LAG1_CAEEL
ID LAG1_CAEEL Reviewed; 790 AA.
AC V6CLJ5; G5EDU7; Q8MXE7; V6CK60;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Suppressor of hairless protein homolog {ECO:0000305};
DE AltName: Full=CSL transcription factor lag-1 {ECO:0000303|PubMed:18706403, ECO:0000305};
DE AltName: Full=Lin-12 and glp-1 phenotype protein {ECO:0000312|WormBase:K08B4.1d};
GN Name=lag-1 {ECO:0000312|WormBase:K08B4.1d};
GN ORFNames=K08B4.1 {ECO:0000312|WormBase:K08B4.1d};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAB03858.1}
RP FUNCTION, NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND MUTAGENESIS OF
RP 743-TRP--TYR-790.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB03858.1};
RX PubMed=8625826; DOI=10.1242/dev.122.5.1373;
RA Christensen S., Kodoyianni V., Bosenberg M., Friedman L., Kimble J.;
RT "lag-1, a gene required for lin-12 and glp-1 signaling in Caenorhabditis
RT elegans, is homologous to human CBF1 and Drosophila Su(H).";
RL Development 122:1373-1383(1996).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=9003776; DOI=10.1002/j.1460-2075.1996.tb01092.x;
RA Roehl H., Bosenberg M., Blelloch R., Kimble J.;
RT "Roles of the RAM and ANK domains in signaling by the C. elegans GLP-1
RT receptor.";
RL EMBO J. 15:7002-7012(1996).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH LAG-3.
RX PubMed=10830967; DOI=10.1038/35012645;
RA Petcherski A.G., Kimble J.;
RT "LAG-3 is a putative transcriptional activator in the C. elegans Notch
RT pathway.";
RL Nature 405:364-368(2000).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18706403; DOI=10.1016/j.ydbio.2008.07.018;
RA Ghai V., Gaudet J.;
RT "The CSL transcription factor LAG-1 directly represses hlh-6 expression in
RT C. elegans.";
RL Dev. Biol. 322:334-344(2008).
RN [6] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=23615264; DOI=10.5483/bmbrep.2013.46.4.269;
RA Choi V.N., Park S.K., Hwang B.J.;
RT "Clustered LAG-1 binding sites in lag-1/CSL are involved in regulating lag-
RT 1 expression during lin-12/Notch-dependent cell-fate specification.";
RL BMB Rep. 46:219-224(2013).
RN [7] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=32839181; DOI=10.1242/dev.193482;
RA Luo K.L., Underwood R.S., Greenwald I.;
RT "Positive autoregulation of lag-1 in response to LIN-12 activation in cell
RT fate decisions during C. elegans reproductive system development.";
RL Development 147:0-0(2020).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=32196486; DOI=10.1371/journal.pgen.1008650;
RA Chen J., Mohammad A., Pazdernik N., Huang H., Bowman B., Tycksen E.,
RA Schedl T.;
RT "GLP-1 Notch-LAG-1 CSL control of the germline stem cell fate is mediated
RT by transcriptional targets lst-1 and sygl-1.";
RL PLoS Genet. 16:e1008650-e1008650(2020).
RN [9] {ECO:0007744|PDB:1TTU}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 309-780 IN COMPLEX WITH DNA, AND
RP FUNCTION.
RX PubMed=15297877; DOI=10.1038/sj.emboj.7600349;
RA Kovall R.A., Hendrickson W.A.;
RT "Crystal structure of the nuclear effector of Notch signaling, CSL, bound
RT to DNA.";
RL EMBO J. 23:3441-3451(2004).
RN [10] {ECO:0007744|PDB:2FO1}
RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 309-780 IN COMPLEX WITH LIN-12;
RP LAG-3 AND DNA.
RX PubMed=16530045; DOI=10.1016/j.cell.2006.01.035;
RA Wilson J.J., Kovall R.A.;
RT "Crystal structure of the CSL-Notch-Mastermind ternary complex bound to
RT DNA.";
RL Cell 124:985-996(2006).
