KV320_HUMAN
ID KV320_HUMAN Reviewed; 116 AA.
AC P01619; A0A0B4J1Z6; P01620; P01621; P01622; P01623; P04206; P06311; P18135;
AC P18136;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Immunoglobulin kappa variable 3-20 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.10};
DE AltName: Full=Ig kappa chain V-III region B6 {ECO:0000305|PubMed:11946339};
DE AltName: Full=Ig kappa chain V-III region GOL {ECO:0000305|PubMed:3086710};
DE AltName: Full=Ig kappa chain V-III region HAH {ECO:0000305|PubMed:3127527};
DE AltName: Full=Ig kappa chain V-III region HIC {ECO:0000305|PubMed:3127527};
DE AltName: Full=Ig kappa chain V-III region IARC/BL41 {ECO:0000305|PubMed:2997711};
DE AltName: Full=Ig kappa chain V-III region NG9 {ECO:0000305|PubMed:6419127};
DE AltName: Full=Ig kappa chain V-III region SIE {ECO:0000305|PubMed:6794615};
DE AltName: Full=Ig kappa chain V-III region Ti {ECO:0000305|PubMed:5027703};
DE AltName: Full=Ig kappa chain V-III region WOL {ECO:0000305|PubMed:6794615};
DE Flags: Precursor;
GN Name=IGKV3-20 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.10};
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].
RX PubMed=2997711; DOI=10.1093/nar/13.18.6499;
RA Klobeck H.G., Meindl A., Combriato G., Solomon A., Zachau H.G.;
RT "Human immunoglobulin kappa light chain genes of subgroups II and III.";
RL Nucleic Acids Res. 13:6499-6513(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3127527; DOI=10.1084/jem.167.3.840;
RA Kipps T.J., Tomhave E., Chen P.P., Carson D.A.;
RT "Autoantibody-associated kappa light chain variable region gene expressed
RT in chronic lymphocytic leukemia with little or no somatic mutation.
RT Implications for etiology and immunotherapy.";
RL J. Exp. Med. 167:840-852(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV3-20*01).
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-116.
RX PubMed=6419127; DOI=10.1038/307077a0;
RA Bentley D.L.;
RT "Most kappa immunoglobulin mRNA in human lymphocytes is homologous to a
RT small family of germ-line V genes.";
RL Nature 307:77-80(1984).
RN [5]
RP PROTEIN SEQUENCE OF 21-116.
RX PubMed=11946339; DOI=10.1016/0014-5793(69)80048-7;
RA Milstein C.;
RT "The basic sequences of immunoglobulin kappa chains: sequence studies of
RT Bence Jones proteins Rad, Fr4 and B6.";
RL FEBS Lett. 2:301-304(1969).
RN [6]
RP PROTEIN SEQUENCE OF 21-116.
RX PubMed=5027703;
RA Suter L., Barnikol H.U., Watanabe S., Hilschmann N.;
RT "Rule of antibody structure. The primary structure of a monoclonal
RT immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein Ti).
RT IV. The complete amino acid sequence and its significance for the mechanism
RT of antibody production.";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:189-208(1972).
RN [7]
RP PROTEIN SEQUENCE OF 21-116.
RX PubMed=6794615; DOI=10.1021/bi00523a026;
RA Andrews D.W., Capra J.D.;
RT "Amino acid sequence of the variable regions of light chains from two
RT idiotypically cross-reactive human IgM anti-gamma-globulins of the Wa
RT group.";
RL Biochemistry 20:5816-5822(1981).
RN [8]
RP PROTEIN SEQUENCE OF 21-116.
RX PubMed=3086710; DOI=10.1016/0161-5890(86)90049-0;
RA Newkirk M., Chen P.P., Carson D.A., Posnett D., Capra J.D.;
RT "Amino acid sequence of a light chain variable region of a human rheumatoid
RT factor of the Wa idiotypic group, in part predicted by its reactivity with
RT antipeptide antibodies.";
RL Mol. Immunol. 23:239-244(1986).
