YPT1_SCHPO
ID YPT1_SCHPO Reviewed; 203 AA.
AC P11620;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=GTP-binding protein ypt1;
GN Name=ypt1; ORFNames=SPBC1703.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2328721; DOI=10.1002/j.1460-2075.1990.tb08257.x;
RA Miyake S., Yamamoto M.;
RT "Identification of ras-related, YPT family genes in Schizosaccharomyces
RT pombe.";
RL EMBO J. 9:1417-1422(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2740223; DOI=10.1093/nar/17.11.4373;
RA Fawell E., Hook S., Armstrong J.;
RT "Nucleotide sequence of a gene encoding a YPT1-related protein from
RT Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 17:4373-4373(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP ISOPRENYLATION AT CYS-202 AND CYS-203.
RX PubMed=1597466; DOI=10.1016/s0021-9258(19)49914-6;
RA Newman C.M., Giannakouros T., Hancock J.F., Fawell E.H., Armstrong J.,
RA Magee A.I.;
RT "Post-translational processing of Schizosaccharomyces pombe YPT proteins.";
RL J. Biol. Chem. 267:11329-11336(1992).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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}.
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; X52099; CAA36319.1; -; Genomic_DNA.
DR EMBL; X15082; CAA33192.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB66454.1; -; Genomic_DNA.
DR PIR; S04590; S04590.
DR PIR; T50323; T50323.
DR RefSeq; NP_596205.1; NM_001022124.2.
DR AlphaFoldDB; P11620; -.
DR SMR; P11620; -.
DR BioGRID; 276334; 5.
DR STRING; 4896.SPBC1703.10.1; -.
DR iPTMnet; P11620; -.
DR MaxQB; P11620; -.
DR PaxDb; P11620; -.
DR PRIDE; P11620; -.
DR EnsemblFungi; SPBC1703.10.1; SPBC1703.10.1:pep; SPBC1703.10.
DR GeneID; 2539784; -.
DR KEGG; spo:SPBC1703.10; -.
DR PomBase; SPBC1703.10; ypt1.
DR VEuPathDB; FungiDB:SPBC1703.10; -.
DR eggNOG; KOG0084; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P11620; -.
DR OMA; KERMGNT; -.
DR PhylomeDB; P11620; -.
DR Reactome; R-SPO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-SPO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-SPO-8873719; RAB geranylgeranylation.
DR Reactome; R-SPO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P11620; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0000139; C:Golgi membrane; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IGI:PomBase.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
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 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Endoplasmic reticulum; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..203
FT /note="GTP-binding protein ypt1"
FT /id="PRO_0000121308"
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 SITE 203
FT /note="Not methylated"
FT /evidence="ECO:0000269|PubMed:1597466"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT LIPID 202
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1597466"
FT LIPID 203
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1597466"
FT CONFLICT 1..4
FT /note="MNPE -> MNANINR (in Ref. 2; CAA33192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22817 MW; 59B3524F42BB3094 CRC64;
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTF ELEGKTVKLQ
IWDTAGQERF RTITSSYYRG AHGIIIVYDV TDQDSFNNVK QWLQEIDRYA VEGVNRLLVG
NKSDMVDKKV VEYSVAKEFA DSLNIPFLET SAKDSTNVEQ AFLTMSRQIK ERMGNNTFAS
SNAKSSVKVG QGTNVSQSSS NCC
