DEF4_HUMAN
ID DEF4_HUMAN Reviewed; 97 AA.
AC P12838; Q6EZF8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Defensin alpha 4 {ECO:0000312|HGNC:HGNC:2763};
DE AltName: Full=Corticostatin HP-4 {ECO:0000303|PubMed:8469233};
DE AltName: Full=HNP-4 {ECO:0000303|PubMed:2500436};
DE Short=HP-4 {ECO:0000303|PubMed:2500436};
DE AltName: Full=Neutrophil defensin 4 {ECO:0000303|PubMed:15616305};
DE Flags: Precursor;
GN Name=DEFA4 {ECO:0000312|HGNC:HGNC:2763};
GN Synonyms=DEF4 {ECO:0000312|HGNC:HGNC:2763};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=8469233; DOI=10.1210/mend.7.2.8469233;
RA Palfree R.G.E., Sadro L.C., Solomon S.;
RT "The gene encoding the human corticostatin HP-4 precursor contains a recent
RT 86-base duplication and is located on chromosome 8.";
RL Mol. Endocrinol. 7:199-205(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
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 [5]
RP PROTEIN SEQUENCE OF 64-96, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=2843187; DOI=10.1016/s0006-291x(88)81118-5;
RA Singh A., Bateman A., Zhu Q., Shimasaki S., Esch F., Solomon S.;
RT "Structure of a novel human granulocyte peptide with anti-ACTH activity.";
RL Biochem. Biophys. Res. Commun. 155:524-529(1988).
RN [6]
RP PROTEIN SEQUENCE OF 64-96, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2500436; DOI=10.1016/s0021-9258(18)60449-1;
RA Wilde C.G., Griffith J.E., Marra M.N., Snable J.L., Scott R.W.;
RT "Purification and characterization of human neutrophil peptide 4, a novel
RT member of the defensin family.";
RL J. Biol. Chem. 264:11200-11203(1989).
RN [7]
RP PROTEIN SEQUENCE OF 64-83, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N.,
RA Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [8]
RP FUNCTION.
RX PubMed=15317502; DOI=10.1111/j.1399-3011.2004.00179.x;
RA Wu Z., Ericksen B., Tucker K., Lubkowski J., Lu W.;
RT "Synthesis and characterization of human alpha-defensins 4-6.";
RL J. Pept. Res. 64:118-125(2004).
RN [9]
RP FUNCTION.
RX PubMed=15616305; DOI=10.1128/aac.49.1.269-275.2005;
RA Ericksen B., Wu Z., Lu W., Lehrer R.I.;
RT "Antibacterial activity and specificity of the six human alpha-defensins.";
RL Antimicrob. Agents Chemother. 49:269-275(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH CD4 AND HIV-1 GP120.
RX PubMed=15620707; DOI=10.1016/j.febslet.2004.11.062;
RA Wu Z., Cocchi F., Gentles D., Ericksen B., Lubkowski J., Devico A.,
RA Lehrer R.I., Lu W.;
RT "Human neutrophil alpha-defensin 4 inhibits HIV-1 infection in vitro.";
RL FEBS Lett. 579:162-166(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 64-96, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=17088326; DOI=10.1110/ps.062336606;
RA Szyk A., Wu Z., Tucker K., Yang D., Lu W., Lubkowski J.;
RT "Crystal structures of human alpha-defensins HNP4, HD5, and HD6.";
RL Protein Sci. 15:2749-2760(2006).
RN [12] {ECO:0007744|PDB:6DMM, ECO:0007744|PDB:6DMQ}
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-96 OF MUTANTS ALA-86 AND
RP ALA-90, FUNCTION, SUBUNIT, INTERACTION WITH HIV-1 GP120 AND BACILLUS
RP ANTHRACIS LEF, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-65; CYS-67; LEU-69;
RP PHE-71; CYS-72; ARG-73; ARG-74; ARG-78; CYS-82; PHE-89; TYR-91; CYS-92;
RP CYS-93 AND ARG-95.
