B3A2_CAVPO
ID B3A2_CAVPO Reviewed; 1238 AA.
AC Q9Z0S8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH 2; TISSUE=Organ of Corti;
RX PubMed=9804866; DOI=10.1016/s0005-2736(98)00110-2;
RA Mhatre A.N., Charachon G., Alper A.L., Lalwani A.K.;
RT "The guinea pig cochlear AE2 anion exchanger: cDNA cloning and in situ
RT localization within the cochlea.";
RL Biochim. Biophys. Acta 1414:1-15(1998).
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; AF121253; AAD19700.1; -; mRNA.
DR RefSeq; NP_001166488.1; NM_001173017.1.
DR AlphaFoldDB; Q9Z0S8; -.
DR SMR; Q9Z0S8; -.
DR STRING; 10141.ENSCPOP00000011907; -.
DR GeneID; 100135618; -.
DR KEGG; cpoc:100135618; -.
DR CTD; 6522; -.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q9Z0S8; -.
DR OrthoDB; 265068at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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..1238
FT /note="Anion exchange protein 2"
FT /id="PRO_0000079214"
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..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 845..897
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1007
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1054
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1088..1133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1160..1196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..315
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 705..1238
FT /note="Membrane (anion exchange)"
FT REGION 858..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 137..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1170
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 856
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1238 AA; 137360 MW; FA1739862ED5ADBF CRC64;
MSGTPRRPAS GADSFHKPEP EIVGPGTPGF PEQEEDDLHR TLGVERFEEI LQEAGSRGGE
ELGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GQVRKPRRRP GATPAGETPT
IEEGEEDEDE TSEAEGPVSH TDPSPASTPT SVQFFLQEDE GTDRKAERTS PSPPAQLPHQ
EAAPQATKKA QPDALVEEAI MVSGGTAGGD DGGASGRPLS KAQPGHRSYN LQERRRIGSM
TGVEQALLPR VPTDESEAQT LATADLDLMK SHRFEDVPGV RRHLVRKNAK GSSQSSREGR
EPGPTPRTRP RAPHKPHEVF VELNELLLDK NQEPQWRETA RWIKFEEDVE EETERWGKPH
VASLSFRSLL ELRRTLAHGA VLLDLDQQTL PGVAHQVVEQ MVISDQIKAE DRANVLRALL
LKHSHPSDEK EFSFPRNISA GSLGSLLGHH HTQGAESDPH VTEPLIGGVP ETRLEVERER
ELPPPAPPAG ITRSKSKHEL KLLEKIPENA EATVVLVGCV EFLSRPTMAF VRLREAVELD
AVLEVPVPVR FLFLLLGPSS ANMDYHEIGR SISTLMSDKQ FHEAAYLADE REDLLTAINA
FLDCSVVLPP SEVQGEELLR SVAHFQRQML KKREEQGRLL PPGVGLEPKS AQEKAFLQMV
EAVGAVEDDD PLRRTGRPFG GLIRDVKRRY PHYLSDFRDA LDPQCLAAVI FIYFAALSPA
ITFGGLLGEK THDLIGVSEL IMSTALQGVT FCLLGAQPLL VIGFSGPLLV FEEAFYSFCR
SNELEYLVGR VWIGFWLVLS ALLMVALEGS FLVRFGSRFT QEIFAFLISL IFIYETFYKL
VKIFQEHPLH GCLASNSSEA DGGKNTTWTE AAPTPGHGNT SSAEQAGVER PQGQPNTALL
SLVLMAGTFF IAFFLRKFKN SRFFPGRIRR VIGDFGVPIA ILIMVLVDYS IQDTYTQKLS
VPSGFSVTAP EKRGWIINPL GEEEPFPVWM MVASLLPAIL VFILIFMETQ ITTLIISKKE
RMLQKGSGFH LDLLLIVAMG GICALFGLLW LAAATVRSVT HANALTVMSK AVAPGDKPKI
QEVKEQRVTG LLVALLVGLS LVIGDLLRQI PLAVLFGIFL YMGVTSLNGI QFYERLHLLL
MPPKHHPDVM YVKKVRTMRM HLFKALQLLC LALLWAVMST AASLAFPFIL ILTVPLRMVV
LTRIFTEREM KCLDANEAEP VFDEREGVDE YNEMPMPV
