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P04919

- B3AT_MOUSE

UniProt

P04919 - B3AT_MOUSE

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Protein
Band 3 anion transport protein
Gene
Slc4a1, Ae1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine.

GO - Molecular functioni

  1. anion:anion antiporter activity Source: UniProtKB
  2. bicarbonate transmembrane transporter activity Source: UniProtKB
  3. chloride transmembrane transporter activity Source: UniProtKB
  4. inorganic anion exchanger activity Source: UniProtKB
  5. protein binding Source: MGI

GO - Biological processi

  1. bicarbonate transport Source: UniProtKB
  2. chloride transmembrane transport Source: GOC
  3. chloride transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Anion exchange, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Band 3 anion transport protein
Alternative name(s):
Anion exchange protein 1
Short name:
AE 1
Short name:
Anion exchanger 1
MEB3
Solute carrier family 4 member 1
CD_antigen: CD233
Gene namesi
Name:Slc4a1
Synonyms:Ae1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:109393. Slc4a1.

Subcellular locationi

Cell membrane; Multi-pass membrane protein By similarity. Basolateral cell membrane; Multi-pass membrane protein By similarity
Note: Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney By similarity.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 422422Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei423 – 44321Helical; Reviewed prediction
Add
BLAST
Transmembranei456 – 47520Helical; Reviewed prediction
Add
BLAST
Transmembranei479 – 49820Helical; Reviewed prediction
Add
BLAST
Transmembranei510 – 52920Helical; Reviewed prediction
Add
BLAST
Transmembranei542 – 56019Helical; Reviewed prediction
Add
BLAST
Topological domaini561 – 58626Extracellular Reviewed prediction
Add
BLAST
Transmembranei587 – 60620Helical; Reviewed prediction
Add
BLAST
Topological domaini607 – 62115Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei622 – 64221Helical; Reviewed prediction
Add
BLAST
Topological domaini643 – 67836Extracellular Reviewed prediction
Add
BLAST
Transmembranei679 – 69820Helical; Reviewed prediction
Add
BLAST
Transmembranei717 – 73721Helical; Reviewed prediction
Add
BLAST
Transmembranei781 – 79818Helical; Reviewed prediction
Add
BLAST
Transmembranei803 – 82422Helical; Reviewed prediction
Add
BLAST
Transmembranei862 – 88322Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Z disc Source: UniProtKB
  2. basolateral plasma membrane Source: UniProtKB
  3. cortical cytoskeleton Source: MGI
  4. integral component of plasma membrane Source: UniProtKB
  5. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Gypa is not incorporated in the erythrocyte membrane.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929Band 3 anion transport protein
PRO_0000079210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei31 – 311Phosphotyrosine By similarity
Modified residuei56 – 561Phosphotyrosine By similarity
Modified residuei372 – 3721Phosphotyrosine By similarity
Glycosylationi660 – 6601N-linked (GlcNAc...) Inferred
Lipidationi861 – 8611S-palmitoyl cysteine By similarity
Modified residuei922 – 9221Phosphotyrosine By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP04919.
PaxDbiP04919.
PRIDEiP04919.

PTM databases

PhosphoSiteiP04919.

Expressioni

Tissue specificityi

Erythrocytes.

Gene expression databases

ArrayExpressiP04919.
BgeeiP04919.
GenevestigatoriP04919.

Interactioni

Subunit structurei

A dimer in solution, but in its membrane environment, it exists primarily as a mixture of dimers and tetramers and spans the membrane asymmetrically. Interacts (via cytoplasmic N-terminal domain) with ANK1 (via N-terminal ANK repeats); tetramer formation is critical for ankyrin association. Interacts with STOM By similarity.

Protein-protein interaction databases

BioGridi203312. 2 interactions.
IntActiP04919. 4 interactions.
MINTiMINT-1861446.

Structurei

3D structure databases

ProteinModelPortaliP04919.
SMRiP04919. Positions 70-368, 408-449, 821-853.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 303235Globular By similarity
Add
BLAST
Regioni190 – 19910Interaction with ANK1 By similarity
Regioni317 – 37054Dimerization arm By similarity
Add
BLAST
Regioni423 – 929507Membrane (anion exchange)
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG268067.
HOGENOMiHOG000280683.
HOVERGENiHBG004326.
InParanoidiP04919.
KOiK06573.
OMAiEYDEVAM.
OrthoDBiEOG7TMZR0.
PhylomeDBiP04919.
TreeFamiTF313630.

