NUMB_DROME
ID NUMB_DROME Reviewed; 556 AA.
AC P16554; B8A413; B8A419; Q8IPE9; Q961A6; Q9VLB8;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein numb;
GN Name=numb; ORFNames=CG3779;
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] (ISOFORMS MATERNAL AND ZYGOTIC), ALTERNATIVE
RP INITIATION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2752427; DOI=10.1016/0092-8674(89)90849-0;
RA Uemura T., Shepherd S., Ackerman L., Jan L.Y., Jan Y.N.;
RT "Numb, a gene required in determination of cell fate during sensory organ
RT formation in Drosophila embryos.";
RL Cell 58:349-360(1989).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE INITIATION.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MATERNAL AND ZYGOTIC).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-556 (ISOFORMS
RP MATERNAL/ZYGOTIC).
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18342578; DOI=10.1016/j.devcel.2008.03.004;
RA Bowman S.K., Rolland V., Betschinger J., Kinsey K.A., Emery G.,
RA Knoblich J.A.;
RT "The tumor suppressors Brat and Numb regulate transit-amplifying neuroblast
RT lineages in Drosophila.";
RL Dev. Cell 14:535-546(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-430; SER-537 AND SER-543, AND
RP 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 [8]
RP FUNCTION.
RX PubMed=24550111; DOI=10.1242/dev.106534;
RA Janssens D.H., Komori H., Grbac D., Chen K., Koe C.T., Wang H., Lee C.Y.;
RT "Earmuff restricts progenitor cell potential by attenuating the competence
RT to respond to self-renewal factors.";
RL Development 141:1036-1046(2014).
RN [9]
RP SUBCELLULAR LOCATION, DOMAIN, PHOSPHORYLATION, AND MUTAGENESIS OF
RP 15-GLY--LYS-86; 36-LYS-LYS-37; 46-ARG-ARG-47; SER-48; SER-52 AND
RP 54-ARG-ARG-55.
RX PubMed=26481050; DOI=10.1016/j.devcel.2015.09.016;
RA Bailey M.J., Prehoda K.E.;
RT "Establishment of Par-Polarized Cortical Domains via Phosphoregulated
RT Membrane Motifs.";
RL Dev. Cell 35:199-210(2015).
RN [10]
RP FUNCTION.
RX PubMed=28899667; DOI=10.1016/j.ydbio.2017.09.011;
RA Li X., Chen R., Zhu S.;
RT "bHLH-O proteins balance the self-renewal and differentiation of Drosophila
RT neural stem cells by regulating Earmuff expression.";
RL Dev. Biol. 431:239-251(2017).
RN [11]
RP STRUCTURE BY NMR OF 58-205.
RX PubMed=9846878; DOI=10.1038/4185;
RA Li S.-C., Zwahlen C., Vincent S.J., McGlade C.J., Kay L.E., Pawson T.,
RA Forman-Kay J.D.;
RT "Structure of a Numb PTB domain-peptide complex suggests a basis for
RT diverse binding specificity.";
RL Nat. Struct. Biol. 5:1075-1083(1998).
RN [12]
RP STRUCTURE BY NMR OF 67-201 IN COMPLEX WITH NAK, AND MUTAGENESIS OF ILE-144;
RP VAL-147; PHE-149 AND PHE-195.
RX PubMed=10747019; DOI=10.1093/emboj/19.7.1505;
RA Zwahlen C., Li S.-C., Kay L.E., Pawson T., Forman-Kay J.D.;
RT "Multiple modes of peptide recognition by the PTB domain of the cell fate
RT determinant Numb.";
RL EMBO J. 19:1505-1515(2000).
CC -!- FUNCTION: Required in determination of cell fate during sensory organ
CC formation in embryos (PubMed:2752427). Restricts developmental
CC potential and promote maturation of intermediary neuronal progenitor
CC (INP) cells probably acting as an antagonist of Notch signaling
CC (PubMed:24550111, PubMed:28899667, PubMed:18342578).
CC {ECO:0000269|PubMed:24550111, ECO:0000269|PubMed:2752427,
CC ECO:0000269|PubMed:28899667, ECO:0000303|PubMed:2752427}.
CC -!- SUBUNIT: Interacts with Nak. {ECO:0000269|PubMed:10747019}.
CC -!- INTERACTION:
CC P16554; Q05513: PRKCZ; Xeno; NbExp=2; IntAct=EBI-429581, EBI-295351;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2752427}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:18342578, ECO:0000269|PubMed:26481050}.
CC Cytoplasm {ECO:0000269|PubMed:26481050}. Note=In larval brain, shows
CC asymmetric localization and asymmetrically sized divisions in type II
CC secondary neuroblasts. {ECO:0000269|PubMed:18342578}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Zygotic; Synonyms=A;
CC IsoId=P16554-1; Sequence=Displayed;
CC Name=Maternal; Synonyms=B;
CC IsoId=P16554-2; Sequence=VSP_018787;
CC -!- DOMAIN: PTB domain recognizes multiple ligands by engaging different
CC amounts of surface area dictated by tertiary contacts rather than
CC primary sequence. This may allow interactions with a diverse set of
CC proteins during asymmetric division and specification of cell fate.
