SPIKE_CVH22
ID SPIKE_CVH22 Reviewed; 1173 AA.
AC P15423; P89342; P89343; P89344; Q66174; Q990M1; Q990M2; Q990M3; Q990M4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04200};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04200};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04200}; ORFNames=2;
OS Human coronavirus 229E (HCoV-229E).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Duvinacovirus.
OX NCBI_TaxID=11137;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2345367; DOI=10.1099/0022-1317-71-5-1065;
RA Raabe T., Schelle-Prinz B., Siddell S.G.;
RT "Nucleotide sequence of the gene encoding the spike glycoprotein of human
RT coronavirus HCV 229E.";
RL J. Gen. Virol. 71:1065-1073(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11369870; DOI=10.1099/0022-1317-82-6-1273;
RA Thiel V., Herold J., Schelle B., Siddell S.G.;
RT "Infectious RNA transcribed in vitro from a cDNA copy of the human
RT coronavirus genome cloned in vaccinia virus.";
RL J. Gen. Virol. 82:1273-1281(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-1113, AND VARIANTS.
RC STRAIN=Isolate P100E, Isolate P11A, Isolate P11B, and Isolate RW Stock;
RA Bonavia A., Holmes K.V.;
RT "Viral and cellular changes in a human cell line persistently infected with
RT human coronavirus HCoV-229E.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-1113, AND VARIANTS.
RC STRAIN=Isolate A162, Isolate ATCC VR-740, and Isolate LRI 281;
RX PubMed=9870593; DOI=10.1016/s0166-0934(98)00116-5;
RA Hays J.P., Myint S.H.;
RT "PCR sequencing of the spike genes of geographically and chronologically
RT distinct human coronaviruses 229E.";
RL J. Virol. Methods 75:179-193(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1159-1173.
RX PubMed=2701946; DOI=10.1093/nar/17.15.6387;
RA Raabe T., Siddell S.G.;
RT "Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 and mRNA 5
RT unique regions.";
RL Nucleic Acids Res. 17:6387-6387(1989).
RN [6]
RP FUNCTION, AND INTERACTION WITH HUMAN ANPEP.
RX PubMed=1350662; DOI=10.1038/357420a0;
RA Yeager C.L., Ashmun R.A., Williams R.K., Cardellichio C.B., Shapiro L.H.,
RA Look A.T., Holmes K.V.;
RT "Human aminopeptidase N is a receptor for human coronavirus 229E.";
RL Nature 357:420-422(1992).
RN [7]
RP FUNCTION, AND INTERACTION WITH FELINE ANPEP.
RX PubMed=8970993; DOI=10.1128/jvi.70.12.8669-8674.1996;
RA Tresnan D.B., Levis R., Holmes K.V.;
RT "Feline aminopeptidase N serves as a receptor for feline, canine, porcine,
RT and human coronaviruses in serogroup I.";
RL J. Virol. 70:8669-8674(1996).
RN [8]
RP FUNCTION, INTERACTION WITH HUMAN ANPEP, AND RECEPTOR-BINDING DOMAIN.
RX PubMed=12551991; DOI=10.1128/jvi.77.4.2530-2538.2003;
RA Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.;
RT "Identification of a receptor-binding domain of the spike glycoprotein of
RT human coronavirus HCoV-229E.";
RL J. Virol. 77:2530-2538(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH HUMAN ANPEP.
RX PubMed=12634402; DOI=10.1128/jvi.77.7.4435-4438.2003;
RA Breslin J.J., Mork I., Smith M.K., Vogel L.K., Hemmila E.M., Bonavia A.,
RA Talbot P.J., Sjoestrom H., Noren O., Holmes K.V.;
RT "Human coronavirus 229E: receptor binding domain and neutralization by
RT soluble receptor at 37 degrees C.";
RL J. Virol. 77:4435-4438(2003).
RN [10]
RP REVIEW.
RX PubMed=11162792; DOI=10.1006/viro.2000.0757;
RA Gallagher T.M., Buchmeier M.J.;
RT "Coronavirus spike proteins in viral entry and pathogenesis.";
RL Virology 279:371-374(2001).
