関: band 3 erythrocyte membrane protein band 3 anion exchanger 1 Diego blood group, solute carrier family 4, ion exchanger member 1

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2022/10/20 18:16:41」(JST)

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Band 3 anion transport protein, also known as anion exchanger 1 (AE1) or band 3 or solute carrier family 4 member 1 (SLC4A1), is a protein that is encoded by the SLC4A1 gene in humans.

Band 3 anion transport protein is a phylogenetically-preserved transport protein responsible for mediating the exchange of chloride (Cl⁻) with bicarbonate (HCO₃⁻) across plasma membranes. Functionally similar members of the AE clade are AE2 and AE3.^[5]

Function

Band 3 is present in the basolateral face of the α-intercalated cells of the collecting ducts of the nephron, which are the main acid-secreting cells of the kidney. They generate hydrogen ions and bicarbonate ions from carbon dioxide and water – a reaction catalysed by carbonic anhydrase. The hydrogen ions are pumped into the collecting duct tubule by vacuolar H⁺ ATPase, the apical proton pump, which thus excretes acid into the urine. kAE1 exchanges bicarbonate for chloride on the basolateral surface, essentially returning bicarbonate to the blood. Here it performs two functions:^{[citation needed]}

Electroneutral chloride and bicarbonate exchange across the plasma membrane on a one-for-one basis. This is crucial for CO₂ uptake by the red blood cell and conversion (by hydration catalysed by carbonic anhydrase) into a proton and a bicarbonate ion. The bicarbonate is then excreted (in exchange for a chloride) from the cell by band 3.
Physical linkage of the plasma membrane to the underlying membrane skeleton (via binding with ankyrin and protein 4.2). This appears to be to prevent membrane surface loss, rather than having to do with membrane skeleton assembly.

Distribution

It is ubiquitous throughout the vertebrates. In mammals, it is present in two specific sites:^{[citation needed]}

the erythrocyte (red blood cell) cell membrane and
the basolateral surface of the alpha-intercalated cell (the acid secreting cell type) in the collecting duct of the kidney.

Gene products

The erythrocyte and kidney forms are different isoforms of the same protein.^[6]

The erythrocyte isoform of AE1, known as eAE1, is composed of 911 amino acids. eAE1 is an important structural component of the erythrocyte cell membrane, making up to 25% of the cell membrane surface. Each red cell contains approximately one million copies of eAE1.^{[citation needed]}

The kidney isoform of AE1, known as kAE1 (which is 65 amino acids shorter than erythroid AE1) is found in the basolateral membrane of alpha-intercalated cells in the cortical collecting duct of the kidney.^{[citation needed]}

Clinical significance

Mutations of kidney AE1 cause distal (type 1) renal tubular acidosis, which is an inability to acidify the urine, even if the blood is too acidic. These mutations are disease causing as they cause mistargetting of the mutant band 3 proteins so that they are retained within the cell or occasionally addressed to the wrong (i.e. apical) surface.^{[citation needed]}

Mutations of erythroid AE1 affecting the extracellular domains of the molecule may cause alterations in the individual's blood group, as band 3 determines the Diego antigen system (blood group).^{[citation needed]}

More importantly erythroid AE1 mutations cause 15–25% of cases of hereditary spherocytosis (a disorder associated with progressive red cell membrane loss), and also cause the hereditary conditions of hereditary stomatocytosis^[7] and Southeast Asian ovalocytosis.^[8]

Interactions

Band 3 has been shown to interact with CA2^[9]^[10]^[11]^[12] and CA4.^[13]

