ID A0A287D2F6_ICTTR Unreviewed; 1131 AA.
AC A0A287D2F6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A7 {ECO:0000313|Ensembl:ENSSTOP00000027761.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000027761.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000027761.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGTP01006400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01006401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01006402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005317348.1; XM_005317291.2.
DR AlphaFoldDB; A0A287D2F6; -.
DR Ensembl; ENSSTOT00000032260.1; ENSSTOP00000027761.1; ENSSTOG00000012151.3.
DR GeneID; 101976493; -.
DR CTD; 9497; -.
DR GeneTree; ENSGT00940000157045; -.
DR OrthoDB; 1013180at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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:UP000005215};
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..760
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 968..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..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..98
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 1095..1131
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"
FT COMPBIAS 1095..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 127039 MW; 5BA1C38F16FE7087 CRC64;
MEADGAGEQM RPLLTRGPDE EAVVDLGKTS STVNTKFEKE ELESHRAVYI GVHVPFSKES
RRRHRHRGHK HHHRRRKDKE SDKEDGRESP SYDTPSQRVQ FILGTEDDDE EHIPHDLFTE
MDELCYRDGE EYEWKETARW LKFEEDVEDG GDRWSKPYVA TLSLHSLFEL RSCILNGTVM
LDMRASTLDE IADMVLDNMI ASGQLDESIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA
DIGKKHSDPH LLERNGILAS PQSAPGNLDN SKSGEIKGNG SGGSRENSTV DFSKVDMNFM
RKIPTGAEAS NVLVGEVDFL ERPIIAFVRL APAVLLSGLT EVPVPTRFLF LLLGPAGKAP
QYHEIGRSIA TLMTDEIFHD VAYKAKDRND LLSGIDEFLD QVTVLPPGEW DPSIRIEPPK
SVPSQEKRKI PVFPNGSAPI SGETPKEAAH HAGPELQRTG RLFGGLILDI KRKAPFFLSD
FKDALSLQCL ASILFLYCAC MSPVITFGGL LGEATEGRIS AIESLFGASL TGIAYSLFAG
QPLTILGSTG PVLVFEKILF KFCRDYHLSY LSLRTSIGLW TSFLCIVLVA TDASSLVCYI
TRFTEEAFAA LICIIFIYEA LEKLFHLGEI YAFNMHNNLN KLTSYSCVCI EPPDPSNETL
ELWKKENITA HSISWGNLTV SECKTFHGAF VGSACSPHGP YIPDVLFWCV ILFFTTFFLS
SFLKQFKTKR YFPTKVRSTI SDFAVFLTIV IMVAIDYLVG VPSPKLHVPE KFEPTDPNRG
WIISPLGDNP WWTLLIAAIP ALLCTILIFM DQQITAVIIN RKEHKLKKGA GYHLDLLMVG
VMLGVCSVMG LPWFVAATVL SISHVNSLKV ESECSAPGEQ PKFLGIREQR VTGLMIFILM
GLSVFMTSVL KFIPMPVLYG VFLYMGVSSL KGIQFFDRIK LFGMPAKHQP DLIYLRYVPL
WKVHIFTVIQ LTCLVLLWVI KASAAAVVFP MMVLALVFVR KLMDLCFTKR ELSWLDDLMP
ESKKKKEDDK KKKEKEEAER MLQDDDDTVH LPFEGGSLLQ IPVKALKYSV DPSVVNISDE
MAKTAQWKAL SMNTENAKVT RSNTSPEKPV SVTINFEDEP SKKYMDAETS L
//
