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RAB7L_MOUSE
ID   RAB7L_MOUSE             Reviewed;         204 AA.
AC   Q91YQ1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Ras-related protein Rab-7L1;
DE   AltName: Full=Rab-7-like protein 1;
GN   Name=Rab29; Synonyms=Rab7l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3]
RP   INTERACTION WITH LRRK2.
RX   PubMed=23395371; DOI=10.1016/j.neuron.2012.11.033;
RA   MacLeod D.A., Rhinn H., Kuwahara T., Zolin A., Di Paolo G., McCabe B.D.,
RA   MacCabe B.D., Marder K.S., Honig L.S., Clark L.N., Small S.A.,
RA   Abeliovich A.;
RT   "RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and
RT   Parkinson's disease risk.";
RL   Neuron 77:425-439(2013).
CC   -!- FUNCTION: The small GTPases Rab are key regulators in vesicle
CC       trafficking (By similarity). Essential for maintaining the integrity of
CC       endosome-trans-Golgi network structure (By similarity). Together with
CC       LRRK2, plays a role in the retrograde trafficking pathway for recycling
CC       proteins, such as mannose 6 phosphate receptor (M6PR), between
CC       lysosomes and the Golgi apparatus in a retromer-dependent manner (By
CC       similarity). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2
CC       kinase activity (By similarity). Regulates also neuronal process
CC       morphology in the intact central nervous system (CNS) (By similarity).
CC       {ECO:0000250|UniProtKB:O14966, ECO:0000250|UniProtKB:Q63481}.
CC   -!- SUBUNIT: Interacts with LRRK2. {ECO:0000269|PubMed:23395371}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O14966}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:O14966}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:O14966}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:O14966}. Note=Colocalizes with GM130 at the
CC       Golgi apparatus (By similarity). Colocalizes with LRRK2 at dynamic
CC       tubules emerging from and retracting to the Golgi apparatus (By
CC       similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN)
CC       (By similarity). {ECO:0000250|UniProtKB:O14966,
CC       ECO:0000250|UniProtKB:Q63481}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; BC016133; AAH16133.1; -; mRNA.
DR   EMBL; BC029056; AAH29056.1; -; mRNA.
DR   CCDS; CCDS15276.1; -.
DR   AlphaFoldDB; Q91YQ1; -.
DR   SMR; Q91YQ1; -.
DR   IntAct; Q91YQ1; 2.
DR   STRING; 10090.ENSMUSP00000027693; -.
DR   iPTMnet; Q91YQ1; -.
DR   PhosphoSitePlus; Q91YQ1; -.
DR   jPOST; Q91YQ1; -.
DR   MaxQB; Q91YQ1; -.
DR   PaxDb; Q91YQ1; -.
DR   PRIDE; Q91YQ1; -.
DR   ProteomicsDB; 253154; -.
DR   ABCD; Q91YQ1; 21 sequenced antibodies.
DR   MGI; MGI:2385107; Rab29.
DR   eggNOG; KOG4423; Eukaryota.
DR   InParanoid; Q91YQ1; -.
DR   PhylomeDB; Q91YQ1; -.
DR   Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR   ChiTaRS; Rab29; mouse.
DR   PRO; PR:Q91YQ1; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q91YQ1; protein.
DR   GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0005773; C:vacuole; ISO:MGI.
DR   GO; GO:0031982; C:vesicle; IDA:MGI.
DR   GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR   GO; GO:0019003; F:GDP binding; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; IDA:MGI.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0007030; P:Golgi organization; IGI:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR   GO; GO:0044788; P:modulation by host of viral process; ISO:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR   GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
DR   GO; GO:1903441; P:protein localization to ciliary membrane; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0072657; P:protein localization to membrane; ISO:MGI.
DR   GO; GO:1901214; P:regulation of neuron death; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; ISO:MGI.
DR   GO; GO:0009617; P:response to bacterium; ISO:MGI.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; ISO:MGI.
DR   GO; GO:0042110; P:T cell activation; ISO:MGI.
DR   GO; GO:1901998; P:toxin transport; ISO:MGI.
DR   CDD; cd04107; Rab32_Rab38; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR030697; Rab29/Rab38/Rab32.
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; Cytoplasm; Cytoskeleton; Differentiation; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Prenylation; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..204
FT                   /note="Ras-related protein Rab-7L1"
FT                   /id="PRO_0000121128"
FT   MOTIF           36..44
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         33..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..128
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         71
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O14966"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14966"
FT   LIPID           203
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           204
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23089 MW;  1D05E98967E120F3 CRC64;
     MGSRDHLFKV LVVGDAAVGK TSLVQRYSQD SFSKHYKSTV GVDFALKVLQ WSDSEMVRLQ
     LWDIAGQERF TSMTRLYYRD ASACVIMFDV TNATTFSNSQ RWKQDLDSKL TLPSGEPVPC
     LLLANKSDLS PWAVSRDQID RFSKENGFTG WTETSVKENK NINEAMRVLV EKMMNNSRED
     VMSLSTQGNY INLQAKPSSG WTCC
 
 
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