Band 3 anion transport protein - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P02730 (B3AT_HUMAN)

Last modified March 2, 2010. Version 149. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Band 3 anion transport protein

Alternative name(s):
Anion exchange protein 1
Short name=Anion exchanger 1
Short name=AE 1
Solute carrier family 4 member 1
CD_antigen=CD233

Gene names

Name:	SLC4A1
Synonyms:	AE1, DI, EPB3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	911 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Band 3 is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin.
Subunit structure	A dimer in solution, it spans the membrane asymmetrically and appears to be tetrameric.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Erythrocytes.
Post-translational modification	Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation. Ref.14 Ref.16 Ref.17 Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 phosphorylation. Ref.14 Ref.16 Ref.17
Polymorphism	SLC4A1 is responsible for the Diego blood group system. The molecular basis of the Di(a)=Di1/Di(b)/Di2 blood group antigens is a single variation in position 854; Leu-854 corresponds to Di(a) and Pro-854 to Di(b). The molecular basis of the Wr(a)=Di3/Wr(b)/Di4 blood group antigens is a single variation in position 658; Lys-658 corresponds to Wr(a) and Glu-658 to Wr(b). The blood group antigens Wd(a)=Di5 (Waldner-type) has Met-557; Rb(a)=Di6 has Leu-548 and WARR=Di7 has Ile-552. SLC4A1 is responsible for the Swann blood group system (SW) [MIM:601550]. Sw(a+) has a Gln or a Trp at position 646 and Sw(a-) has an Arg. SLC4A1 is responsible for the Froese blood group system (FR) [MIM:601551]. FR(a+) has a Lys at position 480 and FR(a-) has a Glu.
Involvement in disease	Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:109270]. EL4 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape. Ref.27 Ref.29 Defects in SLC4A1 are the cause of spherocytosis type 4 (SPH4) [MIM:612653]; also known as hereditary spherocytosis type 4 (HS4). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Ref.12 Ref.28 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.43 Ref.48 Ref.50 Ref.51 Ref.56 Ref.59 Ref.60 Defects in SLC4A1 are the cause of autosomal dominant distal renal tubular acidosis (dRTA) [MIM:179800]. This disease is characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. Defects in SLC4A1 are the cause of autosomal recessive distal renal tubular acidosis (dRTA) [MIM:611590].
Miscellaneous	Phenyl isothiocyanate inhibits anion transport in vitro.
Sequence similarities	Belongs to the anion exchanger (TC 2.A.31) family. [View classification]

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Ontologies

Keywords
Biological process	Anion exchange Ion transport Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Elliptocytosis Hereditary hemolytic anemia
Domain	Transmembrane
Molecular function	Blood group antigen
PTM	Acetylation Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anion transport Ref.58 Inferred from direct assay. Source: UniProtKB cellular ion homeostasis Traceable author statement. Source: ProtInc
Cellular component	basolateral plasma membrane Ref.58 Inferred from direct assay. Source: UniProtKB cortical cytoskeleton Inferred from direct assay. Source: UniProtKB integral to plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ankyrin binding Inferred from physical interaction. Source: UniProtKB inorganic anion exchanger activity Inferred from electronic annotation. Source: InterPro protein anchor Traceable author statement. Source: UniProtKB protein homodimerization activity Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 911

911

Band 3 anion transport protein

PRO_0000079209

Regions

Topological domain

1 – 403

403

Cytoplasmic

Transmembrane

404 – 424

Potential

Transmembrane

437 – 456

Potential

Transmembrane

460 – 479

Potential

Transmembrane

491 – 510

Potential

Transmembrane

523 – 541

Potential

Topological domain

542 – 568

Extracellular Potential

Transmembrane

569 – 588

Potential

Topological domain

589 – 603

Cytoplasmic Potential

Transmembrane

604 – 624

Potential

Topological domain

625 – 660

Extracellular Potential

Transmembrane

661 – 680

Potential

Transmembrane

699 – 719

Potential

Transmembrane

763 – 780

Potential

Transmembrane

785 – 806

Potential

Transmembrane

844 – 865

Potential

Region

404 – 911

508

Membrane (anion exchange)

Region

559 – 630

Involved in anion transport

Sites

Site

590

Important for anion transport

Site

681

Important for anion-proton cotransport

Amino acid modifications

Modified residue

N-acetylmethionine Ref.8

Modified residue

Phosphotyrosine Ref.14 Ref.16

Modified residue

Phosphotyrosine Ref.14 Ref.16

Modified residue

Phosphotyrosine Ref.14

Modified residue

350

Phosphoserine By similarity

Modified residue

359

Phosphotyrosine Ref.16 Ref.17

Modified residue

904

Phosphotyrosine Ref.16 Ref.17

Lipidation

843

S-palmitoyl cysteine Ref.15

Glycosylation

642

N-linked (GlcNAc...) Probable

Natural variations

Natural variant

P → H: dbSNP rs55777403. Ref.5

VAR_058035

Natural variant

D → A: dbSNP rs5035. Ref.38 Ref.51 Ref.3 Ref.4

VAR_014612

Natural variant

E → K in hemolytic anemia; Montefiore. dbSNP rs45562031. Ref.36 Ref.31

VAR_000798

Natural variant

D → E: dbSNP rs34700496.