RN [11] {ECO:0007744|PDB:3BRD}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 309-780 IN COMPLEX WITH LIN-12
RP AND DNA, AND FUNCTION.
RX PubMed=18381292; DOI=10.1074/jbc.m709501200;
RA Friedmann D.R., Wilson J.J., Kovall R.A.;
RT "RAM-induced allostery facilitates assembly of a notch pathway active
RT transcription complex.";
RL J. Biol. Chem. 283:14781-14791(2008).
RN [12]
RP FUNCTION.
RX PubMed=21737278; DOI=10.1016/j.cub.2011.06.016;
RA Bertrand V., Bisso P., Poole R.J., Hobert O.;
RT "Notch-dependent induction of left/right asymmetry in C. elegans
RT interneurons and motoneurons.";
RL Curr. Biol. 21:1225-1231(2011).
CC -!- FUNCTION: Transcriptional regulator that plays a central role in lin-
CC 12/Notch and glp-1/Notch signaling pathways, involved in cell-cell
CC communication that regulate a broad spectrum of cell-fate
CC determinations (PubMed:8625826). Binds directly to the 5'-[A/G]TGGGAA-
CC 3' DNA consensus sequence, which is present in the regulatory region of
CC several genes (PubMed:8625826, PubMed:18706403, PubMed:23615264,
CC PubMed:15297877, PubMed:32196486, PubMed:21737278). Acts as a
CC transcriptional repressor when it is not associated with Notch proteins
CC (By similarity). When in a complex with a Notch intracellular domain
CC (NICD) product of lin-12/Notch or glp-1/Notch, and transcription
CC regulator lag-3, it may act as a transcriptional activator that
CC activates transcription of target genes(PubMed:18381292,
CC PubMed:10830967, PubMed:32196486, PubMed:9003776). Probably represses
CC or activates transcription via the recruitment of chromatin remodeling
CC complexes containing histone deacetylase or histone acetylase proteins,
CC respectively (By similarity). Autonomously required in the germline for
CC the stem cell fate, acting in the glp-1-dependent transcriptional
CC activation of genes, including lst-1 and sygl-1 (PubMed:32196486).
CC Involved in cell-fate specification during reproductive system
CC development, by positively autoregulating its own expression, in
CC response to lin-12/Notch signaling (PubMed:23615264, PubMed:32839181).
CC Plays a role in Notch-dependent induction of left-right asymmetry in
CC interneurons and motoneurons (PubMed:21737278). May repress expression
CC of hlh-6, in a lin-12/Notch-independent manner (PubMed:18706403).
CC {ECO:0000250|UniProtKB:P28159, ECO:0000269|PubMed:10830967,
CC ECO:0000269|PubMed:15297877, ECO:0000269|PubMed:18381292,
CC ECO:0000269|PubMed:18706403, ECO:0000269|PubMed:21737278,
CC ECO:0000269|PubMed:23615264, ECO:0000269|PubMed:32196486,
CC ECO:0000269|PubMed:32839181, ECO:0000269|PubMed:8625826}.
CC -!- SUBUNIT: Component of a complex consisting of at least a lin-12/Notch
CC intracellular domain (NICD), lag-1, and lag-3 (PubMed:16530045,
CC PubMed:10830967, PubMed:18381292). An NICD product of lin-12/Notch,
CC including the RBP-j associated molecule (RAM) and ankyrin repeat (ANK)
CC domains, interacts directly with lag-1 (PubMed:16530045,
CC PubMed:10830967, PubMed:18381292, PubMed:9003776).
