LAR_DROME
ID LAR_DROME Reviewed; 2029 AA.
AC P16621; Q960M3; Q9VIS8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Tyrosine-protein phosphatase Lar;
DE EC=3.1.3.48 {ECO:0000269|PubMed:2554325};
DE AltName: Full=Protein-tyrosine-phosphate phosphohydrolase;
DE AltName: Full=dLAR;
DE Flags: Precursor;
GN Name=Lar; ORFNames=CG10443;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2554325; DOI=10.1073/pnas.86.22.8698;
RA Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.;
RT "A family of receptor-linked protein tyrosine phosphatases in humans and
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=8598047; DOI=10.1016/s0092-8674(00)81036-3;
RA Krueger N.X., van Vactor D., Wan H.I., Gelbart W.M., Goodman C.S.,
RA Saito H.;
RT "The transmembrane tyrosine phosphatase DLAR controls motor axon guidance
RT in Drosophila.";
RL Cell 84:611-622(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 428-2029.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1572, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=24174674; DOI=10.1523/jneurosci.1878-13.2013;
RA Cameron S., Chang W.T., Chen Y., Zhou Y., Taran S., Rao Y.;
RT "Visual circuit assembly requires fine tuning of the novel Ig transmembrane
RT protein Borderless.";
RL J. Neurosci. 33:17413-17421(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 32-237, HEPARIN-BINDING REGION,
RP AND DISULFIDE BONDS.
RX PubMed=21402080; DOI=10.1016/j.jmb.2011.03.013;
RA Biersmith B.H., Hammel M., Geisbrecht E.R., Bouyain S.;
RT "The immunoglobulin-like domains 1 and 2 of the protein tyrosine
RT phosphatase LAR adopt an unusual horseshoe-like conformation.";
RL J. Mol. Biol. 408:616-627(2011).
CC -!- FUNCTION: Possible cell adhesion receptor (Probable). It possesses an
CC intrinsic protein tyrosine phosphatase activity (PTPase)
CC (PubMed:2554325). It controls motor axon guidance (PubMed:8598047). In
CC the developing eye, has a role in normal axonal targeting of the R7
CC photoreceptor, where it negatively regulates bdl (PubMed:24174674).
CC Inhibits bdl cell adhesion activity in vitro; this effect is
CC independent of its PTPase function (PubMed:24174674).
CC {ECO:0000269|PubMed:24174674, ECO:0000269|PubMed:2554325,
CC ECO:0000269|PubMed:8598047, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:2554325};
CC -!- INTERACTION:
CC P16621; P00522: Abl; NbExp=4; IntAct=EBI-668630, EBI-534090;
CC P16621; Q8T4F7: ena; NbExp=2; IntAct=EBI-668630, EBI-466810;
CC P16621; Q9VM93: Liprin-alpha; NbExp=6; IntAct=EBI-668630, EBI-113116;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Selectively expressed in a subset of axons and
CC pioneer neurons in the embryo. {ECO:0000269|PubMed:8598047}.
CC -!- DOMAIN: The extracellular domain (1-1412) is sufficient to inhibit bdl
CC function. {ECO:0000269|PubMed:24174674}.
CC -!- DISRUPTION PHENOTYPE: In the eye, axonal targeting of the R7
CC photoreceptor is disrupted in approximately 80% of axons. Double
CC knockouts of Lar and bdl partially rescue the R7 axonal targeting
CC phenotype. {ECO:0000269|PubMed:24174674}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93409.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M27700; AAA28668.1; -; mRNA.
DR EMBL; U36857; AAC47002.1; -; Genomic_DNA.
DR EMBL; U36849; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; U36850; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; U36851; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; U36852; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; U36853; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; U36854; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; U36855; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; U36856; AAC47002.1; JOINED; Genomic_DNA.
DR EMBL; AE014134; AAF53837.3; -; Genomic_DNA.
DR EMBL; AY051985; AAK93409.1; ALT_INIT; mRNA.
DR PIR; A36182; TDFFLK.
DR RefSeq; NP_523604.2; NM_078880.3.
DR PDB; 2YD1; X-ray; 1.80 A; A=33-232.
DR PDB; 3PXJ; X-ray; 2.30 A; A/B/C/D=32-237.
DR PDB; 6X38; X-ray; 1.30 A; A=706-812.