VAR_036693

Natural variant

K → E in Di(a)/Memphis-II antigen. dbSNP rs5036. Ref.27 Ref.51 Ref.4 Ref.26 Ref.32

VAR_000799

Natural variant

E → K: dbSNP rs13306787.

VAR_039290

Natural variant

E → D

VAR_058036

Natural variant

L → M

VAR_039291

Natural variant

E → K in SPH4; Cape Town. dbSNP rs28929480. Ref.56

VAR_013784

Natural variant

112

R → S: dbSNP rs5037.

VAR_014613

Natural variant

130

G → R in SPH4; Fukoka. Ref.51

VAR_013785

Natural variant

147

P → S in SPH4; Mondego. Ref.37

VAR_013786

Natural variant

285

A → D in SPH4; Boston. Ref.35

VAR_013787

Natural variant

327

P → R in SPH4; Tuscaloosa. dbSNP rs28931583. Ref.28

VAR_000800

Natural variant

400 – 408

Missing in EL4.

VAR_000801

Natural variant

429

E → D in NFLD+ antigen. Ref.53

VAR_058037

Natural variant

432

R → W in ELO antigen.

VAR_013788

Natural variant

442

I → F: dbSNP rs5018.

VAR_014614

Natural variant

455

G → E in SPH4; Benesov. Ref.35

VAR_013789

Natural variant

455

G → R in SPH4; Yamagata. Ref.51

VAR_058038

Natural variant

480

E → K in FR(a+) antigen. Ref.54

VAR_013790

Natural variant

488

V → M in SPH4; Coimbra; also in dRTA autosomal recessive form. dbSNP rs28931584. Ref.37 Ref.50

VAR_013791

Natural variant

490

R → C in SPH4; Bicetre I. Ref.39

VAR_013792

Natural variant

490

R → H in SPH4; Pinhal. Ref.48

VAR_058039

Natural variant

508

E → K: dbSNP rs45568837. Ref.4

VAR_025090

Natural variant

518

R → C in SPH4; Dresden. Ref.36

VAR_000802

Natural variant

548

P → L in RB(A) antigen.

VAR_000803

Natural variant

551

K → N in TR(A) antigen.

VAR_013793

Natural variant

552

T → I in WARR antigen.

VAR_000804

Natural variant

555

Y → H in VG(a) antigen.

VAR_013794

Natural variant

557

V → M in WD(a) antigen.

VAR_000805

Natural variant

561

P → A in NFLD+ antigen. Ref.53

VAR_058040

Natural variant

561

P → S in BOW antigen. Ref.53

VAR_013795

Natural variant

565

G → A in WU antigen.

VAR_013796

Natural variant

566

P → A in KREP antigen.

VAR_013797

Natural variant

566

P → S in PN(a) antigen.

VAR_013798

Natural variant

569

N → K in BP(a) antigen.

VAR_013799

Natural variant

586

M → L: dbSNP rs5019.

VAR_014615

Natural variant

589

R → C in dRTA; autosomal dominant form; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. Ref.41

VAR_015104

Natural variant

589

R → H in dRTA; autosomal dominant form. Ref.41 Ref.46

VAR_015105

Natural variant

589

R → S in dRTA; autosomal dominant form. Ref.46

VAR_015106

Natural variant

602

R → P in dRTA; autosomal recessive form; with hemolytic anemia. Ref.57

VAR_039292

Natural variant

609

G → R in dRTA; autosomal dominant form; detected subapically and at the apical membrane as well as at the basolateral membrane in contrast to the normal basolateral appearance of wild-type protein. Ref.58

VAR_058041

Natural variant

613

S → F in dRTA; autosomal dominant form; markedly increased red cell sulfate transport but almost normal red cell iodide transport. Ref.41

VAR_015107

Natural variant

646

R → Q in SW(a+) antigen. Ref.55

VAR_013800

Natural variant

646

R → W in SW(a+) antigen. Ref.55

VAR_013801

Natural variant

656

R → C in HG(a) antigen.

