ID H2QVM4_PANTR Unreviewed; 1239 AA.
AC H2QVM4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A2 {ECO:0000313|Ensembl:ENSPTRP00000034034.3,
GN ECO:0000313|VGNC:VGNC:8762};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000034034.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000034034.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) +
CC hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00034408};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004554}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Lateral cell membrane
CC {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034693}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362035}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362035}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000256|ARBA:ARBA00010993, ECO:0000256|RuleBase:RU362035}.
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DR RefSeq; XP_003318957.1; XM_003318909.1.
DR AlphaFoldDB; H2QVM4; -.
DR PaxDb; 9598-ENSPTRP00000034034; -.
DR Ensembl; ENSPTRT00000036813.4; ENSPTRP00000034034.3; ENSPTRG00000019873.6.
DR GeneID; 463890; -.
DR KEGG; ptr:463890; -.
DR CTD; 6522; -.
DR VGNC; VGNC:8762; SLC4A2.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000158259; -.
DR HOGENOM; CLU_002289_1_0_1; -.
DR InParanoid; H2QVM4; -.
DR OrthoDB; 1013180at2759; -.
DR TreeFam; TF313630; -.
DR Proteomes; UP000002277; Unplaced.
DR Bgee; ENSPTRG00000019873; Expressed in cortex of kidney and 21 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022853; F:active monoatomic ion transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0098660; P:inorganic ion transmembrane transport; IEA:UniProt.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.287.570; Helical hairpin bin; 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 NCBIfam; TIGR00834; ae; 1.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF14; ANION EXCHANGE PROTEIN 2; 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; Phoshotransferase/anion transport protein; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE 3: Inferred from homology;
KW Anion exchange {ECO:0000256|ARBA:ARBA00022681};
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU362035};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362035};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362035};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035}.
FT TRANSMEM 707..728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 749..772
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 792..817
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 824..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 899..916
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 989..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1029..1053
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1089..1108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1114..1134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 350..617
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 678..1167
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..469
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 COMPBIAS 304..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 136922 MW; B3A7E3E49C9733D7 CRC64;
MSSAPRRPAK GADSFRTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE
EPGRSYGEED FEYHRQSSHH IHHPLSTHLP PDARRRKTPQ GPGRKPRRRP GASPTGETPT
IEEGEEDEDE ASEAEGARTL 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 PHVTEPLMGG 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 RVWIGFWLVF LALLMVALEG SFLVRFVSRF TQEIFAFLIS LIFIYETFYK
LVKIFQEHPL HGCSASNSSE VDGGENMTWA GARPMLGPGN 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
//
