468-473(1979) [PubMed] [Europe PMC] [Abstract]
• bicarbonate transmembrane transporter activity Source: UniProtKB
• chloride transmembrane transporter activity Source: UniProtKB
• enzyme binding Source: RGDInferred from physical interactionⁱ
  • "Interactions of transmembrane carbonic anhydrase, CAIX, with bicarbonate transporters."
    Morgan P.E., Pastorekova S., Stuart-Tilley A.K., Alper S.L., Casey J.R.
    Am. J. Physiol., Cell Physiol. 293:C738-48(2007) [PubMed] [Europe PMC] [Abstract]
  • "Glyceraldehyde 3-phosphate dehydrogenase is required for band 3 (anion exchanger 1) membrane residency in the mammalian kidney."
    Su Y., Blake-Palmer K.G., Fry A.C., Best A., Brown A.C., Hiemstra T.F., Horita S., Zhou A., Toye A.M., Karet F.E.
    Am. J. Physiol. Renal Physiol. 300:F157-66(2011) [PubMed] [Europe PMC] [Abstract]
• hemoglobin binding Source: RGDInferred from sequence orthologyⁱ
  • "Interaction of deoxyhemoglobin with the cytoplasmic domain of murine erythrocyte band 3."
    Sega M.F., Chu H., Christian J., Low P.S.
    Biochemistry 51:3264-3272(2012) [PubMed] [Europe PMC] [Abstract]
• inorganic anion exchanger activity Source: UniProtKB
• protein-containing complex binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Atorvastatin acts synergistically with N-acetyl cysteine to provide therapeutic advantage against Fas-activated erythrocyte apoptosis during chronic arsenic exposure in rats."
    Biswas D., Sen G., Sarkar A., Biswas T.
    Toxicol. Appl. Pharmacol. 250:39-53(2011) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: RGDInferred from physical interactionⁱ
  • "alpha-cardiac actin (ACTC) binds to the band 3 (AE1) cardiac isoform."
    Moura Lima P.R., Salles T.S., Costa F.F., Saad S.T.
    J. Cell. Biochem. 89:1215-1221(2003) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: RGDInferred from sequence orthologyⁱ
  • "The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes."
    Bennett V., Stenbuck P.J.
    Nature 280:468-473(1979) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• anion transport Source: UniProtKB
• bicarbonate transport Source: UniProtKB
• blood coagulation Source: RGDInferred from sequence orthologyⁱ
  • "Targeted inactivation of murine band 3 (AE1) gene produces a hypercoagulable state causing widespread thrombosis in vivo."
    Hassoun H., Wang Y., Vassiliadis J., Lutchman M., Palek J., Aish L., Aish I.S., Liu S.C., Chishti A.H.
    Blood 92:1785-1792(1998) [PubMed] [Europe PMC] [Abstract]
• chloride transport Source: UniProtKB
• circadian rhythm Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Circadian regulation of electrolyte absorption in the rat colon."
    Sotak M., Polidarova L., Musilkova J., Hock M., Sumova A., Pacha J.
    Am. J. Physiol. Gastrointest. Liver Physiol. 301:G1066-74(2011) [PubMed] [Europe PMC] [Abstract]
• erythrocyte development Source: RGDInferred from sequence orthologyⁱ
  • "An 11-amino acid beta-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes."
    Stefanovic M., Markham N.O., Parry E.M., Garrett-Beal L.J., Cline A.P., Gallagher P.G., Low P.S., Bodine D.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:13972-13977(2007) [PubMed] [Europe PMC] [Abstract]
• negative regulation of glycolytic process through fructose-6-phosphate Source: RGDInferred from sequence orthologyⁱ
  • "Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice."
    Campanella M.E., Chu H., Wandersee N.J., Peters L.L., Mohandas N., Gilligan D.M., Low P.S.
    Blood 112:3900-3906(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of oxidoreductase activity Source: RGDInferred from sequence orthologyⁱ
  • "Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice."
    Campanella M.E., Chu H., Wandersee N.J., Peters L.L., Mohandas N., Gilligan D.M., Low P.S.
    Blood 112:3900-3906(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of urine volume Source: RGDInferred from sequence orthologyⁱ
  • "Distal renal tubular acidosis in mice lacking the AE1 (band3) Cl-/HCO3- exchanger (slc4a1)."