VAR_013802

Natural variant

656

R → H in MO(a) antigen.

VAR_013803

Natural variant

658

E → K in WR(a) antigen. Ref.33

VAR_000806

Natural variant

663

M → K in SPH4; Tambau. Ref.59

VAR_058042

Natural variant

663

Missing in SPH4; Osnabruck II.

VAR_000807

Natural variant

687

L → P in SPH4. Ref.60

VAR_039293

Natural variant

688

I → V: dbSNP rs5022.

VAR_014616

Natural variant

690

S → G: dbSNP rs5023.

VAR_014617

Natural variant

701

G → D in dRTA; autosomal recessive form. Ref.45 Ref.49

VAR_015171

Natural variant

705

D → Y in SPH4. Ref.60

VAR_039294

Natural variant

707

L → P in SPH4; Most. Ref.35 Ref.52

VAR_013804

Natural variant

714

G → R in SPH4; Okinawa. Ref.51

VAR_013805

Natural variant

731

S → P in SPH4. Ref.60

VAR_039295

Natural variant

734

H → R in SPH4. Ref.60

VAR_039296

Natural variant

760

R → Q in SPH4; Prague II. Ref.34 Ref.51 Ref.60 Ref.52

VAR_013806

Natural variant

760

R → W in SPH4; Hradec Kralove. Ref.34 Ref.51 Ref.52

VAR_013807

Natural variant

771

G → D in SPH4; Chur. Ref.12

VAR_013808

Natural variant

773

S → P in dRTA; autosomal recessive form; with normal red cell morphology. Ref.57

VAR_039297

Natural variant

783

I → N in SPH4; Napoli II. Ref.38

VAR_013809

Natural variant

808

R → C in SPH4; Jablonec. Ref.34 Ref.52

VAR_013810

Natural variant

808

R → H in SPH4; Nara. Ref.51

VAR_013811

Natural variant

832

R → H: dbSNP rs5025.

VAR_014618

Natural variant

834

H → P in SPH4; Birmingham. Ref.35 Ref.52

VAR_013812

Natural variant

837

T → A in SPH4; Tokyo. Ref.43

VAR_013813

Natural variant

837

T → M in SPH4; Philadelphia. Ref.35 Ref.39 Ref.51 Ref.52

VAR_013814

Natural variant

837

T → R in SPH4; Nagoya. Ref.51

VAR_058043

Natural variant

850

Missing in dRTA; autosomal recessive form.

VAR_015109

Natural variant

854

P → L in Di(a)/Memphis-II antigen. dbSNP rs2285644. Ref.51 Ref.32

VAR_000808

Natural variant

858

A → D in dRTA; autosomal dominant form. Ref.49

VAR_015108

Natural variant

862

V → I: dbSNP rs5026. Ref.4

VAR_014619

Natural variant

868

P → L in acanthocytosis; due to band 3 high transport. Ref.30

VAR_013815

Natural variant

870

R → W in SPH4; Prague III. dbSNP rs28931585. Ref.34 Ref.56 Ref.52

VAR_013816

Experimental info

Sequence conflict

M → D AA sequence Ref.7

Sequence conflict

E → EE AA sequence Ref.7

Sequence conflict

759

Q → H in ABD74692. Ref.3

Secondary structure

911

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P02730-1 [UniParc].

Last modified April 1, 1990. Version 3.
Checksum: 35EC3EE7AFF27D2F
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FASTA

911

101,792

        10         20         30         40         50         60 
MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE 

        70         80         90        100        110        120 
LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS HLTFWSLLEL RRVFTKGTVL 

       130        140        150        160        170        180 
LDLQETSLAG VANQLLDRFI FEDQIRPQDR EELLRALLLK HSHAGELEAL GGVKPAVLTR 

       190        200        210        220        230        240 
SGDPSQPLLP QHSSLETQLF CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP 

       250        260        270        280        290        300 
VLGFVRLQEA AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM 

       310        320        330        340        350        360 
AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS PAKPDSSFYK 

       370        380        390        400        410        420 
GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA FSPQVLAAVI FIYFAALSPA 

       430        440        450        460        470        480 
ITFGGLLGEK TRNQMGVSEL LISTAVQGIL FALLGAQPLL VVGFSGPLLV FEEAFFSFCE 

       490        500        510        520        530        540 
TNGLEYIVGR VWIGFWLILL VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL 

       550        560        570        580        590        600 
IKIFQDHPLQ KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK 

       610        620        630        640        650        660 
LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI HPLGLRSEFP 

