KVD33_HUMAN
ID KVD33_HUMAN Reviewed; 117 AA.
AC P01593; A0A0B4J1U0; P01595; P01605; P01607; P01608; P01609; P01613; P80362;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Immunoglobulin kappa variable 1D-33 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.15};
DE AltName: Full=Ig kappa chain V-I region AG {ECO:0000305|PubMed:4893682};
DE AltName: Full=Ig kappa chain V-I region Bi {ECO:0000305|PubMed:4563064};
DE AltName: Full=Ig kappa chain V-I region Lay {ECO:0000305|PubMed:2496160, ECO:0000305|PubMed:824717};
DE AltName: Full=Ig kappa chain V-I region Ni {ECO:0000305|PubMed:4709625};
DE AltName: Full=Ig kappa chain V-I region Rei {ECO:0000305|PubMed:809329};
DE AltName: Full=Ig kappa chain V-I region Roy {ECO:0000305|PubMed:5595110};
DE AltName: Full=Ig kappa chain V-I region Scw {ECO:0000305|PubMed:4435756};
DE AltName: Full=Ig kappa chain V-I region WAT {ECO:0000305|PubMed:6167731, ECO:0000305|PubMed:7993911};
DE Flags: Precursor;
GN Name=IGKV1D-33 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.15};
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 [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV1D-33*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 [2]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=5595110;
RA Hilschmann N.;
RT "Chemical structure of 2 kappa-type Bence Jones proteins (Roy and Cum.).";
RL Hoppe-Seyler's Z. Physiol. Chem. 348:1077-1080(1967).
RN [3]
RP SEQUENCE REVISION TO 61 AND 63.
RA Hilschmann N., Barnikol H.U., Hess M., Langer B., Ponstingl H.,
RA Steinmetz-Kayne M., Suter L., Watanabe S.;
RL (In) Franek F., Shugar D. (eds.);
RL Gamma globulins: structure and function, pp.57-74, Academic Press, New York
RL (1969).
RN [4]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=4893682; DOI=10.1016/s0021-9258(18)83405-6;
RA Titani K., Shinoda T., Putnam F.W.;
RT "The amino acid sequence of a kappa type Bence-Jones protein. 3. The
RT complete sequence and the location of the disulfide bridges.";
RL J. Biol. Chem. 244:3550-3560(1969).
RN [5]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=4563064;
RA Braun M., Leibold W., Barnikol H.U., Hilschmann N.;
RT "Principle of antibody structure. The primary structure of a monoclonal
RT kappa I-type immunoglobulin L-chain (Bence Jones protein Bi). 3. The
RT complete amino acid sequence and the genetic significance of the
RT variability principles for the mechanism of antibody formation.";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:1284-1306(1972).
RN [6]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=4709625;
RA Shinoda T.;
RT "Amino acid sequence of a human kappa type Bence-Jones protein. II.
RT Chymotryptic peptides and sequence of protein Ni.";
RL J. Biochem. 73:433-446(1973).
RN [7]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=4435756;
RA Eulitz M., Hilschmann N.;
RT "The primary structure of a human immunoglobulin L-chain of kappa-type
RT (Bence-Jones protein Scw.), II: the chymotryptic peptides and the complete
RT amino acid sequence.";
RL Hoppe-Seyler's Z. Physiol. Chem. 355:842-866(1974).
RN [8]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=809329;
RA Palm W., Hilschmann N.;
RT "The primary structure of a crystalline monoclonal immunoglobulin kappa-
RT type L-chain, subgroup I (Bence-Jones protein Rei); isolation and
RT characterization of the tryptic peptides; the complete amino acid sequence
RT of the protein; a contribution to the elucidation of the three-dimensional
RT structure of antibodies, in particular their combining site.";
RL Hoppe-Seyler's Z. Physiol. Chem. 356:167-191(1975).
RN [9]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=824717; DOI=10.1111/j.1365-3083.1976.tb03017.x;
RA Capra J.D., Klapper D.G.;
RT "Complete amino acid sequence of the variable domains of two human IgM
RT anti-gamma globulins (Lay/Pom) with shared idiotypic specificities.";
RL Scand. J. Immunol. 5:677-684(1976).
