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RAB7L_PONAB
ID   RAB7L_PONAB             Reviewed;         203 AA.
AC   Q5R7A4; Q5R6Z5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Ras-related protein Rab-7L1;
DE   AltName: Full=Rab-7-like protein 1;
GN   Name=RAB29; Synonyms=RAB7L1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:O14966}.
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; CR860214; CAH92356.1; -; mRNA.
DR   EMBL; CR860328; CAH92465.1; -; mRNA.
DR   RefSeq; NP_001126387.1; NM_001132915.1.
DR   RefSeq; XP_009236948.1; XM_009238673.1.
DR   AlphaFoldDB; Q5R7A4; -.
DR   SMR; Q5R7A4; -.
DR   STRING; 9601.ENSPPYP00000000318; -.
DR   Ensembl; ENSPPYT00000000335; ENSPPYP00000000318; ENSPPYG00000000298.
DR   GeneID; 100173368; -.
DR   KEGG; pon:100173368; -.
DR   CTD; 8934; -.
DR   eggNOG; KOG4423; Eukaryota.
DR   GeneTree; ENSGT00940000159363; -.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q5R7A4; -.
DR   OrthoDB; 1240760at2759; -.
DR   TreeFam; TF324491; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0005773; C:vacuole; IEA:Ensembl.
DR   GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR   GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
DR   GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR   GO; GO:0042110; P:T cell activation; IEA:Ensembl.
DR   GO; GO:1901998; P:toxin transport; IEA:Ensembl.
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   2: Evidence at transcript 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..203
FT                   /note="Ras-related protein Rab-7L1"
FT                   /id="PRO_0000260747"
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           202
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           203
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        135
FT                   /note="S -> N (in Ref. 1; CAH92465)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  23155 MW;  40E7CAB02446DF97 CRC64;
     MGSRDHLFKV LVVGDAAVGK TSLVQRYSQD SFSKHYKSTV GVDFALKVLQ WSDYEIVRLQ
     LWDIAGQERF TSMTRLYYRD ASACVIMFDV TNATTFSNSQ RWKQDLDSKL TLPNGEPVPC
     LLLANKCDLS PWAVSRDQID RFSKENGFTG WTETSVKENK NINEAMRVLI EKMMRNSTED
     IMSLSTQGDY INLQTKSSSW SCC
 
 
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