S1PR3_HUMAN
ID S1PR3_HUMAN Reviewed; 378 AA.
AC Q99500; Q5SQD8; Q7Z5I2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Sphingosine 1-phosphate receptor 3;
DE Short=S1P receptor 3;
DE Short=S1P3;
DE AltName: Full=Endothelial differentiation G-protein coupled receptor 3;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-3;
DE Short=S1P receptor Edg-3;
GN Name=S1PR3 {ECO:0000312|HGNC:HGNC:3167};
GN Synonyms=C9orf108 {ECO:0000312|HGNC:HGNC:3167},
GN C9orf47 {ECO:0000312|HGNC:HGNC:3167}, EDG3 {ECO:0000312|HGNC:HGNC:3167};
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 [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8878560; DOI=10.1006/bbrc.1996.1553;
RA Yamaguchi F., Tokuda M., Hatase O., Brenner S.;
RT "Molecular cloning of the novel human G protein-coupled receptor (GPCR)
RT gene mapped on chromosome 9.";
RL Biochem. Biophys. Res. Commun. 227:608-614(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9409733; DOI=10.1016/s0014-5793(97)01301-x;
RA An S., Bleu T., Huang W., Hallmark O.G., Coughlin S.R., Goetzl E.J.;
RT "Identification of cDNAs encoding two G protein-coupled receptors for
RT lysosphingolipids.";
RL FEBS Lett. 417:279-282(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 PHARMACOLOGICAL CHARACTERIZATION.
RX PubMed=10383399; DOI=10.1074/jbc.274.27.18997;
RA Ancellin N., Hla T.;
RT "Differential pharmacological properties and signal transduction of the
RT sphingosine 1-phosphate receptors EDG-1, EDG-3, and EDG-5.";
RL J. Biol. Chem. 274:18997-19002(1999).
RN [9]
RP FUNCTION.
RX PubMed=10617617; DOI=10.1074/jbc.275.1.288;
RA An S., Zheng Y., Bleu T.;
RT "Sphingosine 1-phosphate-induced cell proliferation, survival, and related
RT signaling events mediated by G protein-coupled receptors Edg3 and Edg5.";
RL J. Biol. Chem. 275:288-296(2000).
RN [10]
RP SPHINGOSINE 1-PHOSPHATE ACTIVATION.
RX PubMed=10908314; DOI=10.1124/mol.58.2.449;
RA Himmel H.M., Meyer Zu Heringdorf D., Graf E., Dobrev D., Kortner A.,
RA Schueler S., Jakobs K.H., Ravens U.;
RT "Evidence for Edg-3 receptor-mediated activation of I(K.ACh) by
RT sphingosine-1-phosphate in human atrial cardiomyocytes.";
RL Mol. Pharmacol. 58:449-454(2000).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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: Receptor for the lysosphingolipid sphingosine 1-phosphate
CC (S1P). S1P is a bioactive lysophospholipid that elicits diverse
CC physiological effect on most types of cells and tissues. When expressed
CC in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell
CC proliferation and suppression of apoptosis.
CC {ECO:0000269|PubMed:10617617}.
CC -!- INTERACTION:
CC Q99500; P21964: COMT; NbExp=3; IntAct=EBI-10634734, EBI-372265;
CC Q99500; P06028: GYPB; NbExp=3; IntAct=EBI-10634734, EBI-10194756;
CC Q99500; P16144: ITGB4; NbExp=3; IntAct=EBI-10634734, EBI-948678;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues, but most abundantly in
CC heart, placenta, kidney, and liver.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X83864; CAA58744.1; -; Genomic_DNA.
DR EMBL; AF022139; AAC51906.1; -; mRNA.
DR EMBL; AY322540; AAP84353.1; -; Genomic_DNA.
DR EMBL; AK312798; BAG35658.1; -; mRNA.
DR EMBL; AL772202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62758.1; -; Genomic_DNA.
DR EMBL; BC060827; AAH60827.1; -; mRNA.
DR EMBL; BC069579; AAH69579.1; -; mRNA.
DR CCDS; CCDS6680.1; -.
DR PIR; JC5245; JC5245.
DR RefSeq; NP_005217.2; NM_005226.3.
DR PDB; 7C4S; X-ray; 3.20 A; A/B=1-378.
DR PDB; 7EW2; EM; 3.10 A; R=1-378.
DR PDB; 7EW3; EM; 3.10 A; R=1-378.
DR PDB; 7EW4; EM; 3.20 A; R=1-378.
DR PDBsum; 7C4S; -.
DR PDBsum; 7EW2; -.
DR PDBsum; 7EW3; -.
DR PDBsum; 7EW4; -.
DR AlphaFoldDB; Q99500; -.
DR SMR; Q99500; -.
DR BioGRID; 108227; 40.
DR CORUM; Q99500; -.
DR IntAct; Q99500; 10.
