HIPPO_DROME
ID HIPPO_DROME Reviewed; 669 AA.
AC Q8T0S6; Q9V8W4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Serine/threonine-protein kinase hippo;
DE EC=2.7.11.1;
DE AltName: Full=Drosophila homolog of MST1 and MST2;
DE AltName: Full=STE20-like kinase MST;
DE AltName: Full=dMST;
GN Name=hpo; ORFNames=CG11228;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH SAV AND WTS.
RX PubMed=12941274; DOI=10.1016/s0092-8674(03)00557-9;
RA Harvey K.F., Pfleger C.M., Hariharan I.K.;
RT "The Drosophila Mst ortholog, hippo, restricts growth and cell
RT proliferation and promotes apoptosis.";
RL Cell 114:457-467(2003).
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.
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].
RC STRAIN=Berkeley; TISSUE=Head;
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]
RP TISSUE SPECIFICITY.
RX PubMed=11900973; DOI=10.1016/s0925-4773(02)00010-2;
RA Brody T., Stivers C., Nagle J., Odenwald W.F.;
RT "Identification of novel Drosophila neural precursor genes using a
RT differential embryonic head cDNA screen.";
RL Mech. Dev. 113:41-59(2002).
RN [6]
RP INDUCTION.
RX PubMed=12091301; DOI=10.1242/dev.129.14.3295;
RA Egger B., Leemans R., Loop T., Kammermeier L., Fan Y., Radimerski T.,
RA Strahm M.C., Certa U., Reichert H.;
RT "Gliogenesis in Drosophila: genome-wide analysis of downstream genes of
RT glial cells missing in the embryonic nervous system.";
RL Development 129:3295-3309(2002).
RN [7]
RP FUNCTION IN PHOSPHORYLATION OF SAV AND WTS, MUTANT HPO42-47, AND
RP MUTAGENESIS OF LYS-71.
RX PubMed=12941273; DOI=10.1016/s0092-8674(03)00549-x;
RA Wu S., Huang J., Dong J., Pan D.;
RT "hippo encodes a Ste-20 family protein kinase that restricts cell
RT proliferation and promotes apoptosis in conjunction with salvador and
RT warts.";
RL Cell 114:445-456(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH SAV AND WTS.
RX PubMed=14561774; DOI=10.1101/gad.1134003;
RA Jia J., Zhang W., Wang B., Trinko R., Jiang J.;
RT "The Drosophila Ste20 family kinase dMST functions as a tumor suppressor by
RT restricting cell proliferation and promoting apoptosis.";
RL Genes Dev. 17:2514-2519(2003).
RN [9]
RP FUNCTION, HOMODIMERIZATION, AND INTERACTION WITH SAV.
RX PubMed=14502294; DOI=10.1038/ncb1050;
RA Udan R.S., Kango-Singh M., Nolo R., Tao C., Halder G.;
RT "Hippo promotes proliferation arrest and apoptosis in the Salvador/Warts
RT pathway.";
RL Nat. Cell Biol. 5:914-920(2003).
RN [10]
RP FUNCTION, AUTOPHOSPHORYLATION, AND INTERACTION WITH SAV.
RX PubMed=14502295; DOI=10.1038/ncb1051;
RA Pantalacci S., Tapon N., Leopold P.;
RT "The Salvador partner Hippo promotes apoptosis and cell-cycle exit in
RT Drosophila.";
RL Nat. Cell Biol. 5:921-927(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-33, 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 [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KIBRA; EX AND SAV.
RX PubMed=20159598; DOI=10.1016/j.devcel.2009.12.012;
RA Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.;
RT "Kibra functions as a tumor suppressor protein that regulates Hippo
RT signaling in conjunction with Merlin and Expanded.";
RL Dev. Cell 18:288-299(2010).
RN [13]
RP PHOSPHORYLATION AT THR-195, AND MUTAGENESIS OF THR-195.