RN [9]
RP NOMEMCLATURE.
RX PubMed=11549845; DOI=10.1159/000049195;
RA Lefranc M.P.;
RT "Nomenclature of the human immunoglobulin kappa (IGK) genes.";
RL Exp. Clin. Immunogenet. 18:161-174(2001).
RN [10]
RP NOMENCLATURE.
RA Lefranc M.P., Lefranc G.;
RT "The Immunoglobulin FactsBook.";
RL (In) Lefranc M.P., Lefranc G. (eds.);
RL The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. (2001).
RN [11]
RP REVIEW ON SOMATIC HYPERMUTATION.
RX PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
RA Teng G., Papavasiliou F.N.;
RT "Immunoglobulin somatic hypermutation.";
RL Annu. Rev. Genet. 41:107-120(2007).
RN [12]
RP REVIEW ON IMMUNOGLOBULINS.
RX PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
RA Schroeder H.W. Jr., Cavacini L.;
RT "Structure and function of immunoglobulins.";
RL J. Allergy Clin. Immunol. 125:S41-S52(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=22158414; DOI=10.1038/nri3128;
RA McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
RT "Molecular programming of B cell memory.";
RL Nat. Rev. Immunol. 12:24-34(2012).
RN [15]
RP NOMENCLATURE.
RX PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
RA Lefranc M.P.;
RT "Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and Rise
RT of Immunoinformatics.";
RL Front. Immunol. 5:22-22(2014).
CC -!- FUNCTION: V region of the variable domain of immunoglobulin light
CC chains that participates in the antigen recognition (PubMed:24600447).
CC Immunoglobulins, also known as antibodies, are membrane-bound or
CC secreted glycoproteins produced by B lymphocytes. In the recognition
CC phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC receptors which, upon binding of a specific antigen, trigger the clonal
CC expansion and differentiation of B lymphocytes into immunoglobulins-
CC secreting plasma cells. Secreted immunoglobulins mediate the effector
CC phase of humoral immunity, which results in the elimination of bound
CC antigens (PubMed:20176268, PubMed:22158414). The antigen binding site
CC is formed by the variable domain of one heavy chain, together with that
CC of its associated light chain. Thus, each immunoglobulin has two
CC antigen binding sites with remarkable affinity for a particular
CC antigen. The variable domains are assembled by a process called V-(D)-J
CC rearrangement and can then be subjected to somatic hypermutations
CC which, after exposure to antigen and selection, allow affinity
CC maturation for a particular antigen (PubMed:20176268, PubMed:17576170).
CC {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked.
CC {ECO:0000303|PubMed:20176268}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}. Cell membrane
CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGKV3-20*01.
CC -!- CAUTION: For an example of a full-length immunoglobulin kappa light
CC chain see AC P0DOX7. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA77316.1; Type=Miscellaneous discrepancy; Note=Chimeric DNA. A chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
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DR EMBL; Z00021; CAA77316.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC245015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01891; K3HUB6.
DR PIR; A01892; K3HUSI.
DR PIR; A01893; K3HUGO.
DR PIR; A01894; K3HUNG.
DR PIR; A01895; K3HUTI.
DR PIR; A01896; K3HUWL.
DR PIR; A01899; K3HU41.
DR PIR; C27594; C27594.
DR PIR; E30607; E30607.
DR PIR; PL0021; K3HUHI.
DR PIR; PL0022; K3HUHA.
DR PDB; 4LRN; X-ray; 1.89 A; L=21-116.
DR PDB; 4M62; X-ray; 1.80 A; L/M=21-116.
DR PDB; 4M8Q; X-ray; 2.89 A; B/L=21-116.
DR PDB; 4OB5; X-ray; 1.70 A; L=21-116.