       670        680        690        700        710        720 
IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS GFHLDLLLVV GMGGVAALFG 

       730        740        750        760        770        780 
MPWLSATTVR SVTHANALTV MGKASTPGAA AQIQEVKEQR ISGLLVAVLV GLSILMEPIL 

       790        800        810        820        830        840 
SRIPLAVLFG IFLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ 

       850        860        870        880        890        900 
IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG 

       910 
RDEYDEVAMP V

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References

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[1]	"The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence." Tanner M.J.A., Martin P.G., High S. Biochem. J. 256:703-712(1988) [PubMed: 3223947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.
[2]	"Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)." Lux S.E., John K.M., Kopito R.R., Lodish H.F. Proc. Natl. Acad. Sci. U.S.A. 86:9089-9093(1989) [PubMed: 2594752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations." Choo K.E., Nicoli T.K., Bruce L.J., Tanner M.J., Ruiz-Linares A., Wrong O.M. Pediatr. Nephrol. 21:212-217(2006) [PubMed: 16252102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-38.
[4]	SeattleSNPs variation discovery resource Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-38; GLU-56; LYS-508 AND ILE-862.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-27. Tissue: Cerebellum.
[6]	"Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse." Yannoukakos D., Vasseur C., Blouquit Y., Bursaux E., Wajcman H. Biochim. Biophys. Acta 998:43-49(1989) [PubMed: 2790053] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-199; 220-292 AND 347-370.
[7]	"Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3." Kaul R.K., Murthy S.N.P., Reddy A.G., Steck T.L., Kohler H. J. Biol. Chem. 258:7981-7990(1983) [PubMed: 6345535] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-201.
[8]	"Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment." Drickamer L.K. J. Biol. Chem. 253:7242-7248(1978) [PubMed: 701248] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-3.
[9]	"Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus." Kollert-Jons A., Wagner S., Hubner S., Appelhans H., Drenckhahn D. Am. J. Physiol. 265:F813-F821(1993) [PubMed: 7506871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-180.
[10]	"The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange." Brock C.J., Tanner M.J.A., Kempf C. Biochem. J. 213:577-586(1983) [PubMed: 6615451] [Abstract] Cited for: PROTEIN SEQUENCE OF 559-630.
[11]	"Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681." Jennings M.L., Smith J.S. J. Biol. Chem. 267:13964-13971(1992) [PubMed: 1352774] [Abstract] Cited for: PROTEIN SEQUENCE OF 665-688, ROLE OF GLU-681.
[12]	"Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11." Maillet P., Vallier A., Reinhart W.H., Wyss E.J., Ott P., Texier P., Baklouti F., Tanner M.J.A., Delaunay J., Alloisio N. Br. J. Haematol. 91:804-810(1995) [PubMed: 8547122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 757-778, VARIANT SPH4 ASP-771.
[13]	"Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein." Kawano Y., Okubo K., Tokunaga F., Miyata T., Iwanaga S., Hamasaki N. J. Biol. Chem. 263:8232-8238(1988) [PubMed: 3372523] [Abstract] Cited for: PROTEIN SEQUENCE OF 834-911.
[14]	"Phosphorylation sites in human erythrocyte band 3 protein." Yannoukakos D., Vasseur C., Piau J.-P., Wajcman H., Bursaux E. Biochim. Biophys. Acta 1061:253-266(1991) [PubMed: 1998697] [Abstract] Cited for: PHOSPHORYLATION AT TYR-8; TYR-21 AND TYR-46.
[15]	"Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F--I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus." Okubo K., Hamasaki N., Hara K., Kageura M. J. Biol. Chem. 266:16420-16424(1991) [PubMed: 1885574] [Abstract] Cited for: PALMITOYLATION AT CYS-843.
