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Immunoglobulin kappa variable 1D-33 (Ig kappa chain V-I region AG) (Ig kappa chain V-I region Bi) (Ig kappa chain V-I region Lay) (Ig kappa chain V-I region Ni) (Ig kappa chain V-I region Rei) (Ig kappa chain V-I region Roy) (Ig kappa chain V-I region Scw) (Ig kappa chain V-I region WAT)

 KVD33_HUMAN             Reviewed;         117 AA.
P01593; A0A0B4J1U0; P01595; P01605; P01607; P01608; P01609; P01613;
P80362;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
02-NOV-2016, sequence version 2.
20-JUN-2018, entry version 109.
RecName: Full=Immunoglobulin kappa variable 1D-33 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.15};
AltName: Full=Ig kappa chain V-I region AG {ECO:0000305|PubMed:4893682};
AltName: Full=Ig kappa chain V-I region Bi {ECO:0000305|PubMed:4563064};
AltName: Full=Ig kappa chain V-I region Lay {ECO:0000305|PubMed:2496160, ECO:0000305|PubMed:824717};
AltName: Full=Ig kappa chain V-I region Ni {ECO:0000305|PubMed:4709625};
AltName: Full=Ig kappa chain V-I region Rei {ECO:0000305|PubMed:809329};
AltName: Full=Ig kappa chain V-I region Roy {ECO:0000305|PubMed:5595110};
AltName: Full=Ig kappa chain V-I region Scw {ECO:0000305|PubMed:4435756};
AltName: Full=Ig kappa chain V-I region WAT {ECO:0000305|PubMed:6167731, ECO:0000305|PubMed:7993911};
Flags: Precursor;
Name=IGKV1D-33 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.15};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE
IGKV1D-33*01).
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[2]
PROTEIN SEQUENCE OF 23-117.
PubMed=5595110;
Hilschmann N.;
"Chemical structure of 2 kappa-type Bence Jones proteins (Roy and
Cum.).";
Hoppe-Seyler's Z. Physiol. Chem. 348:1077-1080(1967).
[3]
SEQUENCE REVISION TO 61 AND 63.
Hilschmann N., Barnikol H.U., Hess M., Langer B., Ponstingl H.,
Steinmetz-Kayne M., Suter L., Watanabe S.;
(In) Franek F., Shugar D. (eds.);
Gamma globulins: structure and function, pp.57-74, Academic Press, New
York (1969).
[4]
PROTEIN SEQUENCE OF 23-117.
PubMed=4893682;
Titani K., Shinoda T., Putnam F.W.;
"The amino acid sequence of a kappa type Bence-Jones protein. 3. The
complete sequence and the location of the disulfide bridges.";
J. Biol. Chem. 244:3550-3560(1969).
[5]
PROTEIN SEQUENCE OF 23-117.
PubMed=4563064;
Braun M., Leibold W., Barnikol H.U., Hilschmann N.;
"Principle of antibody structure. The primary structure of a
monoclonal kappa I-type immunoglobulin L-chain (Bence Jones protein
Bi). 3. The complete amino acid sequence and the genetic significance
of the variability principles for the mechanism of antibody
formation.";
Hoppe-Seyler's Z. Physiol. Chem. 353:1284-1306(1972).
[6]
PROTEIN SEQUENCE OF 23-117.
PubMed=4709625;
Shinoda T.;
"Amino acid sequence of a human kappa type Bence-Jones protein. II.
Chymotryptic peptides and sequence of protein Ni.";
J. Biochem. 73:433-446(1973).
[7]
PROTEIN SEQUENCE OF 23-117.
PubMed=4435756;
Eulitz M., Hilschmann N.;
"The primary structure of a human immunoglobulin L-chain of kappa-type
(Bence-Jones protein Scw.), II: the chymotryptic peptides and the
complete amino acid sequence.";
Hoppe-Seyler's Z. Physiol. Chem. 355:842-866(1974).
[8]
PROTEIN SEQUENCE OF 23-117.