CC -!- FUNCTION: S1 region attaches the virion to the cell membrane by
CC interacting with host ANPEP/aminopeptidase N, initiating the infection.
CC Binding to the receptor probably induces conformational changes in the
CC S glycoprotein unmasking the fusion peptide of S2 region and activating
CC membranes fusion. S2 region belongs to the class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC regions assume a trimer-of-hairpins structure, positioning the fusion
CC peptide in close proximity to the C-terminal region of the ectodomain.
CC The formation of this structure appears to drive apposition and
CC subsequent fusion of viral and target cell membranes.
CC {ECO:0000255|HAMAP-Rule:MF_04200, ECO:0000269|PubMed:12551991,
CC ECO:0000269|PubMed:12634402, ECO:0000269|PubMed:1350662,
CC ECO:0000269|PubMed:8970993}.
CC -!- SUBUNIT: Homotrimer. During virus morphogenesis, found in a complex
CC with M and HE proteins. Interacts with host ANPEP. {ECO:0000255|HAMAP-
CC Rule:MF_04200, ECO:0000269|PubMed:12551991,
CC ECO:0000269|PubMed:12634402, ECO:0000269|PubMed:1350662,
CC ECO:0000269|PubMed:8970993}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04200}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04200}. Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04200}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04200}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval signal.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- SIMILARITY: Belongs to the alphacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- CAUTION: In contrast to beta- and gammacoronaviruses, S glycoprotein is
CC not cleaved into S1 and S2. {ECO:0000255|HAMAP-Rule:MF_04200}.
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DR EMBL; X16816; CAA34723.1; -; Genomic_RNA.
DR EMBL; AF304460; AAG48592.1; -; Genomic_RNA.
DR EMBL; AF344186; AAK32188.1; -; Genomic_RNA.
DR EMBL; AF344187; AAK32189.1; -; Genomic_RNA.
DR EMBL; AF344188; AAK32190.1; -; Genomic_RNA.
DR EMBL; AF344189; AAK32191.1; -; Genomic_RNA.
DR EMBL; Y09923; CAA71056.1; -; Genomic_RNA.
DR EMBL; Y10051; CAA71146.1; -; Genomic_RNA.
DR EMBL; Y10052; CAA71147.1; -; Genomic_RNA.
DR EMBL; X15654; CAA33680.1; -; Genomic_RNA.
DR PIR; A34766; VGIHHC.
DR RefSeq; NP_073551.1; NC_002645.1.
DR PDB; 5YL9; X-ray; 1.86 A; A=784-872, B=1052-1104.
DR PDB; 5ZHY; X-ray; 2.44 A; A/B/C/D/E/F=789-856.
DR PDB; 5ZUV; X-ray; 2.21 A; A/B/C=785-873.
DR PDB; 6ATK; X-ray; 3.50 A; D/E/F=293-435.
DR PDB; 6U7H; EM; 3.10 A; A/B/C=1-1113.
DR PDB; 7CYC; EM; 3.21 A; A/B/C=1-1116.
DR PDB; 7CYD; EM; 3.55 A; A/B/C=1-1116.
DR PDBsum; 5YL9; -.
DR PDBsum; 5ZHY; -.
DR PDBsum; 5ZUV; -.
DR PDBsum; 6ATK; -.
DR PDBsum; 6U7H; -.
DR PDBsum; 7CYC; -.
DR PDBsum; 7CYD; -.
DR SMR; P15423; -.
DR PRIDE; P15423; -.
DR DNASU; 918758; -.
DR GeneID; 918758; -.
DR KEGG; vg:918758; -.
DR SABIO-RK; P15423; -.
DR Proteomes; UP000006716; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04200; ALPHA_CORONA_SPIKE; 1.