[16]	"Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites." Brunati A.M., Bordin L., Clari G., James P., Quadroni M., Baritono E., Pinna L.A., Donella-Deana A. Blood 96:1550-1557(2000) [PubMed: 10942405] [Abstract] Cited for: PHOSPHORYLATION AT TYR-8; TYR-21; TYR-359 AND TYR-904.
[17]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-359 AND TYR-904, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane." Wang D.N., Kuehlbrandt W., Sarabia V.E., Reithmeier R.A.F. EMBO J. 12:2233-2239(1993) [PubMed: 8508760] [Abstract] Cited for: STRUCTURE BY ELECTRON CRYOMICROSCOPY.
[20]	"Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3." Wang D.N., Sarabia V.E., Reithmeier R.A.F., Kuehlbrandt W. EMBO J. 13:3230-3235(1994) [PubMed: 8045253] [Abstract] Cited for: STRUCTURE BY ELECTRON CRYOMICROSCOPY.
[21]	"The solution structures of the first and second transmembrane-spanning segments of band 3." Gargaro A.R., Bloomberg G.B., Dempsey C.E., Murray M., Tanner M.J.A. Eur. J. Biochem. 221:445-454(1994) [PubMed: 8168533] [Abstract] Cited for: STRUCTURE BY NMR OF 405-424 AND 436-456.
[22]	"Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation." Schneider M.L., Post C.B. Biochemistry 34:16574-16584(1995) [PubMed: 8527430] [Abstract] Cited for: STRUCTURE BY NMR OF 1-16.
[23]	"Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase." Eisenmesser E.Z., Post C.B. Biochemistry 37:867-877(1998) [PubMed: 9454576] [Abstract] Cited for: STRUCTURE BY NMR OF 1-16.
[24]	"Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger." Chambers E.J., Askin D., Bloomberg G.B., Ring S.M., Tanner M.J. Biochem. Soc. Trans. 26:516-520(1998) [PubMed: 9765907] [Abstract] Cited for: STRUCTURE BY NMR OF 389-430.
[25]	"NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3." Askin D., Bloomberg G.B., Chambers E.J., Tanner M.J. Biochemistry 37:11670-11678(1998) [PubMed: 9709005] [Abstract] Cited for: STRUCTURE BY NMR OF 803-835.
[26]	"Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods." Yannoukakos D., Vasseur C., Driancourt C., Blouquit Y., Delauney J., Wajcman H., Bursaux E. Blood 78:1117-1120(1991) [PubMed: 1678289] [Abstract] Cited for: VARIANT MEMPHIS GLU-56.
[27]	"Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis." Jarolim P., Palek J., Amato D., Hassan K., Sapak P., Nurse G.T., Rubin H.L., Zhai S., Sahr K.E., Liu S.-C. Proc. Natl. Acad. Sci. U.S.A. 88:11022-11026(1991) [PubMed: 1722314] [Abstract] Cited for: VARIANT EL4 400-ALA--ALA-408 DEL, VARIANT MEMPHIS GLU-56.
[28]	"Band 3 Tuscaloosa: Pro-327-->Arg substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2." Jarolim P., Palek J., Rubin H.L., Prchal J.T., Korsgren C., Cohen C.M. Blood 80:523-529(1992) [PubMed: 1378323] [Abstract] Cited for: VARIANT SPH4 ARG-327.
[29]	"Basis of unique red cell membrane properties in hereditary ovalocytosis." Schofield A.E., Tanner M.J.A., Pinder J.C., Clough B., Bayley P.M., Nash G.B., Dluzewski A.R., Reardon D.M., Cox T.M., Wilson R.J.M., Gratzer W.B. J. Mol. Biol. 223:949-958(1992) [PubMed: 1538405] [Abstract] Cited for: VARIANT EL4 400-ALA--ALA-408 DEL.
[30]	"Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3." Bruce L.J., Kay M.M., Lawrence C., Tanner M.J. Biochem. J. 293:317-320(1993) [PubMed: 8343110] [Abstract] Cited for: VARIANT ACANTHOCYTOSIS LEU-868.
[31]	"Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia and a homozygous 40 glutamic acid-->lysine substitution in the cytoplasmic domain of band 3 (band 3Montefiore)." Rybicki A.C., Qiu J.J.H., Musto S., Rosen N.L., Nagel R.L., Schwartz R.S. Blood 81:2155-2165(1993) [PubMed: 8471774] [Abstract] Cited for: VARIANT HEMOLYTIC ANEMIA LYS-40.
[32]	"Band 3 Memphis variant II. Altered stilbene disulfonate binding and the Diego (Dia) blood group antigen are associated with the human erythrocyte band 3 mutation Pro-854-->Leu." Bruce L.J., Anstee D.J., Spring F.A., Tanner M.J. J. Biol. Chem. 269:16155-16158(1994) [PubMed: 8206915] [Abstract] Cited for: VARIANTS BLOOD GROUP DI(A)/MEMPHIS-II GLU-56 AND LEU-854.
[33]	"Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: a site of interaction between band 3 and glycophorin A under certain conditions." Bruce L.J., Ring S.M., Anstee D.J., Reid M.E., Wilkinson S., Tanner M.J. Blood 85:541-547(1995) [PubMed: 7812009] [Abstract] Cited for: VARIANT BLOOD GROUP WR(A) LYS-658.
