SCM_DROME
ID SCM_DROME Reviewed; 877 AA.
AC Q9VHA0; Q24191;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Polycomb protein Scm;
DE AltName: Full=Sex comb on midleg protein;
GN Name=Scm {ECO:0000312|EMBL:AAF54419.2}; ORFNames=CG9495;
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] {ECO:0000305, ECO:0000312|EMBL:AAB57632.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:8625848};
RX PubMed=8625848; DOI=10.1242/dev.122.5.1621;
RA Bornemann D., Miller E., Simon J.A.;
RT "The Drosophila polycomb group gene Sex comb on midleg (Scm) encodes a zinc
RT finger protein with similarity to polyhomeotic protein.";
RL Development 122:1621-1630(1996).
RN [2] {ECO:0000312|EMBL:AAF54419.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF54419.2}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAN71320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAN71320.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [5] {ECO:0000305}
RP INTERACTION WITH PH-P, AND MUTAGENESIS OF ILE-834; GLY-836; 840-LEU-LEU-841
RP AND LYS-854.
RX PubMed=9343432; DOI=10.1128/mcb.17.11.6683;
RA Peterson A.J., Kyba M., Bornemann D., Morgan K., Brock H.W., Simon J.A.;
RT "A domain shared by the polycomb group proteins Scm and ph mediates
RT heterotypic and homotypic interactions.";
RL Mol. Cell. Biol. 17:6683-6692(1997).
RN [6] {ECO:0000305}
RP INTERACTION WITH CORTO.
RX PubMed=12771214; DOI=10.1093/nar/gkg381;
RA Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.;
RT "The Drosophila Corto protein interacts with Polycomb-group proteins and
RT the GAGA factor.";
RL Nucleic Acids Res. 31:2873-2882(2003).
RN [7] {ECO:0000305}
RP FUNCTION, ASSOCIATION WITH PRC1 COMPLEX, AND MUTAGENESIS OF GLU-816;
RP GLY-836; MET-846; MET-848; MET-851 AND LYS-860.
RX PubMed=15280237; DOI=10.1534/genetics.104.027474;
RA Peterson A.J., Mallin D.R., Francis N.J., Ketel C.S., Stamm J.,
RA Voeller R.K., Kingston R.E., Simon J.A.;
RT "Requirement for sex comb on midleg protein interactions in Drosophila
RT polycomb group repression.";
RL Genetics 167:1225-1239(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-546; SER-549; SER-550 AND
RP SER-585, AND IDENTIFICATION BY 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 [9] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 795-871, AND INTERACTION WITH
RP PH-P.
RX PubMed=15905166; DOI=10.1074/jbc.m503055200;
RA Kim C.A., Sawaya M.R., Cascio D., Kim W., Bowie J.U.;
RT "Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.";
RL J. Biol. Chem. 280:27769-27775(2005).
CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by forming
CC multiprotein complexes, which are required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development. PcG proteins are not required to initiate repression, but
CC to maintain it during later stages of development. They probably act
CC via the methylation of histones, rendering chromatin heritably changed
CC in its expressibility. {ECO:0000250|UniProtKB:Q9W3C1,
CC ECO:0000269|PubMed:15280237}.
CC -!- SUBUNIT: Scm associates with the PRC1 core complex containing PSC, PC,
CC PH and Sce/RING1. Forms homotypic and heterotypic interactions.
CC Interacts with the SAM domain of ph-p via its SAM domain in vitro.
CC Interacts with corto in vitro. {ECO:0000269|PubMed:12771214,
CC ECO:0000269|PubMed:15280237, ECO:0000269|PubMed:15905166,
CC ECO:0000269|PubMed:9343432}.
CC -!- INTERACTION:
CC Q9VHA0; P41046: corto; NbExp=2; IntAct=EBI-89256, EBI-300379;
CC Q9VHA0; P02299: His3:CG33854; NbExp=4; IntAct=EBI-89256, EBI-522090;
CC Q9VHA0; P39769: ph-p; NbExp=6; IntAct=EBI-89256, EBI-300360;
CC Q9VHA0; Q9VHA0: Scm; NbExp=4; IntAct=EBI-89256, EBI-89256;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Levels
CC are highest in 0-2 hours embryos and at lower levels during later
CC embryonic and larval stages. A modest increase in expression is seen
CC during the pupal stage. Expressed throughout the 9 hours embryo. After
CC 12 hours expression is concentrated in the central nervous system.
CC {ECO:0000269|PubMed:8625848}.
