ID A0A1S3FGU2_DIPOR Unreviewed; 959 AA.
AC A0A1S3FGU2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=Slc4a9 {ECO:0000313|RefSeq:XP_012875818.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012875818.1};
RN [1] {ECO:0000313|RefSeq:XP_012875818.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012875818.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: 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_012875818.1; XM_013020364.1.
DR AlphaFoldDB; A0A1S3FGU2; -.
DR STRING; 10020.ENSDORP00000011794; -.
DR GeneID; 105988690; -.
DR CTD; 83697; -.
DR OrthoDB; 1013180at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR NCBIfam; TIGR00834; ae; 1.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF52; ANION EXCHANGE PROTEIN 4; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU362035};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
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 391..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 423..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 474..495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 507..530
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 603..621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 641..660
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 689..708
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 729..753
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 789..808
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 815..834
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 181..304
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 361..867
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 106201 MW; 1075A89B2EDA4EE9 CRC64;
MKLPGQEEFE TSSAGENVPA GELDNVLGPG PDVPLDTDSR DMVVPNNPML FIQLNELVGW
PQALEWRETG RWVLFEEKLE VGAGRWSAPH VPTLALASLQ KLRSLLAEGL ILLDCPAQSL
LELVEQVIRV ESLSPELKEQ LQALLLQRPQ HNIQMRGTKL CWDSCFVEST DIRKDSHDED
APLKEQHRNP LRQKLPPGAE AAVVLAGELG FLARPLGAFI RLQNPVVLGP LTEVPIPSRF
FCLLLGPPMP GRAYHEMGRA MAVLLSDLQF QGSVRQASNL QDLLAALDAF LQKVTVLPPG
RWDPTARIPP PKCLPFQHKR LSSQVWEVRG ISGLRGAPAE DRHHHRGPHM PNPELQRTGW
LFGGLVQDVR RKALWYSSDF LDALHPQCLS AVLYIYLATI TNAITFGGLL GDATEGAQGV
LESFLGTAVT GAAFCLMAGQ PLTILSSTGP VLVFERLLFT FCRDYHLDYL PFRLWVGIWV
ATFCLVLVAT EASVLVRYFT RFTEEGFCAL ISLIFIYDAL GKMLSLARAY PIQRPGSPAY
GCFCQYPGPG ENVSQWTRTK PNDRDDILSM DLGLVNASLL PPPECTQKGG YPRGPGCHTV
PDIALFSLLL FLTSFFFATA LKHVKNSRLF PSMVRKVFSD FSSVLAILLG CVLDAFLGLA
TPKLLVPTEF KPTLPGRSWL VSPFGANSWW LSVAAALPAL LLSILIFMDQ QITAVILNRT
EYKLQKGAGF HLDLFCVAVL ILLTSVLGLP WYVSATVISL AHMDSLRRES RAYAPGEAPS
FLGIREQRLT GLMVFILTGT SIFLAPVLKF IPMPVLYGIF LYMGVAALSS IQFMKRVKLL
LMPAKHQPDL LFLRHVPLSR VHLFTAIQLA CLGLLWIIKS TPAAIIFPIM LLGLVGVRKA
LEWVFSPQEL LWLDELMPEE ERSIPEKGLE PDHSFNGSDS EDSQLMYQPK APEINISVN
//