[34]	"Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis." Jarolim P., Rubin H.L., Brabec V., Chrobak L., Zolotarev A.S., Alper S.L., Brugnara C., Wichterle H., Palek J. Blood 85:634-640(1995) [PubMed: 7530501] [Abstract] Cited for: VARIANTS SPH4 GLN-760; TRP-760; CYS-808 AND TRP-870.
[35]	"Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency." Jarolim P., Murray J.L., Rubin H.L., Taylor W.M., Prchal J.T., Ballas S.K., Snyder L.M., Chrobak L., Melrose W.D., Brabec V., Palek J. Blood 88:4366-4374(1996) [PubMed: 8943874] [Abstract] Cited for: VARIANTS SPH4 ASP-285; GLU-455; PRO-707; PRO-834 AND MET-837.
[36]	"Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis." Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M., Herbers J., Kugler W., Oezcan R., Pekrun A., Gallagher P.G., Schroeter W., Forget B.G., Lux S.E. Nat. Genet. 13:214-218(1996) [PubMed: 8640229] [Abstract] Cited for: VARIANTS SPH4 LYS-40; CYS-518 AND MET-663 DEL.
[37]	"Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis." Alloisio N., Texier P., Vallier A., Ribeiro M.L., Morle L., Bozon M., Bursaux E., Maillet P., Goncalves P., Tanner M.J., Tamagnini G., Delaunay J. Blood 90:414-420(1997) [PubMed: 9207478] [Abstract] Cited for: VARIANTS SPH4 SER-147 AND MET-488.
[38]	"Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated with hereditary spherocytosis and band 3 deficiency: status of the D38A polymorphism within the EPB3 locus." Miraglia del Giudice E., Vallier A., Maillet P., Perrotta S., Cutillo S., Iolascon A., Tanner M.J., Delaunay J., Alloisio N. Br. J. Haematol. 96:70-76(1997) [PubMed: 9012689] [Abstract] Cited for: VARIANT SPH4 ASN-783, VARIANTS ALA-38 AND MET-73.
[39]	"Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects." Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T., Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M. Br. J. Haematol. 98:32-40(1997) [PubMed: 9233560] [Abstract] Cited for: VARIANTS SPH4 CYS-490 AND MET-837.
[40]	Erratum Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T., Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M. Br. J. Haematol. 99:474-474(1997)
[41]	"Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene." Bruce L.J., Cope D.L., Jones G.K., Schofield A.E., Burley M., Povey S., Unwin R.J., Wrong O., Tanner M.J. J. Clin. Invest. 100:1693-1707(1997) [PubMed: 9312167] [Abstract] Cited for: VARIANTS DRTA CYS-589; HIS-589 AND PHE-613.
[42]	"Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3." Jarolim P., Murray J.L., Rubin H.L., Smart E., Moulds J.M. Transfusion 37:607-615(1997) [PubMed: 9191821] [Abstract] Cited for: VARIANTS BLOOD GROUPS RB(A); TR(A) AND WD(A).
[43]	"Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis." Iwase S., Ideguchi H., Takao M., Horiguchi-Yamada J., Iwasaki M., Takahara S., Sekikawa T., Mochizuki S., Yamada H. Acta Haematol. 100:200-203(1998) [PubMed: 9973643] [Abstract] Cited for: VARIANT SPH4 ALA-837.
[44]	"Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein." Jarolim P., Rubin H.L., Zakova D., Storry J., Reid M.E. Blood 92:4836-4843(1998) [PubMed: 9845551] [Abstract] Cited for: VARIANTS BLOOD GROUPS BOW; BP(A); ELO; HG(A); MO(A); VG(A) AND WU.
[45]	"Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A." Tanphaichitr V.S., Sumboonnanonda A., Ideguchi H., Shayakul C., Brugnara C., Takao M., Veerakul G., Alper S.L. J. Clin. Invest. 102:2173-2179(1998) [PubMed: 9854053] [Abstract] Cited for: VARIANT DRTA ASP-701.
[46]	"Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis." Karet F.E., Gainza F.J., Gyory A.Z., Unwin R.J., Wrong O., Tanner M.J.A., Nayir A., Alpay H., Santos F., Hulton S.A., Bakkaloglu A., Ozen S., Cunningham M.J., di Pietro A., Walker W.G., Lifton R.P. Proc. Natl. Acad. Sci. U.S.A. 95:6337-6342(1998) [PubMed: 9600966] [Abstract] Cited for: VARIANTS DRTA HIS-589 AND SER-589.
[47]	"A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism." Zelinski T., McManus K., Punter F., Moulds M., Coghlan G. Transfusion 38:745-748(1998) [PubMed: 9709782] [Abstract] Cited for: VARIANTS BLOOD GROUP WU.