RN [10]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=2496160;
RA Goni F.R., Chen P.P., McGinnis D., Arjonilla M.L., Fernandez J., Carson D.,
RA Solomon A., Mendez E., Frangione B.;
RT "Structural and idiotypic characterization of the L chains of human IgM
RT autoantibodies with different specificities.";
RL J. Immunol. 142:3158-3163(1989).
RN [11]
RP ERRATUM OF PUBMED:2496160.
RA Goni F.R., Chen P.P., McGinnis D., Arjonilla M.L., Fernandez J., Carson D.,
RA Solomon A., Mendez E., Frangione B.;
RL J. Immunol. 143:3864-3864(1989).
RN [12]
RP PROTEIN SEQUENCE OF 23-117, AND X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF
RP 23-117.
RX PubMed=7993911; DOI=10.1021/bi00253a024;
RA Huang D.-B., Chang C.-H., Ainsworth C., Bruenger A.T., Eulitz M.,
RA Solomon A., Stevens F.J., Schiffer M.;
RT "Comparison of crystal structures of two homologous proteins: structural
RT origin of altered domain interactions in immunoglobulin light-chain
RT dimers.";
RL Biochemistry 33:14848-14857(1994).
RN [13]
RP PROTEIN SEQUENCE OF 23-57.
RX PubMed=6167731; DOI=10.1016/0022-2836(81)90086-3;
RA Stevens F.J., Westholm F.A., Panagiotopoulos N., Schiffer M., Popp R.A.,
RA Solomon A.;
RT "Characterization and preliminary crystallographic data on the VL-related
RT fragment of the human kI Bence Jones protein Wat.";
RL J. Mol. Biol. 147:185-193(1981).
RN [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-117, AND DISULFIDE BOND.
RX PubMed=1182131; DOI=10.1021/bi00693a025;
RA Epp O., Lattman E.E., Schiffer M., Huber R., Palm W.;
RT "The molecular structure of a dimer composed of the variable portions of
RT the Bence-Jones protein REI refined at 2.0-A resolution.";
RL Biochemistry 14:4943-4952(1975).
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 IGKV1D-33*01.
CC -!- CAUTION: For an example of a full-length immunoglobulin kappa light
CC chain see AC P0DOX7. {ECO:0000305}.
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DR EMBL; AC233264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01861; K1HUAG.
DR PIR; A01863; K1HUBI.
DR PIR; A01871; K1HULY.
DR PIR; A01875; K1HUSW.
DR PIR; A01880; K1HUNY.
DR PIR; A91638; K1HURY.
DR PIR; A91663; K1HURE.
DR PDB; 1AR2; X-ray; 2.80 A; A=23-117.
DR PDB; 1BWW; X-ray; 1.70 A; A/B=23-117.
DR PDB; 1REI; X-ray; 2.00 A; A/B=23-117.
DR PDB; 1WTL; X-ray; 1.90 A; A/B=23-117.
DR PDB; 4L1H; X-ray; 1.68 A; A=23-117.
DR PDB; 5XP1; X-ray; 2.88 A; A/B/C/D/E/F/G/H=23-117.
DR PDBsum; 1AR2; -.
DR PDBsum; 1BWW; -.
DR PDBsum; 1REI; -.
DR PDBsum; 1WTL; -.
DR PDBsum; 4L1H; -.
DR PDBsum; 5XP1; -.
DR AlphaFoldDB; P01593; -.
DR SMR; P01593; -.
DR IntAct; P01593; 3.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR IMGT_GENE-DB; IGKV1D-33; -.
DR GlyGen; P01593; 2 sites, 1 O-linked glycan (2 sites).
DR BioMuta; IGKV1D-33; -.
DR DMDM; 125759; -.
DR jPOST; P01593; -.
DR MassIVE; P01593; -.
DR PeptideAtlas; P01593; -.
DR PRIDE; P01593; -.
DR Ensembl; ENST00000390265.2; ENSP00000374800.2; ENSG00000239975.3.
DR GeneCards; IGKV1D-33; -.
DR HGNC; HGNC:5753; IGKV1D-33.
