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Tyrosine-protein kinase receptor TYRO3 (EC 2.7.10.1) (Tyrosine-protein kinase BYK) (Tyrosine-protein kinase DTK) (Tyrosine-protein kinase RSE) (Tyrosine-protein kinase SKY) (Tyrosine-protein kinase TIF)

 TYRO3_HUMAN             Reviewed;         890 AA.
Q06418; O14953; Q86VR3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
28-FEB-2018, entry version 182.
RecName: Full=Tyrosine-protein kinase receptor TYRO3;
EC=2.7.10.1;
AltName: Full=Tyrosine-protein kinase BYK;
AltName: Full=Tyrosine-protein kinase DTK;
AltName: Full=Tyrosine-protein kinase RSE;
AltName: Full=Tyrosine-protein kinase SKY;
AltName: Full=Tyrosine-protein kinase TIF;
Flags: Precursor;
Name=TYRO3; Synonyms=BYK, DTK, RSE, SKY, TIF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7511603;
Mark M.R., Scadden D.T., Wang Z., Gu Q., Goddard A., Godowski P.J.;
"RSE, a novel receptor-type tyrosine kinase with homology to Axl/Ufo,
is expressed at high levels in the brain.";
J. Biol. Chem. 269:10720-10728(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8108112;
Ohashi K., Mizuno K., Kuma K., Miyata T., Nakamura T.;
"Cloning of the cDNA for a novel receptor tyrosine kinase, Sky,
predominantly expressed in brain.";
Oncogene 9:699-705(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-815.
TISSUE=Brain;
PubMed=7857658; DOI=10.3109/08977199409001055;
Crosier K.E., Hall L.R., Lewis P.M., Morris C.M., Wood C.R.,
Morris J.C., Crosier P.S.;
"Isolation and characterization of the human DTK receptor tyrosine
kinase.";
Growth Factors 11:137-144(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9175267; DOI=10.1016/S0248-4900(97)86830-X;
Kajii Y., Ninomiya D., Kato M., Mizuguchi M., Saji M., Katsumoto T.,
Ohno K., Takashima S., Onodera K.;
"A tyrosine kinase-like molecule is localized in the nuclear membrane
of neurons: hippocampal behavior under stress.";
Biol. Cell 88:45-54(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-21; SER-542;
MET-819 AND GLY-824.
TISSUE=Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 519-720.
PubMed=8262388; DOI=10.1016/0378-1119(93)90109-G;
Polvi A., Armstrong E., Lai C., Lemke G., Huebner K., Spritz R.A.,
Giuda L.C., Nicholls R.D., Alitalo K.;
"The human TYRO3 gene and pseudogene are located in chromosome 15q14-
q25.";
Gene 134:289-293(1993).
[7]
AUTOPHOSPHORYLATION.
PubMed=7537495; DOI=10.1006/bbrc.1995.1549;
Toshima J., Ohashi K., Iwashita S., Mizuno K.;
"Autophosphorylation activity and association with Src family kinase
of Sky receptor tyrosine kinase.";
Biochem. Biophys. Res. Commun. 209:656-663(1995).
[8]
INTERACTION WITH GAS6.
PubMed=7634325; DOI=10.1016/0092-8674(95)90424-7;
Godowski P.J., Mark M.R., Chen J., Sadick M.D., Raab H.,
Hammonds R.G.;
"Reevaluation of the roles of protein S and Gas6 as ligands for the
receptor tyrosine kinase Rse/Tyro 3.";
Cell 82:355-358(1995).
[9]
REVIEW ON FUNCTION.
PubMed=16737840; DOI=10.1016/j.cytogfr.2006.04.004;
Hafizi S., Dahlback B.;
"Signalling and functional diversity within the Axl subfamily of
receptor tyrosine kinases.";
Cytokine Growth Factor Rev. 17:295-304(2006).
[10]
FUNCTION (MICROBIAL INFECTION).
PubMed=17005688; DOI=10.1128/JVI.01157-06;
Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K.,
Irimura T., Jones S., Feldmann H., Kawaoka Y.;
"Tyro3 family-mediated cell entry of Ebola and Marburg viruses.";
J. Virol. 80:10109-10116(2006).
[11]
REVIEW ON FUNCTION.
PubMed=18421305; DOI=10.1038/nri2303;
Lemke G., Rothlin C.V.;
"Immunobiology of the TAM receptors.";
Nat. Rev. Immunol. 8:327-336(2008).