[48]	"Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis." Lima P.R.M., Sales T.S.I., Costa F.F., Saad S.T.O. Eur. J. Haematol. 63:360-361(1999) [PubMed: 10580570] [Abstract] Cited for: VARIANT SPH4 HIS-490.
[49]	"Band 3 mutations, renal tubular acidosis and South-East Asian ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red cells." Bruce L.J., Wrong O., Toye A.M., Young M.T., Ogle G., Ismail Z., Sinha A.K., McMaster P., Hwaihwanje I., Nash G.B., Hart S., Lavu E., Palmer R., Othman A., Unwin R.J., Tanner M.J.A. Biochem. J. 350:41-51(2000) [PubMed: 10926824] [Abstract] Cited for: VARIANTS DRTA ASP-701; VAL-850 DEL AND ASP-858.
[50]	"Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3." Ribeiro M.L., Alloisio N., Almeida H., Gomes C., Texier P., Lemos C., Mimoso G., Morle L., Bey-Cabet F., Rudigoz R.-C., Delaunay J., Tamagnini G. Blood 96:1602-1604(2000) [PubMed: 10942416] [Abstract] Cited for: VARIANT SPH4 MET-488.
[51]	"Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population." Yawata Y., Kanzaki A., Yawata A., Doerfler W., Oezcan R., Eber S.W. Int. J. Hematol. 71:118-135(2000) [PubMed: 10745622] [Abstract] Cited for: VARIANTS SPH4 ARG-130; ARG-455; ARG-714; TRP-760; GLN-760; HIS-808; ARG-837 AND MET-837, VARIANTS ALA-38; GLU-56; ASP-72 AND LEU-854.
[52]	"Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger." Quilty J.A., Reithmeier R.A. Traffic 1:987-998(2000) [PubMed: 11208088] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS PRO-707; GLN-760; TRP-760; CYS-808; PRO-834; MET-837 AND TRP-870.
[53]	"Amino acid substitutions in human erythroid protein band 3 account for the low-incidence antigens NFLD and BOW." McManus K., Pongoski J., Coghlan G., Zelinski T. Transfusion 40:325-329(2000) [PubMed: 10738034] [Abstract] Cited for: VARIANTS BLOOD GROUP NFLD+ ASP-429 AND ALA-561, VARIANT BLOOD GROUP BOW+ SER-561.
[54]	"An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism." McManus K., Lupe K., Coghlan G., Zelinski T. Transfusion 40:1246-1249(2000) [PubMed: 11061863] [Abstract] Cited for: VARIANT BLOOD GROUP FR(A+) LYS-480.
[55]	"Distinctive Swann blood group genotypes: molecular investigations." Zelinski T., Rusnak A., McManus K., Coghlan G. Vox Sang. 79:215-218(2000) [PubMed: 11155072] [Abstract] Cited for: VARIANTS BLOOD GROUP SW(A+) GLN-646 AND TRP-646.
[56]	"Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III." Bracher N.A., Lyons C.A., Wessels G., Mansvelt E., Coetzer T.L. Br. J. Haematol. 113:689-693(2001) [PubMed: 11380459] [Abstract] Cited for: VARIANTS SPH4 LYS-90 AND TRP-870.
[57]	"Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis." Sritippayawan S., Sumboonnanonda A., Vasuvattakul S., Keskanokwong T., Sawasdee N., Paemanee A., Thuwajit P., Wilairat P., Nimmannit S., Malasit P., Yenchitsomanus P.T. Am. J. Kidney Dis. 44:64-70(2004) [PubMed: 15211439] [Abstract] Cited for: VARIANTS DRTA PRO-602 AND PRO-773.
[58]	"A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells." Rungroj N., Devonald M.A.J., Cuthbert A.W., Reimann F., Akkarapatumwong V., Yenchitsomanus P.-T., Bennett W.M., Karet F.E. J. Biol. Chem. 279:13833-13838(2004) [PubMed: 14734552] [Abstract] Cited for: VARIANT DRTA ARG-609.
[59]	"Band 3Tambau: a de novo mutation in the AE1 gene associated with hereditary spherocytosis. Implications for anion exchange and insertion into the red blood cell membrane." Lima P.R.M., Baratti M.O., Chiattone M.L., Costa F.F., Saad S.T.O. Eur. J. Haematol. 74:396-401(2005) [PubMed: 15813913] [Abstract] Cited for: VARIANT SPH4 LYS-663.
[60]	"Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1." Bruce L.J., Robinson H.C., Guizouarn H., Borgese F., Harrison P., King M.-J., Goede J.S., Coles S.E., Gore D.M., Lutz H.U., Ficarella R., Layton D.M., Iolascon A., Ellory J.C., Stewart G.W. Nat. Genet. 37:1258-1263(2005) [PubMed: 16227998] [Abstract] Cited for: VARIANTS SPH4 PRO-687; TYR-705; PRO-731; ARG-734 AND GLN-760.
+	Additional computationally mapped references.

