B3A3_RAT
ID B3A3_RAT Reviewed; 1227 AA.
AC P23348;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Anion exchange protein 3;
DE Short=AE 3;
DE Short=Anion exchanger 3;
DE AltName: Full=Band 3-related protein 3;
DE Short=B3RP-3;
DE AltName: Full=Neuronal band 3-like protein;
DE AltName: Full=Solute carrier family 4 member 3;
GN Name=Slc4a3; Synonyms=Ae3, B3rp3;
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].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-170; SER-175 AND
RP SER-198, AND 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.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Neuronal.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; J05167; AAA40798.1; -; mRNA.
DR PIR; B34911; B34911.
DR RefSeq; NP_058745.1; NM_017049.1.
DR AlphaFoldDB; P23348; -.
DR SMR; P23348; -.
DR BioGRID; 246905; 1.
DR STRING; 10116.ENSRNOP00000027337; -.
DR GlyGen; P23348; 1 site.
DR iPTMnet; P23348; -.
DR PhosphoSitePlus; P23348; -.
DR PaxDb; P23348; -.
DR PRIDE; P23348; -.
DR GeneID; 24781; -.
DR KEGG; rno:24781; -.
DR UCSC; RGD:3712; rat.
DR CTD; 6508; -.
DR RGD; 3712; Slc4a3.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; P23348; -.
DR PhylomeDB; P23348; -.
DR Reactome; R-RNO-425381; Bicarbonate transporters.
DR PRO; PR:P23348; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0015301; F:anion:anion antiporter activity; ISO:RGD.
DR GO; GO:0015106; F:bicarbonate 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:0015701; P:bicarbonate transport; ISO:RGD.
DR GO; GO:0061337; P:cardiac conduction; ISO:RGD.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; ISO: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; IPR002979; Anion_exchange_3.
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:SF15; PTHR11453:SF15; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01189; ANIONEXHNGR3.
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..1227
FT /note="Anion exchange protein 3"
FT /id="PRO_0000079222"
FT TOPO_DOM 1..707
FT /note="Cytoplasmic"
FT TRANSMEM 708..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 975..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1023..1044
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1078..1123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1150..1186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..1227
FT /note="Membrane (anion exchange)"
FT COMPBIAS 7..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 294
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P16283"
FT LIPID 1160
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1227 AA; 135407 MW; 3EB1620EE011730E CRC64;
MANGVIPPPG GPSPLPQVRV PLEEPPLGPD VEEEDDDLGK TLAVSRFGDL ISKTPAWDPE
KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRLPP TSARHARRKR KKEKTSAPPS
EGTPPIQEEG GAGAEEEEEE EEEEEGESEA EPVEPPPPGP PQKAKFSIGS DEDDSPGLSI
KAPCAKALPS VGLPSDQSPQ RSGSSPSPRA RASRISTEKS RPWSPSASYD LRERLCPGSA
LGNPGPEQRV PTDEAEAQML GSADLDDMKS HRLEDNPGVR RHLVKKPSRI QGGRGSPSGL
APILRRKKKK KKLDRRPHEV FVELNELMLD RSQEPHWRET ARWIKFEEDV EEETERWGKP
HVASLSFRSL LELRRTIAQG AALLDLEQTT LPGIAHLVVE TMIVSDQIRP EDRASVLRTL
LLKHSHPNDD KDSGFFPRNP SSSSVNSVLG NHHPTPSHGP DGAVPTMADD LGEPAPLWPH
DPDAKEKPLH MPGGDGHRGK SLKLLEKIPE DAEATVVLVG SVPFLEQPAA AFVRLSEAVL
LESVLEVPVP VRFLFVMLGP SHTSTDYHEL GRSIATLMSD KLFHEAAYQA DDRQDLLGAI
SEFLDGSIVI PPSEVEGRDL LRSVAAFQRE LLRKRREREQ TKVEMTTRGG YVAPGKELSL
EMGGSEATSE DDPLQRTGSV FGGLVRDVKR RYPHYPSDLR DALHSQCVAA VLFIYFAALS
PAITFGGLLG EKTEGLMGVS ELIVSTAVLG VLFSLLGAQP LLVVGFSGPL LVFEEAFFKF
CRAQDLEYLT GRVWVGLWLV VFVLALVAAE GSFLVRYISP FTQEIFAFLI SLIFIYETFH
KLYKVFTEHP LLPFYPPEEA LEPGLELNSS ALPPTEGPPG PRNQPNTALL SLILMLGTFL
IAFFLRKFRN SRFLGGKARR VIGDFGIPIS ILVMVLVDYS ITDTYTQKLT VPTGLSVTSP
HKRTWFIPPL GSARPFPPWM MVAAAVPALL VLILIFMETQ ITALIVSQKA RRLLKGSGFH
LDLLLIGSLG GLCGLFGLPW LTAATVRSVT HVNALTVMRT AIAPGDKPQI QEVREQRVTG
VLIASLVGLS IVMGAVLRRI PLAVLFGIFL YMGVTSLSGI QLSQRLLLIF MPAKHHPEQP
YVTKVKTWRM HLFTFIQLGC IALLWVVKST VASLAFPFLL LLTVPLRRCL LPRLFQDREL
QALDSEDAEP NFDEDGQDEY NELHMPV