    Stehberger P.A., Shmukler B.E., Stuart-Tilley A.K., Peters L.L., Alper S.L., Wagner C.A.
    J. Am. Soc. Nephrol. 18:1408-1418(2007) [PubMed] [Europe PMC] [Abstract]
• pH elevation Source: RGDInferred from sequence orthologyⁱ
  • "Distal renal tubular acidosis in mice lacking the AE1 (band3) Cl-/HCO3- exchanger (slc4a1)."
    Stehberger P.A., Shmukler B.E., Stuart-Tilley A.K., Peters L.L., Alper S.L., Wagner C.A.
    J. Am. Soc. Nephrol. 18:1408-1418(2007) [PubMed] [Europe PMC] [Abstract]
• plasma membrane phospholipid scrambling Source: RGDInferred from sequence orthologyⁱ
  • "Targeted inactivation of murine band 3 (AE1) gene produces a hypercoagulable state causing widespread thrombosis in vivo."
    Hassoun H., Wang Y., Vassiliadis J., Lutchman M., Palek J., Aish L., Aish I.S., Liu S.C., Chishti A.H.
    Blood 92:1785-1792(1998) [PubMed] [Europe PMC] [Abstract]
• positive regulation of T cell proliferation Source: RGDInferred from direct assayⁱ
  • "T-cell specificity in murine autoimmune haemolytic anaemia induced by rat red blood cells."
    Barker R.N., Shen C.R., Elson C.J.
    Clin. Exp. Immunol. 129:208-213(2002) [PubMed] [Europe PMC] [Abstract]
• protein localization to plasma membrane Source: RGDInferred from sequence orthologyⁱ
  • "Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice."
    Campanella M.E., Chu H., Wandersee N.J., Peters L.L., Mohandas N., Gilligan D.M., Low P.S.
    Blood 112:3900-3906(2008) [PubMed] [Europe PMC] [Abstract]
• regulation of intracellular pH Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• response to acidic pH Source: RGDInferred from expression patternⁱ
  • "Expression of rat kidney anion exchanger 1 in type A intercalated cells in metabolic acidosis and alkalosis."
    Huber S., Asan E., Jons T., Kerscher C., Puschel B., Drenckhahn D.
    Am. J. Physiol. 277:F841-9(1999) [PubMed] [Europe PMC] [Abstract]
• response to activity Source: RGDInferred from direct assayⁱ
  • "Cluster of erythrocyte band 3: a potential molecular target of exhaustive exercise-induced dysfunction of erythrocyte deformability."
    Xiong Y., Li Y., Xiong Y., Zhao Y., Tang F., Wang X.
    Can. J. Physiol. Pharmacol. 91:1127-1134(2013) [PubMed] [Europe PMC] [Abstract]
• response to alkaline pH Source: RGDInferred from expression patternⁱ
  • "Expression of rat kidney anion exchanger 1 in type A intercalated cells in metabolic acidosis and alkalosis."
    Huber S., Asan E., Jons T., Kerscher C., Puschel B., Drenckhahn D.
    Am. J. Physiol. 277:F841-9(1999) [PubMed] [Europe PMC] [Abstract]
• response to arsenic-containing substance Source: RGDInferred from direct assayⁱ
  • "Atorvastatin acts synergistically with N-acetyl cysteine to provide therapeutic advantage against Fas-activated erythrocyte apoptosis during chronic arsenic exposure in rats."
    Biswas D., Sen G., Sarkar A., Biswas T.
    Toxicol. Appl. Pharmacol. 250:39-53(2011) [PubMed] [Europe PMC] [Abstract]
• response to carbon dioxide Source: RGDInferred from direct assayⁱ
  • "Acid-base effects on intestinal Cl- absorption and vesicular trafficking."
    Charney A.N., Egnor R.W., Henner D., Rashid H., Cassai N., Sidhu G.S.
    Am. J. Physiol., Cell Physiol. 286:C1062-70(2004) [PubMed] [Europe PMC] [Abstract]
• response to hydrogen peroxide Source: RGDInferred from direct assayⁱ
  • "Atorvastatin acts synergistically with N-acetyl cysteine to provide therapeutic advantage against Fas-activated erythrocyte apoptosis during chronic arsenic exposure in rats."
    Biswas D., Sen G., Sarkar A., Biswas T.
