VPS15_YEAST
ID VPS15_YEAST Reviewed; 1454 AA.
AC P22219; D6VQ98;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Serine/threonine-protein kinase VPS15;
DE EC=2.7.11.1;
DE AltName: Full=Golgi-retention defective mutant protein 8;
DE AltName: Full=Vacuolar protein sorting-associated protein 15;
GN Name=VPS15; Synonyms=GRD8, VAC4, VPL19; OrderedLocusNames=YBR097W;
GN ORFNames=YBR0825;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF ASP-165 AND GLU-200, AND AUTOPHOSPHORYLATION.
RX PubMed=1988155; DOI=10.1016/0092-8674(91)90650-n;
RA Herman P.K., Stack J.H., Demodena J.A., Emr S.D.;
RT "A novel protein kinase homolog essential for protein sorting to the yeast
RT lysosome-like vacuole.";
RL Cell 64:425-437(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 134 AND 851.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=3062374; DOI=10.1128/mcb.8.11.4936-4948.1988;
RA Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.;
RT "Protein sorting in Saccharomyces cerevisiae: isolation of mutants
RT defective in the delivery and processing of multiple vacuolar hydrolases.";
RL Mol. Cell. Biol. 8:4936-4948(1988).
RN [6]
RP FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-2; LYS-54; ASP-147;
RP LYS-149 AND GLU-151, AND MYRISTOYLATION AT GLY-2.
RX PubMed=1756716; DOI=10.1002/j.1460-2075.1991.tb04981.x;
RA Herman P.K., Stack J.H., Emr S.D.;
RT "A genetic and structural analysis of the yeast Vps15 protein kinase:
RT evidence for a direct role of Vps15p in vacuolar protein delivery.";
RL EMBO J. 10:4049-4060(1991).
RN [7]
RP FUNCTION, INTERACTION WITH VPS34, AND MUTAGENESIS OF GLU-200.
RX PubMed=8387919; DOI=10.1002/j.1460-2075.1993.tb05867.x;
RA Stack J.H., Herman P.K., Schu P.V., Emr S.D.;
RT "A membrane-associated complex containing the Vps15 protein kinase and the
RT Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-
RT like vacuole.";
RL EMBO J. 12:2195-2204(1993).
RN [8]
RP FUNCTION.
RX PubMed=8509446; DOI=10.1083/jcb.121.6.1245;
RA Vida T.A., Huyer G., Emr S.D.;
RT "Yeast vacuolar proenzymes are sorted in the late Golgi complex and
RT transported to the vacuole via a prevacuolar endosome-like compartment.";
RL J. Cell Biol. 121:1245-1256(1993).
RN [9]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=7989323; DOI=10.1016/s0021-9258(18)31729-0;
RA Stack J.H., Emr S.D.;
RT "Vps34p required for yeast vacuolar protein sorting is a multiple
RT specificity kinase that exhibits both protein kinase and
RT phosphatidylinositol-specific PI 3-kinase activities.";
RL J. Biol. Chem. 269:31552-31562(1994).
RN [10]
RP FUNCTION.
RX PubMed=8649377; DOI=10.1128/mcb.16.6.2700;
RA Nothwehr S.F., Bryant N.J., Stevens T.H.;
RT "The newly identified yeast GRD genes are required for retention of late-
RT Golgi membrane proteins.";
RL Mol. Cell. Biol. 16:2700-2707(1996).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS30; VPS34; VPS38
RP AND ATG14.
RX PubMed=11157979; DOI=10.1083/jcb.152.3.519;
RA Kihara A., Noda T., Ishihara N., Ohsumi Y.;
RT "Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in
RT autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae.";
RL J. Cell Biol. 152:519-530(2001).
RN [12]
RP FUNCTION.
RX PubMed=12244127; DOI=10.1242/jcs.00090;
RA Burda P., Padilla S.M., Sarkar S., Emr S.D.;
RT "Retromer function in endosome-to-Golgi retrograde transport is regulated
RT by the yeast Vps34 PtdIns 3-kinase.";
RL J. Cell Sci. 115:3889-3900(2002).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [14]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP AUTOPHAGY-SPECIFIC VPS34 PI3-KINASE COMPLEX I.
