LRIG1_HUMAN
ID LRIG1_HUMAN Reviewed; 1093 AA.
AC Q96JA1; Q6IQ51; Q96CF9; Q9BYB8; Q9UFI4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein 1;
DE Short=LIG-1 {ECO:0000303|Ref.2};
DE Flags: Precursor;
GN Name=LRIG1 {ECO:0000303|PubMed:15282549}; Synonyms=LIG1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP VAL-615.
RX PubMed=11414704; DOI=10.1006/bbrc.2001.5092;
RA Nilsson J., Vallbo C., Guo D., Golovleva I., Hallberg B., Henriksson R.,
RA Hedman H.;
RT "Cloning, characterization, and expression of human LIG1.";
RL Biochem. Biophys. Res. Commun. 284:1155-1161(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Suzuki Y.;
RT "Human membrane glycoprotein LIG-1.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 611-1093, AND VARIANT VAL-615.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INDUCTION, AND INTERACTION WITH
RP EGFR; ERBB2; ERBB3 AND ERBB4.
RX PubMed=15282549; DOI=10.1038/sj.emboj.7600342;
RA Gur G., Rubin C., Katz M., Amit I., Citri A., Nilsson J., Amariglio N.,
RA Henriksson R., Rechavi G., Hedman H., Wides R., Yarden Y.;
RT "LRIG1 restricts growth factor signaling by enhancing receptor
RT ubiquitylation and degradation.";
RL EMBO J. 23:3270-3281(2004).
RN [6] {ECO:0007744|PDB:4U7L, ECO:0007744|PDB:4U7M}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 42-781, INTERACTION WITH EGFR,
RP DOMAIN, GLYCOSYLATION AT ASN-74; ASN-150; ASN-246; ASN-292; ASN-318 AND
RP ASN-684, AND DISULFIDE BONDS.
RX PubMed=25765764; DOI=10.1016/j.jmb.2015.03.001;
RA Xu Y., Soo P., Walker F., Zhang H.H., Redpath N., Tan C.W., Nicola N.A.,
RA Adams T.E., Garrett T.P., Zhang J.G., Burgess A.W.;
RT "LRIG1 extracellular domain: structure and function analysis.";
RL J. Mol. Biol. 427:1934-1948(2015).
CC -!- FUNCTION: Acts as a feedback negative regulator of signaling by
CC receptor tyrosine kinases, through a mechanism that involves
CC enhancement of receptor ubiquitination and accelerated intracellular
CC degradation. {ECO:0000269|PubMed:15282549}.
CC -!- SUBUNIT: Interacts (via extracellular LRR and Ig-like domains) with
CC EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 (via extracellular domain)
CC (PubMed:15282549). The physiological relevance of the interaction is
CC controversial; LRIG1 may have low affinity for EGFR, and interaction
CC may occur only when high levels of both proteins are present
CC (PubMed:25765764). {ECO:0000269|PubMed:15282549,
CC ECO:0000269|PubMed:25765764}.
CC -!- INTERACTION:
CC Q96JA1; P22681: CBL; NbExp=2; IntAct=EBI-2865191, EBI-518228;
CC Q96JA1; P00533: EGFR; NbExp=6; IntAct=EBI-2865191, EBI-297353;
CC Q96JA1; P04626: ERBB2; NbExp=7; IntAct=EBI-2865191, EBI-641062;
CC Q96JA1; P21860: ERBB3; NbExp=2; IntAct=EBI-2865191, EBI-720706;
CC Q96JA1; Q15303: ERBB4; NbExp=3; IntAct=EBI-2865191, EBI-80371;
CC Q96JA1; Q6UXM1: LRIG3; NbExp=7; IntAct=EBI-2865191, EBI-9207843;
CC Q96JA1-2; P41271-2: NBL1; NbExp=3; IntAct=EBI-13067910, EBI-12135485;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15282549};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:15282549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JA1-2; Sequence=VSP_011730, VSP_011731;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11414704}.
