ID A0A287B1T3_PIG Unreviewed; 1323 AA.
AC A0A287B1T3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A4 {ECO:0000313|Ensembl:ENSSSCP00000050046.2,
GN ECO:0000313|VGNC:VGNC:93133};
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:ENSSSCP00000050046.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000050046.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000050046.2,
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:ENSSSCP00000050046.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a
CC Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate
CC bicarbonate influx/efflux at the basolateral membrane of cells and
CC regulate intracellular pH. {ECO:0000256|ARBA:ARBA00037277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 hydrogencarbonate(out) + Na(+)(out) = 2
CC hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72215,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000256|ARBA:ARBA00036309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 hydrogencarbonate(out) + Na(+)(out) = 3
CC hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72219,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000256|ARBA:ARBA00035820};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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; A0A287B1T3; -.
DR Ensembl; ENSSSCT00000052823.3; ENSSSCP00000050046.2; ENSSSCG00000008943.5.
DR VGNC; VGNC:93133; SLC4A4.
DR GeneTree; ENSGT00940000156290; -.
DR OrthoDB; 1013180at2759; -.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000008943; Expressed in metanephros cortex and 43 other cell types or tissues.
DR ExpressionAtlas; A0A287B1T3; baseline and differential.
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:0008510; F:sodium:bicarbonate symporter activity; IEA:UniProt.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR NCBIfam; TIGR00834; ae; 1.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF10; ELECTROGENIC SODIUM BICARBONATE COTRANSPORTER 1; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF01712; dNK; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:UP000008227};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Symport {ECO:0000256|ARBA:ARBA00022847};
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 736..759
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 771..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 820..838
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 997..1015
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1045..1064
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1085..1109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1145..1164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 24..250
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT DOMAIN 405..654
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 708..1200
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 307..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 150039 MW; AE347628AFD0DE66 CRC64;
MATPPKRSCP SSPASSEGNR IKKISIEGNI AAGKSTFVNI LKQVCEDWEV VPEPVARWCN
VQSTQNEFEE LTTSQKSGGN VLQMMYEKPE RWSFTFQSYA CLSRIRAQLA ALNGKLKDAE
KPVLFFERSV YSDRYIFASN LYESDCMNET EWTIYQDWHD WMNNQFGQSL ELDGIIYLRA
TPEKCLNRIY LRGRNEEQGI PLEYLEKLHY KHESWLLHRT LKTNFDYLQE VPILTLDVNE
DFKDKHSSLV EKVLMPSISE LFQCSGWMED EAVLDRGASF LKHVCDEEEV EGHHTIYIGV
HVPKSYRRRR RHKRKAGHRE KKEKERVSEN YSDKSDVENA DESSSSILKP LISPAAERIR
FILGEEDDSP APPQLFTELD ELLAVDGQEM EWKETARWIK FEEKVEQGGE RWSKPHVATL
SLHSLFELRT CMEKGSIMLD REAASLPQLV EMIVDHQIET GLLKPDLKDK VTYTLLRKHR
HQTKKSNLRS LADIGKTVSS ASRMFTSPEN GSPAMTHRNL TSSSLNDISD KPEKDQLKNK
FMKKLPRDAE ASNVLVGEVD FLDSPFIAFV RLQQAVMLGA LTEVPVPTRF LFILLGPKGK
AKSYHEIGRA IATLMSDEVF HDIAYKAKDR QDLIAGIDEF LDEVIVLPPG EWDPAIRIEP
PKSLPSSDKR KNMYSGGENV QMNGDTPHDG GHGGGGHADC EELQRTGRFC GGLIKDIKRK
APFFASDFYD ALNIQALSAI LFIYLATVTN AITFGGLLGD ATDNMQGVLE SFLGTAVSGA
VFCLFAGQPL TILSSTGPVL VFERLLFNFS KDHNFDYLEF RLWIGLWSAF LCLILVATDA
SFLVQYFTRF TEEGFSSLIS FIFIYDAFKK MIKLADYYPI NSNFKVGYNT QFSCVCVPPN
PVNISVSNDT TLAPEDLQTV SSADMYHNAT FDWALLTKKE CLKYEGKLVG NNCDFVPDIT
LMSFILFLGT YTSSMALKKF KTSRYFPTTA RKLISDFAII LSILIFCVID ALVGVDTPKL
IVPSEFKPTS PNRGWFVPPF GGNPWWVYLA AAIPALLVTI LIFMDQQITA VIVNRKEHKL
KKGAGYHLDL FWVAILMVVC SFMALPWYVA ATVISIAHID SLKMETETSA PGEQPKFLGV
REQRVTGTLV FILTGLSVFM APILKFMDRL KLLLMPLKHQ PDFIYLRHVP LRRVHLFTFL
QVLCLALLWI LKSTVAAIIF PVMILALVAV RKGMDYLFSQ HDLSFLDDVI PEKDKKKKED
EKKKKKKKGS LDSDNDDSDC PYSEKVPSIK IPMDIMEQQP FLSDSKPSDR ERSPTFLERH
TSC
//