Family and domain databases

Gene3Di3.40.1100.10. 1 hit.
InterProiIPR001717. Anion_exchange.
IPR002977. Anion_exchange_1.
IPR018241. Anion_exchange_CS.
IPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
[Graphical view]
PANTHERiPTHR11453. PTHR11453. 1 hit.
PfamiPF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 2 hits.
[Graphical view]
PRINTSiPR00165. ANIONEXCHNGR.
PR01187. ANIONEXHNGR1.
PR01231. HCO3TRNSPORT.
SUPFAMiSSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00834. ae. 1 hit.
PROSITEiPS00219. ANION_EXCHANGER_1. 1 hit.
PS00220. ANION_EXCHANGER_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Erythrocyte (identifier: P04919-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGDMRDHEEV LEIPDRDSEE ELENIIGQIA YRDLTIPVTE MQDPEALPTE    50
QTATDYVPSS TSTPHPSSGQ VYVELQELMM DQRNQELQWV EAAHWIGLEE 100
NLREDGVWGR PHLSYLTFWS LLELQKVFSK GTFLLGLAET SLAGVANHLL 150
DCFIYEDQIR PQDREELLRA LLLKRSHAED LGNLEGVKPA VLTRSGGASE 200
PLLPHQPSLE TQLYCGQAEG GSEGPSTSGT LKIPPDSETT LVLVGRANFL 250
EKPVLGFVRL KEAVPLEDLV LPEPVGFLLV LLGPEAPHVD YTQLGRAAAT 300
LMTERVFRIT ASMAHNREEL LRSLESFLDC SLVLPPTDAP SEKALLNLVP 350
VQKELLRRRY LPSPAKPDPN LYNTLDLNGG KGGPGDEDDP LRRTGRIFGG 400
LIRDIRRRYP YYLSDITDAL SPQVLAAVIF IYFAALSPAV TFGGLLGEKT 450
RNLMGVSELL ISTAVQGILF ALLGAQPLLV LGFSGPLLVF EEAFFSFCES 500
NNLEYIVGRA WIGFWLILLV MLVVAFEGSF LVQYISRYTQ EIFSFLISLI 550
FIYETFSKLI KIFQDYPLQQ TYAPVVMKPK PQGPVPNTAL FSLVLMAGTF 600
LLAMTLRKFK NSTYFPGKLR RVIGDFGVPI SILIMVLVDS FIKGTYTQKL 650
SVPDGLKVSN SSARGWVIHP LGLYRLFPTW MMFASVLPAL LVFILIFLES 700
QITTLIVSKP ERKMIKGSGF HLDLLLVVGM GGVAALFGMP WLSATTVRSV 750
THANALTVMG KASGPGAAAQ IQEVKEQRIS GLLVSVLVGL SILMEPILSR 800
IPLAVLFGIF LYMGVTSLSG IQLFDRILLL FKPPKYHPDV PFVKRVKTWR 850
MHLFTGIQII CLAVLWVVKS TPASLALPFV LILTVPLRRL ILPLIFRELE 900
LQCLDGDDAK VTFDEENGLD EYDEVPMPV 929
Length:929
Mass (Da):103,136
Last modified:August 13, 1987 - v1
Checksum:i5C0E281C394FB614
GO
Isoform Kidney (identifier: P04919-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Show »
Length:850
Mass (Da):94,234
Checksum:i492427A73FAA811A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7979Missing in isoform Kidney.
VSP_000454Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti467 – 4671G → S in CAA27555. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02677 mRNA. Translation: CAA26506.1.
M29379 mRNA. Translation: AAA37187.1.
J02756 Genomic DNA. Translation: AAA37278.1.
BC052419 mRNA. Translation: AAH52419.1.
BC053429 mRNA. Translation: AAH53429.1.
X03917 mRNA. Translation: CAA27555.1.
CCDSiCCDS25496.1. [P04919-1]
PIRiA25314.
RefSeqiNP_035533.1. NM_011403.2. [P04919-1]
UniGeneiMm.7248.

