S4A4_RAT
ID S4A4_RAT Reviewed; 1079 AA.
AC Q9JI66; O35422; O54815; Q9JJ32; Q9QXH6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Electrogenic sodium bicarbonate cotransporter 1;
DE Short=Sodium bicarbonate cotransporter;
DE AltName: Full=NBC-like protein;
DE AltName: Full=Na(+)/HCO3(-) cotransporter;
DE AltName: Full=Solute carrier family 4 member 4;
GN Name=Slc4a4; Synonyms=Nbc, Nbc1, Nbce1, Rnbc1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Kidney cortex;
RX PubMed=9486238; DOI=10.1152/ajprenal.1998.274.2.f425;
RA Romero M.F., Fong P., Berger U.V., Hediger M.A., Boron W.F.;
RT "Cloning and functional expression of rNBC, an electrogenic Na(+)-HCO3-
RT cotransporter from rat kidney.";
RL Am. J. Physiol. 274:F425-F432(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=9841505; DOI=10.1152/ajprenal.1998.274.6.f1119;
RA Burnham C.E., Flagella M., Wang Z., Amlal H., Shull G.E., Soleimani M.;
RT "Cloning, renal distribution, and regulation of the rat Na+-HCO3-
RT cotransporter.";
RL Am. J. Physiol. 274:F1119-F1126(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, REGULATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10837348; DOI=10.1152/ajpcell.2000.278.6.c1200;
RA Bevensee M.O., Schmitt B.M., Choi I., Romero M.F., Boron W.F.;
RT "An electrogenic Na(+)-HCO3(-) cotransporter (NBC) with a novel COOH-
RT terminus, cloned from rat brain.";
RL Am. J. Physiol. 278:C1200-C1211(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=10648705; DOI=10.1523/jneurosci.20-03-01001.2000;
RA Giffard R.G., Papadopoulos M.C., van Hooft J.A., Xu L., Giuffrida R.,
RA Monyer H.;
RT "The electrogenic sodium bicarbonate cotransporter: developmental
RT expression in rat brain and possible role in acid vulnerability.";
RL J. Neurosci. 20:1001-1008(2000).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11592950; DOI=10.1152/ajprenal.2001.281.5.f920;
RA Bok D., Schibler M.J., Pushkin A., Sassani P., Abuladze N., Naser Z.,
RA Kurtz I.;
RT "Immunolocalization of electrogenic sodium-bicarbonate cotransporters pNBC1
RT and kNBC1 in the rat eye.";
RL Am. J. Physiol. 281:F920-F935(2001).
RN [6]
RP INDUCTION.
RX PubMed=11703600; DOI=10.1046/j.1523-1755.2001.00995.x;
RA Amlal H., Chen Q., Greeley T., Pavelic L., Soleimani M.;
RT "Coordinated down-regulation of NBC-1 and NHE-3 in sodium and bicarbonate
RT loading.";
RL Kidney Int. 60:1824-1836(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12444017; DOI=10.1152/ajpcell.00166.2002;
RA Satoh H., Moriyama N., Hara C., Yamada H., Horita S., Kunimi M.,
RA Tsukamoto K., Iso-O N., Inatomi J., Kawakami H., Kudo A., Endou H.,
RA Igarashi T., Goto A., Fujita T., Seki G.;
RT "Localization of Na+-HCO-3 cotransporter (NBC-1) variants in rat and human
RT pancreas.";
RL Am. J. Physiol. 284:C729-C737(2003).
RN [8]
RP MUTAGENESIS OF ASN-243; ASN-252; ASN-541; ASN-636; ASN-641 AND ASN-661, AND
RP GLYCOSYLATION AT ASN-641 AND ASN-661.