[12]
FUNCTION IN PLATELET ACTIVATION.
PubMed=20546121; DOI=10.1111/j.1538-7836.2010.03935.x;
Cosemans J.M., Van Kruchten R., Olieslagers S., Schurgers L.J.,
Verheyen F.K., Munnix I.C., Waltenberger J., Angelillo-Scherrer A.,
Hoylaerts M.F., Carmeliet P., Heemskerk J.W.;
"Potentiating role of Gas6 and Tyro3, Axl and Mer (TAM) receptors in
human and murine platelet activation and thrombus stabilization.";
J. Thromb. Haemost. 8:1797-1808(2010).
[13]
FUNCTION (MICROBIAL INFECTION).
PubMed=22156524; DOI=10.1128/JVI.06451-11;
Shimojima M., Stroher U., Ebihara H., Feldmann H., Kawaoka Y.;
"Identification of cell surface molecules involved in dystroglycan-
independent Lassa virus cell entry.";
J. Virol. 86:2067-2078(2012).
[14]
FUNCTION (MICROBIAL INFECTION).
PubMed=22673088; DOI=10.1292/jvms.12-0176;
Shimojima M., Kawaoka Y.;
"Cell surface molecules involved in infection mediated by lymphocytic
choriomeningitis virus glycoprotein.";
J. Vet. Med. Sci. 74:1363-1366(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND SER-818, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
FUNCTION (MICROBIAL INFECTION), AND REVIEW.
PubMed=25277499; DOI=10.1016/j.virol.2014.09.009;
Moller-Tank S., Maury W.;
"Phosphatidylserine receptors: enhancers of enveloped virus entry and
infection.";
Virology 468:565-580(2014).
[17]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 41-222, SUBUNIT, INTERACTION
WITH GAS6, MUTAGENESIS OF ILE-99, AND DISULFIDE BONDS.
PubMed=14623883; DOI=10.1074/jbc.M311750200;
Heiring C., Dahlbaeck B., Muller Y.A.;
"Ligand recognition and homophilic interactions in Tyro3: structural
insights into the Axl/Tyro3 receptor tyrosine kinase family.";
J. Biol. Chem. 279:6952-6958(2004).
[18]
VARIANT [LARGE SCALE ANALYSIS] THR-831.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Receptor tyrosine kinase that transduces signals from
the extracellular matrix into the cytoplasm by binding to several
ligands including TULP1 or GAS6. Regulates many physiological
processes including cell survival, migration and differentiation.
Ligand binding at the cell surface induces dimerization and
autophosphorylation of TYRO3 on its intracellular domain that
provides docking sites for downstream signaling molecules.
Following activation by ligand, interacts with PIK3R1 and thereby
enhances PI3-kinase activity. Activates the AKT survival pathway,
including nuclear translocation of NF-kappa-B and up-regulation of
transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays
a role in various processes such as neuron protection from
excitotoxic injury, platelet aggregation and cytoskeleton
reorganization. Plays also an important role in inhibition of
Toll-like receptors (TLRs)-mediated innate immune response by
activating STAT1, which selectively induces production of
suppressors of cytokine signaling SOCS1 and SOCS3.
{ECO:0000269|PubMed:20546121}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for lassa virus
and lymphocytic choriomeningitis virus, possibly through GAS6
binding to phosphatidyl-serine at the surface of virion envelope.
{ECO:0000269|PubMed:22156524, ECO:0000269|PubMed:22673088,
ECO:0000269|PubMed:25277499}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus,
possibly through GAS6 binding to phosphatidyl-serine at the
surface of virion envelope. {ECO:0000269|PubMed:17005688}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Monomer and homodimer. Interacts (via N-terminus) with
extracellular ligands TULP1 and GAS6 (By similarity). Interacts
with PIK3R1; this interaction increases PI3-kinase activity (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q9Y5K2:KLK4; NbExp=3; IntAct=EBI-3951628, EBI-10224152;
Q6A162:KRT40; NbExp=3; IntAct=EBI-3951628, EBI-10171697;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-3951628, EBI-10172290;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-3951628, EBI-10171774;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-3951628, EBI-10172052;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-3951628, EBI-10172511;
P26371:KRTAP5-9; NbExp=4; IntAct=EBI-3951628, EBI-3958099;
Q99750:MDFI; NbExp=3; IntAct=EBI-3951628, EBI-724076;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Abundant in the brain and lower levels in
other tissues.