CC -!- DOMAIN: The SAM domain is essential for function.
CC {ECO:0000269|PubMed:15280237}.
CC -!- SIMILARITY: Belongs to the SCM family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U49793; AAB57632.1; -; mRNA.
DR EMBL; AE014297; AAF54419.2; -; Genomic_DNA.
DR EMBL; BT001565; AAN71320.1; -; mRNA.
DR RefSeq; NP_001247006.1; NM_001260077.2.
DR RefSeq; NP_731385.1; NM_169299.2.
DR PDB; 1PK1; X-ray; 1.80 A; B/D=795-871.
DR PDB; 1PK3; X-ray; 1.85 A; A/B/C=795-871.
DR PDB; 2R57; X-ray; 2.20 A; A=175-435.
DR PDB; 2R58; X-ray; 2.00 A; A=175-435.
DR PDB; 2R5A; X-ray; 2.30 A; A=175-435.
DR PDB; 2R5M; X-ray; 2.65 A; A=175-435.
DR PDB; 5J8Y; X-ray; 1.98 A; A/B=803-877.
DR PDBsum; 1PK1; -.
DR PDBsum; 1PK3; -.
DR PDBsum; 2R57; -.
DR PDBsum; 2R58; -.
DR PDBsum; 2R5A; -.
DR PDBsum; 2R5M; -.
DR PDBsum; 5J8Y; -.
DR AlphaFoldDB; Q9VHA0; -.
DR SMR; Q9VHA0; -.
DR BioGRID; 66327; 57.
DR DIP; DIP-17570N; -.
DR IntAct; Q9VHA0; 22.
DR MINT; Q9VHA0; -.
DR STRING; 7227.FBpp0081580; -.
DR iPTMnet; Q9VHA0; -.
DR PaxDb; Q9VHA0; -.
DR PRIDE; Q9VHA0; -.
DR EnsemblMetazoa; FBtr0082102; FBpp0081580; FBgn0003334.
DR EnsemblMetazoa; FBtr0306008; FBpp0297150; FBgn0003334.
DR GeneID; 41168; -.
DR KEGG; dme:Dmel_CG9495; -.
DR CTD; 41168; -.
DR FlyBase; FBgn0003334; Scm.
DR VEuPathDB; VectorBase:FBgn0003334; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000175826; -.
DR HOGENOM; CLU_015000_0_0_1; -.
DR InParanoid; Q9VHA0; -.
DR OMA; KILNNAM; -.
DR OrthoDB; 229086at2759; -.
DR PhylomeDB; Q9VHA0; -.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DME-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR SignaLink; Q9VHA0; -.
DR BioGRID-ORCS; 41168; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9VHA0; -.
DR GenomeRNAi; 41168; -.
DR PRO; PR:Q9VHA0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003334; Expressed in cleaving embryo and 27 other tissues.
DR ExpressionAtlas; Q9VHA0; baseline and differential.
DR Genevisible; Q9VHA0; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0140259; F:PRC1 complex binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0030708; P:germarium-derived female germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0022008; P:neurogenesis; IMP:FlyBase.
DR GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.90.1150.190; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR021987; SLED.
DR InterPro; IPR038348; SLED_sf.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR010507; Znf_MYM.
DR Pfam; PF02820; MBT; 2.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF12140; SLED; 1.
DR Pfam; PF06467; zf-FCS; 1.
DR SMART; SM00561; MBT; 2.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Developmental protein; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..877
FT /note="Polycomb protein Scm"
FT /id="PRO_0000114333"
FT REPEAT 175..273
FT /note="MBT 1"
FT /evidence="ECO:0000255"
FT REPEAT 281..382
FT /note="MBT 2"
FT /evidence="ECO:0000255"
FT DOMAIN 806..876
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 54..93
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 546
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 816
FT /note="E->G: No effect on function. Shows self- and ph-p
FT binding activity comparable to wild-type; when associated
FT with V-846 and R-860."
FT /evidence="ECO:0000269|PubMed:15280237"
FT MUTAGEN 834
FT /note="I->T: Complete loss of function. Significant loss of
FT self-binding activity. Moderate loss of ph-p binding
FT activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT MUTAGEN 836
FT /note="G->D: Complete loss of function. Complete loss of
FT self- and ph-p binding activity."
FT /evidence="ECO:0000269|PubMed:15280237,
FT ECO:0000269|PubMed:9343432"
FT MUTAGEN 836
FT /note="G->S: Loss of self- and ph-p binding activity."