DR HPA; ENSG00000239975; Tissue enhanced (lymphoid tissue, salivary gland).
DR neXtProt; NX_P01593; -.
DR VEuPathDB; HostDB:ENSG00000239975; -.
DR PhylomeDB; P01593; -.
DR PathwayCommons; P01593; -.
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; P01593; -.
DR ChiTaRS; IGKV1D-33; human.
DR Pharos; P01593; Tdark.
DR PRO; PR:P01593; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01593; protein.
DR Bgee; ENSG00000239975; Expressed in bone marrow cell and 87 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; 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; -; 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..22
FT /evidence="ECO:0000269|PubMed:2496160,
FT ECO:0000269|PubMed:4435756, ECO:0000269|PubMed:4563064,
FT ECO:0000269|PubMed:4709625, ECO:0000269|PubMed:4893682,
FT ECO:0000269|PubMed:5595110, ECO:0000269|PubMed:6167731,
FT ECO:0000269|PubMed:7993911, ECO:0000269|PubMed:809329,
FT ECO:0000269|PubMed:824717"
FT CHAIN 23..117
FT /note="Immunoglobulin kappa variable 1D-33"
FT /evidence="ECO:0000269|PubMed:2496160,
FT ECO:0000269|PubMed:4435756, ECO:0000269|PubMed:4563064,
FT ECO:0000269|PubMed:4709625, ECO:0000269|PubMed:4893682,
FT ECO:0000269|PubMed:5595110, ECO:0000269|PubMed:7993911,
FT ECO:0000269|PubMed:809329, ECO:0000269|PubMed:824717"
FT /id="PRO_0000059737"
FT DOMAIN 24..>117
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 23..45
FT /note="Framework-1"
FT REGION 46..56
FT /note="Complementarity-determining-1"
FT REGION 57..71
FT /note="Framework-2"
FT REGION 72..78
FT /note="Complementarity-determining-2"
FT REGION 79..110
FT /note="Framework-3"
FT REGION 111..117
FT /note="Complementarity-determining-3"
FT DISULFID 45..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:1182131"
FT CONFLICT 32
FT /note="S -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="A -> V (in Ref. 9; AA sequence and 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="S -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="R -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..46
FT /note="ITCQ -> LLCE (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="Q -> R (in Ref. 12; AA sequence and 13; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..56
FT /note="DISNYLN -> SVLESGNTFLA (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..53
FT /note="DISN -> NVNA (in Ref. 9; AA sequence and 10; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..56
FT /note="SNYLN -> RNSLI (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..54
FT /note="SNY -> RKH (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="SN -> IK (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="SN -> NH (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> T (in Ref. 12; AA sequence and 13; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="NY -> IF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="N -> D (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="L -> V (in Ref. 12; AA sequence and 13; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Y -> F (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="Q -> D (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="K -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="K -> R (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="K -> T (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="G -> K (in Ref. 6; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="K -> L (in Ref. 9; AA sequence and 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="K -> Q (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="K -> R (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> V (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="D -> E (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="D -> G (in Ref. 12; AA sequence, 7; AA sequence, 9;
FT AA sequence and 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="S -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> I (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> T (in Ref. 7; AA sequence, 9; AA sequence and
FT 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="L -> R (in Ref. 9; AA sequence and 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="E -> Q (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="T -> A (in Ref. 2; AA sequence, 9; AA sequence, 10;
FT AA sequence and 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="T -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="S -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="G -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> F (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="F -> Y (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..96
FT /note="TFT -> ALS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="F -> L (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="S -> G (in Ref. 4; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="S -> T (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="I -> F (in Ref. 5; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..107
FT /note="AT -> GN (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="T -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Y -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..116
FT /note="DNL -> NNW (in Ref. 9; AA sequence and 10; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..115
FT /note="DN -> QS (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="D -> Y (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="N -> T (in Ref. 12; AA sequence, 6; AA sequence and
FT 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="L -> V (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4L1H"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:4L1H"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:4L1H"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:4L1H"
SQ SEQUENCE 117 AA; 12848 MW; EE4F871C54A514FB CRC64;
MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD ISNYLNWYQQ
KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL QPEDIATYYC QQYDNLP
