NS7A_SARS
ID NS7A_SARS Reviewed; 122 AA.
AC P59635; Q7TA11; Q7TA17;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ORF7a protein;
DE AltName: Full=Accessory protein 7a;
DE AltName: Full=Protein U122;
DE AltName: Full=Protein X4;
DE Flags: Precursor;
GN ORFNames=7a;
OS Severe acute respiratory syndrome coronavirus (SARS-CoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=694009;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Urbani;
RX PubMed=12730500; DOI=10.1126/science.1085952;
RA Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
RA Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H., Tong S.,
RA Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D.,
RA Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S.,
RA Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R.,
RA Guenther S., Osterhaus A.D.M.E., Drosten C., Pallansch M.A., Anderson L.J.,
RA Bellini W.J.;
RT "Characterization of a novel coronavirus associated with severe acute
RT respiratory syndrome.";
RL Science 300:1394-1399(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Tor2;
RX PubMed=12730501; DOI=10.1126/science.1085953;
RA Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
RA Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
RA Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R.,
RA Mayo M., McDonald H., Montgomery S.B., Pandoh P.K., Petrescu A.S.,
RA Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M.,
RA Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K.,
RA Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R.,
RA Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A.,
RA Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S.,
RA Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M.,
RA Skowronski D.M., Upton C., Roper R.L.;
RT "The genome sequence of the SARS-associated coronavirus.";
RL Science 300:1399-1404(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
RX PubMed=12853594; DOI=10.1056/nejm200307103490216;
RA Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
RT "Coronavirus genomic-sequence variations and the epidemiology of the severe
RT acute respiratory syndrome.";
RL N. Engl. J. Med. 349:187-188(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU-39849;
RX PubMed=12876307; DOI=10.1177/15353702-0322807-13;
RA Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
RA Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
RA Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
RT "The complete genome sequence of severe acute respiratory syndrome
RT coronavirus strain HKU-39849 (HK-39).";
RL Exp. Biol. Med. 228:866-873(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
RC Isolate GD01;
RA Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T.,
RA Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lu F.,
RA Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L., Deng Y., Dong W.,
RA Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H., Li S., Li S., Li W.,
RA Li W., Lin W., Liu J., Liu Z., Lu H., Ni P., Qi Q., Sun Y., Tang L.,
RA Tong Z., Wang J., Wang X., Wu Q., Xi Y., Xu Z., Yang L., Ye C., Ye J.,
RA Zhang B., Zhang F., Zhang J., Zhang X., Zhou J., Yang H.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TW1;
RA Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
RT "The complete genome of SARS coronavirus clone TW1.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate FRA;
RA Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S.,
RA Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J.,
RA Song H.C., Abrignani S., Covacci A., Rappuoli R.;
RT "SARS virus is a close relative of type II coronaviruses.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Frankfurt 1;
RA Thiel V., Hertzig T., Putics A., Ivanov K.A., Schelle B., Bayer S.,
RA Scheiner B., Weinand H., Weissbrich B., Ziebuhr J.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
RA Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L., Shih M.-C.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and Isolate TWY;
RA Shu H.Y., Wu K.M., Tsai S.F.;
RT "The complete genome of SARS coronavirus TWH.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HSR 1;
RA Canducci F., Clementi M., Poli G., Vicenzi E.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate AS;
RA Balotta C., Corvasce S., Violin M., Galli M., Moroni M., Vigevani G.M.,
RA Ruan Y.J., Salemi M.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Shanghai QXC1;
RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RT "Analysis of SARS coronavirus genome in Shanghai isolates.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 32-122.
RC STRAIN=Isolate Shanghai LY;
RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP PEPTIDE SEQUENCE OF 16-29, SUBCELLULAR LOCATION, AND X-RAY CRYSTALLOGRAPHY
RP (1.8 ANGSTROMS) OF 16-96.
RX PubMed=15642263; DOI=10.1016/j.str.2004.10.010;
RA Nelson C.A., Pekosz A., Lee C.A., Diamond M.S., Fremont D.H.;
RT "Structure and intracellular targeting of the SARS-coronavirus Orf7a
RT accessory protein.";
RL Structure 13:75-85(2005).