Discovery

AE1 was discovered following SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) of erythrocyte cell membrane. The large 'third' band on the electrophoresis gel represented AE1, which was thus initially termed 'Band 3'.^[14]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000004939 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000006574 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Alper SL (2009). "Molecular physiology and genetics of Na+-independent SLC4 anion exchangers". Journal of Experimental Biology. 212 (11): 1672–1683. doi:10.1242/jeb.029454. PMC 2683012. PMID 19448077.
^ Schlüter K, Drenckhahn D (August 1986). "Co-clustering of denatured hemoglobin with band 3: its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes". Proc. Natl. Acad. Sci. U.S.A. 83 (16): 6137–41. Bibcode:1986PNAS...83.6137S. doi:10.1073/pnas.83.16.6137. PMC 386454. PMID 3461480.
^ Bruce LJ, Robinson HC, Guizouarn H, Borgese F, Harrison P, King MJ, Goede JS, Coles SE, Gore DM, Lutz HU, Ficarella R, Layton DM, Iolascon A, Ellory JC, Stewart GW (2005). "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". Nat. Genet. 37 (11): 1258–63. doi:10.1038/ng1656. PMID 16227998. S2CID 23554234.
^ Jarolim P, Palek J, Amato D, Hassan K, Sapak P, Nurse GT, Rubin HL, Zhai S, Sahr KE, Liu SC (1991). "Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11022–6. Bibcode:1991PNAS...8811022J. doi:10.1073/pnas.88.24.11022. PMC 53065. PMID 1722314.
^ Sterling D, Reithmeier RA, Casey JR (Dec 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. 276 (51): 47886–94. doi:10.1074/jbc.M105959200. PMID 11606574.
^ Vince JW, Reithmeier RA (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. 273 (43): 28430–7. doi:10.1074/jbc.273.43.28430. PMID 9774471.
^ Vince JW, Carlsson U, Reithmeier RA (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry. 39 (44): 13344–9. doi:10.1021/bi0015111. PMID 11063570.
^ Vince JW, Reithmeier RA (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry. 39 (18): 5527–33. doi:10.1021/bi992564p. PMID 10820026.
^ Sterling D, Alvarez BV, Casey JR (July 2002). "The extracellular component of a transport metabolon. Extracellular loop 4 of the human AE1 Cl-/HCO3- exchanger binds carbonic anhydrase IV". J. Biol. Chem. 277 (28): 25239–46. doi:10.1074/jbc.M202562200. PMID 11994299.
^ Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter. Molecular Biology of the Cell (Fourth ed.). Garland Science. p. 604. ISBN 0815332181.

External links

Diego blood group system at BGMUT Blood Group Antigen Gene Mutation Database at NCBI, NIH
Band+3+Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
Chloride-Bicarbonate+Antiporters at the US National Library of Medicine Medical Subject Headings (MeSH)
Human SLC4A1 genome location and SLC4A1 gene details page in the UCSC Genome Browser.

English Journal

Mass Spectrometry Method to Measure Membrane Proteins in Dried Blood Spots for the Detection of Blood Doping Practices in Sport.

Cox HD1, Eichner D1.
Analytical chemistry.Anal Chem.2017 Sep 19;89(18):10029-10036. doi: 10.1021/acs.analchem.7b02492. Epub 2017 Aug 31.
PMID 28829585

Identification of sheep red blood cell (SRBC) surface immune-responsive peptides detected by antisera from SRBC-immunized rats.

Yamanaka H1, Takeyoshi M.
The Journal of toxicological sciences.J Toxicol Sci.2016 Feb;41(1):13-6. doi: 10.2131/jts.41.13.
PMID 26763388

Identification of a cross-reacting, monoclonal anti-human CD233 antibody for identification and sorting of rhesus macaque erythrocytes.

Byrnes C1, Terry Lee Y, Donahue RE, Miller JL.
Cytometry. Part A : the journal of the International Society for Analytical Cytology.Cytometry A.2012 Feb;81(2):165-8. doi: 10.1002/cyto.a.22005. Epub 2011 Dec 13.
PMID 22170815

Japanese Journal

Identification of sheep red blood cell (SRBC) surface immune-responsive peptides detected by antisera from SRBC-immunized rats

The Journal of Toxicological Sciences 41(1), 13-16, 2016
NAID 130005119788

炎症性腸疾患手術例における腸管外合併症の検討 : 手術が腸管外合併症に与える影響について

日本大腸肛門病学会雑誌 59(7), 378-384, 2006-07-01
NAID 10018260562

Related Pictures

サイズレッド CD233-5-RE 画像1 AN ANCIENT CHINESE BRONZ COIN CD233 Cannibal Chronograph Watch CD233-03 cd233 CD233 T-6 Texan