CC {ECO:0000269|PubMed:10830967, ECO:0000269|PubMed:16530045,
CC ECO:0000269|PubMed:18381292}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32196486}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=d {ECO:0000312|WormBase:K08B4.1d};
CC IsoId=V6CLJ5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:K08B4.1b};
CC IsoId=V6CLJ5-2; Sequence=VSP_060947;
CC Name=a {ECO:0000312|WormBase:K08B4.1a};
CC IsoId=V6CLJ5-3; Sequence=VSP_060946;
CC Name=c {ECO:0000312|WormBase:K08B4.1c};
CC IsoId=V6CLJ5-4; Sequence=VSP_060948;
CC -!- TISSUE SPECIFICITY: In young adults, expressed in germ cells in the
CC distal most ~10 cell diameters of the progenitor zone (PZ), and also in
CC late pachytene, diplotene and diakinesis of oogenesis.
CC {ECO:0000269|PubMed:32196486}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the precursor anchor cell and ventral
CC uterine precursor cell (Z1.ppp, Z1.ppa, Z4.aaa, and Z4.aap) before cell
CC specification, at early larval stage L2 (PubMed:23615264). Expressed in
CC the ventral uterine cell (VU), but not in the anchor cell (AC), after
CC specification, at late larval stage L2 (PubMed:23615264). Expressed in
CC a dynamic pattern in the vulval precursor cells (VPCs) during vulval
CC induction in larval stage L3 (PubMed:32839181). Expressed in somatic
CC gonad cells, the distal tip cell (DTC), and all sheath and spermathecal
CC cells, as well as in polyploid intestinal cells, in both the larval L4
CC and adult stages. {ECO:0000269|PubMed:23615264,
CC ECO:0000269|PubMed:32196486, ECO:0000269|PubMed:32839181}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown ectopically up-regulates
CC expression of hlh-6 outside pharyngeal gland cells.
CC {ECO:0000269|PubMed:18706403}.
CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
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DR EMBL; BX284604; CCD72375.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD72376.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13424.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13425.1; -; Genomic_DNA.
DR EMBL; U49794; AAB03858.1; -; mRNA.
DR EMBL; U49795; AAB03859.1; -; Genomic_DNA.
DR PIR; T33741; T33741.
DR RefSeq; NP_001023278.1; NM_001028107.3. [V6CLJ5-2]
DR RefSeq; NP_001293739.1; NM_001306810.1.
DR RefSeq; NP_001293740.1; NM_001306811.1. [V6CLJ5-1]
DR RefSeq; NP_741410.1; NM_171350.4. [V6CLJ5-3]
DR PDB; 1TTU; X-ray; 2.85 A; A=309-780.
DR PDB; 2FO1; X-ray; 3.12 A; A=309-780.
DR PDB; 3BRD; X-ray; 2.21 A; A=309-780.
DR PDBsum; 1TTU; -.
DR PDBsum; 2FO1; -.
DR PDBsum; 3BRD; -.
DR AlphaFoldDB; V6CLJ5; -.
DR SMR; V6CLJ5; -.
DR ComplexPortal; CPX-3152; CSL-Notch-Mastermind transcription factor complex.
DR IntAct; V6CLJ5; 15.
DR MINT; V6CLJ5; -.
DR STRING; 6239.K08B4.1a; -.
DR EnsemblMetazoa; K08B4.1a.1; K08B4.1a.1; WBGene00002245. [V6CLJ5-3]
DR EnsemblMetazoa; K08B4.1b.1; K08B4.1b.1; WBGene00002245. [V6CLJ5-2]
DR EnsemblMetazoa; K08B4.1c.1; K08B4.1c.1; WBGene00002245. [V6CLJ5-4]
DR EnsemblMetazoa; K08B4.1d.1; K08B4.1d.1; WBGene00002245. [V6CLJ5-1]
DR GeneID; 177373; -.
DR KEGG; cel:CELE_K08B4.1; -.
DR UCSC; K08B4.1a; c. elegans.
DR CTD; 177373; -.
DR WormBase; K08B4.1a; CE28839; WBGene00002245; lag-1.
DR WormBase; K08B4.1b; CE25048; WBGene00002245; lag-1.
DR WormBase; K08B4.1c; CE49374; WBGene00002245; lag-1.
DR WormBase; K08B4.1d; CE49360; WBGene00002245; lag-1.
