B3A2_RAT
ID B3A2_RAT Reviewed; 1234 AA.
AC P23347;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Anion exchange protein 2;
DE Short=AE 2;
DE Short=Anion exchanger 2;
DE AltName: Full=Band 3-related protein 2;
DE Short=B3RP-2;
DE AltName: Full=Non-erythroid band 3-like protein;
DE AltName: Full=Solute carrier family 4 member 2;
GN Name=Slc4a2; Synonyms=Ae2, B3rp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach;
RX PubMed=2294114; DOI=10.1016/s0021-9258(19)40253-6;
RA Kudrycki K.E., Newman P.R., Shull G.E.;
RT "cDNA cloning and tissue distribution of mRNAs for two proteins that are
RT related to the band 3 Cl-/HCO3-exchanger.";
RL J. Biol. Chem. 265:462-471(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2371270; DOI=10.1073/pnas.87.14.5278;
RA Lindsey A.E., Schneider K., Simmons D.M., Baron R., Lee B.S., Kopito R.R.;
RT "Functional expression and subcellular localization of an anion exchanger
RT cloned from choroid plexus.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5278-5282(1990).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND THR-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plasma membrane anion exchange protein of wide distribution.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; J05166; AAA40799.1; -; mRNA.
DR PIR; A34911; A34911.
DR RefSeq; NP_058744.1; NM_017048.2.
DR RefSeq; XP_006235936.1; XM_006235874.3.
DR RefSeq; XP_006235937.1; XM_006235875.3.
DR AlphaFoldDB; P23347; -.
DR SMR; P23347; -.
DR BioGRID; 246904; 1.
DR IntAct; P23347; 1.
DR STRING; 10116.ENSRNOP00000019666; -.
DR GlyGen; P23347; 3 sites.
DR iPTMnet; P23347; -.
DR PhosphoSitePlus; P23347; -.
DR PaxDb; P23347; -.
DR PRIDE; P23347; -.
DR Ensembl; ENSRNOT00000019666; ENSRNOP00000019666; ENSRNOG00000014347.
DR GeneID; 24780; -.
DR KEGG; rno:24780; -.
DR CTD; 6522; -.
DR RGD; 3711; Slc4a2.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000158259; -.
DR HOGENOM; CLU_002289_1_0_1; -.
DR InParanoid; P23347; -.
DR OMA; GFHLDIV; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; P23347; -.
DR TreeFam; TF313630; -.
DR Reactome; R-RNO-425381; Bicarbonate transporters.
DR PRO; PR:P23347; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000014347; Expressed in stomach and 19 other tissues.
DR Genevisible; P23347; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0097186; P:amelogenesis; ISO:RGD.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0070175; P:positive regulation of enamel mineralization; ISO:RGD.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR001717; Anion_exchange.
DR InterPro; IPR002978; Anion_exchange_2.
DR InterPro; IPR018241; Anion_exchange_CS.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR PANTHER; PTHR11453:SF14; PTHR11453:SF14; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01188; ANIONEXHNGR2.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE 1: Evidence at protein level;
KW Anion exchange; Antiport; Glycoprotein; Ion transport; Lipoprotein;
KW Membrane; Methylation; Palmitate; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1234
FT /note="Anion exchange protein 2"
FT /id="PRO_0000079218"
FT TOPO_DOM 1..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 705..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..771
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..893
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 894..911
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 912..926
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 927..947
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1003
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1029..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1084..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1156..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..1234
FT /note="Membrane (anion exchange)"
FT COMPBIAS 33..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 271
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT LIPID 1166
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 856
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 206
FT /note="G -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 925..926
FT /note="RR -> PG (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1018..1019
FT /note="ML -> IV (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1156..1157
FT /note="MH -> ID (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1234 AA; 136636 MW; FAB4ED12BB916216 CRC64;
MSSAPRRPAS GADSLHTPEP ESLSPGTPGF PEQEEEDELR TLGVERFEEI LQEAGSRGGE
EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GPGRKPRRRP GASPTGETPT
IEEGEEDEDE VGEAEGFRAP PQQPSPASSP SAVQFFLQED EGTDRKAERT SPSPPTQTPH
QEAAPRASKG AQTGTLVEEM VAVASGTAGG DDGGAAGRPL TKAQPGHRSY NLQERRRIGS
MTGVEQALLP RVPTDESEAQ TLATADLDLM KSHRFEDVPG VRRHLVRKNA KGSTQAAREG
REPGPTPRAR PRAPHKPHEV FVELNELQLD KNQEPQWRET ARWIKFEEDV EEETERWGKP
HVASLSFRSL LELRRTLAHG AVLLDLDQQT LPGVAHQVVE QMVISDQIKA EDRANVLRAL
LLKHSHPSDE KEFSFPRNIS AGSLGSLLGH HHAQGTESDP HVTEPLIGGV PETRLEVDRE
RELPPPAPPA GITRSKSKHE LKLLEKIPEN AEATVVLVGC VEFLSRPTMA FVRLREAVEL
DAVLEVPVPV RFLFLLLGPS SANMDYHEIG RSISTLMSDK QFHEAAYLAD ERDDLLTAIN
AFLDCSVVLP PSEVQGEELL RSVAHFQRQM LKKREEQGRL LPPGAGLEPK SAQDKALLQM
VEVAGAAEDD PLRRTGRPFG GLIRDVRRRY PHYLSDFRDA LDPQCLAAVI FIYFAALSPA
ITFGGLLGEK TQDLIGVSEL IMSTALQGVI FCLLGAQPLL VIGFSGPLLV FEEAFFSFCK
SNQLEYLVGR VWIGFWLVLL ALLMVALEGS FLVRFVSRFT QEIFAFLISL IFIYETFYKL
IKIFQEHPLH GCSVSNDSEA DSSSNNMTWA ATTLAPDNSS ASGQERPRGQ PNTALLSLVL
MAGTFFIAFF LRKFKNSRFF PGRIRRVIGD FGVPIAILIM VLVDYSIEDT YTQKLSVPSG
FSVTAPDKRG WVINPLGEKT PFPVWMMVAS LLPAVLVFIL IFMETQITTL IISKKERMLQ
KGSGFHLDLL LIVAMGGICA LFGLPWLAAA TVRSVTHANA LTVMSKAVAP GDKPKIQEVK
EQRVTGLLVA LLVGLSMVIG DLLRQIPLAV LFGIFLYMGV TSLNGIQFYE RLHLLLMPPK
HHPDVTYVKK VRTMRMHLFT ALQLLCLALL WAVMSTAASL AFPFILILTV PLRMVVLTRI
FTEREMKCLD ANEAEPVFDE CEGVDEYNEM PMPV