★リンクテーブル★

リンク元	「バンド3蛋白」
関連記事	「CD23」「CD2」

「バンド3蛋白」

Search for
Structures	Swiss-model
Domains	InterPro

solute carrier family 4 (anion exchanger), member 1, adapter protein
solute carrier family 4 (anion exchanger), member 1, adapter protein
Identifiers
Symbol	SLC4A1AP
NCBI gene	22950
HGNC	13813
OMIM	602655
RefSeq	NM_018158
UniProt	P02730
Other data
Locus	Chr. 2 p23.3
Structures
Search for
Structures	Swiss-model
Domains	InterPro

SLC4A1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1BH7, 1BNX, 1BTQ, 1BTR, 1BTS, 1BTT, 1BZK, 1HYN, 3BTB, 2BTA, 2BTB, 4KY9, 4YZF
Identifiers
Aliases	SLC4A1, solute carrier family 4 (anion exchanger), member 1 (Diego blood group), AE1, BND3, CD233, DI, EMPB3, EPB3, FR, RTA1A, SW, WD, WD1, WR, CHC, SAO, SPH4, solute carrier family 4 member 1 (Diego blood group)
External IDs	OMIM: 109270 MGI: 109393 HomoloGene: 133556 GeneCards: SLC4A1
Gene location (Human)
Chr.	Chromosome 17 (human)
End	44,268,141 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	102,257,029 bp
RNA expression pattern
	Top expressed in
	cancellous bone; ; bone marrow; ; bone marrow cells; ; renal medulla; ; blood; ; kidney; ; monocyte; ; kidney tubule; ; vena cava; ; glomerulus;
	Top expressed in
	blood; ; internal carotid artery; ; body of femur; ; external carotid artery; ; yolk sac; ; endocardial cushion; ; spleen; ; belly cord; ; fossa; ; atrium;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein homodimerization activity; protein-membrane adaptor activity; chloride transmembrane transporter activity; transporter activity; anion transmembrane transporter activity; bicarbonate transmembrane transporter activity; protein binding; ankyrin binding; inorganic anion exchanger activity; sodium:bicarbonate symporter activity; hemoglobin binding;
Cellular component	integral component of membrane; blood microparticle; membrane; cortical cytoskeleton; plasma membrane; integral component of plasma membrane; basolateral plasma membrane; extracellular exosome; Z disc; cytoplasmic side of plasma membrane;
Biological process	anion transport; bicarbonate transport; cellular ion homeostasis; chloride transport; ion transport; regulation of intracellular pH; anion transmembrane transport; chloride transmembrane transport; sodium ion transmembrane transport; transport; glycolytic process; blood coagulation; plasma membrane phospholipid scrambling; negative regulation of urine volume; pH elevation; erythrocyte development; protein localization to plasma membrane;
	Sources:Amigo / QuickGO
Orthologs
	6521
	20533
	ENSG00000004939
	ENSMUSG00000006574
	P02730
	P04919
	NM_000342
	NM_011403
	NP_000333
	NP_035533
	Wikidata
View/Edit Human	View/Edit Mouse

　　[★]

英: band 3 protein
関: CD233

「CD23」

　　[★]

同: FcεRII, 低親和性IgE受容体、Leucine-20、Blast-2

発現細胞

成熟B細胞、活性化マクロファージ、好酸球、濾胞樹状細胞、血小板

WCH.37

B lymphocytes, where it appears to be associated with IgD
follicular DCs, especially those in the light zone of the germinal centers
transiently on some T cells in allergic individuals
Langerhans cels
monocytes
platelets
NK cells
nasopharyngeal carcinoma cells
B-CLL
EBV-transformed B cells

機能

IgEの受容体(低親和性)
CD21やα-chain of the β2 integrinsにも結合する。
可溶性のCD23(sCD23)はIgEの産生を亢進したりIgE/Agの提示を促進したりする。またsCD23はいろいろなサイトカイン様の作用を呈する(WCH.37)