RX PubMed=30658057; DOI=10.1016/j.bbamem.2019.01.007;
RA Hu H., Di B., Tolbert W.D., Gohain N., Yuan W., Gao P., Ma B., He Q.,
RA Pazgier M., Zhao L., Lu W.;
RT "Systematic mutational analysis of human neutrophil alpha-defensin HNP4.";
RL Biochim. Biophys. Acta 1861:835-844(2019).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-74.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Host-defense peptide that has antimicrobial activity against
CC Gram-negative bacteria, and to a lesser extent also against Gram-
CC positive bacteria and fungi (PubMed:2500436, PubMed:2501794,
CC PubMed:15317502, PubMed:15616305, PubMed:30658057). Exhibits
CC antimicrobial activity against Gram-negative E.coli and E.aerogenes and
CC Gram-positive S.faecalis, S.aureus and B.cereus and the yeast
CC C.albicans (in vitro) (PubMed:2500436, PubMed:2501794, PubMed:15317502,
CC PubMed:15616305, PubMed:17088326, PubMed:30658057). Interacts with
CC pathogenic surface proteins and toxins, such as HIV-1 surface protein
CC gp120 and B.anthracis anthrax lethal factor lef (PubMed:15620707,
CC PubMed:30658057). Protects blood cells against infection with HIV-1 (in
CC vitro) (PubMed:15620707). Inhibits enzymatic activity of B.anthracis
CC lef/anthrax lethal factor (in vitro) (PubMed:30658057). Inhibits
CC corticotropin (ACTH)-stimulated corticosterone production (in vitro)
CC (PubMed:2843187). {ECO:0000269|PubMed:15317502,
CC ECO:0000269|PubMed:15616305, ECO:0000269|PubMed:15620707,
CC ECO:0000269|PubMed:17088326, ECO:0000269|PubMed:2500436,
CC ECO:0000269|PubMed:2501794, ECO:0000269|PubMed:2843187,
CC ECO:0000269|PubMed:30658057}.
CC -!- SUBUNIT: Homodimer; homodimerization seems to be required for killing
CC S.aureus, but not E.coli (PubMed:17088326, PubMed:30658057). Interacts
CC with CD4 (PubMed:15620707). Interacts with HIV-1 surface protein gp120;
CC homodimerization is required for the interaction (PubMed:15620707,
CC PubMed:30658057). Interacts with Bacillus anthracis lef;
CC homodimerization is required for the interaction (PubMed:30658057).
CC {ECO:0000269|PubMed:15620707, ECO:0000269|PubMed:17088326,
CC ECO:0000269|PubMed:30658057}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:2500436,
CC ECO:0000269|PubMed:2501794}. Note=Stored as mature peptide in
CC neutrophil granules. {ECO:0000269|PubMed:2500436}.
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils (at protein level)
CC (PubMed:2843187, PubMed:2500436, PubMed:2501794). Expressed in bone
CC marrow (PubMed:8469233). {ECO:0000269|PubMed:2500436,
CC ECO:0000269|PubMed:2501794, ECO:0000269|PubMed:2843187,
CC ECO:0000269|PubMed:8469233}.
CC -!- PTM: The three-dimensional structure formed by the three intramolecular
CC disulfide bridges is indispensable for effective bacterial killing.
CC {ECO:0000269|PubMed:17088326, ECO:0000269|PubMed:30658057}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; U18745; AAA64488.1; -; Genomic_DNA.
DR EMBL; AF200455; AAT68877.1; -; Genomic_DNA.
DR EMBL; CH471153; EAW80486.1; -; Genomic_DNA.
DR EMBL; BC093959; AAH93959.1; -; mRNA.
DR EMBL; BC106747; AAI06748.1; -; mRNA.
DR EMBL; BC112091; AAI12092.1; -; mRNA.
DR EMBL; X65977; CAA46792.1; -; mRNA.
DR CCDS; CCDS5961.1; -.
DR PIR; A47365; A47365.
DR RefSeq; NP_001916.1; NM_001925.2.
