B3A2_PONAB
ID B3A2_PONAB Reviewed; 1239 AA.
AC Q5RD44; Q5R7I2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Anion exchange protein 2;
DE Short=AE 2;
DE Short=Anion exchanger 2;
DE AltName: Full=Solute carrier family 4 member 2;
GN Name=SLC4A2; Synonyms=AE2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RD44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RD44-2; Sequence=VSP_035783;
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; CR858074; CAH90313.1; -; mRNA.
DR EMBL; CR860134; CAH92278.1; -; mRNA.
DR RefSeq; NP_001125144.1; NM_001131672.1.
DR RefSeq; NP_001128854.1; NM_001135382.2.
DR AlphaFoldDB; Q5RD44; -.
DR SMR; Q5RD44; -.
DR STRING; 9601.ENSPPYP00000020391; -.
DR GeneID; 100172030; -.
DR KEGG; pon:100172030; -.
DR CTD; 6522; -.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q5RD44; -.
DR OrthoDB; 265068at2759; -.
DR Proteomes; UP000001595; 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 Alternative splicing; Anion exchange; Antiport; Glycoprotein;
KW Ion transport; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1239
FT /note="Anion exchange protein 2"
FT /id="PRO_0000354092"
FT TOPO_DOM 1..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 794..814
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 845..895
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 917..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 987..1007
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1034..1054
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1088..1108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..1239
FT /note="Membrane (anion exchange)"
FT REGION 708..1239
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..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
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 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13808"
FT MOD_RES 272
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT LIPID 1171
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 857
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 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..17
FT /note="MSSAPRRPAKGADSFCT -> MDFLLRPQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035783"
FT CONFLICT 471
FT /note="V -> A (in Ref. 1; CAH92278)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="V -> A (in Ref. 1; CAH92278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="L -> P (in Ref. 1; CAH90313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1239 AA; 136799 MW; F1D8EC8179CE22F5 CRC64;
MSSAPRRPAK GADSFCTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE
EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GPGRKPRRRP GASPTGETPT
IEEGEEDEDE ASEAEGARAL TQPSPVSTPS SVQFFLQEDD SADRKAERTS PSSPAPLPHQ
EATPRASKGA QAGTQVEEAE AVAVASGTAG GDDGGASGRP LPKAQPGHRS YNLQERRRIG
SMTGAEQALL PRVPTDEIEA QTLATADLDL MKSHRFEDVP GVRRHLVRKN AKGSTQSGRE
GREPGPTPRA RPRAPHKPHE VFVELNELLL DKNQEPQWRE TARWIKFEED VEEETERWGK
PHVASLSFRS LLELRRTLAH GAVLLDLDQQ TLPGVAHQVV EQMVISDQIK AEDRANVLRA
LLLKHSHPSD EKDFSFPRNI SAGSLGSLLG HHHGQGAESD PHVTEPLIGG VPETRLEVER
ERELPPPAPP AGITRSKSKH ELKLLEKIPE NAEATVVLVG CVEFLSRPTM AFVRLREAVE
LDAVLEVPVP VRFLFLLLGP SSANMDYHEI GRSISTLMSD KQFHEAAYLA DEREDLLTAI
NAFLDCSVVL PPSEVQGEEL LRSVAHFQRQ MLKKREEQGR LLPTGAGLEP KSAQDKALLQ
MVEAAGAAED DPLRRTGRPF GGLIRDVRRR YPHYLSDFRD ALDPQCLAAV IFIYFAALSP
AITFGGLLGE KTQDLIGVSE LIMSTALQGV VFCLLGAQPL LVIGFSGPLL VFEEAFFSFC
SSNHLEYLVG RVWIGFWLVL LALLMVALEG SFLVRFVSRF TQEIFAFLIS LIFIYETFYK
LVKIFQEHPL HGCSASNSSE VDGGENMTWA VARPTLGPGN RSLAGQSGQG KPRGQPNTAL
LSLVLMAGTF FIAFFLRKFK NSRFFPGRIR RVIGDFGVPI AILIMVLVDY SIEDTYTQKL
SVPSGFSVTA PEKRGWVINP LGEKSPFPVW MMVASLLPAI LVFILIFMET QITTLIISKK
ERMLQKGSGF HLDLLLIVAM GGICALFGLP WLAAATVRSV THANALTVMS KAVAPGDKPK
IQEVKEQRVT GLLVALLVGL SIVIGDLLRQ IPLAVLFGIF LYMGVTSLNG IQFYERLHLL
LMPPKHHPDV TYVKKVRTLR MHLFTALQLL CLALLWAVMS TAASLAFPFI LILTVPLRMV
VLTRIFTDRE MKCLDANEAE PVFDEREGVD EYNEMPMPV
