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   27-MAR-2024, entry version 65.
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.K08B4.1d.1; -.
DR   PaxDb; 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   AGR; WB:WBGene00002245; -.
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. [V6CLJ5-1]
DR   eggNOG; KOG3743; Eukaryota.
DR   GeneTree; ENSGT00390000005197; -.
DR   HOGENOM; CLU_022207_1_0_1; -.
DR   InParanoid; V6CLJ5; -.
DR   OMA; SEQHLPR; -.
DR   OrthoDB; 1384914at2759; -.
DR   SignaLink; V6CLJ5; -.
DR   PRO; PR:V6CLJ5; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00002245; Expressed in embryo and 4 other cell types or tissues.
DR   ExpressionAtlas; V6CLJ5; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:1990433; C:CSL-Notch-Mastermind transcription factor complex; IPI:ComplexPortal.
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:0018991; P:egg-laying behavior; IMP: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:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; 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; 2.80.10.50; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.40.1450; LAG1, DNA binding domain; 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_sf.
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; RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS; 1.
DR   PANTHER; PTHR10665:SF0; SUPPRESSOR OF HAIRLESS PROTEIN; 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; DNA-binding protein LAG-1 (CSL); 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 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
//