    Toxicol. Appl. Pharmacol. 250:39-53(2011) [PubMed] [Europe PMC] [Abstract]
• response to nutrient levels Source: RGDInferred from expression patternⁱ
  • "Circadian regulation of electrolyte absorption in the rat colon."
    Sotak M., Polidarova L., Musilkova J., Hock M., Sumova A., Pacha J.
    Am. J. Physiol. Gastrointest. Liver Physiol. 301:G1066-74(2011) [PubMed] [Europe PMC] [Abstract]
• response to water deprivation Source: RGDInferred from expression patternⁱ
  • "Differential regulation of basolateral Cl-/HCO3- exchangers SLC26A7 and AE1 in kidney outer medullary collecting duct."
    Barone S., Amlal H., Xu J., Kujala M., Kere J., Petrovic S., Soleimani M.
    J. Am. Soc. Nephrol. 15:2002-2011(2004) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• actin binding Source: RGDInferred from physical interactionⁱ
  • "alpha-cardiac actin (ACTC) binds to the band 3 (AE1) cardiac isoform."
    Moura Lima P.R., Salles T.S., Costa F.F., Saad S.T.
    J. Cell. Biochem. 89:1215-1221(2003) [PubMed] [Europe PMC] [Abstract]
• ankyrin binding Source: RGDInferred from sequence orthologyⁱ
  • "An 11-amino acid beta-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes."
    Stefanovic M., Markham N.O., Parry E.M., Garrett-Beal L.J., Cline A.P., Gallagher P.G., Low P.S., Bodine D.M.
    Proc. Natl. Acad. Sci. U.S.A. 104:13972-13977(2007) [PubMed] [Europe PMC] [Abstract]
  • "The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes."
    Bennett V., Stenbuck P.J.
    Nature 280:468-473(1979) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: RGDInferred from physical interactionⁱ
  • "Interactions of transmembrane carbonic anhydrase, CAIX, with bicarbonate transporters."
    Morgan P.E., Pastorekova S., Stuart-Tilley A.K., Alper S.L., Casey J.R.
    Am. J. Physiol., Cell Physiol. 293:C738-48(2007) [PubMed] [Europe PMC] [Abstract]
  • "Glyceraldehyde 3-phosphate dehydrogenase is required for band 3 (anion exchanger 1) membrane residency in the mammalian kidney."
    Su Y., Blake-Palmer K.G., Fry A.C., Best A., Brown A.C., Hiemstra T.F., Horita S., Zhou A., Toye A.M., Karet F.E.
    Am. J. Physiol. Renal Physiol. 300:F157-66(2011) [PubMed] [Europe PMC] [Abstract]
• hemoglobin binding Source: RGDInferred from sequence orthologyⁱ
  • "Interaction of deoxyhemoglobin with the cytoplasmic domain of murine erythrocyte band 3."
    Sega M.F., Chu H., Christian J., Low P.S.
    Biochemistry 51:3264-3272(2012) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: RGDInferred from physical interactionⁱ
  • "alpha-cardiac actin (ACTC) binds to the band 3 (AE1) cardiac isoform."
    Moura Lima P.R., Salles T.S., Costa F.F., Saad S.T.
    J. Cell. Biochem. 89:1215-1221(2003) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: RGDInferred from sequence orthologyⁱ
  • "The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes."
    Bennett V., Stenbuck P.J.
