S26A9_HUMAN
ID S26A9_HUMAN Reviewed; 791 AA.
AC Q7LBE3; A7E2V6; B1AVM8; B1AVM9; B7ZKK2; Q96PK9; Q96RN0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Solute carrier family 26 member 9;
DE AltName: Full=Anion transporter/exchanger protein 9;
GN Name=SLC26A9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=11834742; DOI=10.1074/jbc.m111802200;
RA Lohi H., Kujala M., Maekelae S., Lehtonen E., Kestilae M.,
RA Saarialho-Kere U., Markovich D., Kere J.;
RT "Functional characterization of three novel tissue-specific anion
RT exchangers SLC26A7, -A8, and -A9.";
RL J. Biol. Chem. 277:14246-14254(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Mount D.B.;
RT "Cloning of human SLC26A9, a new member of the sulphate transporter gene
RT family of anion transporter/exchangers.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=15800055; DOI=10.1152/ajpcell.00030.2005;
RA Xu J., Henriksnas J., Barone S., Witte D., Shull G.E., Forte J.G., Holm L.,
RA Soleimani M.;
RT "SLC26A9 is expressed in gastric surface epithelial cells, mediates
RT Cl-/HCO3- exchange, and is inhibited by NH4+.";
RL Am. J. Physiol. 289:C493-C505(2005).
RN [7]
RP VARIANTS ASN-70; ASN-127; THR-384; TRP-575; LEU-606; LEU-622; MET-744 AND
RP ARG-748, AND CHARACTERIZATION OF VARIANTS ASN-70; ASN-127; LEU-622 AND
RP MET-744.
RX PubMed=22544634; DOI=10.1002/humu.22107;
RA Chen A.P., Chang M.H., Romero M.F.;
RT "Functional analysis of nonsynonymous single nucleotide polymorphisms in
RT human SLC26A9.";
RL Hum. Mutat. 33:1275-1284(2012).
CC -!- FUNCTION: DIDS- and thiosulfate- sensitive anion exchanger mediating
CC chloride, sulfate and oxalate transport (PubMed:11834742). Mediates
CC chloride/bicarbonate exchange or chloride-independent bicarbonate
CC extrusion thus assuring bicarbonate secretion (PubMed:15800055). May
CC prefer chloride anions and mediate uncoupled chloride anion transport
CC in an alternate-access mechanism where a saturable binding site is
CC alternately exposed to either one or the other side of the membrane (By
CC similarity). {ECO:0000250|UniProtKB:Q8BU91,
CC ECO:0000269|PubMed:11834742, ECO:0000269|PubMed:15800055}.
CC -!- ACTIVITY REGULATION: Inhibited by ammonium and thiosulfate.
CC {ECO:0000269|PubMed:11834742, ECO:0000269|PubMed:15800055}.
CC -!- SUBUNIT: May form homodimers (in vitro).
CC {ECO:0000250|UniProtKB:Q8BU91}.
CC -!- INTERACTION:
CC Q7LBE3-1; Q9HD26: GOPC; NbExp=2; IntAct=EBI-25464835, EBI-349832;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BU91};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7LBE3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7LBE3-2; Sequence=VSP_054056;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in lung at the luminal side
CC of the bronchiolar and alveolar epithelium of lung. To a lower extent,
CC also expressed in pancreas and prostate. {ECO:0000269|PubMed:11834742}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; AF331525; AAK95667.1; -; mRNA.
DR EMBL; AF314958; AAL26867.1; -; mRNA.
DR EMBL; AL713965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91587.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91588.1; -; Genomic_DNA.
DR EMBL; BC136538; AAI36539.1; -; mRNA.
DR EMBL; BC151208; AAI51209.1; -; mRNA.
DR CCDS; CCDS30989.1; -. [Q7LBE3-2]
DR CCDS; CCDS30990.1; -. [Q7LBE3-1]
DR RefSeq; NP_443166.1; NM_052934.3. [Q7LBE3-1]
DR RefSeq; NP_599152.2; NM_134325.2. [Q7LBE3-2]
DR PDB; 7CH1; EM; 2.60 A; A/B=1-791.