DR eggNOG; KOG3743; Eukaryota.
DR GeneTree; ENSGT00390000005197; -.
DR HOGENOM; CLU_022207_1_0_1; -.
DR OMA; IQFQATQ; -.
DR OrthoDB; 444988at2759; -.
DR SignaLink; V6CLJ5; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002245; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; V6CLJ5; baseline and differential.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:WormBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:WormBase.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0001709; P:cell fate determination; IMP:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0048858; P:cell projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0043054; P:dauer exit; IGI:WormBase.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0007219; P:Notch signaling pathway; IPI:WormBase.
DR GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0048867; P:stem cell fate determination; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1450; -; 1.
DR IDEAL; IID50096; -.
DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR InterPro; IPR036358; BTD_sf.
DR InterPro; IPR040159; CLS_fam.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf.
DR InterPro; IPR038007; RBP-Jkappa_IPT.
DR PANTHER; PTHR10665; PTHR10665; 1.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR Pfam; PF20144; TIG_SUH; 1.
DR SMART; SM01268; BTD; 1.
DR SMART; SM01267; LAG1_DNAbind; 1.
DR SUPFAM; SSF110217; SSF110217; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Notch signaling pathway;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..790
FT /note="Suppressor of hairless protein homolog"
FT /id="PRO_0000452277"
FT DOMAIN 680..776
FT /note="IPT/TIG"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..353
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:15297877,
FT ECO:0000269|PubMed:16530045"
FT REGION 484..489
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:15297877,
FT ECO:0000269|PubMed:16530045"
FT REGION 514..519
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:15297877,
FT ECO:0000269|PubMed:16530045"
FT VAR_SEQ 1..255
FT /note="MFSWRRGDCESQKEENRSEERKGEETIRFPTRSPFHCVLFLLTDGFVLHKPT
FT ASPTVGFSPTIFSFYYSRWESSHRISHDESGFCTAKTPLQDSTFTRHPSTSVPSSPSTP
FT RHSGMDYHQSSSVASSESTASTVAAAAAAAAAASLNQHHHPHLYCDDGLLSRSLTDMVS
FT SGGYDSSSSSLSAAASMCYPTPDAYYYHAPPPPPPPQAQQGFSSTDAWLQMQMQPTYHN
FT FGSTVVSTNSPLPSHLLSYGGQPAFA -> MPLAYSTHDNFYESPKTPQPTWDHVHAQF
FT PLGEPARNLDKFIVPEAMFQSVSPLAGVAAAPSQIAALQQIQALMTFQMQQNNLFPKID
FT TISKSPTPELASPSAKRMRLSPSTSSHSDVASTSKGTNGQDQSKNSPTNS (in
FT isoform a)"
FT /id="VSP_060946"
FT VAR_SEQ 1..255
FT /note="MFSWRRGDCESQKEENRSEERKGEETIRFPTRSPFHCVLFLLTDGFVLHKPT
FT ASPTVGFSPTIFSFYYSRWESSHRISHDESGFCTAKTPLQDSTFTRHPSTSVPSSPSTP
FT RHSGMDYHQSSSVASSESTASTVAAAAAAAAAASLNQHHHPHLYCDDGLLSRSLTDMVS
FT SGGYDSSSSSLSAAASMCYPTPDAYYYHAPPPPPPPQAQQGFSSTDAWLQMQMQPTYHN
FT FGSTVVSTNSPLPSHLLSYGGQPAFA -> MPLAYSTHDNFYESPKTPQPTWDHVHAQF
FT PLGEPARNLDKFIEAMFQSVSPLAGVAAAPSQIAALQQIQALMTFQMQQNNLFPKIDTI
FT SKSPTPELASPSAKRMRLSPSTSSHSDVASTSKGTNGQDQSKNSPTNS (in
FT isoform b)"
FT /id="VSP_060947"
FT VAR_SEQ 1..255
FT /note="MFSWRRGDCESQKEENRSEERKGEETIRFPTRSPFHCVLFLLTDGFVLHKPT
FT ASPTVGFSPTIFSFYYSRWESSHRISHDESGFCTAKTPLQDSTFTRHPSTSVPSSPSTP
FT RHSGMDYHQSSSVASSESTASTVAAAAAAAAAASLNQHHHPHLYCDDGLLSRSLTDMVS
FT SGGYDSSSSSLSAAASMCYPTPDAYYYHAPPPPPPPQAQQGFSSTDAWLQMQMQPTYHN
FT FGSTVVSTNSPLPSHLLSYGGQPAFA -> MFQSVSPLAGVAAAPSQIAALQQIQALMT
FT FQMQQNNLFPKIDTISKSPTPELASPSAKRMRLSPSTSSHSDVASTSKGTNGQDQSKNS
FT PTNS (in isoform c)"
FT /id="VSP_060948"
FT MUTAGEN 743..790
FT /note="Missing: In q385; die as L1 larvae with cell
FT transformations that result in the loss of the excretory
FT cell, loss of the rectum and a twisted nose."