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Web resources

Wikipedia

Band 3 entry

dbRBC/BGMUT

Blood group antigen gene mutation database

GeneReviews

SeattleSNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12609 mRNA. Translation: CAA31128.1.
M27819 mRNA. Translation: AAA35514.1.
DQ419529 mRNA. Translation: ABD74692.1.
DQ072115 Genomic DNA. Translation: AAY57324.1.
BC096106 mRNA. Translation: AAH96106.1.
BC096107 mRNA. Translation: AAH96107.1.
BC099628 mRNA. Translation: AAH99628.1.
BC099629 mRNA. Translation: AAH99629.1.
BC101570 mRNA. Translation: AAI01571.1.
BC101574 mRNA. Translation: AAI01575.1.
S68680 mRNA. Translation: AAC60608.2.

IPI

IPI00926256.

PIR

B3HU. A36218.

RefSeq

NP_000333.1.

UniGene

Hs.443948

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BH7	NMR	-	A	803-835	[»]
1BNX	NMR	-	A	389-430	[»]
1BTQ	NMR	-	A	405-424	[»]
1BTR	NMR	-	A	405-424	[»]
1BTS	NMR	-	A	436-456	[»]
1BTT	NMR	-	A	436-456	[»]
1BZK	NMR	-	A	389-430	[»]
1HYN	X-ray	2.60	P/Q/R/S	1-379	[»]
2BTA	NMR	-	A	1-15	[»]
2BTB	NMR	-	A	1-15	[»]
3BTB	NMR	-	A	1-15	[»]

DisProt

DP00426.

ModBase

Search...

Protein-protein interaction databases

STRING

P02730.

Protein family/group databases

TCDB

2.A.31.1.1. anion exchanger (AE) family.

PTM databases

PhosphoSite

P02730.

Proteomic databases

PRIDE

P02730.

Genome annotation databases

Ensembl

ENST00000262418; ENSP00000262418; ENSG00000004939; Homo sapiens. [Genome view]

GeneID

6521.

KEGG

hsa:6521.

UCSC

uc002igf.2. human.

Organism-specific databases

CTD

6521.

GeneCards

GC17M039683.

H-InvDB

HIX0039232.

HGNC

HGNC:11027. SLC4A1.

HPA

HPA015584.

MIM

109270. gene+phenotype.
110500. phenotype.
112010. phenotype.
112050. phenotype.
130600. phenotype.
179800. phenotype.
601550. phenotype.
601551. phenotype.
611590. phenotype.
612653. phenotype.

Orphanet

288. Elliptocytosis, hereditary.
18. Renal tubular acidosis, distal.
822. Spherocytosis hereditary.

PharmGKB

PA35895.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12370.

HOGENOM

HBG355640.

HOVERGEN

HBG004326.

InParanoid

P02730.

OMA

DYTQLGR.

OrthoDB

EOG93N9XW.

PhylomeDB

P02730.

Enzyme and pathway databases

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P02730.

Bgee

P02730.

Genevestigator

P02730.

GermOnline

ENSG00000004939. Homo sapiens.

Family and domain databases

InterPro

IPR001717. Anion_exchange.
IPR002977. Anion_exchange_1.
IPR018241. Anion_exchange_CS.
IPR011531. HCO3_transpt_C.
IPR013769. HCO3_transpt_cyt.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
[Graphical view]

Gene3D

G3DSA:3.40.1100.10. HCO3_transpt_cyt. 1 hit.

PANTHER

PTHR11453. HCO3_transpt_euk. 1 hit.

Pfam

PF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 2 hits.
[Graphical view]

PRINTS

PR00165. ANIONEXCHNGR.
PR01187. ANIONEXHNGR1.
PR01231. HCO3TRNSPORT.

SUPFAM

SSF55804. PTrfase/Anion_transptr. 1 hit.

TIGRFAMs

TIGR00834. ae. 1 hit.

PROSITE

PS00219. ANION_EXCHANGER_1. 1 hit.
PS00220. ANION_EXCHANGER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

25367.

PMAP-CutDB

P02730.

SOURCE

Search...

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Entry information

Entry name

B3AT_HUMAN

Accession

Primary (citable) accession number: P02730
Secondary accession number(s): P78487

Q9UCY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	March 2, 2010
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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