S4A4_AMBTI
ID S4A4_AMBTI Reviewed; 1035 AA.
AC O13134;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Electrogenic sodium bicarbonate cotransporter 1;
DE Short=Sodium bicarbonate cotransporter;
DE AltName: Full=Na(+)/HCO3(-) cotransporter;
DE AltName: Full=Solute carrier family 4 member 4;
GN Name=SLC4A4; Synonyms=NBC, NBCE1;
OS Ambystoma tigrinum (Eastern tiger salamander).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Ambystomatidae; Ambystoma.
OX NCBI_TaxID=8305;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9163427; DOI=10.1038/387409a0;
RA Romero M.F., Hediger M.A., Boulpaep E.L., Boron W.F.;
RT "Expression cloning and characterization of a renal electrogenic
RT Na+/HCO3- cotransporter.";
RL Nature 387:409-413(1997).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11095641; DOI=10.1681/asn.v11122179;
RA Maunsbach A.B., Vorum H., Kwon T.-H., Nielsen S., Simonsen B., Choi I.,
RA Schmitt B.M., Boron W.F., Aalkjaer C.;
RT "Immunoelectron microscopic localization of the electrogenic Na/HCO(3)
RT cotransporter in rat and ambystoma kidney.";
RL J. Am. Soc. Nephrol. 11:2179-2189(2000).
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:0000269|PubMed:9163427}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y6R1}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:11095641}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11095641}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney and to a lower extent in
CC bladder, brain, intestine, large intestine and eye.
CC {ECO:0000269|PubMed:9163427}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; AF001958; AAB61339.1; -; mRNA.
DR PIR; T31336; T31336.
DR AlphaFoldDB; O13134; -.
DR SMR; O13134; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.930.10; -; 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 PANTHER; PTHR11453; PTHR11453; 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; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1035
FT /note="Electrogenic sodium bicarbonate cotransporter 1"
FT /id="PRO_0000079232"
FT TOPO_DOM 1..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 422..446
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 447..456
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 457..475
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 477..497
FT /note="Discontinuously helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 498..505
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 506..526
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 527..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 541..564
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 565..648
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 649..666
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 667..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 682..701
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 702..735
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 736..763
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 764..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 776..792
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 793
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 794..811
FT /note="Discontinuously helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 812..833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 834..850
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 851..857
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 858..874
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 875..916
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT INTRAMEM 917..942
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 943..1035
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT REGION 192..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 582..584
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 630..642
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
SQ SEQUENCE 1035 AA; 116108 MW; 3CF50B31275A81AF CRC64;
MSSEKECLEN MLNGYAESGR VLSRTSLVIN QAVNRSIFTS TVSPAAERIR FILGEEDDSP
APPQLFTELD ELLAVDGQEM EWKETARWIK FEEKVEQGGE RWSKPHVATL SLHSLFELRT
CIEKGTILLD LEATSLPQIV EIVINNQIEL GLLKADMKEN VTRTLLRKHR HQTKKSNLRS
LADIGKTVSS ASRLFSTPDN GSPTMTHRNL TSTSLNDVSD KPDKEQLKNK FMKKLPRDAE
ASNVLVGEVD FLESPFIAFV RLQQAVMLGS LTEVPVPTRF LFILLGPKGK AKSYHEIGRS
IATLMSDEVF HDIAYKAKNR EDLIAGIDEF LDEVIVLPLG EWDPTIRIEP PKSLPSSDKR
KNMYSGGDNL QMNGDAPHDD GGGGHGDSEE LQRTGRFCGG LIKDIQRKAP FFASDFYDAL
SIQSLSAILF IYLGTVTNAI TFGGLLGDAT ENMQGVLESF LGTAVSGAVF CLFGGQPLTI
LSSTGPVLVF ERLLFNFSKD NDFDYLEFRL WIGLWSAFQC LILVATDASF LVKYFTRFTE
EGFSSLISFI FIYDAFKKMI KLADYYPINS HFKVDYITQY SCACFPPEPA NSSWFNMTTA
ATTTQFLTNA STDMAYNGTI DWSLLSKKEC LKYGGLLVGS NCKYVPDITL MSFILFLGTY
TCSMALKKFK TSRYFPTTAR KLISDFAIIL SILIFCGLDA LLGVDTPKLI VPSEFKPTSP
NRGWFVPPFG GNPWWVYLAA AIPALLVTIL IFMDQQITGV IVNRKEHKLK KGAGYHLDLF
WVAILMVVCS FMALPWYVAA TVISIAHIDS LKMETETSAP GEQPKFLGVR EQRVTGTVVF
LLTGLSVFMA PILKFIPMPV LYGVFLYMGV ASLNGVQFMD RLKLLLMPPK YQPDFIYLRH
VPLRRVHLFT FLQVVCLAML WILKSTVAAI IFPVMILALV AVRKAMDYFF SQHDLSFLDD
VIPEKDKKKK EDEKKKKKKK GSIDSDVEDS DCPYPEKVPS IKIPMDIMEK EPFLIDSKPS
DRENSPTFLE RHTSC