RX PubMed=22075147; DOI=10.1016/j.devcel.2011.08.028;
RA Boggiano J.C., Vanderzalm P.J., Fehon R.G.;
RT "Tao-1 phosphorylates Hippo/MST kinases to regulate the Hippo-Salvador-
RT Warts tumor suppressor pathway.";
RL Dev. Cell 21:888-895(2011).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=26954546; DOI=10.1016/j.devcel.2016.02.004;
RA Chung H.L., Augustine G.J., Choi K.W.;
RT "Drosophila Schip1 links Expanded and Tao-1 to regulate hippo signaling.";
RL Dev. Cell 36:511-524(2016).
CC -!- FUNCTION: Plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling
CC pathway, a signaling pathway that plays a pivotal role in organ size
CC control and tumor suppression by restricting proliferation and
CC promoting apoptosis. The core of this pathway is composed of a kinase
CC cascade wherein Hippo (Hpo), in complex with its regulatory protein
CC Salvador (Sav), phosphorylates and activates Warts (Wts) in complex
CC with its regulatory protein Mats, which in turn phosphorylates and
CC inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling
CC pathway inhibits the activity of the transcriptional complex formed by
CC Scalloped (sd) and Yki and the target genes of this pathway include
CC cyclin-E (cycE), diap1 and bantam. Phosphorylates Sav, Wts and
CC Th/DIAP1. Regulates the level of Th/DIAP1 apoptosis inhibitor.
CC {ECO:0000269|PubMed:12941273, ECO:0000269|PubMed:12941274,
CC ECO:0000269|PubMed:14502294, ECO:0000269|PubMed:14502295,
CC ECO:0000269|PubMed:14561774}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Homodimer. Interacts with Sav and Wts. Interacts (via SARAH
CC domain) with Ex. Interacts with Kibra. {ECO:0000269|PubMed:12941274,
CC ECO:0000269|PubMed:14502294, ECO:0000269|PubMed:14502295,
CC ECO:0000269|PubMed:14561774, ECO:0000269|PubMed:20159598}.
CC -!- INTERACTION:
CC Q8T0S6; Q95RA8: mats; NbExp=2; IntAct=EBI-101858, EBI-143689;
CC Q8T0S6; Q6NPA6: par-1; NbExp=3; IntAct=EBI-101858, EBI-3415099;
CC Q8T0S6; Q9VCR6: sav; NbExp=3; IntAct=EBI-101858, EBI-145004;
CC Q8T0S6; Q9NBK5-2: trc; NbExp=2; IntAct=EBI-101858, EBI-15596484;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:26954546}. Cytoplasm
CC {ECO:0000269|PubMed:26954546}.
CC -!- TISSUE SPECIFICITY: Expressed in CNS during embryogenesis. In third
CC instar larvae, it is expressed throughout all imaginal disks.
CC {ECO:0000269|PubMed:11900973, ECO:0000269|PubMed:12941274}.
CC -!- INDUCTION: Transcriptionally regulated by Gcm (Glial cells missing).
CC {ECO:0000269|PubMed:12091301}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AE013599; AAF57543.2; -; Genomic_DNA.
DR EMBL; AY069088; AAL39233.1; -; mRNA.
DR RefSeq; NP_001261092.1; NM_001274163.1.
DR RefSeq; NP_611427.1; NM_137583.5.
DR PDB; 6BN1; X-ray; 2.60 A; A=606-662.
DR PDBsum; 6BN1; -.
DR AlphaFoldDB; Q8T0S6; -.
DR SMR; Q8T0S6; -.
DR BioGRID; 62905; 99.
DR DIP; DIP-17921N; -.
DR IntAct; Q8T0S6; 11.
DR MINT; Q8T0S6; -.
DR STRING; 7227.FBpp0304253; -.
DR iPTMnet; Q8T0S6; -.
DR PaxDb; Q8T0S6; -.
DR PRIDE; Q8T0S6; -.
DR DNASU; 37247; -.
DR EnsemblMetazoa; FBtr0086500; FBpp0085688; FBgn0261456.
DR EnsemblMetazoa; FBtr0331920; FBpp0304253; FBgn0261456.
DR GeneID; 37247; -.
DR KEGG; dme:Dmel_CG11228; -.
DR UCSC; CG11228-RA; d. melanogaster.
DR CTD; 37247; -.
DR FlyBase; FBgn0261456; hpo.
DR VEuPathDB; VectorBase:FBgn0261456; -.
DR eggNOG; KOG0574; Eukaryota.