RN [16]
RP INTERACTION WITH ACCESSORY PROTEIN 3A.
RX PubMed=15194747; DOI=10.1128/jvi.78.13.6723-6734.2004;
RA Tan Y.-J., Teng E., Shen S., Tan T.H.P., Goh P.-Y., Fielding B.C.,
RA Ooi E.-E., Tan H.-C., Lim S.G., Hong W.;
RT "A novel severe acute respiratory syndrome coronavirus protein, U274, is
RT transported to the cell surface and undergoes endocytosis.";
RL J. Virol. 78:6723-6734(2004).
RN [17]
RP SUBCELLULAR LOCATION, DI-LYSINE MOTIF, AND MUTAGENESIS OF 14-SER--TYR-18
RP AND 118-LYS--LYS-120.
RX PubMed=15220404; DOI=10.1128/jvi.78.14.7311-7318.2004;
RA Fielding B.C., Tan Y.-J., Shuo S., Tan T.H.P., Ooi E.-E., Lim S.G.,
RA Hong W., Goh P.-Y.;
RT "Characterization of a unique group-specific protein (U122) of the severe
RT acute respiratory syndrome coronavirus.";
RL J. Virol. 78:7311-7318(2004).
RN [18]
RP FUNCTION.
RX PubMed=15564512; DOI=10.1128/jvi.78.24.14043-14047.2004;
RA Tan Y.-J., Fielding B.C., Goh P.-Y., Shen S., Tan T.H.P., Lim S.G.,
RA Hong W.;
RT "Overexpression of 7a, a protein specifically encoded by the severe acute
RT respiratory syndrome coronavirus, induces apoptosis via a caspase-dependent
RT pathway.";
RL J. Virol. 78:14043-14047(2004).
RN [19]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPIKE GLYCOPROTEIN.
RX PubMed=16840309; DOI=10.1128/jvi.00414-06;
RA Huang C., Ito N., Tseng C.-T.K., Makino S.;
RT "Severe acute respiratory syndrome coronavirus 7a accessory protein is a
RT viral structural protein.";
RL J. Virol. 80:7287-7294(2006).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=17037516; DOI=10.1007/978-0-387-33012-9_20;
RA Pekosz A., Schaecher S.R., Diamond M.S., Fremont D.H., Sims A.C.,
RA Baric R.S.;
RT "Structure, expression, and intracellular localization of the SARS-CoV
RT accessory proteins 7a and 7b.";
RL Adv. Exp. Med. Biol. 581:115-120(2006).
RN [21]
RP INTERACTION WITH M PROTEIN; E PROTEIN AND HUMAN SGT.
RX PubMed=16580632; DOI=10.1016/j.bbrc.2006.03.091;
RA Fielding B.C., Gunalan V., Tan T.H.P., Chou C.-F., Shen S., Khan S.,
RA Lim S.G., Hong W., Tan Y.-J.;
RT "Severe acute respiratory syndrome coronavirus protein 7a interacts with
RT hSGT.";
RL Biochem. Biophys. Res. Commun. 343:1201-1208(2006).
RN [22]
RP STRUCTURE BY NMR OF 16-99.
RX PubMed=16328780; DOI=10.1007/s11373-005-9043-9;
RA Haenel K., Stangler T., Stoldt M., Willbold D.;
RT "Solution structure of the X4 protein coded by the SARS related coronavirus
RT reveals an immunoglobulin like fold and suggests a binding activity to
RT integrin I domains.";
RL J. Biomed. Sci. 13:281-293(2006).
RN [23]
RP FUNCTION, AND INTERACTION WITH HOST ITGAL.
RX PubMed=18020948; DOI=10.1515/bc.2007.157;
RA Haenel K., Willbold D.;
RT "SARS-CoV accessory protein 7a directly interacts with human LFA-1.";
RL Biol. Chem. 388:1325-1332(2007).
RN [24]
RP FUNCTION.