FT /evidence="ECO:0000269|PubMed:15280237,
FT ECO:0000269|PubMed:9343432"
FT MUTAGEN 840..841
FT /note="LL->SS: Several-fold reduction of self-binding
FT activity. Partial loss of ph-p binding activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT MUTAGEN 846
FT /note="M->V: No effect on function. Shows self- and ph-p
FT binding activity comparable to wild-type; when associated
FT with G-816 and R-860."
FT /evidence="ECO:0000269|PubMed:15280237"
FT MUTAGEN 848
FT /note="Missing: Complete loss of function. Significant loss
FT of self-binding activity. Partial loss of ph-p binding
FT activity."
FT /evidence="ECO:0000269|PubMed:15280237"
FT MUTAGEN 851
FT /note="M->R: Complete loss of function. Complete loss of
FT self- and ph-p binding activity."
FT /evidence="ECO:0000269|PubMed:15280237"
FT MUTAGEN 854
FT /note="K->A: Partial loss of self- and ph-p binding
FT activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT MUTAGEN 860
FT /note="K->E: Complete loss of function. Partial loss of
FT self-binding activity. Complete loss of ph-p binding
FT activity."
FT /evidence="ECO:0000269|PubMed:15280237"
FT MUTAGEN 860
FT /note="K->R: No effect on function. Shows self- and ph-p
FT binding activity comparable to wild-type; when associated
FT with G-816 and V-846."
FT /evidence="ECO:0000269|PubMed:15280237"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 218..231
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2R58"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:2R58"
FT HELIX 797..800
FT /evidence="ECO:0007829|PDB:1PK3"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:1PK1"
FT HELIX 808..818
FT /evidence="ECO:0007829|PDB:1PK1"
FT HELIX 820..825
FT /evidence="ECO:0007829|PDB:1PK1"
FT HELIX 826..831
FT /evidence="ECO:0007829|PDB:1PK1"
FT HELIX 836..840
FT /evidence="ECO:0007829|PDB:1PK1"
FT HELIX 844..850
FT /evidence="ECO:0007829|PDB:1PK1"
FT HELIX 855..868
FT /evidence="ECO:0007829|PDB:1PK1"
SQ SEQUENCE 877 AA; 93551 MW; 7859FD0C7B91589E CRC64;
MSGGRDSSTS SGSNSAAPGA STNATSSASA SASSTSTSAS PGSTTSPAST QRQRGRPAKR
ATCTWCGEGK LPLQYVLPTQ TGKKEFCSET CIAEFRKAYS KGACTQCDNV IRDGAPNKEF
CSIMCMNKHQ KKNCSTRHSG GSASGKGLAE SERKLLASGA PAPTGPFQYE SFHVFDWDAY
LEETGSEAAP AKCFKQAQNP PNNDFKIGMK LEALDPRNVT STCIATVVGV LGSRLRLRLD
GSDSQNDFWR LVDSTEIHAI GHCEKNGGML QPPLGFRMNA SSWPGYLCKI LNNAMVAPEE
IFQPEPPEPE ENLFKVGQKL EAVDKKNPQL ICCATVDAIK DDQIHVTFDG WRGAFDYWCN
YRSRDIFPAG WCARSCHPMQ PPGHKSRMDS SSSKQRCPRP RYTVVAESEA MVPASPATAH
FHPNCKGGPF INNSKLPCMV TGPTYQTLAK LCLQEVLAAS TDTQQLSKLL FALEGDVHIV
TAAGKNFTVK IPSPMRMKDD ESLAQFIETL CTTCRACANL ISLVHETEEC KKCANSRKRQ
LTQSATPPSS PVLADKRNRQ SNSATTSPSE KIIKQELAVK SPVESKSKTS TNNGKEPASQ
QNSNHSLNNN NNSASKSSNK VVIKSEPNGA NAQTSSTTQA LRKVRFQHHA NTNTNSSATN
GNQDTSQTTH VSTSHCSSSS TSSSTSLAGG SANTSTIGKY LAPLVAEVHP EQANVKPSNS
YYKSPTTLSS SASLPTSVST PFTGCQSASS TALAAGGVTA AKAATAPAGA AATAGASPSY
TAITSPVSTP TSALANSHLR SQPIDWTIEE VIQYIESNDN SLAVHGDLFR KHEIDGKALL
LLNSEMMMKY MGLKLGPALK ICNLVNKVNG RRNNLAL
