VPS15_ARATH
ID VPS15_ARATH Reviewed; 1494 AA.
AC Q9M0E5;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase VPS15 {ECO:0000303|PubMed:21833541};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Vacuolar protein sorting-associated protein 15 {ECO:0000303|PubMed:21833541};
DE Short=AtVPS15 {ECO:0000303|PubMed:21833541};
GN Name=VPS15 {ECO:0000303|PubMed:21833541};
GN OrderedLocusNames=At4g29380 {ECO:0000312|Araport:AT4G29380};
GN ORFNames=F17A13.200 {ECO:0000312|EMBL:CAB79696.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=21833541; DOI=10.1007/s11103-011-9806-9;
RA Xu N., Gao X.-Q., Zhao X.Y., Zhu D.Z., Zhou L.Z., Zhang X.S.;
RT "Arabidopsis AtVPS15 is essential for pollen development and germination
RT through modulating phosphatidylinositol 3-phosphate formation.";
RL Plant Mol. Biol. 77:251-260(2011).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH VPS34,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22361507; DOI=10.1016/j.jgg.2012.01.002;
RA Wang W.-Y., Zhang L., Xing S., Ma Z., Liu J., Gu H., Qin G., Qu L.-J.;
RT "Arabidopsis AtVPS15 plays essential roles in pollen germination possibly
RT by interacting with AtVPS34.";
RL J. Genet. Genomics 39:81-92(2012).
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 (By similarity). Required for
CC pollen development and germination, probably via the modulation of
CC phosphatidylinositol 3-phosphate (PI3P) formation and vacuolar
CC organization (PubMed:21833541, PubMed:22361507).
CC {ECO:0000250|UniProtKB:P22219, ECO:0000269|PubMed:21833541,
CC ECO:0000269|PubMed:22361507}.
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with VPS34. {ECO:0000269|PubMed:22361507}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21833541}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P22219};
CC Lipid-anchor {ECO:0000250|UniProtKB:P22219}. Endosome membrane
CC {ECO:0000269|PubMed:22361507}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P22219}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in anthers, pollen grains and
CC pollen tubes, and, to a lower extent, in other tissues and organs
CC including seedlings, roots, stems, leaves, flowers, pitils and
CC siliques. {ECO:0000269|PubMed:21833541, ECO:0000269|PubMed:22361507}.
CC -!- DEVELOPMENTAL STAGE: In anthers, barely detected in microsporocytes at
CC stage 6, but accumulates strongly in tetrads at stage 7, microspores,
CC mature pollen grains, and tapetum cells. Also detectable in the growing
CC pollen tubes on the stigma. {ECO:0000269|PubMed:21833541,
CC ECO:0000269|PubMed:22361507}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P22219}.
CC -!- DISRUPTION PHENOTYPE: Reduced male gametophyte transmission. Abnormal
CC pollen grains with unusual large vacuoles. Reduced pollen germination
CC rescued by phosphatidylinositol 3-phosphate (PI3P) treatment.
CC {ECO:0000269|PubMed:21833541, ECO:0000269|PubMed:22361507}.
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; AL161574; CAB79696.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85624.1; -; Genomic_DNA.
DR RefSeq; NP_194667.1; NM_119083.3.
DR AlphaFoldDB; Q9M0E5; -.
DR STRING; 3702.AT4G29380.1; -.
DR iPTMnet; Q9M0E5; -.
DR PaxDb; Q9M0E5; -.
DR PRIDE; Q9M0E5; -.
DR ProteomicsDB; 242669; -.
DR EnsemblPlants; AT4G29380.1; AT4G29380.1; AT4G29380.
DR GeneID; 829059; -.
DR Gramene; AT4G29380.1; AT4G29380.1; AT4G29380.
DR KEGG; ath:AT4G29380; -.
DR Araport; AT4G29380; -.
DR TAIR; locus:2118234; AT4G29380.
DR eggNOG; KOG1240; Eukaryota.
DR HOGENOM; CLU_001696_0_1_1; -.
DR InParanoid; Q9M0E5; -.
DR OMA; RELILHM; -.
DR OrthoDB; 1312453at2759; -.
DR PhylomeDB; Q9M0E5; -.
DR PRO; PR:Q9M0E5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0E5; baseline and differential.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0071561; C:nucleus-vacuole junction; IBA:GO_Central.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.130.10.10; -; 3.