Genome annotation databases

EnsembliENSMUST00000006749; ENSMUSP00000006749; ENSMUSG00000006574. [P04919-1]
GeneIDi20533.
KEGGimmu:20533.
UCSCiuc007lrp.2. mouse. [P04919-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02677 mRNA. Translation: CAA26506.1 .
M29379 mRNA. Translation: AAA37187.1 .
J02756 Genomic DNA. Translation: AAA37278.1 .
BC052419 mRNA. Translation: AAH52419.1 .
BC053429 mRNA. Translation: AAH53429.1 .
X03917 mRNA. Translation: CAA27555.1 .
CCDSi CCDS25496.1. [P04919-1 ]
PIRi A25314.
RefSeqi NP_035533.1. NM_011403.2. [P04919-1 ]
UniGenei Mm.7248.

3D structure databases

ProteinModelPortali P04919.
SMRi P04919. Positions 70-368, 408-449, 821-853.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203312. 2 interactions.
IntActi P04919. 4 interactions.
MINTi MINT-1861446.

PTM databases

PhosphoSitei P04919.

Proteomic databases

MaxQBi P04919.
PaxDbi P04919.
PRIDEi P04919.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006749 ; ENSMUSP00000006749 ; ENSMUSG00000006574 . [P04919-1 ]
GeneIDi 20533.
KEGGi mmu:20533.
UCSCi uc007lrp.2. mouse. [P04919-1 ]

Organism-specific databases

CTDi 6521.
MGIi MGI:109393. Slc4a1.

Phylogenomic databases

eggNOGi NOG268067.
HOGENOMi HOG000280683.
HOVERGENi HBG004326.
InParanoidi P04919.
KOi K06573.
OMAi EYDEVAM.
OrthoDBi EOG7TMZR0.
PhylomeDBi P04919.
TreeFami TF313630.

Enzyme and pathway databases

Reactomei REACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

Miscellaneous databases

ChiTaRSi SLC4A1. mouse.
NextBioi 298795.
PROi P04919.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04919.
Bgeei P04919.
Genevestigatori P04919.

Family and domain databases

Gene3Di 3.40.1100.10. 1 hit.
InterProi IPR001717. Anion_exchange.
IPR002977. Anion_exchange_1.
IPR018241. Anion_exchange_CS.
IPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
[Graphical view ]
PANTHERi PTHR11453. PTHR11453. 1 hit.
Pfami PF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 2 hits.
[Graphical view ]
PRINTSi PR00165. ANIONEXCHNGR.
PR01187. ANIONEXHNGR1.
PR01231. HCO3TRNSPORT.
SUPFAMi SSF55804. SSF55804. 1 hit.
TIGRFAMsi TIGR00834. ae. 1 hit.
PROSITEi PS00219. ANION_EXCHANGER_1. 1 hit.
PS00220. ANION_EXCHANGER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and transmembrane orientation of the murine anion exchange protein."
    Kopito R.R., Lodish H.F.
    Nature 316:234-238(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "Structure of the murine anion exchange protein."
    Kopito R.R., Lodish H.F.
    J. Cell. Biochem. 29:1-17(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structure and organization of the murine band 3 gene."
    Kopito R.R., Andersson M., Lodish H.F.
    J. Biol. Chem. 262:8035-8040(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Kopito R.R.
    Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ERYTHROCYTE).
    Strain: C57BL/6.
    Tissue: Brain and Limb.
  6. "Cloning and structural characterization of a human non-erythroid band 3-like protein."
    Demuth D.R., Showe L.C., Ballantine M., Palumbo A., Fraser P.J., Cioe L., Rovera G., Curtis P.J.
    EMBO J. 5:1205-1214(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-929.
  7. "Major proteolytic fragments of the murine band 3 protein as obtained after in situ proteolysis."
    Raida M., Wendel J., Kojro E., Fahrenholz F., Fasold H., Legrum B., Passow H.
    Biochim. Biophys. Acta 980:291-298(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-47; 360-375; 382-395 AND 578-590.
  8. "Complete deficiency of glycophorin A in red blood cells from mice with targeted inactivation of the band 3 (AE1) gene."
    Hassoun H., Hanada T., Lutchman M., Sahr K.E., Palek J., Hanspal M., Chishti A.H.
    Blood 91:2146-2151(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiB3AT_MOUSE
AccessioniPrimary (citable) accession number: P04919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 3, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi