B3A2_RABIT
ID B3A2_RABIT Reviewed; 1237 AA.
AC P48746;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Anion exchange protein 2;
DE Short=AE 2;
DE Short=Anion exchanger 2;
DE AltName: Full=Band 3-related protein;
DE Short=B3RP;
DE AltName: Full=Solute carrier family 4 member 2;
GN Name=SLC4A2; Synonyms=AE2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RX PubMed=1415547; DOI=10.1152/ajpgi.1992.263.3.g345;
RA Chow A., Dobbins J.W., Aronson P.S., Igarashi P.;
RT "cDNA cloning and localization of a band 3-related protein from ileum.";
RL Am. J. Physiol. 263:G345-G352(1992).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S45791; AAB23488.1; -; mRNA.
DR PIR; A56764; A56764.
DR RefSeq; NP_001075788.1; NM_001082319.1.
DR AlphaFoldDB; P48746; -.
DR SMR; P48746; -.
DR PRIDE; P48746; -.
DR GeneID; 100009159; -.
DR KEGG; ocu:100009159; -.
DR CTD; 6522; -.
DR InParanoid; P48746; -.
DR OrthoDB; 265068at2759; -.
DR Proteomes; UP000001811; 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_0000079217"
FT TOPO_DOM 1..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..896
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 897..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 984..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1032..1053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1087..1132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1159..1195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..464
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 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 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; 136536 MW; 2811D11051552BB2 CRC64;
MSSAPRRPAS GADSFRTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE
EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GPGRKPRRRP GASPTGATPT
IEEGEEDEEE ANEAEGARAP TEPSPASTPS SVQFFLQEDE GAERKAERTS PSPPTLLPHQ
EAAPWATEGA QTGVPVEEVA VVASGTAGGD NGGASGRPLT KAQPGHRSYN LQERRRIGSM
TGAEQALLPR VPTDESEAQT LATADLDLMK SHRFEDVPGV RRHLVRKNAK GSAQSSREGR
EPGPTPRSRP RAPHKPHEVF VELNELLLDK NQEPQWRETA RWIKFEEDVE EETERWGKPH
VASLSFRSLL ELRRTLAHGA VLLDLDQQTL PGVAHQVVEQ MVISDQIKAE DRANVLRALL
LKHSHPSDEK DFSFPRNISA GSLGSLLGHH HGQGAESDPH VTEPLIGGIP ETRLDVERER
DVPPSAPPAG ITRSKSKHEL KLLEKIPENA EATVVLVGCV EFLSRPTMAF VRLREAVELD
AVLEVPVPVR FLFLLLGPSS ANMDYHEIGR SISTLMSDKQ FHEAAYLADE REDLLTAINA
FLDCSVVLPP SEVQGEELLR SVAHFQRQML KKREEQGRLL PPGLGLEPKS AQDKALLQMV
EAAGAAEDDP LRRTGRPFGG LIRDVRRRYP HYLSDFRDAL DPQCVAAVIF IYFAALSPAI
TFGGLLGEKT QDLIGVSELI MSTALQGVIF CLLGAQPLLV IGFSGPLLVF EEAFFTFCSS
NQLEYLVGRV WIGFWLVLLA LLMVALEGSF LVRFVSRFTQ EIFAFLISLI FIYETFYKLI
KIFQEHPLHG CSVSNSSETD SSENATWAGA GSTLGPANRS SAGQAGQGRP RGQPNTALLS
LVLMAGTFFI AFFLRKFKNS RFFPGRIRRV IGDFGVPIAI LIMVLVDYSI EDTYTQKLSV
PSGFSVTAPD KRGWVINPLG EKSPFPVWMM 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