DR PDBsum; 2YD1; -.
DR PDBsum; 3PXJ; -.
DR PDBsum; 6X38; -.
DR AlphaFoldDB; P16621; -.
DR SMR; P16621; -.
DR BioGRID; 61235; 21.
DR DIP; DIP-38648N; -.
DR IntAct; P16621; 7.
DR MINT; P16621; -.
DR STRING; 7227.FBpp0303681; -.
DR GlyGen; P16621; 12 sites.
DR iPTMnet; P16621; -.
DR PaxDb; P16621; -.
DR PRIDE; P16621; -.
DR EnsemblMetazoa; FBtr0081260; FBpp0080801; FBgn0000464.
DR GeneID; 35259; -.
DR KEGG; dme:Dmel_CG10443; -.
DR UCSC; CG10443-RA; d. melanogaster.
DR CTD; 104121; -.
DR FlyBase; FBgn0000464; Lar.
DR VEuPathDB; VectorBase:FBgn0000464; -.
DR eggNOG; KOG2408; Eukaryota.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000166904; -.
DR InParanoid; P16621; -.
DR PhylomeDB; P16621; -.
DR Reactome; R-DME-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; P16621; -.
DR BioGRID-ORCS; 35259; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P16621; -.
DR GenomeRNAi; 35259; -.
DR PRO; PR:P16621; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000464; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; P16621; baseline.
DR Genevisible; P16621; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; IPI:FlyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:CACAO.
DR GO; GO:0032093; F:SAM domain binding; IPI:FlyBase.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007412; P:axon target recognition; IMP:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060269; P:centripetally migrating follicle cell migration; IMP:FlyBase.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:1903386; P:negative regulation of homophilic cell adhesion; IGI:FlyBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:FlyBase.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0120034; P:positive regulation of plasma membrane bounded cell projection assembly; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IMP:FlyBase.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR CDD; cd00063; FN3; 9.
DR Gene3D; 2.60.40.10; -; 12.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 9.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 9.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 6.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein; Heparin-binding;
KW Hydrolase; Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW Protein phosphatase; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT CHAIN 33..2029
FT /note="Tyrosine-protein phosphatase Lar"
FT /id="PRO_0000025431"
FT TOPO_DOM 33..1377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1378..1402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1403..2029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..128
FT /note="Ig-like C2-type 1"
FT DOMAIN 140..224
FT /note="Ig-like C2-type 2"
FT DOMAIN 234..316
FT /note="Ig-like C2-type 3"
FT DOMAIN 324..414
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 419..513
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 517..608
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 613..707
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 711..810
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 815..911
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 912..1005
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1009..1102
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1104..1206
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1474..1729
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1761..2020
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1346..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1670
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1961