DR InterPro; IPR042552; ALPHA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR002551; Spike_S1_CoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR043614; Spike_S2_CoV_C.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF01600; CoV_S1; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Glycoprotein; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virulence; Virus entry into host cell.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 16..1173
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000037203"
FT TOPO_DOM 16..1115
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1116..1135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1136..1173
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 16..536
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 417..547
FT /note="Interaction with ANPEP"
FT REGION 417..547
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 537..1173
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 753..773
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 767..886
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1031..1127
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 834..878
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1063..1105
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1169..1173
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT VARIANT 98
FT /note="N -> S (in strain: Isolate LRI 281)"
FT VARIANT 120
FT /note="N -> I (in strain: Isolate LRI 281)"
FT VARIANT 127..128
FT /note="LR -> IS (in strain: Isolate A162)"
FT VARIANT 176
FT /note="N -> T (in strain: Isolate P100E)"
FT VARIANT 210
FT /note="T -> S (in strain: Isolate A162)"
FT VARIANT 223
FT /note="T -> N (in strain: Isolate A162)"
FT VARIANT 228..229
FT /note="DF -> V (in strain: Isolate A162)"
FT VARIANT 230
FT /note="C -> F (in strain: Isolate RW Stock, Isolate P11A,
FT Isolate P11B, Isolate P100E and Isolate ATCC VR-74)"
FT VARIANT 230
FT /note="C -> L (in strain: Isolate LRI 281)"
FT VARIANT 248
FT /note="S -> A (in strain: Isolate A162)"
FT VARIANT 270
FT /note="D -> Y (in strain: Isolate P100E)"
FT VARIANT 295
FT /note="V -> A (in strain: Isolate LRI 281)"
FT VARIANT 300
FT /note="T -> M (in strain: Isolate P100E)"
FT VARIANT 307
FT /note="D -> N (in strain: Isolate A162)"
FT VARIANT 310..311
FT /note="PQ -> LR (in strain: Isolate A162)"
FT VARIANT 314..324
FT /note="GGKCFNCYPAG -> VGRCYNCRPAV (in strain: Isolate
FT A162)"
FT VARIANT 336
FT /note="K -> N (in strain: Isolate LRI 281)"
FT VARIANT 349..358
FT /note="KYVAVYANVG -> QFVGAKFD (in strain: Isolate A162)"
FT VARIANT 401
FT /note="V -> M (in strain: Isolate A162)"
FT VARIANT 404..411
FT /note="WAYSKYYT -> LANLNSHN (in strain: Isolate A162)"
FT VARIANT 414
FT /note="S -> T (in strain: Isolate P100E)"
FT VARIANT 424
FT /note="G -> V (in strain: Isolate A162)"
FT VARIANT 430
FT /note="Q -> K (in strain: Isolate A162)"
FT VARIANT 441
FT /note="V -> A (in strain: Isolate LRI 281)"
FT VARIANT 444
FT /note="D -> N (in strain: Isolate A162)"
FT VARIANT 462
FT /note="V -> I (in strain: Isolate A162)"
FT VARIANT 481
FT /note="L -> V (in strain: Isolate A162)"
FT VARIANT 488
FT /note="K -> N (in strain: Isolate A162)"
FT VARIANT 530
FT /note="L -> M (in strain: Isolate A162)"
FT VARIANT 577
FT /note="I -> T (in strain: Isolate P11A)"
FT VARIANT 578
FT /note="V -> G (in strain: Isolate P11B)"
FT VARIANT 590
FT /note="T -> I (in strain: Isolate P100E)"
FT VARIANT 642
FT /note="R -> M (in strain: Isolate A162)"
FT VARIANT 681
FT /note="T -> R (in strain: Isolate A162)"
FT VARIANT 700
FT /note="L -> I (in strain: Isolate RW Stock, Isolate P11A,
FT Isolate P11B and Isolate P100E)"
FT VARIANT 711
FT /note="D -> N (in strain: Isolate LRI 281)"
FT VARIANT 714
FT /note="K -> N (in strain: Isolate RW Stock, Isolate P11A,
FT Isolate P11B and Isolate P100E)"
FT VARIANT 765
FT /note="V -> A (in strain: Isolate A162)"
FT VARIANT 775