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC necessary and sufficient for interaction with phospholipids permitting
CC cortical localization (PubMed:26481050). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (PubMed:26481050). {ECO:0000269|PubMed:26481050}.
CC -!- PTM: Phosphorylated by aPKC which lowers lipid affinity and promotes
CC dissociation from the cell cortex. {ECO:0000269|PubMed:26481050}.
CC -!- DISRUPTION PHENOTYPE: In larval brain, leads to overgrowth and
CC defective differentiation halting the development of secondary
CC neuroblasts beyond the stage of immature type II intermediary neuronal
CC progenitors (INP). {ECO:0000269|PubMed:18342578}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93152.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M27815; AAA28730.1; -; mRNA.
DR EMBL; AE014134; AAF52776.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10693.1; -; Genomic_DNA.
DR EMBL; BT056305; ACL68752.1; -; mRNA.
DR EMBL; BT056311; ACL68758.1; -; mRNA.
DR EMBL; AY051728; AAK93152.1; ALT_INIT; mRNA.
DR PIR; A32466; A32466.
DR RefSeq; NP_001260291.1; NM_001273362.1. [P16554-1]
DR RefSeq; NP_523523.2; NM_078799.3. [P16554-1]
DR RefSeq; NP_723460.1; NM_164855.2. [P16554-2]
DR PDB; 1DDM; NMR; -; A=67-201.
DR PDB; 2NMB; NMR; -; A=58-205.
DR PDB; 5YI7; X-ray; 1.70 A; A/C=64-203.
DR PDB; 5YI8; X-ray; 2.00 A; A=64-203.
DR PDBsum; 1DDM; -.
DR PDBsum; 2NMB; -.
DR PDBsum; 5YI7; -.
DR PDBsum; 5YI8; -.
DR AlphaFoldDB; P16554; -.
DR BMRB; P16554; -.
DR SMR; P16554; -.
DR BioGRID; 60366; 48.
DR ELM; P16554; -.
DR IntAct; P16554; 8.
DR MINT; P16554; -.
DR STRING; 7227.FBpp0303726; -.
DR TCDB; 8.A.87.3.1; the tbc1 domain (tbc1) family.
DR iPTMnet; P16554; -.
DR PaxDb; P16554; -.
DR PRIDE; P16554; -.
DR DNASU; 34263; -.
DR EnsemblMetazoa; FBtr0079821; FBpp0079419; FBgn0002973. [P16554-2]
DR EnsemblMetazoa; FBtr0079822; FBpp0079420; FBgn0002973. [P16554-1]
DR EnsemblMetazoa; FBtr0339526; FBpp0308609; FBgn0002973. [P16554-1]
DR GeneID; 34263; -.
DR KEGG; dme:Dmel_CG3779; -.
DR UCSC; CG3779-RA; d. melanogaster. [P16554-1]
DR CTD; 8650; -.
DR FlyBase; FBgn0002973; numb.
DR VEuPathDB; VectorBase:FBgn0002973; -.
DR eggNOG; KOG3537; Eukaryota.
DR GeneTree; ENSGT00940000172612; -.
DR InParanoid; P16554; -.
DR OMA; IMPNATQ; -.
DR PhylomeDB; P16554; -.
DR Reactome; R-DME-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-DME-5632684; Hedgehog 'on' state.
DR SignaLink; P16554; -.
DR BioGRID-ORCS; 34263; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P16554; -.
DR GenomeRNAi; 34263; -.
DR PRO; PR:P16554; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002973; Expressed in adult Malpighian tubule (Drosophila) and 53 other tissues.
DR ExpressionAtlas; P16554; baseline and differential.
DR Genevisible; P16554; DM.
DR GO; GO:0045178; C:basal part of cell; TAS:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005112; F:Notch binding; IDA:FlyBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0035050; P:embryonic heart tube development; IGI:FlyBase.
DR GO; GO:0035883; P:enteroendocrine cell differentiation; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0061382; P:Malpighian tubule tip cell differentiation; IMP:FlyBase.
DR GO; GO:0042694; P:muscle cell fate specification; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:FlyBase.
DR GO; GO:0001920; P:negative regulation of receptor recycling; IMP:FlyBase.
DR GO; GO:0014019; P:neuroblast development; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0061320; P:pericardial nephrocyte differentiation; IMP:FlyBase.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:FlyBase.
DR GO; GO:0051960; P:regulation of nervous system development; IMP:FlyBase.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0045035; P:sensory organ precursor cell division; IMP:FlyBase.
DR GO; GO:0016360; P:sensory organ precursor cell fate determination; IDA:FlyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016698; Numb/numb-like.
DR InterPro; IPR010449; Numb_domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR47368; PTHR47368; 1.
DR Pfam; PF06311; NumbF; 1.
DR Pfam; PF00640; PID; 1.
DR PIRSF; PIRSF017607; Numb/numb-like; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; ATP-binding; Cytoplasm;
KW Developmental protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..556
FT /note="Protein numb"
FT /id="PRO_0000021869"
FT DOMAIN 81..208
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 15..86
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000269|PubMed:26481050"
FT REGION 519..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform Maternal)"
FT /evidence="ECO:0000303|PubMed:2752427, ECO:0000303|Ref.4"
FT /id="VSP_018787"
FT MUTAGEN 24..56
FT /note="Missing: Reduced cortical localization and increased
FT cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 36..37
FT /note="KK->DD: Slight reduction in cortical localization."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 46..47
FT /note="RR->DD: In 4R-D; phosphomimetic mutant that displays
FT decreased phospholipid binding and reduced cortical
FT localization; when associated with D-54 and D-55."
FT MUTAGEN 48
FT /note="S->A: In 2S-A; loss of phosphorylation. In the
FT presence of aPKC remains localized to the cell cortex and
FT does not display any decrease in phospholipid binding; when
FT associated with A-52."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 48
FT /note="S->D: In 2S-D; phosphomimetic mutant that displays
FT reduced cortical localization but no significant decrease
FT in phospholipid binding; when associated with D-52."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 52
FT /note="S->A: In 2S-A; loss of phosphorylation. In the
FT presence of aPKC remains localized to the cell cortex and
FT does not display any decrease in phospholipid binding; when
FT associated with A-48."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 52
FT /note="S->D: In 2S-D; phosphomimetic mutant that displays
FT reduced cortical localization but no significant decrease
FT in phospholipid binding; when associated with D-48."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 54..55
FT /note="RR->DD: In 4R-D; phosphomimetic mutant that displays
FT decreased phospholipid binding and reduced cortical
FT localization; when associated with D-46 and D-47."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 144
FT /note="I->A: Loss of binding affinity to Nak and drop in
FT binding to single helical peptide."
FT /evidence="ECO:0000269|PubMed:10747019"
FT MUTAGEN 147
FT /note="V->A: Loss of binding affinity to Nak and drop in
FT binding to single helical peptide."
FT /evidence="ECO:0000269|PubMed:10747019"
FT MUTAGEN 149
FT /note="F->V: Loss of binding affinity to Nak and single
FT helical peptide."
FT /evidence="ECO:0000269|PubMed:10747019"
FT MUTAGEN 195
FT /note="F->V: Loss of binding affinity to Nak and single
FT helical peptide."
FT /evidence="ECO:0000269|PubMed:10747019"
FT CONFLICT 322
FT /note="T -> A (in Ref. 1; AAA28730)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="G -> D (in Ref. 1; AAA28730)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="M -> L (in Ref. 1; AAA28730)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="L -> S (in Ref. 1; AAA28730)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="A -> T (in Ref. 1; AAA28730)"
FT /evidence="ECO:0000305"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2NMB"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1DDM"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:5YI7"
FT STRAND 82..96
FT /evidence="ECO:0007829|PDB:5YI7"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:5YI7"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1DDM"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:5YI7"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:5YI7"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5YI7"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5YI7"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5YI7"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:5YI7"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1DDM"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:5YI7"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:5YI7"
FT STRAND 171..182
FT /evidence="ECO:0007829|PDB:5YI7"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:5YI7"
SQ SEQUENCE 556 AA; 60614 MW; 91B26959B5DE8405 CRC64;
MGNSSSHTHE PLERGFTRGK FGDVKNGKSA SFRFSKKSPK KMDRLRRSFR DSFRRRKDRV
PESSKPHQWQ ADEEAVRSAT CSFSVKYLGC VEVFESRGMQ VCEEALKVLR QSRRRPVRGL
LHVSGDGLRV VDDETKGLIV DQTIEKVSFC APDRNHERGF SYICRDGTTR RWMCHGFLAC
KDSGERLSHA VGCAFAVCLE RKQRRDKECG VTMTFDTKNS TFTRTGSFRQ QTLTERLAMA
TVGTNERSVD GPGSAMPGPP AATVKPFNPF AIERPHATPN MLERQSSFRL STIGSQSPFK
RQMSLRINDL PSNADRQRAF LTAAAGNPMQ TPLRSVSPIA EVSPAKSAGA DPLSAAAVAA
DSVSQLCQEL SQGLSLLTQT DALLAAGEDL NFNNNRSINQ NIIAAEKQVQ HVHSYAPPTA
QVTPRVASTT PTYQTLHSQS PSRSEQSIET STELPNAEQW LGHVVRSTSP AAPKRPTYLA
NVGRAQTLAS GTGAAVGGGG PDDPFDAEWV ANVAAAKQLS PDLPIPSTAR SPLARHSTNP
FISPPKAPAQ SFQVQL