RX PubMed=24165940; DOI=10.1083/jcb.201304123;
RA Araki Y., Ku W.C., Akioka M., May A.I., Hayashi Y., Arisaka F.,
RA Ishihama Y., Ohsumi Y.;
RT "Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase
RT complex integrity.";
RL J. Cell Biol. 203:299-313(2013).
RN [16]
RP DISRUPTION PHENOTYPE.
RX PubMed=28483912; DOI=10.1128/mcb.00075-17;
RA Tanigawa M., Maeda T.;
RT "An In Vitro TORC1 Kinase Assay That Recapitulates the Gtr-Independent
RT Glutamine-Responsive TORC1 Activation Mechanism on Yeast Vacuoles.";
RL Mol. Cell. Biol. 37:e00075-e00075(2017).
CC -!- FUNCTION: Serine/threonine-protein kinase required for cytoplasm to
CC vacuole transport (Cvt) and autophagy as a part of the autophagy-
CC specific VPS34 PI3-kinase complex I. This complex is essential to
CC recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5
CC conjugate to the pre-autophagosomal structure. Is also involved in
CC endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase
CC complex II. This second complex is required for the endosome-to-Golgi
CC retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two
CC components of the retromer complex, to endosomal membranes (probably
CC through the synthesis of a specific pool of phosphatidylinositol 3-
CC phosphate recruiting the retromer to the endosomes). By regulating
CC VPS34 kinase activity, VPS15 appears to be essential for the efficient
CC delivery of soluble hydrolases to the yeast vacuole.
CC {ECO:0000269|PubMed:11157979, ECO:0000269|PubMed:12244127,
CC ECO:0000269|PubMed:1756716, ECO:0000269|PubMed:1988155,
CC ECO:0000269|PubMed:3062374, ECO:0000269|PubMed:7989323,
CC ECO:0000269|PubMed:8387919, ECO:0000269|PubMed:8509446,
CC ECO:0000269|PubMed:8649377}.
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: Component of the autophagy-specific VPS34 PI3-kinase complex I
CC composed of VPS15, VPS30, VPS34, ATG14 and ATG38; and of the VPS34 PI3-
CC kinase complex II composed of VPS15, VPS30, VPS34 and VPS38.
CC {ECO:0000269|PubMed:24165940}.
CC -!- INTERACTION:
CC P22219; P08539: GPA1; NbExp=2; IntAct=EBI-20347, EBI-7376;
CC P22219; P22543: VPS34; NbExp=3; IntAct=EBI-20347, EBI-20405;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:11157979, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:1988155}; Lipid-anchor {ECO:0000269|PubMed:1756716}.
CC Endosome membrane {ECO:0000269|PubMed:11157979,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1988155}; Lipid-anchor
CC {ECO:0000269|PubMed:1756716}.
CC -!- DOMAIN: Truncation of 30 residues from the C-terminus results in a
CC temperature-conditional defect in protein sorting.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Decreases TORC1 activation in response to
CC glutamine. {ECO:0000269|PubMed:28483912}.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M59835; AAA35214.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55602.1; -; Genomic_DNA.
DR EMBL; Z35966; CAA85050.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07218.2; -; Genomic_DNA.
DR PIR; S48264; S48264.
DR RefSeq; NP_009655.2; NM_001178445.2.
DR PDB; 3GRE; X-ray; 1.80 A; A=1027-1454.
DR PDB; 5DFZ; X-ray; 4.40 A; B=1-1454.
DR PDB; 5KC2; EM; 28.00 A; B=1-1454.
DR PDBsum; 3GRE; -.
DR PDBsum; 5DFZ; -.
DR PDBsum; 5KC2; -.
DR AlphaFoldDB; P22219; -.
DR SMR; P22219; -.
DR BioGRID; 32803; 101.
DR ComplexPortal; CPX-1677; Phosphatidylinositol 3-kinase complex II.
DR ComplexPortal; CPX-1881; Phosphatidylinositol 3-kinase complex, class III, type I.
DR DIP; DIP-814N; -.
DR IntAct; P22219; 9.