FT /note="A -> S (in strain: Isolate A162)"
FT VARIANT 846
FT /note="H -> Y (in strain: Isolate P11A and Isolate P11B)"
FT VARIANT 871
FT /note="T -> I (in strain: Isolate A162)"
FT VARIANT 937
FT /note="I -> L (in strain: Isolate A162)"
FT VARIANT 971
FT /note="T -> R (in strain: Isolate A162)"
FT VARIANT 1005
FT /note="M -> I (in strain: Isolate A162)"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 65..86
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7CYC"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:7CYC"
FT STRAND 229..245
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7CYC"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 299..309
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:7CYC"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:7CYC"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 381..390
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 408..427
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 454..462
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 501..519
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 583..598
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 608..613
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 617..623
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 629..651
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 656..661
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 683..686
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 691..699
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 715..717
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 724..730
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 742..754
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 755..757
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:7CYC"
FT HELIX 769..778
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 786..871
FT /evidence="ECO:0007829|PDB:5YL9"
FT STRAND 924..941
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 944..959
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 964..968
FT /evidence="ECO:0007829|PDB:6U7H"
FT TURN 969..971
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 972..976
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 981..986
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 989..994
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 1007..1012
FT /evidence="ECO:0007829|PDB:6U7H"
FT STRAND 1018..1021
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 1025..1028
FT /evidence="ECO:0007829|PDB:6U7H"
FT HELIX 1068..1096
FT /evidence="ECO:0007829|PDB:5YL9"
SQ SEQUENCE 1173 AA; 128639 MW; B9CA9A41A796B3BD CRC64;
MFVLLVAYAL LHIAGCQTTN GLNTSYSVCN GCVGYSENVF AVESGGYIPS DFAFNNWFLL
TNTSSVVDGV VRSFQPLLLN CLWSVSGLRF TTGFVYFNGT GRGDCKGFSS DVLSDVIRYN
LNFEENLRRG TILFKTSYGV VVFYCTNNTL VSGDAHIPFG TVLGNFYCFV NTTIGNETTS
AFVGALPKTV REFVISRTGH FYINGYRYFT LGNVEAVNFN VTTAETTDFC TVALASYADV
LVNVSQTSIA NIIYCNSVIN RLRCDQLSFD VPDGFYSTSP IQSVELPVSI VSLPVYHKHT
FIVLYVDFKP QSGGGKCFNC YPAGVNITLA NFNETKGPLC VDTSHFTTKY VAVYANVGRW
SASINTGNCP FSFGKVNNFV KFGSVCFSLK DIPGGCAMPI VANWAYSKYY TIGSLYVSWS
DGDGITGVPQ PVEGVSSFMN VTLDKCTKYN IYDVSGVGVI RVSNDTFLNG ITYTSTSGNL
LGFKDVTKGT IYSITPCNPP DQLVVYQQAV VGAMLSENFT SYGFSNVVEL PKFFYASNGT
YNCTDAVLTY SSFGVCADGS IIAVQPRNVS YDSVSAIVTA NLSIPSNWTT SVQVEYLQIT
STPIVVDCST YVCNGNVRCV ELLKQYTSAC KTIEDALRNS ARLESADVSE MLTFDKKAFT
LANVSSFGDY NLSSVIPSLP TSGSRVAGRS AIEDILFSKL VTSGLGTVDA DYKKCTKGLS
IADLACAQYY NGIMVLPGVA DAERMAMYTG SLIGGIALGG LTSAVSIPFS LAIQARLNYV
ALQTDVLQEN QKILAASFNK AMTNIVDAFT GVNDAITQTS QALQTVATAL NKIQDVVNQQ
GNSLNHLTSQ LRQNFQAISS SIQAIYDRLD TIQADQQVDR LITGRLAALN VFVSHTLTKY
TEVRASRQLA QQKVNECVKS QSKRYGFCGN GTHIFSIVNA APEGLVFLHT VLLPTQYKDV
EAWSGLCVDG TNGYVLRQPN LALYKEGNYY RITSRIMFEP RIPTMADFVQ IENCNVTFVN
ISRSELQTIV PEYIDVNKTL QELSYKLPNY TVPDLVVEQY NQTILNLTSE ISTLENKSAE
LNYTVQKLQT LIDNINSTLV DLKWLNRVET YIKWPWWVWL CISVVLIFVV SMLLLCCCST
GCCGFFSCFA SSIRGCCEST KLPYYDVEKI HIQ
