YPT11_YEAST
ID YPT11_YEAST Reviewed; 417 AA.
AC P48559; D6W0P1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=GTP-binding protein YPT11;
DE AltName: Full=Rab GTPase YPT11;
GN Name=YPT11; OrderedLocusNames=YNL304W; ORFNames=N0410;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH YIP3.
RX PubMed=11785952; DOI=10.1006/bbrc.2001.6242;
RA Calero M., Collins R.N.;
RT "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab
RT proteins.";
RL Biochem. Biophys. Res. Commun. 290:676-681(2002).
RN [5]
RP INTERACTION WITH YIF1; YIP4 AND YIP5.
RX PubMed=11943201; DOI=10.1016/s0014-5793(02)02442-0;
RA Calero M., Winand N.J., Collins R.N.;
RT "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase
RT interacting factors.";
RL FEBS Lett. 515:89-98(2002).
RN [6]
RP FUNCTION, INTERACTION WITH MYO2, AND MUTAGENESIS OF GLY-102 AND ILE-206.
RX PubMed=12391144; DOI=10.1128/mcb.22.22.7744-7757.2002;
RA Itoh T., Watabe A., Toh-e A., Matsui Y.;
RT "Complex formation with Ypt11p, a rab-type small GTPase, is essential to
RT facilitate the function of Myo2p, a class V myosin, in mitochondrial
RT distribution in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 22:7744-7757(2002).
RN [7]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [10]
RP FUNCTION IN MITOCHONDRION INHERITANCE.
RX PubMed=15201867; DOI=10.1038/sj.emboj.7600271;
RA Itoh T., Toh-e A., Matsui Y.;
RT "Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of
RT mitochondria in the budding yeast.";
RL EMBO J. 23:2520-2530(2004).
RN [11]
RP FUNCTION IN MITOCHONDRION INHERITANCE.
RX PubMed=15215313; DOI=10.1091/mbc.e04-01-0053;
RA Boldogh I.R., Ramcharan S.L., Yang H.-C., Pon L.A.;
RT "A type V myosin (Myo2p) and a Rab-like G-protein (Ypt11p) are required for
RT retention of newly inherited mitochondria in yeast cells during cell
RT division.";
RL Mol. Biol. Cell 15:3994-4002(2004).
RN [12]
RP FUNCTION IN ENDOPLASMIC RETICULUM INHERITANCE, AND SUBCELLULAR LOCATION.
RX PubMed=16980630; DOI=10.1128/mcb.02405-05;
RA Buvelot Frei S., Rahl P.B., Nussbaum M., Briggs B.J., Calero M.,
RA Janeczko S., Regan A.D., Chen C.Z., Barral Y., Whittaker G.R.,
RA Collins R.N.;
RT "Bioinformatic and comparative localization of Rab proteins reveals
RT functional insights into the uncharacterized GTPases Ypt10p and Ypt11p.";
RL Mol. Cell. Biol. 26:7299-7317(2006).
RN [13]
RP FUNCTION IN ENDOPLASMIC RETICULUM AND MITOCHONDRION INHERITANCE.
RX PubMed=18245340; DOI=10.1534/genetics.107.083055;
RA Frederick R.L., Okamoto K., Shaw J.M.;
RT "Multiple pathways influence mitochondrial inheritance in budding yeast.";
RL Genetics 178:825-837(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in the positive control of both endoplasmic
CC reticulum (ER) and mitochondrion inheritance during cell divison.
CC Required for the MYO2-dependent retention of newly inherited
CC mitochondria at the bud tip in developing daughter cells.
CC {ECO:0000269|PubMed:12391144, ECO:0000269|PubMed:15201867,
CC ECO:0000269|PubMed:15215313, ECO:0000269|PubMed:16980630,
CC ECO:0000269|PubMed:18245340}.