DR PDBsum; 7CH1; -.
DR AlphaFoldDB; Q7LBE3; -.
DR SMR; Q7LBE3; -.
DR BioGRID; 125409; 2.
DR IntAct; Q7LBE3; 3.
DR STRING; 9606.ENSP00000356102; -.
DR ChEMBL; CHEMBL4523359; -.
DR TCDB; 2.A.53.2.15; the sulfate permease (sulp) family.
DR GlyGen; Q7LBE3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7LBE3; -.
DR PhosphoSitePlus; Q7LBE3; -.
DR BioMuta; SLC26A9; -.
DR DMDM; 74749908; -.
DR EPD; Q7LBE3; -.
DR MassIVE; Q7LBE3; -.
DR PaxDb; Q7LBE3; -.
DR PeptideAtlas; Q7LBE3; -.
DR PRIDE; Q7LBE3; -.
DR ProteomicsDB; 68849; -. [Q7LBE3-1]
DR Antibodypedia; 34575; 52 antibodies from 16 providers.
DR DNASU; 115019; -.
DR Ensembl; ENST00000340781.8; ENSP00000341682.4; ENSG00000174502.19. [Q7LBE3-2]
DR Ensembl; ENST00000367134.2; ENSP00000356102.2; ENSG00000174502.19. [Q7LBE3-2]
DR Ensembl; ENST00000367135.8; ENSP00000356103.3; ENSG00000174502.19. [Q7LBE3-1]
DR GeneID; 115019; -.
DR KEGG; hsa:115019; -.
DR MANE-Select; ENST00000367135.8; ENSP00000356103.3; NM_052934.4; NP_443166.1.
DR UCSC; uc001hdp.5; human. [Q7LBE3-1]
DR CTD; 115019; -.
DR DisGeNET; 115019; -.
DR GeneCards; SLC26A9; -.
DR HGNC; HGNC:14469; SLC26A9.
DR HPA; ENSG00000174502; Group enriched (salivary gland, stomach).
DR MIM; 608481; gene.
DR neXtProt; NX_Q7LBE3; -.
DR OpenTargets; ENSG00000174502; -.
DR Orphanet; 586; Cystic fibrosis.
DR PharmGKB; PA37886; -.
DR VEuPathDB; HostDB:ENSG00000174502; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; Q7LBE3; -.
DR OMA; HLPVLSW; -.
DR PhylomeDB; Q7LBE3; -.
DR TreeFam; TF313784; -.
DR PathwayCommons; Q7LBE3; -.
DR Reactome; R-HSA-427601; Multifunctional anion exchangers.
DR SignaLink; Q7LBE3; -.
DR BioGRID-ORCS; 115019; 13 hits in 1074 CRISPR screens.
DR GenomeRNAi; 115019; -.
DR Pharos; Q7LBE3; Tbio.
DR PRO; PR:Q7LBE3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7LBE3; protein.
DR Bgee; ENSG00000174502; Expressed in parotid gland and 108 other tissues.
DR Genevisible; Q7LBE3; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015301; F:anion:anion antiporter activity; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IDA:UniProtKB.
