RAB7L_RAT
ID RAB7L_RAT Reviewed; 204 AA.
AC Q63481;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, 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;
DE AltName: Full=Ras-related protein Rab-29;
GN Name=Rab29; Synonyms=Rab7l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9177482; DOI=10.1016/s0167-4781(97)00014-6;
RA Massmann S., Schuermann A.H., Joost H.-G.;
RT "Cloning of two splicing variants of the novel Ras-related GTPase Rab29
RT which is predominately expressed in kidney.";
RL Biochim. Biophys. Acta 1352:48-55(1997).
RN [2]
RP FUNCTION IN RETROGRADE TRANSPORT, INTERACTION WITH LRRK2, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF THR-21 AND GLN-67.
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 (PubMed:23395371). Essential for maintaining the integrity
CC of endosome-trans-Golgi network structure (PubMed:23395371). Together
CC with LRRK2, plays a role in the retrograde trafficking pathway for
CC recycling proteins, such as mannose 6 phosphate receptor (M6PR),
CC between lysosomes and the Golgi apparatus in a retromer-dependent
CC manner (PubMed:23395371). Recruits LRRK2 to the Golgi apparatus and
CC stimulates LRRK2 kinase activity (By similarity). Regulates also
CC neuronal process morphology in the intact central nervous system (CNS)
CC (PubMed:23395371). {ECO:0000250|UniProtKB:O14966,
CC ECO:0000269|PubMed:23395371}.
CC -!- SUBUNIT: Interacts with LRRK2. {ECO:0000269|PubMed:23395371}.
CC -!- INTERACTION:
CC Q63481; Q5S007: LRRK2; Xeno; NbExp=3; IntAct=EBI-6513837, EBI-5323863;
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:0000269|PubMed:23395371}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23395371}. Note=Colocalizes with GM130 at the Golgi
CC apparatus (By similarity). Colocalizes with dynamic tubules emerging
CC from and retracting to the Golgi apparatus (By similarity). Colocalizes
CC with TGN46 at the trans-Golgi network (TGN) (By similarity).
CC Colocalized with LRRK2 along tubular structures emerging from Golgi
CC apparatus (PubMed:23395371). {ECO:0000250|UniProtKB:O14966,
CC ECO:0000269|PubMed:23395371}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney and much less in
CC brain, heart, muscle, fat, liver, spleen, adrenal gland, ovary, thymus
CC and lung. Not expressed in testis and intestine.
CC {ECO:0000269|PubMed:9177482}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X96663; CAA65444.1; -; mRNA.
DR RefSeq; NP_598274.1; NM_133590.1.
DR RefSeq; XP_006249806.1; XM_006249744.3.
DR RefSeq; XP_006249807.1; XM_006249745.3.
DR AlphaFoldDB; Q63481; -.
DR SMR; Q63481; -.
DR DIP; DIP-60518N; -.
DR IntAct; Q63481; 2.
DR STRING; 10116.ENSRNOP00000067600; -.
DR CarbonylDB; Q63481; -.
DR iPTMnet; Q63481; -.
DR PhosphoSitePlus; Q63481; -.
DR PaxDb; Q63481; -.
DR Ensembl; ENSRNOT00000073669; ENSRNOP00000067600; ENSRNOG00000049641.
DR GeneID; 171122; -.
DR KEGG; rno:171122; -.
DR CTD; 8934; -.
DR RGD; 620892; Rab29.
DR eggNOG; KOG4423; Eukaryota.
DR GeneTree; ENSGT00940000159363; -.
DR InParanoid; Q63481; -.
DR OMA; SACIIMF; -.
DR OrthoDB; 1240760at2759; -.
DR PhylomeDB; Q63481; -.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:Q63481; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000049641; Expressed in kidney and 20 other tissues.
DR ExpressionAtlas; Q63481; baseline and differential.
DR Genevisible; Q63481; RN.
DR GO; GO:0005801; C:cis-Golgi network; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097708; C:intracellular vesicle; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
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:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0005773; C:vacuole; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0019003; F:GDP binding; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
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:RGD.
DR GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:RGD.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:1903441; P:protein localization to ciliary membrane; ISO:RGD.
DR GO; GO:0072657; P:protein localization to membrane; ISO:RGD.
DR GO; GO:1901214; P:regulation of neuron death; ISS:ParkinsonsUK-UCL.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IMP:ParkinsonsUK-UCL.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR GO; GO:0039694; P:viral RNA genome replication; ISO:RGD.
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_0000276770"
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"
FT MUTAGEN 21
FT /note="T->N: Abolishes localization at trans-Golgi network
FT (TGN) and affects the integrity of the TGN. Inhibits
FT retrograde trafficking of M6PR-associated vesicles."
FT /evidence="ECO:0000269|PubMed:23395371"
FT MUTAGEN 67
FT /note="Q->L: Localizes predominantly in the cytosol."
FT /evidence="ECO:0000269|PubMed:23395371"
SQ SEQUENCE 204 AA; 23117 MW; 4CFAE889718F20E5 CRC64;
MGSRDHLFKV LVVGDAAVGK TSLVQRYSQD SFSKHYKSTV GVDFALKVLQ WSDSEMVRLQ
LWDIAGQERF TSMTRLYYRD ASACVIMFDV TNATTFSNSQ RWKQDLDSKL TLPSGEPVPC
LLLANKSDLS PWAVSRDQID RFSKENGFTG WTETSVKENK NINEAMRVLV EKMMNNSRED
IMSSSTQGNY INLQTKPSPG WTCC