    Nature 280:468-473(1979) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MGDMQDHEKV LEIPDRDSEE ELEHVIEQIA YRDLDIPVTE MQESEALPTE 
        60         70         80         90        100
QTATDYIPTS TSTSHPSSSQ VYVELQELMM DQRNQELQWV EAAHWIGLEE 
       110        120        130        140        150
NLREDGVWGR PHLSYLTFWS LLELQKVFSK GTFLLDLAET SLAGVANKLL 
       160        170        180        190        200
DSFIYEDQIR PQDRDELLRA LLLKRSHAED LKDLEGVKPA VLTRSGAPSE 
       210        220        230        240        250
PLLPHQPSLE TKLYCAQAEG GSEEPSPSGI LKIPPNSETT LVLVGRASFL 
       260        270        280        290        300
VKPVLGFVRL KEAVPLEDLV LPEPVSFLLV LLGPEAPHID YTQLGRAAAT 
       310        320        330        340        350
LMTERVFRVT ASLAQSRGEL LSSLDSFLDC SLVLPPTEAP SEKALLNLVP 
       360        370        380        390        400
VQKELLRKRY LPRPAKPDPN LYEALDGGKE GPGDEDDPLR RTGRIFGGLI 
       410        420        430        440        450
RDIRRRYPYY LSDITDALSP QVLAAVIFIY FAALSPAVTF GGLLGEKTRN 
       460        470        480        490        500
LMGVSELLIS TAVQGILFAL LGAQPLLVLG FSGPLLVFEE AFYSFCESNN 
       510        520        530        540        550
LEYIVGRAWI GFWLILLVVL VVAFEGSFLV QYISRYTQEI FSFLISLIFI 
       560        570        580        590        600
YETFSKLIKI FQDYPLQESY APVVMKPKPQ GPVPNTALLS LVLMVGTFLL 
       610        620        630        640        650
AMMLRKFKNS TYFPGKLRRV IGDFGVPISI LIMVLVDTFI KNTYTQKLSV 
       660        670        680        690        700
PDGLKVSNSS ARGWVIHPLG LYNHFPKWMM FASVLPALLV FILIFLESQI 
       710        720        730        740        750
TTLIVSKPER KMIKGSGFHL DLLLVVGMGG VAALFGMPWL SATTVRSVTH 
       760        770        780        790        800
ANALTVMGKA SGPGAAAQIQ EVKEQRISGL LVSVLVGLSI LMEPILSRIP 
       810        820        830        840        850
LAVLFGIFLY MGITSLSGIQ LFDRILLLFK PPKYHPDVPF VKRVKTWRMH 
       860        870        880        890        900
LFTGIQIICL AVLWVVKSTP ASLALPFVLI LTVPLRRLLL PLIFRELELQ 
       910        920 
CLDGDDAKVT FDEAEGLDEY DEVPMPV                          

        10         20         30         40         50
MDQRNQELQW VEAAHWIGLE ENLREDGVWG RPHLSYLTFW SLLELQKVFS 
        60         70         80         90        100
KGTFLLDLAE TSLAGVANKL LDSFIYEDQI RPQDRDELLR ALLLKRSHAE 
       110        120        130        140        150
DLKDLEGVKP AVLTRSGAPS EPLLPHQPSL ETKLYCAQAE GGSEEPSPSG 
       160        170        180        190        200
ILKIPPNSET TLVLVGRASF LVKPVLGFVR LKEAVPLEDL VLPEPVSFLL 
       210        220        230        240        250
VLLGPEAPHI DYTQLGRAAA TLMTERVFRV TASLAQSRGE LLSSLDSFLD 
       260        270        280        290        300
CSLVLPPTEA PSEKALLNLV PVQKELLRKR YLPRPAKPDP NLYEALDGGK 
       310        320        330        340        350
EGPGDEDDPL RRTGRIFGGL IRDIRRRYPY YLSDITDALS PQVLAAVIFI 
       360        370        380        390        400
YFAALSPAVT FGGLLGEKTR NLMGVSELLI STAVQGILFA LLGAQPLLVL 
       410        420        430        440        450
GFSGPLLVFE EAFYSFCESN NLEYIVGRAW IGFWLILLVV LVVAFEGSFL 
       460        470        480        490        500
VQYISRYTQE IFSFLISLIF IYETFSKLIK IFQDYPLQES YAPVVMKPKP 
       510        520        530        540        550
QGPVPNTALL SLVLMVGTFL LAMMLRKFKN STYFPGKLRR VIGDFGVPIS 
       560        570        580        590        600
ILIMVLVDTF IKNTYTQKLS VPDGLKVSNS SARGWVIHPL GLYNHFPKWM 
       610        620        630        640        650
MFASVLPALL VFILIFLESQ ITTLIVSKPE RKMIKGSGFH LDLLLVVGMG 
       660        670        680        690        700
GVAALFGMPW LSATTVRSVT HANALTVMGK ASGPGAAAQI QEVKEQRISG 
       710        720        730        740        750
LLVSVLVGLS ILMEPILSRI PLAVLFGIFL YMGITSLSGI QLFDRILLLF 
       760        770        780        790        800
KPPKYHPDVP FVKRVKTWRM HLFTGIQIIC LAVLWVVKST PASLALPFVL 
       810        820        830        840 
ILTVPLRRLL LPLIFRELEL QCLDGDDAKV TFDEAEGLDE YDEVPMPV   

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families