VPS15_PICPA
ID VPS15_PICPA Reviewed; 1340 AA.
AC Q9UVG6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Putative serine/threonine-protein kinase VPS15;
DE EC=2.7.11.1;
DE AltName: Full=Vacuolar protein sorting-associated protein 15;
GN Name=VPS15;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1119.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11407 / NRRL Y-11430;
RX PubMed=8628321; DOI=10.1128/mcb.16.5.2527;
RA Waterham H.R., de Vries Y., Russell K.A., Xie W., Veenhuis M., Cregg J.M.;
RT "The Pichia pastoris PER6 gene product is a peroxisomal integral membrane
RT protein essential for peroxisome biogenesis and has sequence similarity to
RT the Zellweger syndrome protein PAF-1.";
RL Mol. Cell. Biol. 16:2527-2536(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1075-1340, AND FUNCTION.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11407 / NRRL Y-11430;
RX PubMed=10591966; DOI=10.1007/s002940050499;
RA Stasyk O.V., van der Klei I.J., Bellu A.R., Shen S., Kiel J.A.K.W.,
RA Cregg J.M., Veenhuis M.;
RT "A Pichia pastoris VPS15 homologue is required in selective peroxisome
RT autophagy.";
RL Curr. Genet. 36:262-269(1999).
RN [3]
RP FUNCTION.
RX PubMed=11533052; DOI=10.1074/jbc.m104087200;
RA Stromhaug P.E., Bevan A., Dunn W.A. Jr.;
RT "GSA11 encodes a unique 208-kDa protein required for pexophagy and
RT autophagy in Pichia pastoris.";
RL J. Biol. Chem. 276:42422-42435(2001).
CC -!- FUNCTION: Involved in glucose-induced micropexophagy and ethanol-
CC induced macropexophagy. Required for ATG2 recruitment to a perivacuolar
CC compartment. {ECO:0000269|PubMed:10591966,
CC ECO:0000269|PubMed:11533052}.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Endosome membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; X96945; CAB59206.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UVG6; -.
DR SMR; Q9UVG6; -.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0045324; P:late endosome to vacuole transport; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endosome; Golgi apparatus; Kinase; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Repeat; Serine/threonine-protein kinase;
KW Transferase; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..1340
FT /note="Putative serine/threonine-protein kinase VPS15"
FT /id="PRO_0000086801"
FT DOMAIN 27..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 432..470
FT /note="HEAT 1"
FT REPEAT 570..608
FT /note="HEAT 2"
FT REPEAT 940..979
FT /note="WD 1"
FT REPEAT 987..1026
FT /note="WD 2"
FT REPEAT 1089..1128
FT /note="WD 3"
FT REPEAT 1133..1182
FT /note="WD 4"
FT REPEAT 1218..1256
FT /note="WD 5"
FT REPEAT 1309..1340
FT /note="WD 6"
FT ACT_SITE 147
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:0000250"
SQ SEQUENCE 1340 AA; 151917 MW; 332D999AD3D9FDCA CRC64;
MGAELSLLAP TAQPIALSVY VDFLSNIQYN KPLGTSRFLK TVKGLNDQGS IVVKVLVKPN
SGLDLSEWVE KLEFLRLKLL DVPNVIPYNL VIDSVRAGYL IRPFQQRTLY ERVSIQPYLE
PIEKKWIAFQ LIHAVMECHE RGQYHGDIKS ENVLLTSWDM VFLTDFAPFK PIYLPGNNPS
QFSFYFDTSR RNVCYVAPER FLGEGTPTQY QEVDKLTSSM DIFSLGCTVA ELFLEGSVLF
TLPQLFKYKK GEYTPSLSGI VDNDLRNMIQ EMIDLDPRKR ISAHDCLRKH RGKVFPEYFY
SFLYDYMLEL STPSDHSVGN WRFDECDRRI ERIYNDMGMI CDKLDVNLDL NIVHSFTEEP
SQNVIPMTLR LPGVEPHIPQ SSKTPYDSAL IILNILLHSM RNTTHSSYRI KSCDLILMIS
EMLSDEQKLD RCLPYLVHLL NDPSIDVQAA ALKYMTQLLL LVDYLTPVNV LIFPEYILPK
LASFLSTTKG SYMRMIFATI LPHLAKTALK FYEMAILLGS HVEKFELLKN FENLTIQLLI
DPDSSAKISL LKNILPLASV FGKDKTNDII LSHMITYLND PDENLRVAFI ESILGLSIFV
GITSLENYIL PLLVQTLTDN SEIVVVNVLR SFAELNNLGL IKKRYKFDLI KVSSKLLLHP
NSWIRLGTLR LLISVVKDLS LTDFYCLLYP LVRPFFEYEV TNFDWATLYP CIIKPIPRSI
YTLSITWALK AEKTLFWQQV KLAKPDPFGS RNSTFLLNRN SKIGESGVVS NNQIPTSPED
IGWLGKLKAS GFDEKDLWKI ATLRDYIFRV ARSRSNIPTQ ENNEVTMQQM GIYPRIVFFE
KGSMYETEGF VTGSSMMANY RILVNSEYSP ESLTKRKTVG GVNTNHTYSG ANPYILKFLE
CIKFRHVLDD SEEFGPSIPS ATVEEGHWKF EGVLVSHLTE HTGSITSLAL SPDQQYFLTG
DSKGIIRLWD VLQLERNGYA TSHVTVSMSS SVKDIKFIEN RNSFCAVTAD GEIKIFRVEI
NSTSSSVRSN GSPHRHESIS LLREHSLEGE HISDMKFIGP NLAVTTLSCK LILFDLRDMQ
IAEEIQNPVS HGFITSFDLD SSQSWLLIGT SKGILDFYDL RFELLVKSWK LKSTSYPIKH
ITVPPAGFTC NRKSERFALI NGGTNDSVTI VFDVSKGQCS ELYFTETVNL NTAIDNYEVL
EVDNGEERTR TSVLATEVED RSITSLTMLG SNQFLTATFD KRVILWDTGN KANSSALISK
LDDFTSSFSS VQVRPHLMAI NEKIVEKDPQ DIGGPKRNMA SANSSTFDLH SDIITGIAVI
QKPLKMLILV DRAGVINIYK