DR GeneTree; ENSGT00940000154984; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q8T0S6; -.
DR OMA; QRMANLD; -.
DR OrthoDB; 967913at2759; -.
DR PhylomeDB; Q8T0S6; -.
DR Reactome; R-DME-390089; Formation of the Hippo kinase cassette.
DR Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
DR Reactome; R-DME-390150; DS ligand bound to FT receptor.
DR Reactome; R-DME-451806; Phosphorylation-independent inhibition of YKI.
DR SignaLink; Q8T0S6; -.
DR BioGRID-ORCS; 37247; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37247; -.
DR PRO; PR:Q8T0S6; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261456; Expressed in wing disc and 24 other tissues.
DR ExpressionAtlas; Q8T0S6; baseline and differential.
DR Genevisible; Q8T0S6; DM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0106037; C:apicomedial cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0001654; P:eye development; IMP:FlyBase.
DR GO; GO:0035329; P:hippo signaling; IDA:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IGI:FlyBase.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:FlyBase.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0035265; P:organ growth; IDA:FlyBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:2001233; P:regulation of apoptotic signaling pathway; IMP:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0070613; P:regulation of protein processing; IDA:FlyBase.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:FlyBase.
DR GO; GO:0046666; P:retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0072089; P:stem cell proliferation; IDA:FlyBase.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024205; Mst1_SARAH_domain.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011524; SARAH_dom.
DR Pfam; PF11629; Mst1_SARAH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50951; SARAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..669
FT /note="Serine/threonine-protein kinase hippo"
FT /id="PRO_0000086001"
FT DOMAIN 42..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 608..655
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT REGION 432..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 195
FT /note="Phosphothreonine; by Tao"
FT /evidence="ECO:0000269|PubMed:22075147"
FT MUTAGEN 71
FT /note="K->R: Abolishes phosphorylation of Sav."
FT /evidence="ECO:0000269|PubMed:12941273"
FT MUTAGEN 166..171
FT /note="Missing: In hpo42-47; null mutant."
FT MUTAGEN 195
FT /note="T->A: Abolishes phosphorylation by Tao."
FT /evidence="ECO:0000269|PubMed:22075147"
FT CONFLICT 503
FT /note="Q -> QQQQ (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 609..613
FT /evidence="ECO:0007829|PDB:6BN1"
FT HELIX 616..658
FT /evidence="ECO:0007829|PDB:6BN1"
SQ SEQUENCE 669 AA; 75110 MW; B3DDDFAF5F4E4EB3 CRC64;
MSEPEVTSVV DMKSPNISSS CSFFKLKKLS EESLLQPPEK VFDIMYKLGE GSYGSVYKAV
HKESSSIVAI KLVPVESDLH EIIKEISIMQ QCDSPYVVRY YGSYFKQYDL WICMEYCGAG
SVSDIMRLRK KTLTEDEIAT ILSDTLQGLV YLHLRRKIHR DIKAANILLN TEGYAKLADF
GVAGQLTDTM AKRNTVIGTP FWMAPEVIEE IGYDCVADIW SLGITALEMA EGKPPYGEIH
PMRAIFMIPQ KPPPSFREPD RWSTEFIDFV SKCLVKEPDD RATATELLEH EFIRNAKHRS
ILKPMLEETC AIREQQRANR SFGGVLAASQ AKSLATQENG MQQHITDNAF MEDPGTLVPE
KFGEYQQSSA SDATMIAHAE QGVDEGTLGP GGLRNLSKAA APAAASSAAS PLDMPAVDSG
TMVELESNLG TMVINSDSDD STTAKNNDDQ KPRNRYRPQF LEHFDRKNAG DGRGDEKPIA
TEYSPAAAEQ QQQQQQQQQQ QQQDEQHLAS GANDLNNWEH NMEMQFQQIS AINQYGLQQH
QQQQQVLMAY PLMNEQLIAL NNQPNLLLSN AAPMGQQGIP AAAPAQPPPA YQNQHMHTQS
HAYVEGEFEF LKFLTFDDLN QRLCNIDHEM ELEIEQLNKK YNAKRQPIVD AMNAKRKRQQ
NINNNLIKI
