S4A7_RAT
ID S4A7_RAT Reviewed; 1218 AA.
AC Q9R1N3; Q9QYD5; Q9R1L1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sodium bicarbonate cotransporter 3;
DE AltName: Full=Electroneutral sodium bicarbonate cotransporter 1;
DE AltName: Full=NBC-like protein;
DE AltName: Full=Solute carrier family 4 member 7;
GN Name=Slc4a7; Synonyms=Nbc, Nbc2, Nbc3, Nbcn1;
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] (ISOFORMS 1; 2 AND 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Aorta, and Smooth muscle;
RX PubMed=10850716; DOI=10.1038/35014615;
RA Choi I., Aalkjaer C., Boulpaep E.L., Boron W.F.;
RT "An electroneutral sodium/bicarbonate cotransporter NBCn1 and associated
RT sodium channel.";
RL Nature 405:571-575(2000).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=10662737; DOI=10.1152/ajprenal.2000.278.2.f327;
RA Kwon T.-H., Pushkin A., Abuladze N., Nielsen S., Kurtz I.;
RT "Immunoelectron microscopic localization of NBC3 sodium-bicarbonate
RT cotransporter in rat kidney.";
RL Am. J. Physiol. 278:F327-F336(2000).
RN [3]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=11053051; DOI=10.1152/ajprenal.2000.279.5.f901;
RA Vorum H., Kwon T.-H., Fulton C., Simonsen B., Choi I., Boron W.F.,
RA Maunsbach A.B., Nielsen S., Aalkjaer C.;
RT "Immunolocalization of electroneutral Na-HCO(3)(-) cotransporter in rat
RT kidney.";
RL Am. J. Physiol. 279:F901-F909(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10975418;
RA Pushkin A., Clark I., Kwon T.-H., Nielsen S., Kurtz I.;
RT "Immunolocalization of NBC3 and NHE3 in the rat epididymis: colocalization
RT of NBC3 and the vacuolar H+-ATPase.";
RL J. Androl. 21:708-720(2000).
RN [5]
RP INTERACTION WITH CFTR.
RX PubMed=12403779; DOI=10.1074/jbc.m201862200;
RA Park M., Ko S.B.H., Choi J.Y., Muallem G., Thomas P.J., Pushkin A.,
RA Lee M.-S., Kim J.Y., Lee M.G., Muallem S., Kurtz I.;
RT "The cystic fibrosis transmembrane conductance regulator interacts with and
RT regulates the activity of the HCO3- salvage transporter human Na+-HCO3-
RT cotransport isoform 3.";
RL J. Biol. Chem. 277:50503-50509(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15075186; DOI=10.1152/ajprenal.00437.2002;
RA Praetorius J., Kim Y.-H., Bouzinova E.V., Frische S., Rojek A.,
RA Aalkjaer C., Nielsen S.;
RT "NBCn1 is a basolateral Na+-HCO3- cotransporter in rat kidney inner
RT medullary collecting ducts.";
RL Am. J. Physiol. 286:F903-F912(2004).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 4 AND 5), TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14673192; DOI=10.1113/jphysiol.2003.046474;
RA Odgaard E., Jakobsen J.K., Frische S., Praetorius J., Nielsen S.,
RA Aalkjaer C., Leipziger J.;
RT "Basolateral Na+-dependent HCO3- transporter NBCn1-mediated HCO3-influx in
RT rat medullary thick ascending limb.";
RL J. Physiol. (Lond.) 555:205-218(2004).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16301216; DOI=10.1093/hmg/ddi417;
RA Reiners J., van Wijk E., Maerker T., Zimmermann U., Juergens K.,
RA te Brinke H., Overlack N., Roepman R., Knipper M., Kremer H., Wolfrum U.;
RT "Scaffold protein harmonin (USH1C) provides molecular links between Usher
RT syndrome type 1 and type 2.";
RL Hum. Mol. Genet. 14:3933-3943(2005).
RN [9]
RP ALTERNATIVE SPLICING (ISOFORM 6), AND TISSUE SPECIFICITY.
RX PubMed=15718246; DOI=10.1074/jbc.m408646200;
RA Cooper D.S., Saxena N.C., Yang H.S., Lee H.J., Moring A.G., Lee A.,
RA Choi I.;
RT "Molecular and functional characterization of the electroneutral Na/HCO3
RT cotransporter NBCn1 in rat hippocampal neurons.";
RL J. Biol. Chem. 280:17823-17830(2005).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=16126812; DOI=10.1152/ajpheart.00713.2005;
RA Damkier H.H., Nielsen S., Praetorius J.;
RT "An anti-NH2-terminal antibody localizes NBCn1 to heart endothelia and
RT skeletal and vascular smooth muscle cells.";
RL Am. J. Physiol. 290:H172-H180(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-155; SER-247; SER-404
RP AND SER-407, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1201 (ISOFORM
RP 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1188 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1078 (ISOFORM 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORMS 4 AND 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067 (ISOFORM 5), AND
RP 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: Electroneutral sodium- and bicarbonate-dependent
CC cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Regulates
CC intracellular pH and may play a role in bicarbonate salvage in
CC secretory epithelia. May also have an associated sodium channel
CC activity. {ECO:0000269|PubMed:10850716}.