PubMed=809329;
Palm W., Hilschmann N.;
"The primary structure of a crystalline monoclonal immunoglobulin
kappa-type L-chain, subgroup I (Bence-Jones protein Rei); isolation
and characterization of the tryptic peptides; the complete amino acid
sequence of the protein; a contribution to the elucidation of the
three-dimensional structure of antibodies, in particular their
combining site.";
Hoppe-Seyler's Z. Physiol. Chem. 356:167-191(1975).
[9]
PROTEIN SEQUENCE OF 23-117.
PubMed=824717; DOI=10.1111/j.1365-3083.1976.tb03017.x;
Capra J.D., Klapper D.G.;
"Complete amino acid sequence of the variable domains of two human IgM
anti-gamma globulins (Lay/Pom) with shared idiotypic specificities.";
Scand. J. Immunol. 5:677-684(1976).
[10]
PROTEIN SEQUENCE OF 23-117.
PubMed=2496160;
Goni F.R., Chen P.P., McGinnis D., Arjonilla M.L., Fernandez J.,
Carson D., Solomon A., Mendez E., Frangione B.;
"Structural and idiotypic characterization of the L chains of human
IgM autoantibodies with different specificities.";
J. Immunol. 142:3158-3163(1989).
[11]
ERRATUM.
Goni F.R., Chen P.P., McGinnis D., Arjonilla M.L., Fernandez J.,
Carson D., Solomon A., Mendez E., Frangione B.;
J. Immunol. 143:3864-3864(1989).
[12]
PROTEIN SEQUENCE OF 23-117, AND X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
OF 23-117.
PubMed=7993911; DOI=10.1021/bi00253a024;
Huang D.-B., Chang C.-H., Ainsworth C., Bruenger A.T., Eulitz M.,
Solomon A., Stevens F.J., Schiffer M.;
"Comparison of crystal structures of two homologous proteins:
structural origin of altered domain interactions in immunoglobulin
light-chain dimers.";
Biochemistry 33:14848-14857(1994).
[13]
PROTEIN SEQUENCE OF 23-57.
PubMed=6167731; DOI=10.1016/0022-2836(81)90086-3;
Stevens F.J., Westholm F.A., Panagiotopoulos N., Schiffer M.,
Popp R.A., Solomon A.;
"Characterization and preliminary crystallographic data on the VL-
related fragment of the human kI Bence Jones protein Wat.";
J. Mol. Biol. 147:185-193(1981).
[14]
NOMEMCLATURE.
PubMed=11549845;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin kappa (IGK) genes.";
Exp. Clin. Immunogenet. 18:161-174(2001).
[15]
NOMENCLATURE.
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
(2001).
[16]
REVIEW ON SOMATIC HYPERMUTATION.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
[17]
REVIEW ON IMMUNOGLOBULINS.
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
[18]
REVIEW ON FUNCTION.
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
[19]
NOMENCLATURE.
PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
Lefranc M.P.;
"Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and
Rise of Immunoinformatics.";
Front. Immunol. 5:22-22(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-117, AND DISULFIDE BOND.
PubMed=1182131; DOI=10.1021/bi00693a025;
Epp O., Lattman E.E., Schiffer M., Huber R., Palm W.;
"The molecular structure of a dimer composed of the variable portions
of the Bence-Jones protein REI refined at 2.0-A resolution.";
Biochemistry 14:4943-4952(1975).
-!- FUNCTION: V region of the variable domain of immunoglobulin light
chains that participates in the antigen recognition
(PubMed:24600447). Immunoglobulins, also known as antibodies, are
membrane-bound or secreted glycoproteins produced by B
lymphocytes. In the recognition phase of humoral immunity, the
membrane-bound immunoglobulins serve as receptors which, upon
binding of a specific antigen, trigger the clonal expansion and
differentiation of B lymphocytes into immunoglobulins-secreting
plasma cells. Secreted immunoglobulins mediate the effector phase
of humoral immunity, which results in the elimination of bound
antigens (PubMed:20176268, PubMed:22158414). The antigen binding
site is formed by the variable domain of one heavy chain, together
with that of its associated light chain. Thus, each immunoglobulin
has two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
ECO:0000303|PubMed:24600447}.
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
{ECO:0000303|PubMed:20176268}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
ECO:0000303|PubMed:22158414}. Cell membrane
{ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGKV1D-33*01.
