CD80_HUMAN
ID CD80_HUMAN Reviewed; 288 AA.
AC P33681; Q5DTA9; Q5DTB0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=T-lymphocyte activation antigen CD80;
DE AltName: Full=Activation B7-1 antigen;
DE AltName: Full=BB1;
DE AltName: Full=CTLA-4 counter-receptor B7.1;
DE Short=B7;
DE AltName: CD_antigen=CD80;
DE Flags: Precursor;
GN Name=CD80; Synonyms=CD28LG, CD28LG1, LAB7;
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] (ISOFORM 1).
RC TISSUE=Lymphoid tissue;
RX PubMed=2794510;
RA Freeman G.J., Freedman A.S., Segil J.M., Lee G., Whitman J.F., Nadler L.M.;
RT "B7, a new member of the Ig superfamily with unique expression on activated
RT and neoplastic B cells.";
RL J. Immunol. 143:2714-2722(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1377173; DOI=10.1007/bf00661094;
RA Selvakumar A., Mohanraj B.K., Eddy R.L., Shows T.B., White P.C., Dupont B.;
RT "Genomic organization and chromosomal location of the human gene encoding
RT the B-lymphocyte activation antigen B7.";
RL Immunogenetics 36:175-181(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE SPLICING.
RX PubMed=17953528; DOI=10.1111/j.1365-3083.2007.02009.x;
RA Kakoulidou M., Giscombe R., Zhao X., Lefvert A.K., Wang X.;
RT "Human Soluble CD80 is generated by alternative splicing, and recombinant
RT soluble CD80 binds to CD28 and CD152 influencing T-cell activation.";
RL Scand. J. Immunol. 66:529-537(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 35-38.
RX PubMed=1714935; DOI=10.1084/jem.174.3.625;
RA Freeman G.J., Gray G.S., Gimmi C.D., Lombard D.B., Zhou L.-J., White M.,
RA Fingeroth J.D., Gribben J.G., Nadler L.M.;
RT "Structure, expression, and T cell costimulatory activity of the murine
RT homologue of the human B lymphocyte activation antigen B7.";
RL J. Exp. Med. 174:625-631(1991).
RN [7]
RP CHARACTERIZATION.
RX PubMed=7527824;
RA Lanier L.L., O'Fallon S., Somoza C., Phillips J.H., Linsley P.S.,
RA Okumura K., Ito D., Azuma M.;
RT "CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T cell
RT proliferation, cytokine production, and generation of CTL.";
RL J. Immunol. 154:97-105(1995).
RN [8]
RP FUNCTION, AND INTERACTION WITH CTLA4.
RX PubMed=10583602; DOI=10.1046/j.1365-2567.1999.00888.x;
RA Vandenborre K., Van Gool S.W., Kasran A., Ceuppens J.L., Boogaerts M.A.,
RA Vandenberghe P.;
RT "Interaction of CTLA-4 (CD152) with CD80 or CD86 inhibits human T-cell
RT activation.";
RL Immunology 98:413-421(1999).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS SUBGROUP B
RP FIBER PROTEINS.
RX PubMed=16920215; DOI=10.1016/j.virusres.2006.07.009;
RA Short J.J., Vasu C., Holterman M.J., Curiel D.T., Pereboev A.;
RT "Members of adenovirus species B utilize CD80 and CD86 as cellular
RT attachment receptors.";
RL Virus Res. 122:144-153(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-234.
RX PubMed=10661405; DOI=10.1016/s1074-7613(00)80158-2;
RA Ikemizu S., Gilbert R.J., Fennelly J.A., Collins A.V., Harlos K.,
RA Jones E.Y., Stuart D.I., Davis S.J.;
RT "Structure and dimerization of a soluble form of B7-1.";
RL Immunity 12:51-60(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-242 IN COMPLEX WITH CTLA4,
RP SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-89; ASN-186;
RP ASN-207 AND ASN-226.
RX PubMed=11279502; DOI=10.1038/35069118;
RA Stamper C.C., Zhang Y., Tobin J.F., Erbe D.V., Ikemizu S., Davis S.J.,
RA Stahl M.L., Seehra J., Somers W.S., Mosyak L.;
RT "Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune
RT responses.";
RL Nature 410:608-611(2001).