DR PDB; 1ZMM; X-ray; 1.60 A; A/B/C/D=64-96.
DR PDB; 6DMM; X-ray; 1.67 A; A/B/C/D/E/F/G/H/I/J/K/L=64-96.
DR PDB; 6DMQ; X-ray; 1.70 A; A/B/C/D/E/F/G/H=64-96.
DR PDBsum; 1ZMM; -.
DR PDBsum; 6DMM; -.
DR PDBsum; 6DMQ; -.
DR AlphaFoldDB; P12838; -.
DR SMR; P12838; -.
DR IntAct; P12838; 1.
DR STRING; 9606.ENSP00000297435; -.
DR BioMuta; DEFA4; -.
DR DMDM; 399352; -.
DR jPOST; P12838; -.
DR MassIVE; P12838; -.
DR PaxDb; P12838; -.
DR PeptideAtlas; P12838; -.
DR PRIDE; P12838; -.
DR ProteomicsDB; 52880; -.
DR Antibodypedia; 22002; 144 antibodies from 22 providers.
DR DNASU; 1669; -.
DR Ensembl; ENST00000297435.3; ENSP00000297435.2; ENSG00000164821.5.
DR Ensembl; ENST00000642522.2; ENSP00000493844.1; ENSG00000285318.2.
DR GeneID; 1669; -.
DR KEGG; hsa:1669; -.
DR MANE-Select; ENST00000297435.3; ENSP00000297435.2; NM_001925.3; NP_001916.1.
DR UCSC; uc003wqu.2; human.
DR CTD; 1669; -.
DR DisGeNET; 1669; -.
DR GeneCards; DEFA4; -.
DR HGNC; HGNC:2763; DEFA4.
DR HPA; ENSG00000164821; Tissue enriched (bone).
DR MIM; 601157; gene.
DR neXtProt; NX_P12838; -.
DR OpenTargets; ENSG00000164821; -.
DR PharmGKB; PA27240; -.
DR VEuPathDB; HostDB:ENSG00000164821; -.
DR eggNOG; ENOG502T2EX; Eukaryota.
DR GeneTree; ENSGT00940000153268; -.
DR HOGENOM; CLU_160803_0_0_1; -.
DR InParanoid; P12838; -.
DR OMA; CRPAERR; -.
DR OrthoDB; 1610714at2759; -.
DR PhylomeDB; P12838; -.
DR TreeFam; TF338414; -.
DR PathwayCommons; P12838; -.
DR Reactome; R-HSA-1461973; Defensins.
DR Reactome; R-HSA-1462054; Alpha-defensins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P12838; -.
DR BioGRID-ORCS; 1669; 20 hits in 1026 CRISPR screens.
DR EvolutionaryTrace; P12838; -.
DR GeneWiki; DEFA4; -.
DR GenomeRNAi; 1669; -.
DR Pharos; P12838; Tbio.
DR PRO; PR:P12838; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P12838; protein.
DR Bgee; ENSG00000164821; Expressed in bone marrow and 78 other tissues.
DR Genevisible; P12838; HS.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0019730; P:antimicrobial humoral response; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0051673; P:membrane disruption in another organism; IBA:GO_Central.
DR GO; GO:0010818; P:T cell chemotaxis; IDA:UniProtKB.
DR InterPro; IPR016327; Alpha-defensin.
DR InterPro; IPR006081; Alpha-defensin_C.
DR InterPro; IPR002366; Alpha-defensin_propep.
DR InterPro; IPR006080; Defensin_beta/alpha.
DR PANTHER; PTHR11876; PTHR11876; 1.
DR Pfam; PF00323; Defensin_1; 1.
DR Pfam; PF00879; Defensin_propep; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
DR SMART; SM00048; DEFSN; 1.