CC -!- SUBUNIT: Interacts with MYO2 (via C-terminal tail domain). Interacts
CC with YIF1, YIP3, YIP4 and YIP5. {ECO:0000269|PubMed:11785952,
CC ECO:0000269|PubMed:11943201, ECO:0000269|PubMed:12391144}.
CC -!- INTERACTION:
CC P48559; P53633: YIP3; NbExp=2; IntAct=EBI-29362, EBI-25301;
CC P48559; P53093: YIP4; NbExp=2; IntAct=EBI-29362, EBI-24124;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16980630}; Lipid-anchor
CC {ECO:0000269|PubMed:16980630}; Cytoplasmic side
CC {ECO:0000269|PubMed:16980630}. Bud tip {ECO:0000269|PubMed:16980630}.
CC Bud neck {ECO:0000269|PubMed:16980630}. Note=Enriched in the peripheral
CC ER of small buds and daughter cells. Concentrates at the site of bud
CC emergence, at the bud tip of the growing bud, and at the bud neck
CC during M phase. Interaction with MYO2 is required for proper
CC localization to the bud.
CC -!- MISCELLANEOUS: Present with 2850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49094.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA96231.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U23084; AAC49094.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z71580; CAA96231.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006947; DAA10257.1; -; Genomic_DNA.
DR PIR; S60396; S60396.
DR RefSeq; NP_014095.2; NM_001183142.1.
DR AlphaFoldDB; P48559; -.
DR SMR; P48559; -.
DR BioGRID; 35535; 192.
DR DIP; DIP-7864N; -.
DR IntAct; P48559; 8.
DR MINT; P48559; -.
DR STRING; 4932.YNL304W; -.
DR iPTMnet; P48559; -.
DR MaxQB; P48559; -.
DR PaxDb; P48559; -.
DR PRIDE; P48559; -.
DR EnsemblFungi; YNL304W_mRNA; YNL304W; YNL304W.
DR GeneID; 855412; -.
DR KEGG; sce:YNL304W; -.
DR SGD; S000005248; YPT11.
DR VEuPathDB; FungiDB:YNL304W; -.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_030444_0_0_1; -.
DR InParanoid; P48559; -.
DR OMA; ERTFNIA; -.
DR BioCyc; YEAST:G3O-33291-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR PRO; PR:P48559; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48559; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0051646; P:mitochondrion localization; IMP:SGD.
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 Endoplasmic reticulum; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..417
FT /note="GTP-binding protein YPT11"
FT /id="PRO_0000121322"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 228..232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 292..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT LIPID 415
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 416
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 102
FT /note="G->D: Impairs interaction with MYO2."
FT /evidence="ECO:0000269|PubMed:12391144"
FT MUTAGEN 206
FT /note="I->N: Abolishes interaction with MYO2."
FT /evidence="ECO:0000269|PubMed:12391144"
SQ SEQUENCE 417 AA; 47116 MW; 26055FCE32A64977 CRC64;
MSQRKRYSLN VVTSPSIPSP TPSAPIRTNE SNWEAASPAS AASSFLPNVH HGGTVLNPGL
GIMRSPSLNK SGAFGRSGSS GSSTVIEPSN IKLLLIGDAN VGKTAMILSY CRELLTRAEM
SRSARLRHQQ QQQHKDLGLK KTVVNHRLSM KEKRKRYSSN DFEKEFKDIN HFADETSDFG
NPNIGDDNNH EMADPNEIVI ETRSTIGIDI KTNLVNIDNR FFNVILWDTA GQERYQNAII
PSLYKKTNAV ILTYDITNAK SFQSCMERWI VQALENFSSQ DLLKARFFLV GNKIDLYKER
QVTHYDVVQM VQEMQLKHGI KISGNFEVSC KWVNVVERTM NMIILDLVEN GCFENNDPCV
SITTSDDVQG HEQEFHDTVE EPFNFTRQRQ HQLEKNNTVD ITKPNDDIAN NQSICCV