DR MINT; P22219; -.
DR STRING; 4932.YBR097W; -.
DR iPTMnet; P22219; -.
DR MaxQB; P22219; -.
DR PaxDb; P22219; -.
DR PRIDE; P22219; -.
DR EnsemblFungi; YBR097W_mRNA; YBR097W; YBR097W.
DR GeneID; 852394; -.
DR KEGG; sce:YBR097W; -.
DR SGD; S000000301; VPS15.
DR VEuPathDB; FungiDB:YBR097W; -.
DR eggNOG; KOG1240; Eukaryota.
DR GeneTree; ENSGT00390000016225; -.
DR HOGENOM; CLU_001696_0_1_1; -.
DR InParanoid; P22219; -.
DR OMA; TIVCENG; -.
DR BioCyc; YEAST:G3O-29061-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SCE-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-SCE-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-SCE-5668599; RHO GTPases Activate NADPH Oxidases.
DR EvolutionaryTrace; P22219; -.
DR PRO; PR:P22219; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P22219; protein.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IC:ComplexPortal.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IDA:SGD.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IDA:SGD.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IDA:ComplexPortal.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IMP:SGD.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045162; Vps15-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17583; PTHR17583; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Autophagy; Endosome; Golgi apparatus; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..1454
FT /note="Serine/threonine-protein kinase VPS15"
FT /id="PRO_0000086802"
FT DOMAIN 27..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 460..497
FT /note="HEAT 1"
FT REPEAT 576..613
FT /note="HEAT 2"
FT REPEAT 615..652
FT /note="HEAT 3"
FT REPEAT 654..691
FT /note="HEAT 4"
FT REPEAT 1078..1118
FT /note="WD 1"
FT REPEAT 1126..1165
FT /note="WD 2"
FT REPEAT 1229..1268
FT /note="WD 3"
FT REPEAT 1275..1315
FT /note="WD 4"
FT REPEAT 1344..1382
FT /note="WD 5"
FT REPEAT 1422..1453
FT /note="WD 6"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT BINDING 33..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:1756716"
FT MUTAGEN 2
FT /note="G->A,W: No myristoylation, but still membrane-
FT association and normal activity."
FT /evidence="ECO:0000269|PubMed:1756716"
FT MUTAGEN 54
FT /note="K->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1756716"
FT MUTAGEN 147
FT /note="D->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1756716"
FT MUTAGEN 149
FT /note="K->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1756716"
FT MUTAGEN 151
FT /note="E->R: Modest effect on activity and normal CPY
FT sorting."
FT /evidence="ECO:0000269|PubMed:1756716"
FT MUTAGEN 165
FT /note="D->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1988155"
FT MUTAGEN 200
FT /note="E->R: Loss of activity. No activation of VPS34
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:1988155,
FT ECO:0000269|PubMed:8387919"
FT CONFLICT 134
FT /note="A -> T (in Ref. 2; CAA55602 and 3; CAA85050)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="L -> PV (in Ref. 1; AAA35214)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="F -> S (in Ref. 1; AAA35214)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="R -> I (in Ref. 1; AAA35214, 2; CAA55602 and 3;
FT CAA85050)"
FT /evidence="ECO:0000305"
FT HELIX 1034..1036
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1046..1048
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1050..1052
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1064..1066
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1070..1075
FT /evidence="ECO:0007829|PDB:3GRE"
FT TURN 1077..1080
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1083..1089
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1091..1093
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1095..1100
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1103..1109
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1110..1114
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1122..1126
