XCT_HUMAN
ID XCT_HUMAN Reviewed; 501 AA.
AC Q9UPY5; A8K2U4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Cystine/glutamate transporter;
DE AltName: Full=Amino acid transport system xc-;
DE AltName: Full=Calcium channel blocker resistance protein CCBR1;
DE AltName: Full=Solute carrier family 7 member 11;
DE AltName: Full=xCT;
GN Name=SLC7A11;
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].
RX PubMed=11213471; DOI=10.1089/ars.2000.2.4-665;
RA Sato H., Tamba M., Kuriyama-Matsumura K., Okuno S., Bannai S.;
RT "Molecular cloning and expression of human xCT, the light chain of amino
RT acid transport system xc-.";
RL Antioxid. Redox Signal. 2:665-671(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Conklin D.S., Beach D.H.;
RT "CCBR1, novel CD98 light chain implicated in redox control and calcium
RT signaling.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=11133847;
RA Bridges C.C., Kekuda R., Wang H., Prasad P.D., Mehta P., Huang W.,
RA Smith S.B., Ganapathy V.;
RT "Structure, function, and regulation of human cystine/glutamate transporter
RT in retinal pigment epithelial cells.";
RL Invest. Ophthalmol. Vis. Sci. 42:47-54(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Borsani G., Manzoni M., Palacin M., Pineda M., Gasol E.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [8]
RP FUNCTION, MEMBRANE TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=15151999; DOI=10.1074/jbc.m402428200;
RA Gasol E., Jimenez-Vidal M., Chillaron J., Zorzano A., Palacin M.;
RT "Membrane topology of system xc- light subunit reveals a re-entrant loop
RT with substrate-restricted accessibility.";
RL J. Biol. Chem. 279:31228-31236(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Sodium-independent, high-affinity exchange of anionic amino
CC acids with high specificity for anionic form of cystine and glutamate.
CC {ECO:0000269|PubMed:15151999}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UPY5; P16070: CD44; NbExp=4; IntAct=EBI-3843348, EBI-490245;
CC Q9UPY5; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-3843348, EBI-11959885;
CC Q9UPY5; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-3843348, EBI-11749135;
CC Q9UPY5; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-3843348, EBI-12832276;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15151999}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:15151999}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
CC {ECO:0000305}.
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DR EMBL; AB026891; BAA82628.1; -; mRNA.
DR EMBL; AF200708; AAG35592.1; -; mRNA.
DR EMBL; AF252872; AAK49111.1; -; mRNA.
DR EMBL; AJ277882; CAC81905.1; -; mRNA.
DR EMBL; AK290359; BAF83048.1; -; mRNA.
DR EMBL; AK314855; BAG37372.1; -; mRNA.
DR EMBL; CH471056; EAX05135.1; -; Genomic_DNA.
DR EMBL; BC012087; AAH12087.1; -; mRNA.
DR CCDS; CCDS3742.1; -.
DR RefSeq; NP_055146.1; NM_014331.3.
DR PDB; 7CCS; EM; 6.20 A; B=1-501.
DR PDB; 7EPZ; EM; 3.40 A; B=2-501.
DR PDB; 7P9U; EM; 3.70 A; B=2-501.
DR PDB; 7P9V; EM; 3.40 A; B=2-501.
DR PDBsum; 7CCS; -.
DR PDBsum; 7EPZ; -.
DR PDBsum; 7P9U; -.
DR PDBsum; 7P9V; -.
DR AlphaFoldDB; Q9UPY5; -.
DR SMR; Q9UPY5; -.
DR BioGRID; 117179; 132.
DR IntAct; Q9UPY5; 14.
DR MINT; Q9UPY5; -.
DR STRING; 9606.ENSP00000280612; -.
DR BindingDB; Q9UPY5; -.
DR ChEMBL; CHEMBL1075149; -.
DR DrugBank; DB06151; Acetylcysteine.
DR DrugBank; DB05540; Alanosine.
DR DrugBank; DB00138; Cystine.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00740; Riluzole.
DR DrugBank; DB01098; Rosuvastatin.
DR DrugBank; DB00795; Sulfasalazine.
DR DrugBank; DB08833; Taurochenodeoxycholic acid.
DR DrugBank; DB04348; Taurocholic acid.
DR DrugBank; DB08834; Tauroursodeoxycholic acid.
DR DrugBank; DB11590; Thimerosal.
DR DrugCentral; Q9UPY5; -.
DR GuidetoPHARMACOLOGY; 902; -.
DR TCDB; 2.A.3.8.18; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; Q9UPY5; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPY5; -.
DR PhosphoSitePlus; Q9UPY5; -.
DR SwissPalm; Q9UPY5; -.
DR BioMuta; SLC7A11; -.
DR DMDM; 12585385; -.
DR EPD; Q9UPY5; -.
DR jPOST; Q9UPY5; -.
DR MassIVE; Q9UPY5; -.
DR MaxQB; Q9UPY5; -.
DR PaxDb; Q9UPY5; -.
