ID LV657_HUMAN Reviewed; 117 AA.
AC P01721; A0A075B6I2; P01722; P06317; P06318; P06319;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Immunoglobulin lambda variable 6-57 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.8};
DE AltName: Full=Ig lambda chain V-VI region AR {ECO:0000305|PubMed:6797401};
DE AltName: Full=Ig lambda chain V-VI region EB4 {ECO:0000305|PubMed:3923440};
DE AltName: Full=Ig lambda chain V-VI region NIG-48 {ECO:0000305|PubMed:118171};
DE AltName: Full=Ig lambda chain V-VI region SUT {ECO:0000305|Ref.6};
DE AltName: Full=Ig lambda chain V-VI region WLT {ECO:0000305|PubMed:4089539};
DE Flags: Precursor;
GN Name=IGLV6-57 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.8};
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].
RX PubMed=3923440; DOI=10.1093/nar/13.8.2931;
RA Anderson M.L.M., Brown L., McKenzie E., Kellow J.E., Young B.D.;
RT "Cloning and sequence analysis of an Ig lambda light chain mRNA expressed
RT in the Burkitt's lymphoma cell line EB4.";
RL Nucleic Acids Res. 13:2931-2941(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLV6-57*01).
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP PROTEIN SEQUENCE OF 20-117.
RX PubMed=118171; DOI=10.1093/oxfordjournals.jbchem.a132670;
RA Takahashi N., Takayasu T., Isobe T., Shinoda T., Okuyama T., Shimizu A.;
RT "Comparative study on the structure of the light chains of human
RT immunoglobulins. II. Assignment of a new subgroup.";
RL J. Biochem. 86:1523-1535(1979).
RN [4]
RP PROTEIN SEQUENCE OF 20-117.
RX PubMed=6797401; DOI=10.1042/bj1950561;
RA Sletten K., Natvig J.B., Husby G., Juul J.;
RT "The complete amino acid sequence of a prototype immunoglobulin-lambda
RT light-chain-type amyloid-fibril protein AR.";
RL Biochem. J. 195:561-572(1981).
RN [5]
RP PROTEIN SEQUENCE OF 20-117.
RX PubMed=4089539; DOI=10.1111/j.1365-3083.1985.tb01927.x;
RA Dwulet F.E., Strako K., Benson M.D.;
RT "Amino acid sequence of a lambda VI primary (AL) amyloid protein (WLT).";
RL Scand. J. Immunol. 22:653-660(1985).
RN [6]
RP PROTEIN SEQUENCE OF 20-117.
RA Solomon A., Kyle R.A., Frangione B.;
RT "Light chain variable region subgroups of monoclonal immunoglobulins in
RT amyloidosis AL.";
RL (In) Glenner G.G., Osserman E.F., Benditt E.P., Calkins E., Cohen A.S.,
RL Zucker-Franklin D. (eds.);
RL Amyloidosis, pp.449-462, Plenum Press, New York (1986).
RN [7]
RP NOMENCLATURE.
RX PubMed=11872955; DOI=10.1159/000049203;
RA Lefranc M.P.;
RT "Nomenclature of the human immunoglobulin lambda (IGL) genes.";
RL Exp. Clin. Immunogenet. 18:242-254(2001).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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:17576170, PubMed:20176268).
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 IGLV6-57*01.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
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DR EMBL; AC245060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01987; L6HUAR.
DR PIR; A01988; L6HUST.
DR PIR; A01989; L6HULT.
DR PIR; A01990; L6HUEB.
DR PIR; A01991; L6HU48.
DR PDB; 1CD0; X-ray; 1.90 A; A/B=20-117.
DR PDB; 1PEW; X-ray; 1.60 A; A/B=20-117.
DR PDB; 2CD0; X-ray; 1.80 A; A/B=20-117.
DR PDB; 5IR3; X-ray; 1.70 A; A=20-117.
DR PDBsum; 1CD0; -.
DR PDBsum; 1PEW; -.
DR PDBsum; 2CD0; -.
DR PDBsum; 5IR3; -.
DR AlphaFoldDB; P01721; -.
DR EMDB; EMD-22497; -.
DR SMR; P01721; -.
DR BindingDB; P01721; -.