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 Pfam; PF00400; WD40; 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; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Autophagy; Cytoplasm; 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 /evidence="ECO:0000255"
FT CHAIN 2..1494
FT /note="Serine/threonine-protein kinase VPS15"
FT /id="PRO_0000441931"
FT DOMAIN 27..307
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 383..421
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 480..517
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 524..562
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 610..646
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 648..685
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 687..724
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 727..764
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1079..1118
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1127..1166
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1184..1226
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1231..1270
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 1276..1323
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 1371..1409
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 1466..1494
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 859..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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:0000255"
SQ SEQUENCE 1494 AA; 168124 MW; 78D71855073E8BFD CRC64;
MGNKIARTTQ VSATEYYLHD LPSSYNLVLK EVLGRGRFLK SIQCKHDEGL VVVKVYFKRG
DSIDLREYER RLVKIKDVFL SLEHPHVWPF QFWQETDKAA YLVRQYFYSN LHDRLSTRPF
LSLVEKKWLA FQLLLAVKQC HEKDICHGDI KCENVLLTSW NWLYLADFAS FKPTYIPYDD
PSDFSFFFDT RGQRLCYLAP ERFYEHGGET QVAQDAPLKP SMDIFAVGCV IAELFLEGQP
LFELAQLLAY RRGQHDPSQH LEKIPDPGIR KMILHMIQLE PEARLSAEDY LQNYVGVVFP
NYFSPFLHTL YCCWNPLPSD MRVATCQGIF QEILKKMMEN KSGDEIGVDS PVTSNPMNAS
TVQETFANHK LNSSKDLIRN TVNSKDEIFY SISDALKKNR HPFLKKITMD DLGTLMSLYD
SRSDTYGTPF LPVEGNMRCE GMVLIASMLC SCIRNIKLPH LRREAILLLR SCSLYIDDDD
RLQRVLPYVV ALLSDPTAIV RCAAMETLCD ILPLVRDFPP SDAKIFPEYI FPMLSMLPED
TEESVRICYA SNIAKLALTA YGFLIHSFQL SDVGVLNELN SQQISTTPAS ETPSHLQKAN
GNAQLQQLRK TIAEVVQELV MGPKQTPNVR RALLQDIGEL CFFFGQRQSN DFLLPILPAF
LNDRDEQLRS VFFEKIVYVC FFVGQRSVEE YLLPYIDQAL SDQTEAVIVN ALECLSTLCK
SSFLRKRALL QMIECVYPLL CYPSQWVRRA VVTFIAASSE CLGAVDSYAF IAPVIRSYLS
RLPASIASEE GLLSCLKPPV TREVVYRIFE KTRNPEFMAK QRKMWYSSSP QSKDWESVDL
FDKDAGELNS VECRAEQKQS VEGKKQIKSA SKQPEVQGKY AEKDAKLRIP RNPRPNASNT
VELRDPVYPE KLQFSGFMAP YVSGANSFIE PENIPLYSFS MDKRAATNPP VASESSLQMN
SLGMGSLSVP WMDSMSKSFN LASSVPVPKL ISGSFHVGTN PKQFYRVVHE PESRENDQIS
SAISKFQDLG VSSSSKSASV TSEDASSPAD LVGEPSLSRT SVPDSGWKPR GVLVAHLQEH
RSAVNDIATS SDHSFFVSAS DDSTVKVWDS RKLEKDISFR SRLTYHLEGS RGMCTTMLRN
STQVVVGASD GVIHMFSIDH ISRGLGNVVE KYSGIVDIKK KDVKEGALVS LLNYTADSLS
GPMVMYSTQN CGIHLWDTRS DLDAWTLKAN PEEGYVSSLV TSPCGNWFVS GSSRGVLTLW
DLRFRVPVNS WQYPIICPIE KMCLCFLPPS VSVSTTMKPL IYVAAGCNEV SLWNAEGGSC
HQVLRVANYE NETDVSEFQW KLPSNKVNPK PNHRQNMSSK YRIEELNEPP PRLPGIRSLL
PLPGGDLLTG GTDLKIRRWD YSSPERSYCI CGPSLKGVGN DDFYELKTNT GVQFVQETKR
RPLATKLTAK AVLAAAATDT AGCHRDSVQS LASVKLNQRL LISSSRDGAI KVWK
