YPT5_SCHPO
ID YPT5_SCHPO Reviewed; 211 AA.
AC P36586;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=GTP-binding protein ypt5;
GN Name=ypt5; ORFNames=SPAC6F6.15;
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=8374169; DOI=10.1091/mbc.4.6.583;
RA Armstrong J., Craighead M.W., Watson R., Ponnambalam S., Bowden S.;
RT "Schizosaccharomyces pombe ypt5: a homologue of the rab5 endosome fusion
RT regulator.";
RL Mol. Biol. Cell 4:583-592(1993).
RN [2]
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 [3]
RP ISOPRENYLATION AT CYS-209 AND CYS-211, AND METHYLATION AT CYS-211.
RX PubMed=8226998; DOI=10.1016/s0021-9258(20)80549-3;
RA Giannakouros T., Newman C.M., Craighead M.W., Armstrong J., Magee A.I.;
RT "Post-translational processing of Schizosaccharomyces pombe YPT5 protein.
RT In vitro and in vivo analysis of processing mutants.";
RL J. Biol. Chem. 268:24467-24474(1993).
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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z22220; CAA80223.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11737.1; -; Genomic_DNA.
DR PIR; A47733; A47733.
DR PIR; S34729; S34729.
DR RefSeq; NP_593907.1; NM_001019337.2.
DR AlphaFoldDB; P36586; -.
DR SMR; P36586; -.
DR BioGRID; 278718; 1.
DR STRING; 4896.SPAC6F6.15.1; -.
DR iPTMnet; P36586; -.
DR MaxQB; P36586; -.
DR PaxDb; P36586; -.
DR PRIDE; P36586; -.
DR EnsemblFungi; SPAC6F6.15.1; SPAC6F6.15.1:pep; SPAC6F6.15.
DR PomBase; SPAC6F6.15; ypt5.
DR VEuPathDB; FungiDB:SPAC6F6.15; -.
DR eggNOG; KOG0092; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P36586; -.
DR OMA; AVHFDIW; -.
DR PhylomeDB; P36586; -.
DR PRO; PR:P36586; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IDA:CACAO.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR GO; GO:0006897; P:endocytosis; ISO:PomBase.
DR GO; GO:0034058; P:endosomal vesicle fusion; IMP:CACAO.
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 Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..211
FT /note="GTP-binding protein ypt5"
FT /id="PRO_0000121312"
FT MOTIF 43..51
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 211
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:8226998"
FT LIPID 209
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:8226998"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:8226998"
SQ SEQUENCE 211 AA; 22985 MW; 759AA52930C4ED2D CRC64;
MASNTAPKNV VTINQKLVLL GDSAVGKSSL VLRFVKDQFD DYRESTIGAA FLTQTLPIDE
NTSVKLEIWD TAGQERYKSL APMYYRNANC AIVVYDITQA ASLEKAKSWI KELQRQAPEG
IVIALAGNKL DLAQERRAVE KADAEAYAAE ANLLFFETSA KTAENVNELF TAIAKKLPLE
DKLNQARGAV NRGVNLSEAR PAAQPSGSCS C
