S4A5_RAT
ID S4A5_RAT Reviewed; 1112 AA.
AC Q6RI88;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Electrogenic sodium bicarbonate cotransporter 4;
DE AltName: Full=Solute carrier family 4 member 5;
GN Name=Slc4a5 {ECO:0000312|RGD:1303009};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS98674.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAS98674.1};
RC TISSUE=Liver {ECO:0000269|PubMed:15151908};
RX PubMed=15151908; DOI=10.1152/ajpcell.00590.2003;
RA Abuladze N., Pushkin A., Tatishchev S., Newman D., Sassani P., Kurtz I.;
RT "Expression and localization of rat NBC4c in liver and renal
RT uroepithelium.";
RL Am. J. Physiol. 287:C781-C789(2004).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=12388414; DOI=10.1152/ajprenal.00055.2002;
RA Xu J., Wang Z., Barone S., Petrovic M., Amlal H., Conforti L., Petrovic S.,
RA Soleimani M.;
RT "Expression of the Na+-HCO-3 cotransporter NBC4 in rat kidney and
RT characterization of a novel NBC4 variant.";
RL Am. J. Physiol. 284:F41-F50(2003).
CC -!- FUNCTION: Mediates sodium- and bicarbonate-dependent electrogenic
CC sodium bicarbonate cotransport, with a Na(+):HCO3(-) stoichiometry of
CC 2:1. May have a housekeeping function in regulating the pH of tissues
CC in which it is expressed. May play a role in mediating Na(+):HCO3(-)
CC cotransport in hepatocytes and intrahepatic cholangiocytes. May also be
CC important in protecting the renal paranchyma from alterations in urine
CC pH. {ECO:0000250|UniProtKB:Q9BY07, ECO:0000269|PubMed:15151908}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15151908};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15151908}. Basolateral
CC cell membrane {ECO:0000269|PubMed:15151908}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:15151908}. Note=Localized predominantly to
CC the basolateral sinusoidal membrane in hepatocytes.
CC {ECO:0000269|PubMed:15151908}.
CC -!- TISSUE SPECIFICITY: Observed in hepatocytes and in the apical region of
CC bile duct intrahepatic cholangiocytes of liver. Also observed in
CC uroepithelium cells lining the outer pelvic wall of the kidney (at
CC protein level). Highly expressed in colon, distal colon, liver, kidney
CC and testis. Moderate expression in duodenum and stomach and weak
CC expression in heart. In kidney, very weakly expressed in the inner
CC medulla, but abundantly expressed in cortex and outer medulla in the
CC medullary thick ascending and cortical thick ascending limbs of the
CC loop of Henle. {ECO:0000269|PubMed:12388414,
CC ECO:0000269|PubMed:15151908}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000255}.
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DR EMBL; AY496959; AAS98674.1; -; mRNA.
DR RefSeq; NP_997677.1; NM_212512.1.
DR AlphaFoldDB; Q6RI88; -.
DR SMR; Q6RI88; -.
DR STRING; 10116.ENSRNOP00000014249; -.
DR CarbonylDB; Q6RI88; -.
DR PaxDb; Q6RI88; -.
DR PRIDE; Q6RI88; -.
DR GeneID; 297386; -.
DR KEGG; rno:297386; -.
DR UCSC; RGD:1303009; rat.
DR CTD; 57835; -.
DR RGD; 1303009; Slc4a5.
DR VEuPathDB; HostDB:ENSRNOG00000010378; -.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q6RI88; -.
DR OMA; WIPSDFY; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q6RI88; -.
DR TreeFam; TF313630; -.
DR Reactome; R-RNO-425381; Bicarbonate transporters.
DR PRO; PR:Q6RI88; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000010378; Expressed in adult mammalian kidney and 9 other tissues.
DR ExpressionAtlas; Q6RI88; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005452; F:inorganic anion exchanger activity; TAS:RGD.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; TAS:RGD.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0033326; P:cerebrospinal fluid secretion; ISO:RGD.
DR GO; GO:0002064; P:epithelial cell development; ISO:RGD.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; ISO:RGD.
DR GO; GO:0048311; P:mitochondrion distribution; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; TAS:RGD.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0003014; P:renal system process; ISO:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Anion exchange; Cell membrane; Disulfide bond; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1112
FT /note="Electrogenic sodium bicarbonate cotransporter 4"
FT /id="PRO_0000328921"
FT TOPO_DOM 1..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..820
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..839
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..880
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 881..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..945
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 967..992
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 993..1010
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1011..1015
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1016..1033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1034..1112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 671..673
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 717..729
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
SQ SEQUENCE 1112 AA; 123944 MW; BE5EF90A543DA35C CRC64;
MKVEEKAGVK KLEPTSYRRR HPEQDFPSIH IGFPVPGYSQ RKSDSKGHLS GLQRVQWSLQ
PDKSQQDLAG PDGIKASSLG GSVDFTKRIR SPAAEQLQDI LGEEDEAPNP TLFTEMDTLQ
HDGDQMEWKE SARWIKFEEK VEEGGERWSK PHVSTLSLHS LFELRTCLQT GTVLLDLDSG
SLPQIIDDVI EKQIEGGLLR PELRERVSYV LLRKHRHQTK KPIHRSLADI GKSVSTTNRS
SARSPSAGPT LHHSTEDLRI RQSTSYGHLC HAQSRSMNDI SHTPNTDQRK NKFMKKIPKD
SEASNVLVGE VDFLDQPFIA FVRLAQSSML GGVTEVPVPT RFLFILLGPS GRAKSYNEIG
RAIATLMVDD LFSDVAYKAR NREDLIAGVD EFLDEVIVLP PGEWDPNIRI EPPKKVPSAD
KRKSVFSLAE LGQMNGSVGR SGASAGGGGS GGGAGGSGAG GGGSGNEAEM PAMHEIGEEL
IWTGRFFGGL RLDVKRKLPW FPSDFYDGFH IQSISAVLFI YLGCITNAIT FGGLLGDATD
NYQGVMESFL GTAMAGSLFC LFSGQPLIIL SSTGPILIFE KLLFDFSKAN GLDYMEFRLW
IGLHSAIQCL ILVATDASFI IKYITRFTEE GFSTLISFIF IYDAIKKMIG AFKYYPINTD
FKPDSITTYK CECVAPDTVN TTTVNDSALL VPNTNMSVYT PLNLTALDWS LLSKKECLSY
GGRLLGSSCQ FVPDLALMSF ILFFGTYSMT LTLKKFKFSR YFPTKVRTLV ADFSIVFSIL
LFCGIDACFG LQTPKLHVPN VIKPTRPDRG WFVAPFGKNP WWVYPASILP ALLVTILIFM
DQQITAVIVN RKENKLRKAA GYHLDLFWVG ILMALCSFMG LPWYVAATVI SIAHIDSLKM
ETETSAPGEQ PQFLGVREQR VTGVMVFILT GISVFLAPIL KYIPMPVLYG VFLYMGVASL
NGIQFWDRCK LFLMPAKHQP DHAFLRHVPL RRIHLFTLVQ ILCLALLWIL KSTMAAIIFP
VMILGLIIVR RLLDLIFSQH DLAWIDNILP EKEKKESDRK KRRKEVHENT DKEPQFLPPS
VVKIPMEGIP SDPQNGIHCV GRKRSSSWSH SL