DR PDB; 4ODX; X-ray; 3.10 A; B/L=21-116.
DR PDBsum; 4LRN; -.
DR PDBsum; 4M62; -.
DR PDBsum; 4M8Q; -.
DR PDBsum; 4OB5; -.
DR PDBsum; 4ODX; -.
DR AlphaFoldDB; P01619; -.
DR SMR; P01619; -.
DR IntAct; P01619; 5.
DR MINT; P01619; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR IMGT_GENE-DB; IGKV3-20; -.
DR BioMuta; IGKV3-20; -.
DR DMDM; 125801; -.
DR jPOST; P01619; -.
DR MassIVE; P01619; -.
DR PeptideAtlas; P01619; -.
DR PRIDE; P01619; -.
DR TopDownProteomics; P01619; -.
DR Ensembl; ENST00000492167.1; ENSP00000418649.1; ENSG00000239951.1.
DR Ensembl; ENST00000632822.1; ENSP00000487628.1; ENSG00000282402.1.
DR GeneCards; IGKV3-20; -.
DR HGNC; HGNC:5817; IGKV3-20.
DR HPA; ENSG00000239951; Tissue enhanced (intestine, lymphoid tissue).
DR neXtProt; NX_P01619; -.
DR OpenTargets; ENSG00000239951; -.
DR VEuPathDB; HostDB:ENSG00000239951; -.
DR GeneTree; ENSGT00940000154413; -.
DR OMA; QDYSCYP; -.
DR PhylomeDB; P01619; -.
DR PathwayCommons; P01619; -.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2029481; FCGR activation.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P01619; -.
DR Pharos; P01619; Tbio.
DR PRO; PR:P01619; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01619; protein.
DR Bgee; ENSG00000239951; Expressed in rectum and 88 other tissues.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0071748; C:monomeric IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0071756; C:pentameric IgM immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
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; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:11946339,
FT ECO:0000269|PubMed:3086710, ECO:0000269|PubMed:5027703,
FT ECO:0000269|PubMed:6794615"
FT CHAIN 21..116
FT /note="Immunoglobulin kappa variable 3-20"
FT /evidence="ECO:0000269|PubMed:11946339,
FT ECO:0000269|PubMed:3086710, ECO:0000269|PubMed:5027703,
FT ECO:0000269|PubMed:6794615"
FT /id="PRO_0000059762"
FT DOMAIN 21..>116
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 21..43
FT /note="Framework-1"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 44..55
FT /note="Complementarity-determining-1"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 56..70
FT /note="Framework-2"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 71..77
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 78..109
FT /note="Framework-3"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 110..>116
FT /note="Complementarity-determining-3"
FT /evidence="ECO:0000303|PubMed:2997711"
FT DISULFID 43..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 17..19
FT /note="DTT -> VPS (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="R -> S (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="T -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..52
FT /note="SQSVSSS -> ALLSSRG (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..52
FT /note="VSSS -> LSGN (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="S -> N (in Ref. 7; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="SY -> N (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="Y -> F (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="A -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="P -> R (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> S (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="I -> M (in Ref. 5; AA sequence and 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..71
FT /note="YG -> RD (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="G -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> T (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="T -> N (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="G -> A (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="T -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="T -> I (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="E -> D (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="G -> S (in Ref. 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..116
FT /note="SSP -> NSQ (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="S -> T (in Ref. 2 and 1; CAA77316)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..116
FT /note="SP -> LG (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 116
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:4OB5"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4OB5"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:4OB5"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4OB5"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:4OB5"
SQ SEQUENCE 116 AA; 12557 MW; FAC198A8B24553DD CRC64;
METPAQLLFL LLLWLPDTTG EIVLTQSPGT LSLSPGERAT LSCRASQSVS SSYLAWYQQK
PGQAPRLLIY GASSRATGIP DRFSGSGSGT DFTLTISRLE PEDFAVYYCQ QYGSSP
