ID   YPTM1_MAIZE             Reviewed;         208 AA.
AC   P16976;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=GTP-binding protein YPTM1;
GN   Name=YPTM1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Coleoptile;
RX   PubMed=1731354; DOI=10.1073/pnas.89.2.787;
RA   Palme K., Diefenthal T., Vingron M., Sander C., Schell J.;
RT   "Molecular cloning and structural analysis of genes from Zea mays (L.)
RT   coding for members of the ras-related ypt gene family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:787-791(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Palme K., Diefenthal T., Sander C., Vingron M., Schell J.;
RT   "Identification of guanine-nucleotide binding proteins in plants:
RT   structural analysis and evolutionary comparisons of the ras-related ypt-
RT   gene family from Zea mays.";
RL   (In) Bosch L., Kraal B., Parmeggiani A. (eds.);
RL   The guanine-nucleotide binding proteins: common structural and functional
RL   properties, pp.273-284, Plenum Press, New York (1989).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Low levels in coleoptiles.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
CC   -!- CAUTION: This sequence does not have the CYS-CYS motif at the C-
CC       terminal as do homologous sequences from yeast species. It may be
CC       either geranylgeranylated at an alternative motif or it may be subject
CC       to farnesylation on CYS-205. {ECO:0000305}.
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; X63277; CAA44918.1; -; mRNA.
DR   PIR; A38202; A38202.
DR   RefSeq; NP_001105546.1; NM_001112076.1.
DR   AlphaFoldDB; P16976; -.
DR   SMR; P16976; -.
DR   STRING; 4577.GRMZM2G108258_P02; -.
DR   PRIDE; P16976; -.
DR   GeneID; 542531; -.
DR   KEGG; zma:542531; -.
DR   MaizeGDB; 65854; -.
DR   eggNOG; KOG0084; Eukaryota.
DR   OrthoDB; 1149105at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P16976; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Prenylation; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..208
FT                   /note="GTP-binding protein YPTM1"
FT                   /id="PRO_0000121297"
FT   REGION          189..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        190..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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           205
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P01123"
FT   LIPID           206
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P01123"
FT   CONFLICT        116..117
FT                   /note="KL -> NV (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  23311 MW;  8FB1C766BE5768F9 CRC64;
     MSNEFDYLFK LLLIGDSSVG KSCFLLRFAD DSYVDSYIST IGVDFKIRTV EVEGKTVKLQ
     IWDTAGQERF RTITSSYYRG AHGIIIVYDI TDMESFNNVK QWLDEIDRYA NDSVRKLLVG
     NKCDLAENRA VDTSVAQAYA QEVGIPFLET SAKESINVEE AFLAMSAAIK KSKAGSQAAL
     ERKPSNVVQM KGRPIQQEQQ KSSRCCST