ID   GTR7_HUMAN              Reviewed;         512 AA.
AC   Q6PXP3; A2A333;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   02-SEP-2026, entry version 163.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 7 {ECO:0000305};
DE   AltName: Full=Glucose transporter type 7 {ECO:0000303|PubMed:15033637};
DE            Short=GLUT-7 {ECO:0000303|PubMed:15033637};
DE            Short=hGLUT7 {ECO:0000303|PubMed:16186102};
GN   Name=SLC2A7 {ECO:0000303|PubMed:15033637,
GN   ECO:0000312|HGNC:HGNC:13445};
GN   Synonyms=GLUT7 {ECO:0000303|PubMed:15033637};
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=15033637; DOI=10.1152/ajpgi.00396.2003;
RA   Li Q., Manolescu A.R., Ritzel M., Yao S., Slugoski M., Young J.D.,
RA   Chen X.-Z., Cheeseman C.I.;
RT   "Cloning and functional characterization of the human GLUT7 isoform SLC2A7
RT   from the small intestine.";
RL   Am. J. Physiol. 287:G236-G242(2004).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-302.
RX   PubMed=16186102; DOI=10.1074/jbc.m508678200;
RA   Manolescu A., Salas-Burgos A.M., Fischbarg J., Cheeseman C.I.;
RT   "Identification of a hydrophobic residue as a key determinant of fructose
RT   transport by the facilitative hexose transporter SLC2A7 (GLUT7).";
RL   J. Biol. Chem. 280:42978-42983(2005).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=28083649; DOI=10.1007/s00232-016-9945-7;
RA   Ebert K., Ludwig M., Geillinger K.E., Schoberth G.C., Essenwanger J.,
RA   Stolz J., Daniel H., Witt H.;
RT   "Reassessment of GLUT7 and GLUT9 as putative fructose and glucose
RT   transporters.";
RL   J. Membr. Biol. 250:171-182(2017).
RN   [6]
RP   SUBCELLULAR LOCATION, FUNCTION, ACTIVITY REGULATION, AND INDUCTION BY
RP   FRUCTOSE.
RX   PubMed=29548810; DOI=10.1016/j.bcp.2018.03.011;
RA   Gauer J.S., Tumova S., Lippiat J.D., Kerimi A., Williamson G.;
RT   "Differential patterns of inhibition of the sugar transporters GLUT2, GLUT5
RT   and GLUT7 by flavonoids.";
RL   Biochem. Pharmacol. 152:11-20(2018).
CC   -!- FUNCTION: Probable sugar transporter (PubMed:28083649). Even if its
CC       physiological substrate is subject to discussion, it is able to
CC       transport glucose and fructose (PubMed:16186102, PubMed:28083649,
CC       PubMed:29548810). Does not transport galactose, 2-deoxy-d-glucose and
CC       xylose (PubMed:15033637). {ECO:0000269|PubMed:15033637,
CC       ECO:0000269|PubMed:16186102, ECO:0000269|PubMed:28083649,
CC       ECO:0000269|PubMed:29548810}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC         ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:16186102,
CC         ECO:0000269|PubMed:29548810};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC         ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:16186102,
CC         ECO:0000269|PubMed:29548810};
CC   -!- ACTIVITY REGULATION: Glucose and fructose transport are inhibited by
CC       the flavonoid apigenin. {ECO:0000269|PubMed:29548810}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=300 uM for glucose {ECO:0000269|PubMed:15033637};
CC   -!- INTERACTION:
CC       Q6PXP3; Q02410: APBA1; NbExp=2; IntAct=EBI-54689289, EBI-368690;
CC       Q6PXP3; Q99767: APBA2; NbExp=2; IntAct=EBI-54689289, EBI-81711;
CC       Q6PXP3; Q12959: DLG1; NbExp=3; IntAct=EBI-54689289, EBI-357481;
CC       Q6PXP3; Q92796: DLG3; NbExp=3; IntAct=EBI-54689289, EBI-80440;
CC       Q6PXP3; P78352: DLG4; NbExp=3; IntAct=EBI-54689289, EBI-80389;
CC       Q6PXP3; Q68DX3: FRMPD2; NbExp=3; IntAct=EBI-54689289, EBI-53993476;
CC       Q6PXP3; A4D2P6: GRID2IP; NbExp=2; IntAct=EBI-54689289, EBI-15893226;
CC       Q6PXP3; Q9Y3R0: GRIP1; NbExp=5; IntAct=EBI-54689289, EBI-5349621;
CC       Q6PXP3; Q9C0E4: GRIP2; NbExp=5; IntAct=EBI-54689289, EBI-949557;