RX PubMed=20631126; DOI=10.1128/jvi.00748-10;
RA Karjee S., Minhas A., Sood V., Ponia S.S., Banerjea A.C., Chow V.T.,
RA Mukherjee S.K., Lal S.K.;
RT "The 7a accessory protein of severe acute respiratory syndrome coronavirus
RT acts as an RNA silencing suppressor.";
RL J. Virol. 84:10395-10401(2010).
RN [25]
RP FUNCTION, AND INTERACTION WITH HOST BST2.
RX PubMed=26378163; DOI=10.1128/jvi.02274-15;
RA Taylor J.K., Coleman C.M., Postel S., Sisk J.M., Bernbaum J.G.,
RA Venkataraman T., Sundberg E.J., Frieman M.B.;
RT "Severe Acute Respiratory Syndrome Coronavirus ORF7a Inhibits Bone Marrow
RT Stromal Antigen 2 Virion Tethering through a Novel Mechanism of
RT Glycosylation Interference.";
RL J. Virol. 89:11820-11833(2015).
CC -!- FUNCTION: Plays a role as antagonist of host tetherin (BST2),
CC disrupting its antiviral effect. Acts by binding to BST2 thereby
CC interfering with its glycosylation. May suppress small interfering RNA
CC (siRNA). May bind to host ITGAL, thereby playing a role in attachment
CC or modulation of leukocytes. {ECO:0000269|PubMed:15564512,
CC ECO:0000269|PubMed:18020948, ECO:0000269|PubMed:20631126,
CC ECO:0000269|PubMed:26378163}.
CC -!- SUBUNIT: Interacts with the spike glycoprotein (PubMed:16840309).
CC Interacts with M protein (PubMed:16580632). Interacts with E protein
CC (PubMed:16580632). Interacts with the ORF3a protein (PubMed:15194747).
CC Interacts with human SGT (PubMed:16580632). Interacts with host ITGAL
CC (PubMed:18020948). Interacts with host BST2 (PubMed:26378163).
CC {ECO:0000269|PubMed:15194747, ECO:0000269|PubMed:16580632,
CC ECO:0000269|PubMed:16840309, ECO:0000269|PubMed:18020948,
CC ECO:0000269|PubMed:26378163}.
CC -!- INTERACTION:
CC P59635; P59594: S; NbExp=3; IntAct=EBI-25492879, EBI-15582614;
CC P59635; O43765: SGTA; Xeno; NbExp=3; IntAct=EBI-25492879, EBI-347996;
CC -!- SUBCELLULAR LOCATION: Virion. Host endoplasmic reticulum membrane;
CC Single-pass membrane protein. Host endoplasmic reticulum-Golgi
CC intermediate compartment membrane; Single-pass type I membrane protein.
CC Host Golgi apparatus membrane; Single-pass membrane protein.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY278741; AAP13449.1; -; Genomic_RNA.
DR EMBL; AY274119; AAP41043.1; -; Genomic_RNA.
DR EMBL; AY282752; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278554; AAP13573.1; -; Genomic_RNA.
DR EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278487; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278488; AAP30036.1; -; Genomic_RNA.
DR EMBL; AY278489; AAP51233.1; -; Genomic_RNA.
DR EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY291451; AAP37023.1; -; Genomic_RNA.
DR EMBL; AY310120; AAP50491.1; -; Genomic_RNA.
DR EMBL; AY291315; AAP33703.1; -; Genomic_RNA.
DR EMBL; AY338174; AAQ01603.1; -; Genomic_RNA.
DR EMBL; AY338175; AAQ01615.1; -; Genomic_RNA.
DR EMBL; AY348314; AAP97888.1; -; Genomic_RNA.
DR EMBL; AP006557; BAC81354.1; -; Genomic_RNA.
DR EMBL; AP006558; BAC81368.1; -; Genomic_RNA.
DR EMBL; AP006559; BAC81382.1; -; Genomic_RNA.
DR EMBL; AP006560; BAC81396.1; -; Genomic_RNA.
DR EMBL; AP006561; BAC81410.1; -; Genomic_RNA.
DR EMBL; AY323977; AAP72980.1; -; Genomic_RNA.
DR EMBL; AY427439; AAQ94066.1; -; Genomic_RNA.
