ID   YPT11_YEAS7             Reviewed;         417 AA.
AC   A6ZSH6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=GTP-binding protein YPT11;
DE   AltName: Full=Rab GTPase YPT11;
GN   Name=YPT11; ORFNames=SCY_4887;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MYO2 (via C-terminal tail domain). Interacts
CC       with YIF1, YIP3, YIP4 and YIP5 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Bud tip
CC       {ECO:0000250}. Bud neck {ECO:0000250}. 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 the M phase. Interaction with MYO2 is required for proper
CC       localization to the bud (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN62524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000068; EDN62524.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZSH6; -.
DR   SMR; A6ZSH6; -.
DR   EnsemblFungi; EDN62524; EDN62524; SCY_4887.
DR   HOGENOM; CLU_030444_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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   Endoplasmic reticulum; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN           1..417
FT                   /note="GTP-binding protein YPT11"
FT                   /id="PRO_0000377661"
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"
SQ   SEQUENCE   417 AA;  47144 MW;  8A18C0F2CBF1942F CRC64;
     MSQRKRYSLN VVTSPSIPSP TPSAPIRTNE SNWEAASPAS AASSFLPNVH HGGTVLNPGL
     GIMRSPSLNK SGAFGRSGSS GSSTVIEPSN IKLLLIGDAN VGKTAMILSY CRELLTRAEM
     SRSVRLRHQQ 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