CC -!- INDUCTION: By EGF. {ECO:0000269|PubMed:15282549}.
CC -!- DOMAIN: Contains LRR and Ig-domains that can mediate low-affinity
CC interaction with EGFR (PubMed:25765764). The LRRs and the Ig-domains
CC are each sufficient for EGFR/ERBB1 binding. This interaction is
CC abolished only when both the LRRs and the Ig-domains are deleted
CC (PubMed:15282549). {ECO:0000269|PubMed:15282549,
CC ECO:0000269|PubMed:25765764}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LRIG1ID41198ch3p14.html";
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DR EMBL; AF381545; AAK62357.1; -; mRNA.
DR EMBL; AB050468; BAB40659.1; -; mRNA.
DR EMBL; BC071561; AAH71561.1; -; mRNA.
DR EMBL; BC014276; AAH14276.2; -; mRNA.
DR EMBL; AL117666; CAB56036.1; -; mRNA.
DR CCDS; CCDS33783.1; -. [Q96JA1-1]
DR PIR; T17346; T17346.
DR RefSeq; NP_056356.2; NM_015541.2. [Q96JA1-1]
DR PDB; 4U7L; X-ray; 2.30 A; A=42-494.
DR PDB; 4U7M; X-ray; 2.76 A; A=494-781.
DR PDBsum; 4U7L; -.
DR PDBsum; 4U7M; -.
DR AlphaFoldDB; Q96JA1; -.
DR SMR; Q96JA1; -.
DR BioGRID; 117489; 60.
DR IntAct; Q96JA1; 32.
DR STRING; 9606.ENSP00000273261; -.
DR TCDB; 8.A.43.1.21; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR GlyGen; Q96JA1; 9 sites.
DR iPTMnet; Q96JA1; -.
DR PhosphoSitePlus; Q96JA1; -.
DR BioMuta; LRIG1; -.
DR DMDM; 143811415; -.
DR CPTAC; CPTAC-1495; -.
DR EPD; Q96JA1; -.
DR jPOST; Q96JA1; -.
DR MassIVE; Q96JA1; -.
DR MaxQB; Q96JA1; -.
DR PaxDb; Q96JA1; -.
DR PeptideAtlas; Q96JA1; -.
DR PRIDE; Q96JA1; -.
DR ProteomicsDB; 76916; -. [Q96JA1-1]
DR ProteomicsDB; 76917; -. [Q96JA1-2]
DR Antibodypedia; 55087; 235 antibodies from 30 providers.
DR DNASU; 26018; -.
DR Ensembl; ENST00000273261.8; ENSP00000273261.3; ENSG00000144749.14. [Q96JA1-1]
DR Ensembl; ENST00000383703.3; ENSP00000373208.3; ENSG00000144749.14. [Q96JA1-2]
DR GeneID; 26018; -.
DR KEGG; hsa:26018; -.
DR MANE-Select; ENST00000273261.8; ENSP00000273261.3; NM_015541.3; NP_056356.2.
DR UCSC; uc003dmx.4; human. [Q96JA1-1]
DR CTD; 26018; -.
DR DisGeNET; 26018; -.
DR GeneCards; LRIG1; -.
DR HGNC; HGNC:17360; LRIG1.
DR HPA; ENSG00000144749; Tissue enhanced (pancreas).
DR MIM; 608868; gene.
DR neXtProt; NX_Q96JA1; -.
DR OpenTargets; ENSG00000144749; -.
DR PharmGKB; PA38450; -.
DR VEuPathDB; HostDB:ENSG00000144749; -.
DR eggNOG; KOG4194; Eukaryota.
DR GeneTree; ENSGT00940000158502; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q96JA1; -.
DR OMA; RRMQVMP; -.
DR OrthoDB; 161719at2759; -.
DR PhylomeDB; Q96JA1; -.
DR TreeFam; TF325380; -.
DR PathwayCommons; Q96JA1; -.
DR Reactome; R-HSA-177929; Signaling by EGFR.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR SignaLink; Q96JA1; -.
DR SIGNOR; Q96JA1; -.