-!- PTM: Autophosphorylated.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAA21781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TYRO3ID42739ch15q15.html";
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EMBL; U05682; AAA19236.1; -; mRNA.
EMBL; D17517; BAA04467.1; -; mRNA.
EMBL; U18934; AAC50070.1; -; mRNA.
EMBL; D50479; BAA21781.1; ALT_INIT; mRNA.
EMBL; BC049368; AAH49368.1; -; mRNA.
EMBL; BC051756; AAH51756.1; -; mRNA.
EMBL; X72886; CAA51396.1; -; mRNA.
CCDS; CCDS10080.1; -.
PIR; A53743; A53743.
PIR; I38912; I38912.
RefSeq; NP_001317193.1; NM_001330264.1.
RefSeq; NP_006284.2; NM_006293.3.
UniGene; Hs.381282; -.
PDB; 1RHF; X-ray; 1.96 A; A/B=41-222.
PDBsum; 1RHF; -.
ProteinModelPortal; Q06418; -.
SMR; Q06418; -.
BioGrid; 113152; 28.
IntAct; Q06418; 17.
MINT; Q06418; -.
STRING; 9606.ENSP00000263798; -.
BindingDB; Q06418; -.
ChEMBL; CHEMBL5314; -.
GuidetoPHARMACOLOGY; 1836; -.
iPTMnet; Q06418; -.
PhosphoSitePlus; Q06418; -.
BioMuta; TYRO3; -.
DMDM; 1717829; -.
EPD; Q06418; -.
MaxQB; Q06418; -.
PaxDb; Q06418; -.
PeptideAtlas; Q06418; -.
PRIDE; Q06418; -.
Ensembl; ENST00000263798; ENSP00000263798; ENSG00000092445.
GeneID; 7301; -.
KEGG; hsa:7301; -.
UCSC; uc001zof.3; human.
CTD; 7301; -.
DisGeNET; 7301; -.
EuPathDB; HostDB:ENSG00000092445.11; -.
GeneCards; TYRO3; -.
HGNC; HGNC:12446; TYRO3.
HPA; HPA071245; -.
MIM; 600341; gene.
neXtProt; NX_Q06418; -.
OpenTargets; ENSG00000092445; -.
PharmGKB; PA37097; -.
eggNOG; ENOG410IG6I; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00810000125384; -.
HOVERGEN; HBG006346; -.
InParanoid; Q06418; -.
KO; K05116; -.
OMA; DHAGQQG; -.
OrthoDB; EOG091G016X; -.
PhylomeDB; Q06418; -.
TreeFam; TF317402; -.
BRENDA; 2.7.10.1; 2681.
SignaLink; Q06418; -.
SIGNOR; Q06418; -.
ChiTaRS; TYRO3; human.
EvolutionaryTrace; Q06418; -.
GeneWiki; TYRO3; -.
GenomeRNAi; 7301; -.
PRO; PR:Q06418; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000092445; -.
CleanEx; HS_TYRO3; -.
ExpressionAtlas; Q06418; baseline and differential.
Genevisible; Q06418; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; NAS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; NAS:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
GO; GO:0021885; P:forebrain cell migration; ISS:UniProtKB.
GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
GO; GO:0051250; P:negative regulation of lymphocyte activation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISS:UniProtKB.
GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; IEA:Ensembl.
GO; GO:0042698; P:ovulation cycle; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; NAS:UniProtKB.
GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0032940; P:secretion by cell; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0060068; P:vagina development; IEA:Ensembl.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF00041; fn3; 2.
Pfam; PF07679; I-set; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 2.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 2.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 40 {ECO:0000255}.
CHAIN 41 890 Tyrosine-protein kinase receptor TYRO3.
/FTId=PRO_0000024478.
TOPO_DOM 41 429 Extracellular. {ECO:0000255}.
TRANSMEM 430 450 Helical. {ECO:0000255}.
TOPO_DOM 451 890 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 128 Ig-like C2-type 1.
DOMAIN 139 220 Ig-like C2-type 2.
DOMAIN 227 320 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 325 416 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 518 790 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 524 532 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 655 655 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 550 550 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 681 681 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 685 685 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 686 686 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 804 804 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 818 818 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 869 869 Phosphoserine.
{ECO:0000250|UniProtKB:P55146}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 380 380 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 64 117 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:14623883}.
DISULFID 160 203 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:14623883}.