CC -!- FUNCTION: Involved in the costimulatory signal essential for T-
CC lymphocyte activation. T-cell proliferation and cytokine production is
CC induced by the binding of CD28, binding to CTLA-4 has opposite effects
CC and inhibits T-cell activation. {ECO:0000269|PubMed:10583602}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for adenovirus
CC subgroup B. {ECO:0000269|PubMed:16920215}.
CC -!- SUBUNIT: Homodimer; CD80 dimers on the antigen presenting cells (APCs)
CC bridge CTLA4/CD152 dimers on T-cells in a periodic zipper-like
CC arrangement. {ECO:0000269|PubMed:10583602,
CC ECO:0000269|PubMed:11279502}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus subgroup B
CC fiber proteins. {ECO:0000269|PubMed:16920215}.
CC -!- INTERACTION:
CC P33681; Q9NZQ7: CD274; NbExp=11; IntAct=EBI-1031024, EBI-4314282;
CC P33681; P16410: CTLA4; NbExp=7; IntAct=EBI-1031024, EBI-1030991;
CC P33681; P08138: NGFR; NbExp=3; IntAct=EBI-1031024, EBI-1387782;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P33681-1; Sequence=Displayed;
CC Name=2; Synonyms=s1CD80;
CC IsoId=P33681-2; Sequence=VSP_047700;
CC Name=3; Synonyms=s2CD80;
CC IsoId=P33681-3; Sequence=VSP_047698, VSP_047699;
CC -!- TISSUE SPECIFICITY: Expressed on activated B-cells, macrophages and
CC dendritic cells.
CC -!- MISCELLANEOUS: [Isoform 2]: Soluble isoform. Expressed in unstimulated
CC B-cells and monocytes, but not T-cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Soluble isoform. Expressed in T-cells
CC activated by ConA, non-activated monocytes and monocytes activated with
CC IFN-c. {ECO:0000305}.
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DR EMBL; M27533; AAA36045.1; -; mRNA.
DR EMBL; M83077; AAA58390.1; -; Genomic_DNA.
DR EMBL; M83072; AAA58390.1; JOINED; Genomic_DNA.
DR EMBL; M83073; AAA58390.1; JOINED; Genomic_DNA.
DR EMBL; M83074; AAA58390.1; JOINED; Genomic_DNA.
DR EMBL; AY197777; AAO39208.1; -; mRNA.
DR EMBL; AY197778; AAO39209.1; -; mRNA.
DR EMBL; AC073352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042665; AAH42665.1; -; mRNA.
DR CCDS; CCDS2989.1; -. [P33681-1]
DR PIR; I54495; A45803.
DR RefSeq; NP_005182.1; NM_005191.3. [P33681-1]
DR PDB; 1DR9; X-ray; 3.00 A; A=35-233.
DR PDB; 1I8L; X-ray; 3.00 A; A/B=35-242.
DR PDB; 7TPS; X-ray; 3.15 A; A/C=35-140.
DR PDBsum; 1DR9; -.
DR PDBsum; 1I8L; -.
DR PDBsum; 7TPS; -.
DR AlphaFoldDB; P33681; -.
DR SMR; P33681; -.
DR BioGRID; 107379; 259.
DR DIP; DIP-6044N; -.
DR IntAct; P33681; 6.
DR STRING; 9606.ENSP00000264246; -.
DR ChEMBL; CHEMBL2364157; -.
DR DrugBank; DB01281; Abatacept.
DR DrugBank; DB06681; Belatacept.
DR DrugBank; DB04901; Galiximab.
DR DrugCentral; P33681; -.
DR GuidetoPHARMACOLOGY; 2744; -.
DR GlyGen; P33681; 8 sites.
DR iPTMnet; P33681; -.
DR PhosphoSitePlus; P33681; -.
DR BioMuta; CD80; -.
DR DMDM; 461606; -.
DR MassIVE; P33681; -.
DR PaxDb; P33681; -.
DR PeptideAtlas; P33681; -.
DR PRIDE; P33681; -.
DR ProteomicsDB; 54922; -. [P33681-1]
DR ProteomicsDB; 62752; -.
DR ProteomicsDB; 62753; -.
DR ABCD; P33681; 21 sequenced antibodies.