別名

FcεRII

ファミリー

C-type lectin

臨床関連

慢性リンパ性白血病(CLL)

CD5とCD23を共発現していることが特徴

CLL and WM

　　慢性リンパ性白血病(CLL)と原発性マクログロブリン血症との鑑別
CD5：　　　　陽性　　　　　　　　　　　　陰性
CD23：　　　　陽性　　　　　　　　　　　　陰性

「CD2」

　　[★]

同: Leucine-5, SRBC receptor, LFA-2
関: CD

発現細胞

T細胞、胸腺細胞、NK細胞

分子量

45-58

機能

接着分子、CD58(LFA-3)に結合。細胞内部でLckに結合し、T細胞を活性化

リンパ球が抗原提示細胞と相互作用するのに重要 (IMM.343)

別名

LFA-2, T11

ファミリー

immunoglobulin

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000004939 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000006574 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Alper SL (2009). "Molecular physiology and genetics of Na+-independent SLC4 anion exchangers". Journal of Experimental Biology. 212 (11): 1672–1683. doi:10.1242/jeb.029454. PMC 2683012. PMID 19448077.

[pmid3461480-6] Schlüter K, Drenckhahn D (August 1986). "Co-clustering of denatured hemoglobin with band 3: its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes". Proc. Natl. Acad. Sci. U.S.A. 83 (16): 6137–41. Bibcode:1986PNAS...83.6137S. doi:10.1073/pnas.83.16.6137. PMC 386454. PMID 3461480.

[pmid16227998-7] Bruce LJ, Robinson HC, Guizouarn H, Borgese F, Harrison P, King MJ, Goede JS, Coles SE, Gore DM, Lutz HU, Ficarella R, Layton DM, Iolascon A, Ellory JC, Stewart GW (2005). "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". Nat. Genet. 37 (11): 1258–63. doi:10.1038/ng1656. PMID 16227998. S2CID 23554234.

[pmid1722314-8] Jarolim P, Palek J, Amato D, Hassan K, Sapak P, Nurse GT, Rubin HL, Zhai S, Sahr KE, Liu SC (1991). "Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11022–6. Bibcode:1991PNAS...8811022J. doi:10.1073/pnas.88.24.11022. PMC 53065. PMID 1722314.

[pmid11606574-9] Sterling D, Reithmeier RA, Casey JR (Dec 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. 276 (51): 47886–94. doi:10.1074/jbc.M105959200. PMID 11606574.

[pmid9774471-10] Vince JW, Reithmeier RA (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. 273 (43): 28430–7. doi:10.1074/jbc.273.43.28430. PMID 9774471.

[pmid11063570-11] Vince JW, Carlsson U, Reithmeier RA (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry. 39 (44): 13344–9. doi:10.1021/bi0015111. PMID 11063570.

[pmid10820026-12] Vince JW, Reithmeier RA (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry. 39 (18): 5527–33. doi:10.1021/bi992564p. PMID 10820026.

[pmid11994299-13] Sterling D, Alvarez BV, Casey JR (July 2002). "The extracellular component of a transport metabolon. Extracellular loop 4 of the human AE1 Cl-/HCO3- exchanger binds carbonic anhydrase IV". J. Biol. Chem. 277 (28): 25239–46. doi:10.1074/jbc.M202562200. PMID 11994299.

[14] Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter. Molecular Biology of the Cell (Fourth ed.). Garland Science. p. 604. ISBN 0815332181.

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

匿名

検索

案内

案内

CD233

Wikipedia preview

wiki en

Contents

Function

Distribution

Gene products

Clinical significance

Interactions

Discovery

See also

References

Further reading

External links

English Journal

Japanese Journal

Related Links

Related Pictures

★リンクテーブル★

「バンド3蛋白」

「CD23」

発現細胞

WCH.37

機能

別名

ファミリー

臨床関連

CLL and WM

「CD2」

発現細胞

分子量

機能

別名

ファミリー