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 70..82
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT BINDING 1638
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1670..1676
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1714
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1572
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 962
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21402080"
FT DISULFID 161..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21402080"
FT DISULFID 256..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 480..481
FT /note="EL -> DV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2YD1"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2YD1"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 120..130
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2YD1"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2YD1"
FT STRAND 713..721
FT /evidence="ECO:0007829|PDB:6X38"
FT STRAND 724..730
FT /evidence="ECO:0007829|PDB:6X38"
FT STRAND 743..751
FT /evidence="ECO:0007829|PDB:6X38"
FT STRAND 763..769
FT /evidence="ECO:0007829|PDB:6X38"
FT STRAND 771..775
FT /evidence="ECO:0007829|PDB:6X38"
FT STRAND 783..792
FT /evidence="ECO:0007829|PDB:6X38"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:6X38"
SQ SEQUENCE 2029 AA; 229056 MW; DF1F676A94050F2B CRC64;
MGLQMTAARP IAALSLLVLS LLTWTHPTIV DAAHPPEIIR KPQNQGVRVG GVASFYCAAR
GDPPPSIVWR KNGKKVSGTQ SRYTVLEQPG GISILRIEPV RAGRDDAPYE CVAENGVGDA
VSADATLTIY EGDKTPAGFP VITQGPGTRV IEVGHTVLMT CKAIGNPTPN IYWIKNQTKV
DMSNPRYSLK DGFLQIENSR EEDQGKYECV AENSMGTEHS KATNLYVKVR RVPPTFSRPP
ETISEVMLGS NLNLSCIAVG SPMPHVKWMK GSEDLTPENE MPIGRNVLQL INIQESANYT
CIAASTLGQI DSVSVVKVQS LPTAPTDVQI SEVTATSVRL EWSYKGPEDL QYYVIQYKPK
NANQAFSEIS GIITMYYVVR ALSPYTEYEF YVIAVNNIGR GPPSAPATCT TGETKMESAP
RNVQVRTLSS STMVITWEPP ETPNGQVTGY KVYYTTNSNQ PEASWNSQMV DNSELTTVSE
LTPHAIYTVR VQAYTSMGAG PMSTPVQVKA QQGVPSQPSN FRATDIGETA VTLQWTKPTH
SSENIVHYEL YWNDTYANQA HHKRISNSEA YTLDGLYPDT LYYIWLAARS QRGEGATTPP
IPVRTKQYVP GAPPRNITAI ATSSTTISLS WLPPPVERSN GRIIYYKVFF VEVGREDDEA
TTMTLNMTSI VLDELKRWTE YKIWVLAGTS VGDGPRSHPI ILRTQEDVPG DPQDVKATPL
NSTSIHVSWK PPLEKDRNGI IRGYHIHAQE LRDEGKGFLN EPFKFDVVDT LEFNVTGLQP
DTKYSIQVAA LTRKGDGDRS AAIVVKTPGG VPVRPTVSLK IMEREPIVSI ELEWERPAQT
YGELRGYRLR WGVKDQALKE EMLSGPQMTK KRFDNLERGV EYEFRVAGSN HIGIGQETVK
IFQTPEGTPG GPPSNITIRF QTPDVLCVTW DPPTREHRNG IITRYDVQFH KKIDHGLGSE
RNMTLRKAVF TNLEENTEYI FRVRAYTKQG AGPFSDKLIV ETERDMGRAP MSLQAEATSE
QTAEIWWEPV TSRGKLLGYK IFYTMTAVED LDDWQTKTVG LTESADLVNL EKFAQYAVAI
AARFKNGLGR LSEKVTVRIK PEDVPLNLRA HDVSTHSMTL SWSPPIRLTP VNYKISFDAM
KVFVDSQGFS QTQIVPKREI ILKHYVKTHT INELSPFTTY NVNVSAIPSD YSYRPPTKIT
VTTQMAAPQP MVKPDFYGVV NGEEILVILP QASEEYGPIS HYYLVVVPED KSNLHKIPDQ
FLTDDLLPGR NKPERPNAPY IAAKFPQRSI PFTFHLGSGD DYHNFTNRKL EREKRYRIFV
RAVVDTPQKH LYTSSPFSEF LSLDMREAPP GERPHRPDPN WPAEPEVSVN RNKDEPEILW
VVLPLMVSTF IVSTALIVLC VVKRRRQPCK TPDQAAVTRP LMAADLGAGP TPSDPVDMRR
LNFQTPGMIS HPPIPISEFA NHIERLKSND NQKFSQEYES IEPGQQFTWD NSNLEHNKSK
NRYANVTAYD HSRVQLPAVE GVVGSDYINA NYCDGYRKHN AYVATQGPLQ ETFVDFWRMC
WELKTATIVM MTRLEERTRI KCDQYWPTRG TETYGQIFVT ITETQELATY SIRTFQLCRQ
GFNDRREIKQ LQFTAWPDHG VPDHPAPFLQ FLRRCRALTP PESGPVIVHC SAGVGRTGCY
IVIDSMLERM KHEKIIDIYG HVTCLRAQRN YMVQTEDQYI FIHDAILEAI ICGVTEVPAR
NLHTHLQKLL ITEPGETISG MEVEFKKLSN VKMDSSKFVT ANLPCNKHKN RLVHILPYES
SRVYLTPIHG IEGSDYVNAS FIDGYRYRSA YIAAQGPVQD AAEDFWRMLW EHNSTIVVML
TKLKEMGREK CFQYWPHERS VRYQYYVVDP IAEYNMPQYK LREFKVTDAR DGSSRTVRQF
QFIDWPEQGV PKSGEGFIDF IGQVHKTKEQ FGQDGPITVH CSAGVGRSGV FITLSIVLER
MQYEGVLDVF QTVRILRSQR PAMVQTEDQY HFCYRAALEY LGSFDNYTN