RX PubMed=12604466; DOI=10.1152/ajprenal.00131.2002;
RA Choi I., Hu L., Rojas J.D., Schmitt B.M., Boron W.F.;
RT "Role of glycosylation in the renal electrogenic Na+-HCO3-cotransporter
RT (NBCe1).";
RL Am. J. Physiol. 284:F1199-F1206(2003).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15329059; DOI=10.1111/j.1365-201x.2004.01297.x;
RA Kristensen J.M., Kristensen M., Juel C.;
RT "Expression of Na+/HCO3- co-transporter proteins (NBCs) in rat and human
RT skeletal muscle.";
RL Acta Physiol. Scand. 182:69-76(2004).
RN [10]
RP INDUCTION.
RX PubMed=15781297; DOI=10.1016/j.taap.2004.08.021;
RA Ahn D.-W., Chung J.-M., Kim J.-Y., Kim K.-R., Park Y.-S.;
RT "Inhibition of renal Na+/H+ exchange in cadmium-intoxicated rats.";
RL Toxicol. Appl. Pharmacol. 204:91-98(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-245; THR-249;
RP THR-254; SER-257; SER-262; SER-1029; SER-1034 AND SER-1069, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-1026; SER-1029; SER-1060; SER-1064 AND SER-1078 (ISOFORM
RP 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:Q9Y6R1,
CC ECO:0000269|PubMed:10648705, ECO:0000269|PubMed:10837348,
CC ECO:0000269|PubMed:9486238}.
CC -!- FUNCTION: [Isoform 2]: May have a higher activity than isoform 1.
CC {ECO:0000250|UniProtKB:Q9Y6R1}.
CC -!- ACTIVITY REGULATION: Inhibited by stilbene derivatives and regulated by
CC cyclic AMP.
CC -!- SUBUNIT: Homodimer. Interacts with CA2/carbonic anhydrase 2 and
CC CA4/carbonic anhydrase 4 which may regulate transporter activity.
CC Isoform 1 but not isoform 2 interacts with AHCYL1 (via PEST domain when
CC phosphorylated); the interaction increases SLC4A4 isoform 1 activity.
CC Interacts with AHCYL2. {ECO:0000250|UniProtKB:O88343,
CC ECO:0000250|UniProtKB:Q9GL77, ECO:0000250|UniProtKB:Q9Y6R1}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:9486238}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9486238}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=bNBC1, NBCe1-B, pNBC1, pNBC-1, rb1NBC;
CC IsoId=Q9JI66-1; Sequence=Displayed;
CC Name=2; Synonyms=kNBC1, kNBC-1, NBCe1-A, rkNBC, rkNBC1;
CC IsoId=Q9JI66-2; Sequence=VSP_016717, VSP_016718;
CC Name=3; Synonyms=NBCe1-C, rb2NBC;
CC IsoId=Q9JI66-3; Sequence=VSP_016719;
CC -!- TISSUE SPECIFICITY: Specifically expressed in kidney and to a lower
CC extent in liver, lung, spleen, brain, skeletal muscle and heart. In
CC kidney, expressed in proximal tubules at the corticomedullary junction.
CC Isoform 2 is specifically expressed in kidney. Isoform 1 is expressed
CC in kidney and pancreas while isoform 3 is specifically expressed in
CC brain (at protein level). In brain, isoform 1 is expressed in
CC astrocytes while isoform 3 is expressed in neurons (at protein level).
CC In the eye, isoform 1 is expressed in cornea, conjunctiva, lens
CC epithelium, ciliary bodies and retina while isoform 2 is detected only
CC in the conjunctiva. {ECO:0000269|PubMed:10648705,
CC ECO:0000269|PubMed:10837348, ECO:0000269|PubMed:11592950,
CC ECO:0000269|PubMed:12444017, ECO:0000269|PubMed:15329059,
CC ECO:0000269|PubMed:9486238, ECO:0000269|PubMed:9841505}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at E17 in spinal cord
CC and starts in forebrain at birth. Higher expression in brain is
CC detected at postnatal day 15 and persists throughout adulthood.