CC       Q6PXP3; Q14005: IL16; NbExp=3; IntAct=EBI-54689289, EBI-2831580;
CC       Q6PXP3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-54689289, EBI-739832;
CC       Q6PXP3; Q8N448: LNX2; NbExp=2; IntAct=EBI-54689289, EBI-2340947;
CC       Q6PXP3; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-54689289, EBI-924464;
CC       Q6PXP3; Q86UL8: MAGI2; NbExp=4; IntAct=EBI-54689289, EBI-311035;
CC       Q6PXP3; O75970: MPDZ; NbExp=3; IntAct=EBI-54689289, EBI-821405;
CC       Q6PXP3; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-54689289, EBI-8744528;
CC       Q6PXP3; Q8NI35: PATJ; NbExp=9; IntAct=EBI-54689289, EBI-724390;
CC       Q6PXP3; Q5T2W1: PDZK1; NbExp=3; IntAct=EBI-54689289, EBI-349819;
CC       Q6PXP3; Q14160: SCRIB; NbExp=3; IntAct=EBI-54689289, EBI-357345;
CC       Q6PXP3; Q07157: TJP1; NbExp=2; IntAct=EBI-54689289, EBI-79553;
CC       Q6PXP3; Q9P202: WHRN; NbExp=2; IntAct=EBI-54689289, EBI-310886;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16186102,
CC       ECO:0000269|PubMed:28083649}; Multi-pass membrane protein
CC       {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:29548810};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in small intestine and colon
CC       (PubMed:15033637). Weakly expressed in testis and prostate
CC       (PubMed:15033637). {ECO:0000269|PubMed:15033637}.
CC   -!- INDUCTION: Expression is increased in presence of fructose.
CC       {ECO:0000269|PubMed:29548810}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: According to some reports, mediates transmembrane transport of
CC       glucose and fructose (PubMed:15033637, PubMed:16186102,
CC       PubMed:29548810). However, another group could not confirm transporter
CC       activity for glucose or fructose (PubMed:28083649).
CC       {ECO:0000269|PubMed:15033637, ECO:0000269|PubMed:16186102,
CC       ECO:0000269|PubMed:28083649, ECO:0000269|PubMed:29548810}.
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DR   EMBL; AY571960; AAS78590.2; -; mRNA.
DR   EMBL; AL158048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471130; EAW71607.1; -; Genomic_DNA.
DR   CCDS; CCDS98.2; -.
DR   RefSeq; NP_997303.2; NM_207420.3.
DR   PDB; 9J2N; EM; 3.30 A; A=1-512.
DR   AlphaFoldDB; Q6PXP3; -.
DR   EMDB; EMD-61099; -.
DR   SMR; Q6PXP3; -.
DR   BioGRID; 127578; 106.
DR   FunCoup; Q6PXP3; 61.
DR   IntAct; Q6PXP3; 171.
DR   NDEx; IQUERY-CP-SLC2A7; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000383698; -.
DR   DrugBank; DB01914; D-glucose.
DR   DrugBank; DB09341; Dextrose, unspecified form.
DR   DrugBank; DB09502; Fludeoxyglucose (18F).
DR   TCDB; 2.A.1.1.37; the major facilitator superfamily (mfs).
DR   GlyCosmos; Q6PXP3; 1 site, No reported glycans.
DR   GlyGen; Q6PXP3; 2 sites.
DR   iPTMnet; Q6PXP3; -.
DR   BioMuta; SLC2A7; -.
DR   DMDM; 167008866; -.
DR   jPOST; Q6PXP3; -.
DR   MassIVE; Q6PXP3; -.
DR   PaxDb; 9606-ENSP00000383698; -.
DR   PeptideAtlas; Q6PXP3; -.
DR   ProteomicsDB; 67261; -.
DR   Antibodypedia; 49274; 16 antibodies from 8 providers.
DR   DNASU; 155184; -.
DR   Ensembl; ENST00000400906.2; ENSP00000383698.1; ENSG00000197241.4.
DR   GeneID; 155184; -.
DR   KEGG; hsa:155184; -.
DR   MANE-Select; ENST00000400906.2; ENSP00000383698.1; NM_207420.3; NP_997303.2.
DR   UCSC; uc009vmo.1; human.
DR   AGR; HGNC:13445; -.
DR   ClinPGx; PA37770; -.
DR   CTD; 155184; -.
DR   DisGeNET; 155184; -.
DR   GeneCards; SLC2A7; -.
DR   HGNC; HGNC:13445; SLC2A7.
DR   HPA; ENSG00000197241; Tissue enriched (intestine).
DR   MIM; 610371; gene.
DR   VEuPathDB; HostDB:ENSG00000197241; -.
DR   eggNOG; KOG0569; Eukaryota.
DR   GeneTree; ENSGT00940000162742; -.
DR   HOGENOM; CLU_001265_30_11_1; -.