DR BioGRID-ORCS; 26018; 16 hits in 1068 CRISPR screens.
DR ChiTaRS; LRIG1; human.
DR GeneWiki; LRIG1; -.
DR GenomeRNAi; 26018; -.
DR Pharos; Q96JA1; Tbio.
DR PRO; PR:Q96JA1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96JA1; protein.
DR Bgee; ENSG00000144749; Expressed in secondary oocyte and 210 other tissues.
DR Genevisible; Q96JA1; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0022405; P:hair cycle process; IEA:Ensembl.
DR GO; GO:0060384; P:innervation; IEA:Ensembl.
DR GO; GO:0032474; P:otolith morphogenesis; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF01463; LRRCT; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS51450; LRR; 14.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1093
FT /note="Leucine-rich repeats and immunoglobulin-like domains
FT protein 1"
FT /id="PRO_0000014827"
FT TOPO_DOM 35..794
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 816..1093
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..68
FT /note="LRRNT"
FT REPEAT 69..90
FT /note="LRR 1"
FT REPEAT 93..114
FT /note="LRR 2"
FT REPEAT 116..137
FT /note="LRR 3"
FT REPEAT 140..161
FT /note="LRR 4"
FT REPEAT 164..185
FT /note="LRR 5"
FT REPEAT 189..210
FT /note="LRR 6"
FT REPEAT 212..233
FT /note="LRR 7"
FT REPEAT 236..257
FT /note="LRR 8"
FT REPEAT 260..281
FT /note="LRR 9"
FT REPEAT 284..305
FT /note="LRR 10"
FT REPEAT 308..329
FT /note="LRR 11"
FT REPEAT 332..353
FT /note="LRR 12"
FT REPEAT 356..378
FT /note="LRR 13"
FT REPEAT 383..404
FT /note="LRR 14"
FT REPEAT 407..428
FT /note="LRR 15"
FT DOMAIN 440..491
FT /note="LRRCT"
FT DOMAIN 495..594
FT /note="Ig-like C2-type 1"
FT DOMAIN 599..688
FT /note="Ig-like C2-type 2"
FT DOMAIN 693..779
FT /note="Ig-like C2-type 3"
FT REGION 946..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT DISULFID 45..54
FT /evidence="ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT DISULFID 444..468
FT /evidence="ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT DISULFID 446..489
FT /evidence="ECO:0000269|PubMed:25765764,
FT ECO:0007744|PDB:4U7L"
FT DISULFID 516..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25765764, ECO:0007744|PDB:4U7M"
FT DISULFID 620..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25765764, ECO:0007744|PDB:4U7M"
FT DISULFID 714..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25765764, ECO:0007744|PDB:4U7M"
FT VAR_SEQ 387
FT /note="L -> LLLLEPSQSAGCSSPSQPHMSAGGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011730"
FT VAR_SEQ 644..691
FT /note="RERRMHVMPDDDVFFITDVKIDDAGVYSCTAQNSAGSISANATLTVLE ->
FT Q (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011731"
FT VARIANT 24
FT /note="L -> V (in dbSNP:rs1403626)"
FT /id="VAR_049889"
FT VARIANT 615
FT /note="M -> V (in dbSNP:rs2306272)"
FT /evidence="ECO:0000269|PubMed:11414704,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031581"
FT VARIANT 926
FT /note="G -> S (in dbSNP:rs9877201)"
FT /id="VAR_031582"
FT VARIANT 957
FT /note="A -> T (in dbSNP:rs332373)"
FT /id="VAR_031583"
FT VARIANT 993
FT /note="G -> A (in dbSNP:rs2279289)"
FT /id="VAR_049890"
FT VARIANT 1031
FT /note="P -> R (in dbSNP:rs332374)"
FT /id="VAR_031584"
FT VARIANT 1053
FT /note="Q -> P (in dbSNP:rs2279290)"
FT /id="VAR_031585"
FT CONFLICT 24..26
FT /note="LLL -> VLV (in Ref. 1; AAK62357 and 3; AAH71561)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="L -> F (in Ref. 3; AAH71561)"
FT /evidence="ECO:0000305"
FT CONFLICT 612..613