VARIANT 21 21 P -> L (in dbSNP:rs17854578).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_045886.
VARIANT 346 346 I -> N (in dbSNP:rs12148316).
/FTId=VAR_045887.
VARIANT 542 542 G -> S (in dbSNP:rs17857363).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_045888.
VARIANT 815 815 A -> V (in dbSNP:rs1042057).
{ECO:0000269|PubMed:7857658}.
/FTId=VAR_045889.
VARIANT 819 819 L -> M (in dbSNP:rs17854579).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_045890.
VARIANT 824 824 R -> G (in dbSNP:rs17857364).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_045891.
VARIANT 831 831 A -> T. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041876.
MUTAGEN 99 99 I->R: Abolishes dimerization.
{ECO:0000269|PubMed:14623883}.
CONFLICT 29 36 Missing (in Ref. 3; AAC50070).
{ECO:0000305}.
CONFLICT 285 285 L -> F (in Ref. 4; BAA21781).
{ECO:0000305}.
CONFLICT 293 293 N -> I (in Ref. 4; BAA21781).
{ECO:0000305}.
CONFLICT 341 341 E -> V (in Ref. 4; BAA21781).
{ECO:0000305}.
CONFLICT 812 812 E -> D (in Ref. 4; BAA21781).
{ECO:0000305}.
STRAND 50 55 {ECO:0000244|PDB:1RHF}.
STRAND 60 68 {ECO:0000244|PDB:1RHF}.
STRAND 74 78 {ECO:0000244|PDB:1RHF}.
STRAND 85 94 {ECO:0000244|PDB:1RHF}.
STRAND 97 106 {ECO:0000244|PDB:1RHF}.
HELIX 109 111 {ECO:0000244|PDB:1RHF}.
STRAND 113 121 {ECO:0000244|PDB:1RHF}.
STRAND 131 136 {ECO:0000244|PDB:1RHF}.
STRAND 140 143 {ECO:0000244|PDB:1RHF}.
STRAND 148 150 {ECO:0000244|PDB:1RHF}.
STRAND 156 163 {ECO:0000244|PDB:1RHF}.
STRAND 165 167 {ECO:0000244|PDB:1RHF}.
STRAND 170 175 {ECO:0000244|PDB:1RHF}.
STRAND 183 192 {ECO:0000244|PDB:1RHF}.
STRAND 199 207 {ECO:0000244|PDB:1RHF}.
STRAND 210 213 {ECO:0000244|PDB:1RHF}.
STRAND 217 221 {ECO:0000244|PDB:1RHF}.
SEQUENCE 890 AA; 96905 MW; F9EC675077C4E8F1 CRC64;
MALRRSMGRP GLPPLPLPPP PRLGLLLAAL ASLLLPESAA AGLKLMGAPV KLTVSQGQPV
KLNCSVEGME EPDIQWVKDG AVVQNLDQLY IPVSEQHWIG FLSLKSVERS DAGRYWCQVE
DGGETEISQP VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IVWWRGTTKI
GGPAPSPSVL NVTGVTQSTM FSCEAHNLKG LASSRTATVH LQALPAAPFN ITVTKLSSSN
ASVAWMPGAD GRALLQSCTV QVTQAPGGWE VLAVVVPVPP FTCLLRDLVP ATNYSLRVRC
ANALGPSPYA DWVPFQTKGL APASAPQNLH AIRTDSGLIL EWEEVIPEAP LEGPLGPYKL
SWVQDNGTQD ELTVEGTRAN LTGWDPQKDL IVRVCVSNAV GCGPWSQPLV VSSHDRAGQQ
GPPHSRTSWV PVVLGVLTAL VTAAALALIL LRKRRKETRF GQAFDSVMAR GEPAVHFRAA
RSFNRERPER IEATLDSLGI SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE
DGSFVKVAVK MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM
VILPFMKHGD LHAFLLASRI GENPFNLPLQ TLIRFMVDIA CGMEYLSSRN FIHRDLAARN
CMLAEDMTVC VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT VQSDVWAFGV
TMWEIMTRGQ TPYAGIENAE IYNYLIGGNR LKQPPECMED VYDLMYQCWS ADPKQRPSFT
CLRMELENIL GQLSVLSASQ DPLYINIERA EEPTAGGSLE LPGRDQPYSG AGDGSGMGAV
GGTPSDCRYI LTPGGLAEQP GQAEHQPESP LNETQRLLLL QQGLLPHSSC


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