DR PROSITE; PS00269; DEFENSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Cytoplasmic vesicle; Defensin;
KW Direct protein sequencing; Disulfide bond; Fungicide; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..63
FT /id="PRO_0000006781"
FT PEPTIDE 64..96
FT /note="Defensin alpha 4"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="PRO_0000006782"
FT PROPEP 97
FT /id="PRO_0000006783"
FT DISULFID 65..93
FT /evidence="ECO:0000269|PubMed:17088326,
FT ECO:0000269|PubMed:30658057, ECO:0007744|PDB:1ZMM,
FT ECO:0007744|PDB:6DMM, ECO:0007744|PDB:6DMQ"
FT DISULFID 67..82
FT /evidence="ECO:0000269|PubMed:17088326,
FT ECO:0000269|PubMed:30658057, ECO:0007744|PDB:1ZMM,
FT ECO:0007744|PDB:6DMM, ECO:0007744|PDB:6DMQ"
FT DISULFID 72..92
FT /evidence="ECO:0000269|PubMed:17088326,
FT ECO:0000269|PubMed:30658057, ECO:0007744|PDB:1ZMM,
FT ECO:0007744|PDB:6DMM, ECO:0007744|PDB:6DMQ"
FT VARIANT 8
FT /note="A -> P (in dbSNP:rs28661751)"
FT /id="VAR_048861"
FT VARIANT 8
FT /note="A -> V (in dbSNP:rs28488529)"
FT /id="VAR_061132"
FT VARIANT 74
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs762433303)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036315"
FT MUTAGEN 65
FT /note="C->A: Impairs bactericidal activity against E.coli
FT and S.aureus; when associated with Ala-67, Ala-72, Ala-82,
FT Ala-92 and Ala-93."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 67
FT /note="C->A: Impairs bactericidal activity against E.coli
FT and S.aureus; when associated with Ala-65, Ala-72, Ala-82,
FT Ala-92 and Ala-93."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 69
FT /note="L->A: Slight decrease in antibacterial activity
FT against E.coli."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 71
FT /note="F->A: Decreased antibacterial activity against
FT S.aureus."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 72
FT /note="C->A: Impairs bactericidal activity against E.coli
FT and S.aureus; when associated with Ala-65, Ala-67, Ala-82,
FT Ala-92 and Ala-93."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 73
FT /note="R->A: Decreased antibacterial activity against
FT E.coli. Weakens interaction with B.anthracis lef and with
FT HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 74
FT /note="R->A: Decreased antibacterial activity against
FT E.coli. Weakens interaction with B.anthracis lef and with
FT HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 78
FT /note="R->A: Decreased antibacterial activity against
FT E.coli and S.aureus. Weakens interaction with B.anthracis
FT lef and with HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 82
FT /note="C->A: Impairs bactericidal activity against E.coli
FT and S.aureus; when associated with Ala-65, Ala-67, Ala-72,
FT Ala-92 and Ala-93."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 89
FT /note="F->A: Impaired homodimerization. Decreased
FT antibacterial activity against S.aureus. Disrupts
FT interaction with B.anthracis lef and with HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 91
FT /note="Y->A: Slight decrease in antibacterial activity
FT against E.coli and S.aureus."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 92
FT /note="C->A: Impairs bactericidal activity against E.coli
FT and S.aureus; when associated with Ala-65, Ala-67, Ala-72,
FT Ala-82 and Ala-93."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 93
FT /note="C->A: Impairs bactericidal activity against E.coli
FT and S.aureus; when associated with Ala-65, Ala-67, Ala-72,
FT Ala-82 and Ala-92."
FT /evidence="ECO:0000269|PubMed:30658057"
FT MUTAGEN 95
FT /note="R->A: Slight decrease in antibacterial activity
FT against E.coli and S.aureus."
FT /evidence="ECO:0000269|PubMed:30658057"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1ZMM"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1ZMM"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1ZMM"
SQ SEQUENCE 97 AA; 10504 MW; FE14334631EC2FD3 CRC64;
MRIIALLAAI LLVALQVRAG PLQARGDEAP GQEQRGPEDQ DISISFAWDK SSALQVSGST
RGMVCSCRLV FCRRTELRVG NCLIGGVSFT YCCTRVD
