ID A0A286ZNG5_PIG Unreviewed; 1092 AA.
AC A0A286ZNG5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A8 {ECO:0000313|Ensembl:ENSSSCP00000032998.1,
GN ECO:0000313|VGNC:VGNC:98326};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000032998.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000032998.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000032998.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000032998.1}
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 AlphaFoldDB; A0A286ZNG5; -.
DR SMR; A0A286ZNG5; -.
DR STRING; 9823.ENSSSCP00000032998; -.
DR PaxDb; 9823-ENSSSCP00000019697; -.
DR Ensembl; ENSSSCT00000066032.2; ENSSSCP00000032998.1; ENSSSCG00000028060.4.
DR VGNC; VGNC:98326; SLC4A8.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000157422; -.
DR InParanoid; A0A286ZNG5; -.
DR OMA; VCHIEAE; -.
DR Reactome; R-SSC-425381; Bicarbonate transporters.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000028060; Expressed in epididymis and 30 other cell types or tissues.
DR ExpressionAtlas; A0A286ZNG5; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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:SF37; ELECTRONEUTRAL SODIUM BICARBONATE EXCHANGER 1; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZNG5};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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 478..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 512..535
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 555..579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 591..609
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 693..711
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 731..749
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 779..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 819..843
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 879..898
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 905..924
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 956..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 144..402
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 449..957
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..76
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 122802 MW; D2D85D6655E9433F CRC64;
MPAGSNEPDG VLSYQRPDEE AVVDQGGTST ILNIHYEKEE LEGHRTLYVG VRMPLGRQSH
RHHRTHGQKH RRRGRGKGAS QGEEGPEALA HDTPSQRVQF ILGTEEDEEH VPHELFTELD
EICLKEGEDA EWKETARWLK FEEDVEDGGE RWSKPYVATL SLHSLFELRS CLINGTVLLD
MRANSIEEIS DLILDQQELF SDLNDSMRVK VREALLKKHH HQNEKKRNNL IPIVRSFAEV
GKKQSDPHSM DKNGQTVSPQ SVLTTNLEVK NGVNCEHSPV DLSKVDLHFM KKIPTGAEAS
NVLVGEVDSL DRPIVAFVRL SPAVLLSGLT EVPIPTRFLF ILLGPAGKGQ QYHEIGRSMA
TIMTDEIFHD VAYKAKERDD LLAGIDEFLD QVTVLPPGEW DPSIRIEPPK NVPSQEKRKM
PGVPNGNVCH IEPEPHGGHS GPELQRTGRL FGGLVLDVKR KAPWYWSDYR DALSLQCLAS
FLFLYCACMS PVITFGGLLG EATEGRISAI ESLFGASMTG IAYSLFAGQA LTILGSTGPV
LVFEKILFKF CKDYALSYLS LRACIGLWTA FLCIVLVATD ASSLVCYITR FTEEAFASLI
CIIFIYEAIE KLIHLAETYP IHMHSQLDHL SLYYCRCTVP ENPNNHTLQY WKDHNIVITE
VHWANLTVSE CQDMHGEFTG SACGHHGPYT PDVLFWSCIL FFTTFILSST LKTFKTSRYF
PTRVRSMVSD FAVFLTIFTM VIIDFLIGVP SPKLQVPSVF KPTRDDRGWI ISPIGPNPWW
TVIAAIIPAL LCTILIFMDQ QITAVIINRK EHKLKKGCGY HLDLLMVAIM LGVCSIMGLP
WFVAATVLSI THVNSLKLES ECSAPGEQPK FLGIREQRVT GLMIFVLMGC SVFMTAILKF
IPMPVLYGVF LYMGVSSLQG IQFFDRLKLF GMPAKHQPDF IYLRHVPLRK VHLFTLIQLT
CLVLLWVIKA SPAAIVFPMM VLALVFVRKV MDLCFSKREL SWLDDLMPES KKKKLDDAKK
KAKEEEEAEK MLEMGGDKFP LESRKLLSSP GKNSSFRCDP SEINISDEMP KTTVWKALSM
NSGNTKEKSL FN
//