FT /evidence="ECO:0000269|PubMed:8625826"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 332..343
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:3BRD"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:3BRD"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:2FO1"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2FO1"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:1TTU"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:3BRD"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:2FO1"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:1TTU"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 531..537
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 557..562
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1TTU"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:1TTU"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:3BRD"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 611..619
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 631..636
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 653..667
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 681..688
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 695..701
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 707..711
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 718..722
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 725..729
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 733..736
FT /evidence="ECO:0007829|PDB:3BRD"
FT TURN 739..741
FT /evidence="ECO:0007829|PDB:3BRD"
FT HELIX 742..745
FT /evidence="ECO:0007829|PDB:3BRD"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 753..761
FT /evidence="ECO:0007829|PDB:3BRD"
FT STRAND 764..774
FT /evidence="ECO:0007829|PDB:3BRD"
SQ SEQUENCE 790 AA; 87732 MW; AB0EB34D3FCE4EC8 CRC64;
MFSWRRGDCE SQKEENRSEE RKGEETIRFP TRSPFHCVLF LLTDGFVLHK PTASPTVGFS
PTIFSFYYSR WESSHRISHD ESGFCTAKTP LQDSTFTRHP STSVPSSPST PRHSGMDYHQ
SSSVASSEST ASTVAAAAAA AAAASLNQHH HPHLYCDDGL LSRSLTDMVS SGGYDSSSSS
LSAAASMCYP TPDAYYYHAP PPPPPPQAQQ GFSSTDAWLQ MQMQPTYHNF GSTVVSTNSP
LPSHLLSYGG QPAFADPFYT IGQSTPNTSS FLDTSNSSFG APSTVVANPM TNYQLAFQAK
LGSLHSLIGD SVQSLTSDRM IDFLSNKEKY ECVISIFHAK VAQKSYGNEK RFFCPPPCIY
LIGQGWKLKK DRVAQLYKTL KASAQKDAAI ENDPIHEQQA TELVAYIGIG SDTSERQQLD
FSTGKVRHPG DQRQDPNIYD YCAAKTLYIS DSDKRKYFDL NAQFFYGCGM EIGGFVSQRI
KVISKPSKKK QSMKNTDCKY LCIASGTKVA LFNRLRSQTV STRYLHVEGN AFHASSTKWG
AFTIHLFDDE RGLQETDNFA VRDGFVYYGS VVKLVDSVTG IALPRLRIRK VDKQQVILDA
SCSEEPVSQL HKCAFQMIDN ELVYLCLSHD KIIQHQATAI NEHRHQINDG AAWTIISTDK
AEYRFFEAMG QVANPISPCP VVGSLEVDGH GEASRVELHG RDFKPNLKVW FGATPVETTF
RSEESLHCSI PPVSQVRNEQ THWMFTNRTT GDVEVPISLV RDDGVVYSSG LTFSYKSLER
HGPCRIVSNY
