B3A2_HORSE
ID B3A2_HORSE Reviewed; 1237 AA.
AC Q6SJP2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Anion exchange protein 2;
DE Short=AE 2;
DE Short=Anion exchanger 2;
DE AltName: Full=Non-erythroid band 3-like protein;
DE AltName: Full=Solute carrier family 4 member 2;
GN Name=SLC4A2; Synonyms=AE2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Daly K., Nedjadi T., Shirazi-Beechey S.P.;
RT "Equine AE2 mRNA full transcript.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plasma membrane anion exchange protein of wide distribution.
CC {ECO:0000250}.
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; AY457176; AAR21623.1; -; mRNA.
DR RefSeq; NP_001075235.1; NM_001081766.1.
DR AlphaFoldDB; Q6SJP2; -.
DR SMR; Q6SJP2; -.
DR STRING; 9796.ENSECAP00000051157; -.
DR PaxDb; Q6SJP2; -.
DR GeneID; 791243; -.
DR KEGG; ecb:791243; -.
DR CTD; 6522; -.
DR InParanoid; Q6SJP2; -.
DR OrthoDB; 265068at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Anion exchange; Antiport; Glycoprotein; Ion transport; Lipoprotein;
KW Membrane; Methylation; Palmitate; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1237
FT /note="Anion exchange protein 2"
FT /id="PRO_0000354091"
FT TOPO_DOM 1..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 792..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..893
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 915..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1032..1052
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1086..1106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..1237
FT /note="Membrane (anion exchange)"
FT COMPBIAS 32..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 141..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 270
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT LIPID 1169
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1237 AA; 136357 MW; A385FD19EA34402E CRC64;
MSSAPRRPAS GADSFRTPEP EILGPATAGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE
EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDTRRRKTPQ GPGRKSRRRP GASPTGETPT
IEEGEEDEDE ASEAEGARAP TQPSPASTPS SVQFFLQEDD GADRKAERTS PSPPPPLPHQ
EAAPRATKGA QTGALVEEVM AVAGGTAGGD DGGASGRPLT KAQPGHRSYN LQERRRIGSM
TGAEQALLPR VPTDESEAQT LATADLDLMK SHRFEDVPGV RRHLVRKNAK GSVQSGREGR
EPGPTPRARP RAPHKPHEVF VELNELLLDK NQEPQWRETA RWIKFEEDVE EETERWGKPH
VASLSFRSLL ELRRTLAHGA VLLDLDQQTL PGVAHQVVEQ MVISDQIKAE DRADVLRALL
LKHSHPSDEK DFSFPRNISA GSLGSLLGHH HGQGAESDPH VTEPLIGGVP ETRLEVERER
ELSPPAPPAG ITRSKSKHEL KLLEKIPENA EATVVLVGCV EFLSRPTMAF VRLREAVELD
AVLEVPVPVR FLFLLLGPSS ANMDYHEIGR SISTLMSDKQ FHEAAYLADE REDLLTAINA
FLDCSVVLPP SEVQGEELLR SVAHFQRQML KKREEQGRLL PTGAGLEPKS AQDKALLQMV
EAAGAVEDDP LRRTGRPFGG LIRDVRRRYP HYLSDFRDAL DPQCLAAVIF IYFAALSPAI
TFGGLLGEKT QDLIGVSELI MSTALQGVVF CLLGAQPLLV IGFSGPLLVF EEAFFSFCSS
NDLEYLVGRV WIGFWLVLLA LLMVALEGSF LVRFVSRFTQ EIFAFLISLI FIYETFYKLV
KIFQEHPLHG CSVSNSSEAD SGDNATWAGT RVTLGLGNGS SAGPAGQGRP RGQPNTALLS
LVLMAGTFFI AFFLRKFKNG RFFPGRVRRV IGDFGVPIAI LIMVLVDYSI EDTYTQKLSV
PSGFSVTAPE KRGWVINPLG EKSSFPVWMM VASLLPAILV FILIFMETQI TTLIISKKER
MLQKGSGFHL DLLLIVAMGG ICALFGLPWL AAATVRSVTH ANALTVMSKA VAPGDKPKIQ
EVKEQRVTGL LVALLVGLSI VIGDLLRQIP LAVLFGIFLY MGVTSLNGIQ FYERLHLLLM
PPKHHPDVTY VKKVRTLRMH LFTALQLLCL ALLWAVMSTA ASLAFPFILI LTVPLRMVVL
TRIFTEREMK CLDANEAEPV FDEREGVDEY NEMPMPV