DR GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR030306; SLC26A9.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF17; PTHR11814:SF17; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..791
FT /note="Solute carrier family 26 member 9"
FT /id="PRO_0000324492"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 71..96
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 97..100
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 101..109
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 110..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 130..142
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 143..162
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 163..191
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 192..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 225..237
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT INTRAMEM 238..246
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 247..254
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 276..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 287..299
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 300..334
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 335..358
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 359..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 366..379
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 380..390
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 391..400
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 401..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 406..419
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 420..431
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 432..457
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 458..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 462..476
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 477..479
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TRANSMEM 480..498
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT TOPO_DOM 499..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BU91"
FT DOMAIN 519..737
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 602..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 791
FT /note="L -> LESLSAAGGCYPYRSESLVSPLFTRQALAAMDKPPAHSTPPTSALSL
FT AAEGHLDFQLLRVSQKQKDKYNCAGLLYKLQKVSQSPHGSVSDGVRLSRT (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_054056"
FT VARIANT 70
FT /note="Y -> N (displays higher channel activity and
FT enhanced chloride-bicarbonate ion exchange;
FT dbSNP:rs75021701)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_068683"
FT VARIANT 127
FT /note="T -> N (results in smaller halide currents but not
FT for thiocyanate ion; dbSNP:rs77497889)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_068684"
FT VARIANT 384
FT /note="I -> T (in dbSNP:rs112659452)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_068685"
FT VARIANT 575
FT /note="R -> W (in dbSNP:rs201823199)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_068686"
FT VARIANT 606
FT /note="P -> L (in dbSNP:rs74146719)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_068687"
FT VARIANT 622
FT /note="V -> L (decreased plasma membrane expression which
FT partially accounts for decreased whole cell currents;
FT transport is reduced to about 50%; dbSNP:rs34992672)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_068688"
FT VARIANT 744
FT /note="V -> M (decreased plasma membrane expression which
FT partially accounts for decreased whole cell currents;
FT dbSNP:rs3811428)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_039801"
FT VARIANT 748
FT /note="H -> R (in dbSNP:rs16856462)"
FT /evidence="ECO:0000269|PubMed:22544634"
FT /id="VAR_039802"
FT CONFLICT 64
FT /note="K -> N (in Ref. 5; AAI51209)"
FT /evidence="ECO:0000305"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 67..95
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 162..190
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 253..271
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 334..359
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 365..380
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 406..418
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 419..424
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 432..440
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 451..458
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 478..496
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 543..554
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 677..692
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 696..700
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 704..712
FT /evidence="ECO:0007829|PDB:7CH1"
FT TURN 713..719
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:7CH1"
FT STRAND 726..729
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 730..740
FT /evidence="ECO:0007829|PDB:7CH1"
FT HELIX 774..777
FT /evidence="ECO:0007829|PDB:7CH1"
FT CONFLICT Q7LBE3-2:804
FT /note="R -> G (in Ref. 2; AAL26867 and 4; EAW91587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 791 AA; 86988 MW; DC651F4E8DF2BF77 CRC64;
MSQPRPRYVV DRAAYSLTLF DDEFEKKDRT YPVGEKLRNA FRCSSAKIKA VVFGLLPVLS
WLPKYKIKDY IIPDLLGGLS GGSIQVPQGM AFALLANLPA VNGLYSSFFP LLTYFFLGGV
HQMVPGTFAV ISILVGNICL QLAPESKFQV FNNATNESYV DTAAMEAERL HVSATLACLT
AIIQMGLGFM QFGFVAIYLS ESFIRGFMTA AGLQILISVL KYIFGLTIPS YTGPGSIVFT
FIDICKNLPH TNIASLIFAL ISGAFLVLVK ELNARYMHKI RFPIPTEMIV VVVATAISGG
CKMPKKYHMQ IVGEIQRGFP TPVSPVVSQW KDMIGTAFSL AIVSYVINLA MGRTLANKHG
YDVDSNQEMI ALGCSNFFGS FFKIHVICCA LSVTLAVDGA GGKSQVASLC VSLVVMITML
VLGIYLYPLP KSVLGALIAV NLKNSLKQLT DPYYLWRKSK LDCCIWVVSF LSSFFLSLPY
GVAVGVAFSV LVVVFQTQFR NGYALAQVMD TDIYVNPKTY NRAQDIQGIK IITYCSPLYF
ANSEIFRQKV IAKTGMDPQK VLLAKQKYLK KQEKRRMRPT QQRRSLFMKT KTVSLQELQQ
DFENAPPTDP NNNQTPANGT SVSYITFSPD SSSPAQSEPP ASAEAPGEPS DMLASVPPFV
TFHTLILDMS GVSFVDLMGI KALAKLSSTY GKIGVKVFLV NIHAQVYNDI SHGGVFEDGS
LECKHVFPSI HDAVLFAQAN ARDVTPGHNF QGAPGDAELS LYDSEEDIRS YWDLEQEMFG
SMFHAETLTA L