DR   InParanoid; Q6PXP3; -.
DR   OMA; TEVFVII; -.
DR   OrthoDB; 4540492at2759; -.
DR   PAN-GO; Q6PXP3; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6PXP3; -.
DR   PathwayCommons; Q6PXP3; -.
DR   Reactome; R-HSA-189200; Cellular hexose transport.
DR   BioGRID-ORCS; 155184; 11 hits in 1137 CRISPR screens.
DR   ChiTaRS; SLC2A7; human.
DR   GeneWiki; SLC2A7; -.
DR   GenomeRNAi; 155184; -.
DR   Pharos; Q6PXP3; Tdark.
DR   PRO; PR:Q6PXP3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q6PXP3; protein.
DR   Bgee; ENSG00000197241; Expressed in duodenum and 3 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; EXP:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0051119; F:sugar transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:1904659; P:D-glucose transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0070837; P:dehydroascorbic acid transport; IBA:GO_Central.
DR   GO; GO:0015755; P:fructose transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0008645; P:hexose transmembrane transport; TAS:Reactome.
DR   CDD; cd17432; MFS_GLUT_Class2; 1.
DR   FunFam; 1.20.1250.20:FF:000029; solute carrier family 2, facilitated glucose transporter member 4; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR045263; GLUT.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   NCBIfam; TIGR00879; SP; 1.
DR   PANTHER; PTHR23503; SOLUTE CARRIER FAMILY 2; 1.
DR   PANTHER; PTHR23503:SF30; SOLUTE CARRIER FAMILY 2, FACILITATED GLUCOSE TRANSPORTER MEMBER 7; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
DR   PDBsum; 9J2N; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Glycoprotein; Membrane;
KW   Proteomics identification; Reference proteome; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..512
FT                   /note="Solute carrier family 2, facilitated glucose
FT                   transporter member 7"
FT                   /id="PRO_0000317274"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..138
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..321
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        437..445
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        467..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          491..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         294..295
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:P11169"
FT   BINDING         300
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:P11169"
FT   BINDING         331
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /evidence="ECO:0000250|UniProtKB:P11169"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         135
FT                   /note="V -> I (in dbSNP:rs34545462)"
FT                   /id="VAR_052504"
FT   VARIANT         261
FT                   /note="R -> Q (in dbSNP:rs12402973)"
FT                   /id="VAR_061879"
FT   MUTAGEN         302
FT                   /note="I->S: Does not affect glucose or fructose
FT                   transport."
FT                   /evidence="ECO:0000269|PubMed:16186102"
FT   MUTAGEN         302
FT                   /note="I->V: Abolished fructose transport."
FT                   /evidence="ECO:0000269|PubMed:16186102"
FT   HELIX           21..42
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           49..64
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           70..92
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           95..111
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           113..123
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   TURN            124..129
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           132..159
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           165..186
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   TURN            189..192
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   TURN            195..197
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           198..203
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           207..215
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           216..218
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           225..230
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           233..243
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           250..266
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   TURN            272..276
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           281..295
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           299..312
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           320..345
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           347..370
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   TURN            371..374
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           376..378
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           379..395
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   TURN            396..398
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           399..407
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           414..433
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           436..443
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           447..464
FT                   /evidence="ECO:0007829|PDB:9J2N"
FT   HELIX           474..484
FT                   /evidence="ECO:0007829|PDB:9J2N"
SQ   SEQUENCE   512 AA;  55728 MW;  DCA09E35AB720382 CRC64;
     MENKEAGTPP PIPSREGRLQ PTLLLATLSA AFGSAFQYGY NLSVVNTPHK VFKSFYNETY
     FERHATFMDG KLMLLLWSCT VSMFPLGGLL GSLLVGLLVD SCGRKGTLLI NNIFAIIPAI
     LMGVSKVAKA FELIVFSRVV LGVCAGISYS ALPMYLGELA PKNLRGMVGT MTEVFVIVGV
     FLAQIFSLQA ILGNPAGWPV LLALTGVPAL LQLLTLPFFP ESPRYSLIQK GDEATARQAL
     RRLRGHTDME AELEDMRAEA RAERAEGHLS VLHLCALRSL RWQLLSIIVL MAGQQLSGIN
     AINYYADTIY TSAGVEAAHS QYVTVGSGVV NIVMTITSAV LVERLGRRHL LLAGYGICGS
     ACLVLTVVLL FQNRVPELSY LGIICVFAYI AGHSIGPSPV PSVVRTEIFL QSSRRAAFMV
     DGAVHWLTNF IIGFLFPSIQ EAIGAYSFII FAGICLLTAI YIYVVIPETK GKTFVEINRI
     FAKRNRVKLP EEKEETIDAG PPTASPAKET SF
//