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1131..1136
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1140..1147
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1150..1162
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1165..1178
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1179..1182
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1188..1195
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1200..1206
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1209..1215
FT /evidence="ECO:0007829|PDB:3GRE"
FT TURN 1216..1218
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1221..1226
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1229..1231
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1234..1239
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1245..1250
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1255..1259
FT /evidence="ECO:0007829|PDB:3GRE"
FT TURN 1260..1263
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1264..1270
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1275..1282
FT /evidence="ECO:0007829|PDB:3GRE"
FT TURN 1284..1286
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1290..1297
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1300..1306
FT /evidence="ECO:0007829|PDB:3GRE"
FT TURN 1307..1310
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1311..1321
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1325..1328
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1335..1337
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1346..1349
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1352..1355
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1358..1363
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1364..1366
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1368..1373
FT /evidence="ECO:0007829|PDB:3GRE"
FT HELIX 1377..1379
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1381..1384
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1392..1399
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1402..1408
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1427..1445
FT /evidence="ECO:0007829|PDB:3GRE"
FT STRAND 1450..1454
FT /evidence="ECO:0007829|PDB:3GRE"
SQ SEQUENCE 1454 AA; 166372 MW; 247EBA5531E41FFB CRC64;
MGAQLSLVVQ ASPSIAIFSY IDVLEEVHYV SQLNSSRFLK TCKALDPNGE IVIKVFIKPK
DQYSLRPFLQ RIRAQSFKLG QLPHVLNYSK LIETNRAGYM IRQHLKNNLY DRLSLRPYLQ
DIELKFIAFQ LLNALKDIHN LNIVHGDIKT ENILVTSWNW CILTDFAAFI KPVYLPEDNP
GEFLFYFDTS KRRTCYLAPE RFNSKLYQDG KSNNGRLTKE MDIFSLGCVI AEIFAEGRPI
FNLSQLFKYK SNSYDVNREF LMEEMNSTDL RNLVLDMIQL DPSKRLSCDE LLNKYRGIFF
PDYFYTFIYD YFRNLVTMTT STPISDNTCT NSTLEDNVKL LDETTEKIYR DFSQICHCLD
FPLIKDGGEI GSDPPILESY KIEIEISRFL NTNLYFPQNY HLVLQQFTKV SEKIKSVKEE
CALLFISYLS HSIRSIVSTA TKLKNLELLA VFAQFVSDEN KIDRVVPYFV CCFEDSDQDV
QALSLLTLIQ VLTSVRKLNQ LNENIFVDYL LPRLKRLLIS NRQNTNYLRI VFANCLSDLA
IIINRFQEFT FAQHCNDNSM DNNTEIMESS TKYSAKLIQS VEDLTVSFLT DNDTYVKMAL
LQNILPLCKF FGRERTNDII LSHLITYLND KDPALRVSLI QTISGISILL GTVTLEQYIL
PLLIQTITDS EELVVISVLQ SLKSLFKTGL IRKKYYIDIS KTTSPLLLHP NNWIRQFTLM
IIIEIINKLS KAEVYCILYP IIRPFFEFDV EFNFKSMISC CKQPVSRSVY NLLCSWSVRA
SKSLFWKKII TNHVDSFGNN RIEFITKNYS SKNYGFNKRD TKSSSSLKGI KTSSTVYSHD
NKEIPLTAED RNWIDKFHII GLTEKDIWKI VALRGYVIRT ARVMAANPDF PYNNSNYRPL
VQNSPPNLNL TNIMPRNIFF DVEFAEESTS EGQDSNLENQ QIYKYDESEK DSNKLNINGS
KQLSTVMDIN GSLIFKNKSI ATTTSNLKNV FVQLEPTSYH MHSPNHGLKD NANVKPERKV
VVSNSYEGDV ESIEKFLSTF KILPPLRDYK EFGPIQEIVR SPNMGNLRGK LIATLMENEP
NSITSSAVSP GETPYLITGS DQGVIKIWNL KEIIVGEVYS SSLTYDCSST VTQITMIPNF
DAFAVSSKDG QIIVLKVNHY QQESEVKFLN CECIRKINLK NFGKNEYAVR MRAFVNEEKS
LLVALTNLSR VIIFDIRTLE RLQIIENSPR HGAVSSICID EECCVLILGT TRGIIDIWDI
RFNVLIRSWS FGDHAPITHV EVCQFYGKNS VIVVGGSSKT FLTIWNFVKG HCQYAFINSD
EQPSMEHFLP IEKGLEELNF CGIRSLNALS TISVSNDKIL LTDEATSSIV MFSLNELSSS
KAVISPSRFS DVFIPTQVTA NLTMLLRKMK RTSTHSVDDS LYHHDIINSI STCEVDETPL
LVACDNSGLI GIFQ