-!- CAUTION: For an example of a full-length immunoglobulin kappa
light chain see AC P0DOX7. {ECO:0000305}.
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EMBL; AC233264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A01861; K1HUAG.
PIR; A01863; K1HUBI.
PIR; A01871; K1HULY.
PIR; A01875; K1HUSW.
PIR; A01880; K1HUNY.
PIR; A91638; K1HURY.
PIR; A91663; K1HURE.
PDB; 1AR2; X-ray; 2.80 A; A=23-117.
PDB; 1BWW; X-ray; 1.70 A; A/B=23-117.
PDB; 1REI; X-ray; 2.00 A; A/B=23-117.
PDB; 1WTL; X-ray; 1.90 A; A/B=23-117.
PDB; 4L1H; X-ray; 1.68 A; A=23-117.
PDB; 5XP1; X-ray; 2.88 A; A/B/C/D/E/F/G/H=23-117.
PDBsum; 1AR2; -.
PDBsum; 1BWW; -.
PDBsum; 1REI; -.
PDBsum; 1WTL; -.
PDBsum; 4L1H; -.
PDBsum; 5XP1; -.
ProteinModelPortal; P01593; -.
SMR; P01593; -.
DrugBank; DB04147; Lauryl Dimethylamine-N-Oxide.
IMGT_GENE-DB; IGKV1D-33; -.
DMDM; 1170720; -.
DMDM; 125756; -.
DMDM; 125759; -.
DMDM; 125769; -.
DMDM; 125771; -.
DMDM; 125772; -.
DMDM; 125773; -.
DMDM; 125777; -.
PeptideAtlas; P01593; -.
PRIDE; P01593; -.
ProteomicsDB; 51395; -.
ProteomicsDB; 51397; -.
ProteomicsDB; 51407; -.
ProteomicsDB; 51409; -.
ProteomicsDB; 51410; -.
ProteomicsDB; 51411; -.
ProteomicsDB; 51415; -.
ProteomicsDB; 57679; -.
Ensembl; ENST00000390265; ENSP00000374800; ENSG00000239975.
EuPathDB; HostDB:ENSG00000239975.2; -.
EuPathDB; HostDB:ENSG00000242076.2; -.
GeneCards; IGKV1D-33; -.
HGNC; HGNC:5753; IGKV1D-33.
neXtProt; NX_P01593; -.
HOVERGEN; HBG018013; -.
PhylomeDB; P01593; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
ChiTaRS; IGKV1D-33; human.
PRO; PR:P01593; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000239975; -.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Immunity;
Immunoglobulin domain; Immunoglobulin V region; Membrane;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:2496160,
ECO:0000269|PubMed:4435756,
ECO:0000269|PubMed:4563064,
ECO:0000269|PubMed:4709625,
ECO:0000269|PubMed:4893682,
ECO:0000269|PubMed:5595110,
ECO:0000269|PubMed:6167731,
ECO:0000269|PubMed:7993911,
ECO:0000269|PubMed:809329,
ECO:0000269|PubMed:824717}.
CHAIN 23 117 Immunoglobulin kappa variable 1D-33.
{ECO:0000269|PubMed:2496160,
ECO:0000269|PubMed:4435756,
ECO:0000269|PubMed:4563064,
ECO:0000269|PubMed:4709625,
ECO:0000269|PubMed:4893682,
ECO:0000269|PubMed:5595110,
ECO:0000269|PubMed:7993911,
ECO:0000269|PubMed:809329,
ECO:0000269|PubMed:824717}.
/FTId=PRO_0000059737.
DOMAIN 24 >117 Ig-like. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
REGION 23 45 Framework-1.
REGION 46 56 Complementarity-determining-1.
REGION 57 71 Framework-2.
REGION 72 78 Complementarity-determining-2.
REGION 79 110 Framework-3.
REGION 111 117 Complementarity-determining-3.
DISULFID 45 110 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:1182131}.
CONFLICT 32 32 S -> P (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 35 35 A -> V (in Ref. 9; AA sequence and 10; AA
sequence). {ECO:0000305}.
CONFLICT 36 36 S -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 40 40 R -> S (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 43 46 ITCQ -> LLCE (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 46 46 Q -> R (in Ref. 12; AA sequence and 13;
AA sequence). {ECO:0000305}.