DR ChEMBL; CHEMBL4739844; -.
DR IMGT_GENE-DB; IGLV6-57; -.
DR BioMuta; IGLV6-57; -.
DR DMDM; 126575; -.
DR jPOST; P01721; -.
DR MassIVE; P01721; -.
DR PeptideAtlas; P01721; -.
DR Ensembl; ENST00000390285.4; ENSP00000374820.4; ENSG00000211640.4.
DR AGR; HGNC:5927; -.
DR GeneCards; IGLV6-57; -.
DR HGNC; HGNC:5927; IGLV6-57.
DR HPA; ENSG00000211640; Tissue enhanced (lymphoid tissue, urinary bladder).
DR neXtProt; NX_P01721; -.
DR OpenTargets; ENSG00000211640; -.
DR VEuPathDB; HostDB:ENSG00000211640; -.
DR GeneTree; ENSGT00940000161640; -.
DR InParanoid; P01721; -.
DR OMA; YSDDQRP; -.
DR PathwayCommons; P01721; -.
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-9679191; Potential therapeutics for SARS.
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 ChiTaRS; IGLV6-57; human.
DR Pharos; P01721; Tchem.
DR PRO; PR:P01721; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01721; Protein.
DR Bgee; ENSG00000211640; Expressed in duodenum and 94 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR23267:SF108; IMMUNOGLOBULIN LAMBDA VARIABLE 6-57; 1.
DR PANTHER; PTHR23267; IMMUNOGLOBULIN LIGHT CHAIN; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 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..19
FT /evidence="ECO:0000269|PubMed:118171,
FT ECO:0000269|PubMed:4089539, ECO:0000269|PubMed:6797401,
FT ECO:0000269|Ref.6"
FT CHAIN 20..117
FT /note="Immunoglobulin lambda variable 6-57"
FT /evidence="ECO:0000269|PubMed:118171,
FT ECO:0000269|PubMed:4089539, ECO:0000269|PubMed:6797401,
FT ECO:0000269|Ref.6"
FT /id="PRO_0000059850"
FT DOMAIN 20..>117
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 20..41
FT /note="Framework-1"
FT /evidence="ECO:0000303|Ref.6"
FT REGION 42..54
FT /note="Complementarity-determining-1"
FT /evidence="ECO:0000303|PubMed:3923440"
FT REGION 55..69
FT /note="Framework-2"
FT /evidence="ECO:0000303|Ref.6"
FT REGION 65..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..76
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000303|PubMed:3923440"
FT REGION 77..110
FT /note="Framework-3"
FT /evidence="ECO:0000303|Ref.6"
FT REGION 111..>117
FT /note="Complementarity-determining-3"
FT /evidence="ECO:0000303|PubMed:3923440"
FT DISULFID 41..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 16..17
FT /note="GS -> DC (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="N -> D (in Ref. 4; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="F -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="T -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="H -> L (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="H -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="E -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="G -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="T -> I (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="I -> F (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="I -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..47
FT /note="GSSGS -> RSDGT (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..46
FT /note="GSSG -> RTSD (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="A -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="SNY -> DSF (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..51
FT /note="SN -> GY (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="Q -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60..61
FT /note="PG -> RV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> R (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="T -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="T -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="V -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="Y -> F (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="E -> D (in Ref. 4; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="N -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="S -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="G -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="I -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..90
FT /note="SSS -> DSA (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="S -> R (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..109
FT /note="KTEDEADYY -> TNDDTAMYF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="K -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..116
FT /note="YDSS -> FDNT (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..117
FT /note="DSSN -> NSNH (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..117
FT /note="SSN -> NNN (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..117
FT /note="SSN -> RDH (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:5IR3"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1PEW"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1PEW"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1PEW"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1PEW"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1PEW"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1PEW"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1PEW"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1PEW"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1PEW"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1PEW"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1PEW"
SQ SEQUENCE 117 AA; 12566 MW; 1FA030C806D9F49F CRC64;
MAWAPLLLTL LAHCTGSWAN FMLTQPHSVS ESPGKTVTIS CTGSSGSIAS NYVQWYQQRP
GSAPTTVIYE DNQRPSGVPD RFSGSIDSSS NSASLTISGL KTEDEADYYC QSYDSSN
//