DR PeptideAtlas; Q9UPY5; -.
DR PRIDE; Q9UPY5; -.
DR ProteomicsDB; 85473; -.
DR Antibodypedia; 16136; 341 antibodies from 37 providers.
DR DNASU; 23657; -.
DR Ensembl; ENST00000280612.9; ENSP00000280612.5; ENSG00000151012.13.
DR GeneID; 23657; -.
DR KEGG; hsa:23657; -.
DR MANE-Select; ENST00000280612.9; ENSP00000280612.5; NM_014331.4; NP_055146.1.
DR UCSC; uc062zqn.1; human.
DR CTD; 23657; -.
DR DisGeNET; 23657; -.
DR GeneCards; SLC7A11; -.
DR HGNC; HGNC:11059; SLC7A11.
DR HPA; ENSG00000151012; Tissue enhanced (brain).
DR MIM; 607933; gene.
DR neXtProt; NX_Q9UPY5; -.
DR OpenTargets; ENSG00000151012; -.
DR PharmGKB; PA35919; -.
DR VEuPathDB; HostDB:ENSG00000151012; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000160324; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; Q9UPY5; -.
DR OMA; PHWVWVL; -.
DR OrthoDB; 621852at2759; -.
DR PhylomeDB; Q9UPY5; -.
DR TreeFam; TF313355; -.
DR BioCyc; MetaCyc:ENSG00000151012-MON; -.
DR PathwayCommons; Q9UPY5; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; Q9UPY5; -.
DR BioGRID-ORCS; 23657; 22 hits in 1100 CRISPR screens.
DR ChiTaRS; SLC7A11; human.
DR GeneWiki; SLC7A11; -.
DR GenomeRNAi; 23657; -.
DR Pharos; Q9UPY5; Tchem.
DR PRO; PR:Q9UPY5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UPY5; protein.
DR Bgee; ENSG00000151012; Expressed in cranial nerve II and 177 other tissues.
DR ExpressionAtlas; Q9UPY5; baseline and differential.
DR Genevisible; Q9UPY5; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0097449; C:astrocyte projection; IEA:Ensembl.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0015327; F:cystine:glutamate antiporter activity; TAS:ProtInc.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; IEA:Ensembl.
DR GO; GO:0090461; P:glutamate homeostasis; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR GO; GO:0034775; P:glutathione transmembrane transport; IEA:Ensembl.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IEA:Ensembl.
DR GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR GO; GO:1904717; P:regulation of AMPA glutamate receptor clustering; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:1901494; P:regulation of cysteine metabolic process; IEA:Ensembl.
DR GO; GO:2000211; P:regulation of glutamate metabolic process; IEA:Ensembl.
DR GO; GO:1903786; P:regulation of glutathione biosynthetic process; IEA:Ensembl.
DR GO; GO:0048021; P:regulation of melanin biosynthetic process; IEA:Ensembl.
DR GO; GO:0033029; P:regulation of neutrophil apoptotic process; IEA:Ensembl.
DR GO; GO:0051223; P:regulation of protein transport; IEA:Ensembl.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0051775; P:response to redox state; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004760; L_AA_transporter.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00911; 2A0308; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..501
FT /note="Cystine/glutamate transporter"
FT /id="PRO_0000054279"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 77..104
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 134..151
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:7P9V"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 162..182
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 185..210
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 211..216
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 220..225
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:7P9V"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 262..270
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 271..291
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 315..331
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:7P9V"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 385..401
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:7P9V"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:7P9V"
FT TURN 474..477
FT /evidence="ECO:0007829|PDB:7P9V"
FT HELIX 478..491
FT /evidence="ECO:0007829|PDB:7P9V"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:7P9V"
SQ SEQUENCE 501 AA; 55423 MW; 3EF2648B94A9F59E CRC64;
MVRKPVVSTI SKGGYLQGNV NGRLPSLGNK EPPGQEKVQL KRKVTLLRGV SIIIGTIIGA
GIFISPKGVL QNTGSVGMSL TIWTVCGVLS LFGALSYAEL GTTIKKSGGH YTYILEVFGP
LPAFVRVWVE LLIIRPAATA VISLAFGRYI LEPFFIQCEI PELAIKLITA VGITVVMVLN
SMSVSWSARI QIFLTFCKLT AILIIIVPGV MQLIKGQTQN FKDAFSGRDS SITRLPLAFY
YGMYAYAGWF YLNFVTEEVE NPEKTIPLAI CISMAIVTIG YVLTNVAYFT TINAEELLLS
NAVAVTFSER LLGNFSLAVP IFVALSCFGS MNGGVFAVSR LFYVASREGH LPEILSMIHV
RKHTPLPAVI VLHPLTMIML FSGDLDSLLN FLSFARWLFI GLAVAGLIYL RYKCPDMHRP
FKVPLFIPAL FSFTCLFMVA LSLYSDPFST GIGFVITLTG VPAYYLFIIW DKKPRWFRIM
SEKITRTLQI ILEVVPEEDK L