DR MINT; Q99500; -.
DR STRING; 9606.ENSP00000365006; -.
DR BindingDB; Q99500; -.
DR ChEMBL; CHEMBL3892; -.
DR DrugBank; DB08868; Fingolimod.
DR DrugCentral; Q99500; -.
DR GuidetoPHARMACOLOGY; 277; -.
DR GlyGen; Q99500; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q99500; -.
DR PhosphoSitePlus; Q99500; -.
DR BioMuta; S1PR3; -.
DR DMDM; 42560554; -.
DR MassIVE; Q99500; -.
DR MaxQB; Q99500; -.
DR PaxDb; Q99500; -.
DR PeptideAtlas; Q99500; -.
DR PRIDE; Q99500; -.
DR ProteomicsDB; 78299; -.
DR ABCD; Q99500; 1 sequenced antibody.
DR Antibodypedia; 13485; 548 antibodies from 37 providers.
DR DNASU; 1903; -.
DR Ensembl; ENST00000358157.3; ENSP00000350878.2; ENSG00000213694.6.
DR Ensembl; ENST00000375846.3; ENSP00000365006.3; ENSG00000213694.6.
DR GeneID; 1903; -.
DR KEGG; hsa:1903; -.
DR MANE-Select; ENST00000358157.3; ENSP00000350878.2; NM_005226.4; NP_005217.2.
DR UCSC; uc004aqe.5; human.
DR CTD; 1903; -.
DR DisGeNET; 1903; -.
DR GeneCards; S1PR3; -.
DR HGNC; HGNC:3167; S1PR3.
DR HPA; ENSG00000213694; Low tissue specificity.
DR MIM; 601965; gene.
DR neXtProt; NX_Q99500; -.
DR OpenTargets; ENSG00000213694; -.
DR PharmGKB; PA162402362; -.
DR VEuPathDB; HostDB:ENSG00000213694; -.
DR eggNOG; ENOG502R61K; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; Q99500; -.
DR OMA; DVACRVK; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; Q99500; -.
DR TreeFam; TF330052; -.
DR PathwayCommons; Q99500; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-419408; Lysosphingolipid and LPA receptors.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR SignaLink; Q99500; -.
DR SIGNOR; Q99500; -.
DR BioGRID-ORCS; 1903; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; S1PR3; human.
DR GeneWiki; S1PR3; -.
DR GenomeRNAi; 1903; -.
DR Pharos; Q99500; Tclin.
DR PRO; PR:Q99500; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q99500; protein.
DR Bgee; ENSG00000213694; Expressed in left ventricle myocardium and 172 other tissues.
DR ExpressionAtlas; Q99500; baseline and differential.
DR Genevisible; Q99500; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0008289; F:lipid binding; TAS:ProtInc.
DR GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:1903141; P:negative regulation of establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR004062; EDG3_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004061; S1P_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01524; EDG3RECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01523; S1PRECEPTOR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="Sphingosine 1-phosphate receptor 3"
FT /id="PRO_0000069421"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 41..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 66..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 102..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 135..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 154..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 180..195
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 196..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 217..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 244..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 266..281
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 282..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 303..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 327..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 243
FT /note="R -> Q (in dbSNP:rs34075341)"
FT /id="VAR_033465"
FT CONFLICT 359
FT /note="A -> D (in Ref. 1; CAA58744 and 2; AAC51906)"
FT /evidence="ECO:0000305"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:7EW2"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 41..66
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 74..99
FT /evidence="ECO:0007829|PDB:7EW2"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 108..139
FT /evidence="ECO:0007829|PDB:7EW2"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:7C4S"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:7EW2"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:7EW4"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7EW2"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 194..228
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 232..268
FT /evidence="ECO:0007829|PDB:7EW2"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:7EW2"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:7EW2"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:7EW2"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:7EW3"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:7EW2"
SQ SEQUENCE 378 AA; 42250 MW; 79A00300968F439F CRC64;
MATALPPRLQ PVRGNETLRE HYQYVGKLAG RLKEASEGST LTTVLFLVIC SFIVLENLMV
LIAIWKNNKF HNRMYFFIGN LALCDLLAGI AYKVNILMSG KKTFSLSPTV WFLREGSMFV
ALGASTCSLL AIAIERHLTM IKMRPYDANK RHRVFLLIGM CWLIAFTLGA LPILGWNCLH
NLPDCSTILP LYSKKYIAFC ISIFTAILVT IVILYARIYF LVKSSSRKVA NHNNSERSMA
LLRTVVIVVS VFIACWSPLF ILFLIDVACR VQACPILFKA QWFIVLAVLN SAMNPVIYTL
ASKEMRRAFF RLVCNCLVRG RGARASPIQP ALDPSRSKSS SSNNSSHSPK VKEDLPHTAP
SSCIMDKNAA LQNGIFCN