CC {ECO:0000269|PubMed:10648705}.
CC -!- INDUCTION: Down-regulated after cadmium-intoxication and sodium or
CC bicarbonate loading (at protein level). Down-regulated by HCO3[-]
CC loading. {ECO:0000269|PubMed:11703600, ECO:0000269|PubMed:15781297,
CC ECO:0000269|PubMed:9841505}.
CC -!- PTM: Phosphorylation of Ser-1026 by PKA increases the binding of CA2
CC and changes the Na(+):HCO3(-) stoichiometry of the transporter from 3:1
CC to 2:1. Phosphorylated in presence of STK39 and dephosphorylated in
CC presence of PP1 phosphatase; phosphorylation seems to inhibit SLC4A4
CC activity. {ECO:0000250|UniProtKB:O88343, ECO:0000250|UniProtKB:Q9Y6R1}.
CC -!- PTM: N-glycosylation is not necessary for the transporter basic
CC functions. {ECO:0000269|PubMed:12604466}.
CC -!- MISCELLANEOUS: [Isoform 2]: Mutagenesis of Asn-33 into Gln has no
CC effect on N-glycosylation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; AF004017; AAC40034.1; -; mRNA.
DR EMBL; AF027362; AAB83997.1; -; mRNA.
DR EMBL; AF124441; AAF87312.1; -; mRNA.
DR EMBL; AF254802; AAF87553.1; -; mRNA.
DR EMBL; AF210250; AAF21040.1; -; mRNA.
DR PIR; T13962; T13962.
DR PIR; T14110; T14110.
DR RefSeq; NP_445876.1; NM_053424.1. [Q9JI66-1]
DR RefSeq; XP_006250853.1; XM_006250791.3. [Q9JI66-3]
DR AlphaFoldDB; Q9JI66; -.
DR SMR; Q9JI66; -.
DR BioGRID; 249983; 4.
DR IntAct; Q9JI66; 2.
DR MINT; Q9JI66; -.
DR STRING; 10116.ENSRNOP00000004391; -.
DR TCDB; 2.A.31.2.2; the anion exchanger (ae) family.
DR GlyGen; Q9JI66; 2 sites.
DR iPTMnet; Q9JI66; -.
DR PhosphoSitePlus; Q9JI66; -.
DR SwissPalm; Q9JI66; -.
DR PaxDb; Q9JI66; -.
DR PRIDE; Q9JI66; -.
DR GeneID; 84484; -.
DR KEGG; rno:84484; -.
DR UCSC; RGD:68936; rat. [Q9JI66-1]
DR CTD; 8671; -.
DR RGD; 68936; Slc4a4.
DR VEuPathDB; HostDB:ENSRNOG00000003134; -.
DR eggNOG; KOG1172; Eukaryota.
DR HOGENOM; CLU_002289_5_0_1; -.
DR InParanoid; Q9JI66; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q9JI66; -.
DR TreeFam; TF313630; -.
DR Reactome; R-RNO-425381; Bicarbonate transporters.
DR PRO; PR:Q9JI66; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000003134; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; Q9JI66; baseline and differential.
DR Genevisible; Q9JI66; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; ISO:RGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; ISO:RGD.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:RGD.