CC -!- ACTIVITY REGULATION: Transporter activity is regulated by CA2/carbonic
CC anhydrase 2, cAMP and PKA. Insensitive to stilbene derivatives. May be
CC inhibited by 5-(N-ethyl-N-isopropyl)-amiloride (EIPA) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with USH1C. Forms a complex with ATP6V1B1 and
CC SLC9A3R1/EBP50. Interacts in a pH dependent-manner with CA2/carbonic
CC anhydrase 2 (By similarity). Interacts with CFTR probably through
CC SLC9A3R1/EBP50. {ECO:0000250, ECO:0000269|PubMed:12403779}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Apical cell membrane; Multi-pass membrane protein. Cell
CC projection, stereocilium. Note=Also described at the apical cell
CC membrane. Localizes to the stereocilia of cochlear outer hair cells and
CC to the lateral membrane of cochlear inner hair cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=NBCn1-B, NBCn1B;
CC IsoId=Q9R1N3-1; Sequence=Displayed;
CC Name=2; Synonyms=NBCn1-D, NBCn1D;
CC IsoId=Q9R1N3-2; Sequence=VSP_017172;
CC Name=3; Synonyms=NBCn1-C, NBCn1C;
CC IsoId=Q9R1N3-3; Sequence=VSP_017169, VSP_017172;
CC Name=4;
CC IsoId=Q9R1N3-4; Sequence=VSP_017171, VSP_017172;
CC Name=5;
CC IsoId=Q9R1N3-5; Sequence=VSP_017170, VSP_017171, VSP_017172;
CC Name=6; Synonyms=NBCn1-E;
CC IsoId=Q9R1N3-6; Sequence=VSP_017171;
CC -!- TISSUE SPECIFICITY: Expressed in aorta, ventricles, atrium, mesenteric
CC artery, kidney, spleen, duodenum, jejunum, ileum, colon, lung, trachea,
CC gastric fundus and pylorus, cerebrum, cerebellum, pancreas, liver,
CC parotid gland, and epididymis. Expressed in the inner ear by cochlear
CC outer and inner hair cells (at protein level). Highly expressed in
CC testis and spleen. Also detected in heart, brain, lung, liver and
CC kidney. Isoform 4 and isoform 5 are specifically expressed in kidney.
CC Isoform 6 is specifically expressed in hippocampal neurons.
CC {ECO:0000269|PubMed:10850716, ECO:0000269|PubMed:14673192,
CC ECO:0000269|PubMed:15718246, ECO:0000269|PubMed:16126812,
CC ECO:0000269|PubMed:16301216}.
CC -!- INDUCTION: Up-regulated in kidney upon metabolic acidosis.
CC {ECO:0000269|PubMed:14673192}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with the CFTR,
CC SLC9A3R1/EBP50 complex and probably with USH1C. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11053051}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; AF069511; AAF14345.1; -; mRNA.
DR EMBL; AF070475; AAD46389.1; -; mRNA.
DR EMBL; AF080106; AAD47142.1; -; mRNA.
DR RefSeq; NP_001257790.1; NM_001270861.1. [Q9R1N3-1]
DR RefSeq; NP_478118.1; NM_058211.2. [Q9R1N3-2]
DR AlphaFoldDB; Q9R1N3; -.
DR SMR; Q9R1N3; -.
DR BioGRID; 250777; 1.
DR STRING; 10116.ENSRNOP00000008759; -.
DR TCDB; 2.A.31.2.1; the anion exchanger (ae) family.
DR GlyGen; Q9R1N3; 6 sites.
DR iPTMnet; Q9R1N3; -.
DR PhosphoSitePlus; Q9R1N3; -.
DR SwissPalm; Q9R1N3; -.
DR jPOST; Q9R1N3; -.
DR PaxDb; Q9R1N3; -.
DR PRIDE; Q9R1N3; -.
DR DNASU; 117955; -.
DR GeneID; 117955; -.
DR KEGG; rno:117955; -.
DR CTD; 9497; -.
DR RGD; 621208; Slc4a7.
DR VEuPathDB; HostDB:ENSRNOG00000005957; -.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; Q9R1N3; -.
DR OMA; TEENFAC; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q9R1N3; -.