FT /note="TT -> VR (in Ref. 4; CAB56036)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="G -> GA (in Ref. 2; BAB40659)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="M -> I (in Ref. 2; BAB40659)"
FT /evidence="ECO:0000305"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 228..233
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 252..257
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 324..329
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 348..353
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 377..380
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 423..428
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 434..443
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 446..450
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 451..457
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:4U7L"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:4U7L"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:4U7L"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 512..524
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 541..548
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 556..564
FT /evidence="ECO:0007829|PDB:4U7M"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 573..580
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 591..603
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:4U7M"
FT HELIX 641..644
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:4U7M"
FT TURN 652..654
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 656..661
FT /evidence="ECO:0007829|PDB:4U7M"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 668..675
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 680..697
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 710..713
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 716..720
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 723..728
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 747..750
FT /evidence="ECO:0007829|PDB:4U7M"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 759..767
FT /evidence="ECO:0007829|PDB:4U7M"
FT STRAND 770..781
FT /evidence="ECO:0007829|PDB:4U7M"
SQ SEQUENCE 1093 AA; 119113 MW; 7B4F13CA343AF943 CRC64;
MARPVRGGLG APRRSPCLLL LWLLLLRLEP VTAAAGPRAP CAAACTCAGD SLDCGGRGLA
ALPGDLPSWT RSLNLSYNKL SEIDPAGFED LPNLQEVYLN NNELTAVPSL GAASSHVVSL
FLQHNKIRSV EGSQLKAYLS LEVLDLSLNN ITEVRNTCFP HGPPIKELNL AGNRIGTLEL
GAFDGLSRSL LTLRLSKNRI TQLPVRAFKL PRLTQLDLNR NRIRLIEGLT FQGLNSLEVL
KLQRNNISKL TDGAFWGLSK MHVLHLEYNS LVEVNSGSLY GLTALHQLHL SNNSIARIHR
KGWSFCQKLH ELVLSFNNLT RLDEESLAEL SSLSVLRLSH NSISHIAEGA FKGLRSLRVL
DLDHNEISGT IEDTSGAFSG LDSLSKLTLF GNKIKSVAKR AFSGLEGLEH LNLGGNAIRS
VQFDAFVKMK NLKELHISSD SFLCDCQLKW LPPWLIGRML QAFVTATCAH PESLKGQSIF
SVPPESFVCD DFLKPQIITQ PETTMAMVGK DIRFTCSAAS SSSSPMTFAW KKDNEVLTNA
DMENFVHVHA QDGEVMEYTT ILHLRQVTFG HEGRYQCVIT NHFGSTYSHK ARLTVNVLPS
FTKTPHDITI RTTTMARLEC AATGHPNPQI AWQKDGGTDF PAARERRMHV MPDDDVFFIT
DVKIDDAGVY SCTAQNSAGS ISANATLTVL ETPSLVVPLE DRVVSVGETV ALQCKATGNP
PPRITWFKGD RPLSLTERHH LTPDNQLLVV QNVVAEDAGR YTCEMSNTLG TERAHSQLSV
LPAAGCRKDG TTVGIFTIAV VSSIVLTSLV WVCIIYQTRK KSEEYSVTNT DETVVPPDVP
SYLSSQGTLS DRQETVVRTE GGPQANGHIE SNGVCPRDAS HFPEPDTHSV ACRQPKLCAG
SAYHKEPWKA MEKAEGTPGP HKMEHGGRVV CSDCNTEVDC YSRGQAFHPQ PVSRDSAQPS
APNGPEPGGS DQEHSPHHQC SRTAAGSCPE CQGSLYPSNH DRMLTAVKKK PMASLDGKGD
SSWTLARLYH PDSTELQPAS SLTSGSPERA EAQYLLVSNG HLPKACDASP ESTPLTGQLP
GKQRVPLLLA PKS