DR GO; GO:0051453; P:regulation of intracellular pH; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0006885; P:regulation of pH; TAS:RGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; ISO:RGD.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1079
FT /note="Electrogenic sodium bicarbonate cotransporter 1"
FT /id="PRO_0000079231"
FT TOPO_DOM 1..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 467..491
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 492..501
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 502..520
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 522..542
FT /note="Discontinuously helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 543..550
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 551..571
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 572..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 586..609
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 610..692
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 693..710
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 711..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 726..745
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 746..779
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 780..807
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 808..819
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 820..836
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 837
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 838..855
FT /note="Discontinuously helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 856..877
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 878..894
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 895..901
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 902..918
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 919..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT INTRAMEM 961..986
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 987..1079
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT REGION 1..62
FT /note="Required for interaction with AHCYL1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..779
FT /note="Interaction with CA4"
FT /evidence="ECO:0000250"
FT REGION 1002..1004
FT /note="CA2-binding"
FT /evidence="ECO:0000250"
FT REGION 1012..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1033
FT /note="CA2-binding"
FT /evidence="ECO:0000250"
FT REGION 1057..1059
FT /note="Required for basolateral targeting"
FT /evidence="ECO:0000250"
FT COMPBIAS 39..53
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 636
FT /note="Not glycosylated"
FT MOD_RES 30
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88343"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88343"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88343"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88343"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88343"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88343"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1026
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88343"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12604466"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12604466"
FT DISULFID 627..629
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 674..686
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9486238,
FT ECO:0000303|PubMed:9841505"
FT /id="VSP_016717"
FT VAR_SEQ 45..85
FT /note="HKRKAGHKEKKEKERISENYSDKSDVENADESSSSILKPLI -> MSTENVE
FT GKPNNLGERGRARSSTFLRVFQPMFNHSIFTSAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9486238,
FT ECO:0000303|PubMed:9841505"
FT /id="VSP_016718"
FT VAR_SEQ 1034..1079
FT /note="SDCPYSEKVPSIKIPMDITEQQPFLSDNKPLDRERSSTFLERHTSC -> EK
FT DPQHSLNATHHADKIPFLESLGLPSPPRSPVKVVPQIRIELESEDNDYLWRNKGTETTL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10837348"
FT /id="VSP_016719"
FT MUTAGEN 243
FT /note="N->Q: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:12604466"
FT MUTAGEN 252
FT /note="N->Q: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:12604466"
FT MUTAGEN 541
FT /note="N->Q: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:12604466"
FT MUTAGEN 636
FT /note="N->Q: No effect on N-glycosylation. Complete loss of
FT N-glycosylation without effect on transporter basic
FT function; when associated with Q-641 and Q-661."
FT /evidence="ECO:0000269|PubMed:12604466"
FT MUTAGEN 641
FT /note="N->Q: Reduces the extent of N-glycosylation.
FT Complete loss of N-glycosylation without effect on
FT transporter basic function; when associated with Q-636 and
FT Q-661."
FT /evidence="ECO:0000269|PubMed:12604466"
FT MUTAGEN 661
FT /note="N->Q: Reduces the extent of N-glycosylation.
FT Complete loss of N-glycosylation without effect on
FT transporter basic function; when associated with Q-636 and
FT Q-641."
FT /evidence="ECO:0000269|PubMed:12604466"
FT CONFLICT 284..285
FT /note="AS -> VP (in Ref. 2; AAB83997 and 4; AAF21040)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="A -> G (in Ref. 2; AAB83997 and 4; AAF21040)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="S -> Y (in Ref. 2; AAB83997)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="S -> F (in Ref. 2; AAB83997)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="A -> P (in Ref. 2; AAB83997 and 4; AAF21040)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9JI66-2:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9JI66-3:1026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9JI66-3:1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9JI66-3:1060
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9JI66-3:1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9JI66-3:1078
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1079 AA; 121343 MW; F5A187AFE41BA5B4 CRC64;
MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG HKEKKEKERI
SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFSN
PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI
AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA
KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP
HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT
VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF
NFSKDHSFDY LEFRLWIGLW SAFMCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA
FKKMIKLADY YPINSDFRVG YNTHFSCACL PPDPVNLSVS NDTTLAPEDL PTVSSTDMYH
NATFDWAYLS KKECVKFGGK LVGNNCDFVP DITLMSFILF LGTYTSSMAM KKFKTSRYFP
TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPHRGWFV PPFGGNPWWV
CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VVCSFMALPW
YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI
PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTSLQVLC
LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK
KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD ITEQQPFLSD NKPLDRERSS TFLERHTSC