DR Reactome; R-RNO-425381; Bicarbonate transporters.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q9R1N3; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000005957; Expressed in duodenum and 18 other tissues.
DR ExpressionAtlas; Q9R1N3; baseline and differential.
DR Genevisible; Q9R1N3; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
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:0060117; P:auditory receptor cell development; ISO:RGD.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; ISO:RGD.
DR GO; GO:0021747; P:cochlear nucleus development; ISO:RGD.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0046666; P:retinal cell programmed cell death; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; 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; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR Pfam; PF07565; Band_3_cyto; 2.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; SSF55804; 2.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1218
FT /note="Sodium bicarbonate cotransporter 3"
FT /id="PRO_0000079235"
FT TOPO_DOM 1..612
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 634..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..699
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..750
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 751..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..865
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..912
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 934..958
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 959..979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 980..1015
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1016..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1037..1038
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1059
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1060..1096
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1097..1117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1118..1218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1140
FT /note="CA2-binding"
FT /evidence="ECO:0000250"
FT REGION 1148..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1215..1218
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 58..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTY2"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTY2"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BTY2"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT MOD_RES 1171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M7"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 770..772
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 806..818
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT VAR_SEQ 245..257
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10850716"
FT /id="VSP_017169"
FT VAR_SEQ 245..255
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_017170"
FT VAR_SEQ 256..378
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_017171"
FT VAR_SEQ 1192
FT /note="S -> SIDPSVVNISDEMAKTAQWKALSMNTENAKVTRPNMS (in
FT isoform 2, isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10850716"
FT /id="VSP_017172"
FT MOD_RES Q9R1N3-2:1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9R1N3-3:1188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9R1N3-4:263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9R1N3-4:1078
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9R1N3-5:1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9R1N3-6:263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1218 AA; 135954 MW; CF5C8BD4F49CAB00 CRC64;
MEADGAGEQM RPLLTRGPDE EAVVDLGKTS STVNTKFEKE ELESHRAVYV GVHVPFSKES
RRRHRHRGHK HHHRRRKDKD SDKEDGRESP SYDTPSQRVQ FILGTEDDDE EHIPHDLFTE
MDELCYRDGE EYEWKETARW LKFEEDVEDG GDRWSKPYVA TLSLHSLFEL RSCILNGTVM
LDMRASTLDE IADMVLDNMI ASGQLDDSIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA
DIGKKHSDPH LLERNGEGLS ASRHSLRTGL SASNLSLRGE SPLSLLLSHL LPSSRAGTPA
GSRCTTPVPT PQNSPPSSPS LSRLTSRSSQ QTQPQAPEVL VSPDRDDIPR VVIHPPEEDI
EALKGQEQKN EENTDFTPGI LASPQSAPGN LDSSKSGEVK GNGSGGSREN STVDFSKVDM
NFMRKIPTGA EASNVLVGEV DFLERPIIAF VRLAPAVLLS GLTEVPVPTR FLFLLLGPAG
KAPQYHEIGR SIATLMTDEI FHDVAYKAKD RNDLLSGIDE FLDQVTVLPP GEWDPSIRIE
PPKSVPSQEK RKIPAFPNGS APVSADPPKE ADHHAGPELQ RTGRLFGGLI LDIKRKAPFF
LSDFKDALSL QCLASILFLY CACMSPVITF GGLLGEATEG RISAIESLFG ASLTGIAYSL
FAGQPLTILG STGPVLVFEK ILFKFCRDYH LSYLSLRTSI GLWTSFLCIV LVATDASSLV
CYITRFTEEA FAALICIIFI YEALEKLFHL GEIYAFNMHN NLDALTSYTC VCAEPSNPSN
ETVELWERKN VTAASISWAN LTVSECKTFH GMFVGSACGP HGPYVPDVLF WCVVLFFTTF
FLSSFLKQFK TKRYFPTKVR STISDFAVFL TIVIMVAIDY LVGIPSPKLH VPEKFEPTDP
SRGWIISPLG DNPWWTLLIA AVPALLCTIL IFMDQQITAV IINRKEHKLK KGAGYHLDLL
MVAVMLGVCS IMGLPWFVAA TVLSISHVNS LKVESECSAP GEQPKFLGIR EQRVTGLMIF
ILMGLSVFMT SVLKFIPMPV LYGVFLYMGV SSLKGIQFFD RIKLFGMPAK HQPDLIYLRY
VPLWKVHVFT VVQLTCLVLL WVIKASAAAV VFPMMVLALV FVRKLMDLCF TKRELSWLDD
LMPESKKKKE DDKKKKEKEE AERMLQGDGD TVHLPFERGS LLQIPVKTLK YSPEKPVSVT
INFEDEPSKK YMDAETSL