CONFLICT 50 56 DISNYLN -> SVLESGNTFLA (in Ref. 6; AA
sequence). {ECO:0000305}.
CONFLICT 50 53 DISN -> NVNA (in Ref. 9; AA sequence and
10; AA sequence). {ECO:0000305}.
CONFLICT 52 56 SNYLN -> RNSLI (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 52 54 SNY -> RKH (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 52 53 SN -> IK (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 52 53 SN -> NH (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 52 52 S -> T (in Ref. 12; AA sequence and 13;
AA sequence). {ECO:0000305}.
CONFLICT 53 54 NY -> IF (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 53 53 N -> D (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 55 55 L -> V (in Ref. 12; AA sequence and 13;
AA sequence). {ECO:0000305}.
CONFLICT 58 58 Y -> F (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 59 59 Q -> D (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 61 61 K -> G (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 61 61 K -> R (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 61 61 K -> T (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 63 63 G -> K (in Ref. 6; AA sequence and 4; AA
sequence). {ECO:0000305}.
CONFLICT 64 64 K -> L (in Ref. 9; AA sequence and 10; AA
sequence). {ECO:0000305}.
CONFLICT 64 64 K -> Q (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 67 67 K -> R (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 L -> F (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 L -> I (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 L -> V (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 72 72 D -> E (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 72 72 D -> G (in Ref. 12; AA sequence, 7; AA
sequence, 9; AA sequence and 10; AA
sequence). {ECO:0000305}.
CONFLICT 74 74 S -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 75 75 N -> I (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 75 75 N -> K (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 75 75 N -> T (in Ref. 7; AA sequence, 9; AA
sequence and 10; AA sequence).
{ECO:0000305}.
CONFLICT 76 76 L -> R (in Ref. 9; AA sequence and 10; AA
sequence). {ECO:0000305}.
CONFLICT 77 77 E -> Q (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 78 78 T -> A (in Ref. 2; AA sequence, 9; AA
sequence, 10; AA sequence and 8; AA
sequence). {ECO:0000305}.
CONFLICT 78 78 T -> I (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 85 85 S -> R (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 86 86 G -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 87 87 S -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 S -> F (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 93 93 F -> Y (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 94 96 TFT -> ALS (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 95 95 F -> L (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 99 99 S -> G (in Ref. 4; AA sequence and 6; AA
sequence). {ECO:0000305}.
CONFLICT 99 99 S -> T (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 105 105 I -> F (in Ref. 5; AA sequence and 6; AA
sequence). {ECO:0000305}.
CONFLICT 106 107 AT -> GN (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 107 107 T -> V (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 113 113 Y -> F (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 114 116 DNL -> NNW (in Ref. 9; AA sequence and
10; AA sequence). {ECO:0000305}.
CONFLICT 114 115 DN -> QS (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 114 114 D -> Y (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 115 115 N -> T (in Ref. 12; AA sequence, 6; AA
sequence and 4; AA sequence).
{ECO:0000305}.
CONFLICT 116 116 L -> V (in Ref. 7; AA sequence).
{ECO:0000305}.
NON_TER 117 117
STRAND 26 29 {ECO:0000244|PDB:4L1H}.
STRAND 31 35 {ECO:0000244|PDB:4L1H}.
STRAND 41 49 {ECO:0000244|PDB:4L1H}.
STRAND 55 60 {ECO:0000244|PDB:4L1H}.
STRAND 67 71 {ECO:0000244|PDB:4L1H}.
TURN 72 74 {ECO:0000244|PDB:4L1H}.
STRAND 84 89 {ECO:0000244|PDB:4L1H}.
STRAND 92 99 {ECO:0000244|PDB:4L1H}.
HELIX 102 104 {ECO:0000244|PDB:4L1H}.
STRAND 106 112 {ECO:0000244|PDB:4L1H}.
STRAND 114 117 {ECO:0000244|PDB:4L1H}.
SEQUENCE 117 AA; 12848 MW; EE4F871C54A514FB CRC64;
MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD ISNYLNWYQQ
KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL QPEDIATYYC QQYDNLP


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