DR EMBL; AY463059; AAP82982.2; -; Genomic_RNA.
DR EMBL; AY322208; AAP82970.1; -; Genomic_RNA.
DR RefSeq; NP_828857.1; NC_004718.3.
DR PDB; 1XAK; X-ray; 1.80 A; A=14-96.
DR PDB; 1YO4; NMR; -; A=16-99.
DR PDBsum; 1XAK; -.
DR PDBsum; 1YO4; -.
DR BMRB; P59635; -.
DR SMR; P59635; -.
DR BioGRID; 4383920; 45.
DR ELM; P59635; -.
DR IntAct; P59635; 46.
DR GeneID; 1489674; -.
DR Reactome; R-HSA-9678110; Attachment and Entry.
DR Reactome; R-HSA-9679509; Virion Assembly and Release.
DR SIGNOR; P59635; -.
DR EvolutionaryTrace; P59635; -.
DR Proteomes; UP000000354; Genome.
DR Proteomes; UP000103670; Genome.
DR Proteomes; UP000109640; Genome.
DR Proteomes; UP000116947; Genome.
DR Proteomes; UP000121636; Genome.
DR Proteomes; UP000131569; Genome.
DR Proteomes; UP000131955; Genome.
DR Proteomes; UP000137377; Genome.
DR Proteomes; UP000138690; Genome.
DR Proteomes; UP000143093; Genome.
DR Proteomes; UP000145651; Genome.
DR Proteomes; UP000146108; Genome.
DR Proteomes; UP000146181; Genome.
DR Proteomes; UP000146296; Genome.
DR Proteomes; UP000148194; Genome.
DR Proteomes; UP000153467; Genome.
DR Proteomes; UP000160648; Genome.
DR Proteomes; UP000164441; Genome.
DR Proteomes; UP000172416; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; TAS:Reactome.
DR GO; GO:0019051; P:induction by virus of host apoptotic process; IDA:DIBU.
DR GO; GO:0039646; P:modulation by virus of host G0/G1 transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0039587; P:suppression by virus of host tetherin activity; IDA:UniProtKB.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1550; -; 1.
DR InterPro; IPR014888; ORF7a_SARS-CoV-like.
DR InterPro; IPR044871; ORF7a_SARS-CoV-like_X4e.
DR InterPro; IPR036495; ORF7a_sf_CoV.
DR Pfam; PF08779; bCoV_NS7A; 1.
DR SUPFAM; SSF117066; SSF117066; 1.
DR PROSITE; PS51919; X4E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond;
KW G0/G1 host cell cycle checkpoint dysregulation by virus;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host tetherin by virus; Membrane;
KW Modulation of host cell cycle by virus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral immunoevasion; Virion.
FT SIGNAL 1..15
FT CHAIN 16..122
FT /note="ORF7a protein"
FT /id="PRO_0000037435"
FT TOPO_DOM 16..96
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..122
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT DOMAIN 16..81
FT /note="X4e"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01267"
FT MOTIF 118..122
FT /note="Di-lysine motif"
FT DISULFID 23..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01267"
FT DISULFID 35..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01267"
FT VARIANT 38
FT /note="G -> A (in strain: Isolate Shanghai LY)"
FT MUTAGEN 14..18
FT /note="SCELY->LLLLL: Complete loss of signal sequence
FT cleavage."
FT /evidence="ECO:0000269|PubMed:15220404"
FT MUTAGEN 118..120
FT /note="KRK->ERE: Induces rapid exit from the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:15220404"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:1XAK"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1XAK"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1YO4"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1XAK"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1XAK"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1XAK"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1XAK"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:1XAK"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1YO4"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1YO4"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1YO4"
SQ SEQUENCE 122 AA; 13941 MW; 6D8D8D949B0DB4B5 CRC64;
MKIILFLTLI VFTSCELYHY QECVRGTTVL LKEPCPSGTY EGNSPFHPLA DNKFALTCTS
THFAFACADG TRHTYQLRAR SVSPKLFIRQ EEVQQELYSP LFLIVAALVF LILCFTIKRK
TE
