ID   YPT1_PHYIN              Reviewed;         201 AA.
AC   Q01890;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Ras-like GTP-binding protein YPT1;
GN   Name=YPT1;
OS   Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 52009 / 135;
RX   PubMed=8973313; DOI=10.1016/s0378-1119(96)00469-6;
RA   Chen Y., Roxby R.;
RT   "Characterization of a Phytophthora infestans gene involved in vesicle
RT   transport.";
RL   Gene 181:89-94(1996).
CC   -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC       membrane trafficking, from the formation of transport vesicles to their
CC       fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC       and an active GTP-bound form that is able to recruit to membranes
CC       different set of downstream effectors directly responsible for vesicle
CC       formation, movement, tethering and fusion. YPT1 regulates the
CC       trafficking of secretory vesicles from the endoplasmic reticulum (ER)
CC       to the Golgi. Plays a role in the initial events of the autophagic
CC       vacuole development which take place at specialized regions of the
CC       endoplasmic reticulum. Also involved in the recycling of membrane
CC       proteins. {ECO:0000250|UniProtKB:P01123}.
CC   -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC       exchange factor (GEF), while inactivation through hydrolysis of bound
CC       GTP is catalyzed by a GTPase activating protein (GAP). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P01123}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P01123}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P01123}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P01123}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P01123}. Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:P01123}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; U30474; AAB40355.1; -; Genomic_DNA.
DR   PIR; JC5337; JC5337.
DR   AlphaFoldDB; Q01890; -.
DR   SMR; Q01890; -.
DR   PRIDE; Q01890; -.
DR   VEuPathDB; FungiDB:PITG_03392; -.
DR   OMA; QRYACDS; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Endoplasmic reticulum; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Membrane; Nucleotide-binding; Prenylation; Protein transport;
KW   Transport.
FT   CHAIN           1..201
FT                   /note="Ras-like GTP-binding protein YPT1"
FT                   /id="PRO_0000121306"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         15..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         33..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         151..153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   LIPID           200
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P01123"
FT   LIPID           201
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P01123"
SQ   SEQUENCE   201 AA;  22293 MW;  89EE553A693C8AC5 CRC64;
     MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ
     IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESFNNVK QWLHEIDRYA CENVNKLLVG
     NKSDLTAKRV VSTDAAKEFA ESLGIEFLET SAKNAANVEK AFMMMAAQIK KRMANAPVAP
     KAGVKLTPGQ QVPSNGGSKC C