DR Antibodypedia; 16574; 2279 antibodies from 52 providers.
DR DNASU; 941; -.
DR Ensembl; ENST00000264246.8; ENSP00000264246.3; ENSG00000121594.12. [P33681-1]
DR Ensembl; ENST00000383669.3; ENSP00000373165.3; ENSG00000121594.12. [P33681-2]
DR Ensembl; ENST00000478182.5; ENSP00000418364.1; ENSG00000121594.12. [P33681-1]
DR GeneID; 941; -.
DR KEGG; hsa:941; -.
DR MANE-Select; ENST00000264246.8; ENSP00000264246.3; NM_005191.4; NP_005182.1.
DR UCSC; uc003ecq.4; human. [P33681-1]
DR CTD; 941; -.
DR DisGeNET; 941; -.
DR GeneCards; CD80; -.
DR HGNC; HGNC:1700; CD80.
DR HPA; ENSG00000121594; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 112203; gene.
DR neXtProt; NX_P33681; -.
DR OpenTargets; ENSG00000121594; -.
DR PharmGKB; PA26239; -.
DR VEuPathDB; HostDB:ENSG00000121594; -.
DR eggNOG; ENOG502S5B5; Eukaryota.
DR GeneTree; ENSGT00940000162632; -.
DR HOGENOM; CLU_071073_2_0_1; -.
DR InParanoid; P33681; -.
DR OMA; YLPRHVC; -.
DR PhylomeDB; P33681; -.
DR TreeFam; TF351094; -.
DR PathwayCommons; P33681; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-389356; CD28 co-stimulation.
DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; P33681; -.
DR SIGNOR; P33681; -.
DR BioGRID-ORCS; 941; 7 hits in 1082 CRISPR screens.
DR ChiTaRS; CD80; human.
DR EvolutionaryTrace; P33681; -.
DR GeneWiki; CD80; -.
DR GenomeRNAi; 941; -.
DR Pharos; P33681; Tclin.
DR PRO; PR:P33681; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P33681; protein.
DR Bgee; ENSG00000121594; Expressed in lower lobe of lung and 100 other tissues.
DR ExpressionAtlas; P33681; baseline and differential.
DR Genevisible; P33681; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:MGI.
DR GO; GO:0015026; F:coreceptor activity; NAS:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; NAS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; NAS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0009967; P:positive regulation of signal transduction; NAS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
DR CDD; cd16083; IgC_CD80; 1.
DR CDD; cd16086; IgV_CD80; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR037676; CD80_IgC.
DR InterPro; IPR042711; CD80_IgV.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:1714935"
FT CHAIN 35..288
FT /note="T-lymphocyte activation antigen CD80"
FT /id="PRO_0000014547"
FT TOPO_DOM 35..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..135
FT /note="Ig-like V-type"
FT DOMAIN 145..230
FT /note="Ig-like C2-type"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11279502"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11279502"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11279502"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11279502"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11279502"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:11279502"
FT DISULFID 162..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:11279502"
FT VAR_SEQ 140
FT /note="A -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17953528"
FT /id="VSP_047698"
FT VAR_SEQ 141..266
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17953528"
FT /id="VSP_047699"
FT VAR_SEQ 234..266
FT /note="TKQEHFPDNLLPSWAITLISVNGIFVICCLTYC -> S (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17953528"
FT /id="VSP_047700"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1DR9"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1DR9"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1DR9"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1DR9"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 127..139
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 157..169
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1DR9"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:1DR9"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:1DR9"
SQ SEQUENCE 288 AA; 33048 MW; BA453EE34528B1F4 CRC64;
MGHTRRQGTS PSKCPYLNFF QLLVLAGLSH FCSGVIHVTK EVKEVATLSC GHNVSVEELA
QTRIYWQKEK KMVLTMMSGD MNIWPEYKNR TIFDITNNLS IVILALRPSD EGTYECVVLK
YEKDAFKREH LAEVTLSVKA DFPTPSISDF EIPTSNIRRI ICSTSGGFPE PHLSWLENGE
ELNAINTTVS QDPETELYAV SSKLDFNMTT NHSFMCLIKY GHLRVNQTFN WNTTKQEHFP
DNLLPSWAIT LISVNGIFVI CCLTYCFAPR CRERRRNERL RRESVRPV
