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Database: UniProt
Entry: A0A3Q0CW22_MESAU
LinkDB: A0A3Q0CW22_MESAU
Original site: A0A3Q0CW22_MESAU 
ID   A0A3Q0CW22_MESAU        Unreviewed;      1095 AA.
AC   A0A3Q0CW22;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=Slc4a7 {ECO:0000313|RefSeq:XP_021086515.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021086515.1};
RN   [1] {ECO:0000313|RefSeq:XP_021086515.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28071753;
RA   McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT   "De novo assembly, annotation, and characterization of the whole brain
RT   transcriptome of male and female Syrian hamsters.";
RL   Sci. Rep. 7:40472-40472(2017).
RN   [2] {ECO:0000313|RefSeq:XP_021086515.1}
RP   IDENTIFICATION.
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_021086515.1; XM_021230856.1.
DR   AlphaFoldDB; A0A3Q0CW22; -.
DR   Proteomes; UP000189706; 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:SF105; SODIUM BICARBONATE COTRANSPORTER 3; 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:UP000189706};
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        490..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        519..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        577..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        607..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        705..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        743..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        791..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        831..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        891..910
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        917..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        975..999
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          146..412
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          461..969
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..77
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1095 AA;  123196 MW;  70D99058C03929A6 CRC64;
     MEADGAGEQM RPLLTRGPDE EAIVDLGKTS STVNTKFEKE ELESHRAVYV GVHVPFSKES
     RRRHKHRGHK HHHRRRKDKD SDKEDGRESP SYDTPSQRVQ FILGTEDDDE EHIPHDLFTE
     MDELCYRDGE EYEWKETARW LKFEEDVEDG GDRWSKPYVA TLSLHSLFEL RSCILNGTVM
     LDMRASTLDE IADMVLDNMI ASGQLDDSIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA
     DIGKKHSDPH LLERNGILAS PQSAPGNLDN SKSGEMKGNG SGGSRENSTV DFSKVDMNFM
     RKIPTGAEAS NVLVGEVDFL ERPIIAFVRL APAVLLSGLT EVPVPTRFLF LLLGPAGKAP
     QYHEIGRSIA TLMTDEIFHD VAYKAKDRND LLSGIDEFLD QVTVLPPGEW DPSIRIEPPK
     SVPSQEKRKI PVFPNGSAPV STEPPKEAAH HAGPELQRTG RLFGGLILDI KRKAPFFLSD
     FKDALSLQCL ASILFLYCAC MSPVITFGGL LGEATEGRIS AIESLFGASL TGIAYSLFAG
     QPLTILGSTG PVLVFEKILF KFCRDYHLSY LSLRTSIGLW TSFLCIVLVA TDASSLVCYI
     TRFTEEAFAA LICIIFIYEA LEKLFHLGEI YAFNMHNNLD ELTSYTCVCT EPSNPSNETI
     ELWKRKNVTS HSIFWGNLTV SECKAFHGMF VGSACGPHGP YVPDVLFWCV VLFFTTFFLS
     SFLKQFKTKR YFPTKVRSTI SDFAVFLTIV IMVAIDYLVG IPSPKLNVPE KFEPTDPSRG
     WIISPLGDNP WWTLLIAAVP ALLCTILIFM DQQITAVIIN RKEHKLKKGA GYHLDLLMVG
     VMLGVCSIMG LPWFVAATVL SISHVNSLKV ESECSAPGEQ PKFLGIREQR VTGLMIFILM
     GLSVFMTSVL KFIPMPVLYG VFLYMGVSSL KGIQFFDRIK LFGMPAKHQP DLIYLRYVPL
     WKVHVFTVVQ LTCLILLWVI KASAAAVVFP MMVLALVFVR KLMDLCFTKR ELSWLDDLMP
     ESKKKKEDDK KKKEKEEAER MLQDDGDTVH LPFERGSLLQ IPVKTLKYSP EKPVSVTINF
     EDEPSKKYMD AETSL
//
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