RAB7L_HUMAN
ID RAB7L_HUMAN Reviewed; 203 AA.
AC O14966; B4E1K3; C9JE77;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 197.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9284931; DOI=10.1159/000134591;
RA Shimizu F., Katagiri T., Suzuki M., Watanabe T.K., Okuno S., Kuga Y.,
RA Nagata M., Fujiwara T., Nakamura Y., Takahashi E.;
RT "Cloning and chromosome assignment to 1q32 of a human cDNA (RAB7L1)
RT encoding a small GTP-binding protein, a member of the RAS superfamily.";
RL Cytogenet. Cell Genet. 77:261-263(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Thymus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP FUNCTION IN SALMONELLA INFECTION, CLEAVAGE BY GIFSY-2 BACTERIOPHAGE GTGE,
RP AND SUBCELLULAR LOCATION.
RX PubMed=22042847; DOI=10.1073/pnas.1111959108;
RA Spano S., Liu X., Galan J.E.;
RT "Proteolytic targeting of Rab29 by an effector protein distinguishes the
RT intracellular compartments of human-adapted and broad-host Salmonella.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18418-18423(2011).
RN [8]
RP FUNCTION IN RETROGRADE TRANSPORT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24788816; DOI=10.1371/journal.pone.0096242;
RA Wang S., Ma Z., Xu X., Wang Z., Sun L., Zhou Y., Lin X., Hong W., Wang T.;
RT "A role of rab29 in the integrity of the trans-Golgi network and retrograde
RT trafficking of mannose-6-phosphate receptor.";
RL PLoS ONE 9:E96242-E96242(2014).
RN [9]
RP FUNCTION, INTERACTION WITH LRRK2, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP THR-71; SER-72; MET-73 AND ARG-75, AND PHOSPHORYLATION AT THR-71 AND
RP SER-72.
RX PubMed=29212815; DOI=10.15252/embj.201798099;
RA Purlyte E., Dhekne H.S., Sarhan A.R., Gomez R., Lis P., Wightman M.,
RA Martinez T.N., Tonelli F., Pfeffer S.R., Alessi D.R.;
RT "Rab29 activation of the Parkinson's disease-associated LRRK2 kinase.";
RL EMBO J. 37:1-18(2018).
CC -!- FUNCTION: The small GTPases Rab are key regulators in vesicle
CC trafficking (PubMed:24788816). Essential for maintaining the integrity
CC of the endosome-trans-Golgi network structure (By similarity). 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:24788816). Recruits LRRK2 to the Golgi complex and
CC stimulates LRRK2 kinase activity (PubMed:29212815). Regulates neuronal
CC process morphology in the intact central nervous system (CNS) (By
CC similarity). May play a role in the formation of typhoid toxin
CC transport intermediates during Salmonella enterica serovar Typhi
CC (S.Typhi) epithelial cell infection (PubMed:22042847).
CC {ECO:0000250|UniProtKB:Q63481, ECO:0000269|PubMed:22042847,
CC ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}.
CC -!- SUBUNIT: Interacts with LRRK2. {ECO:0000269|PubMed:29212815}.
CC -!- INTERACTION:
CC O14966; O95751: LDOC1; NbExp=4; IntAct=EBI-372165, EBI-740738;
CC O14966; Q5S007: LRRK2; NbExp=15; IntAct=EBI-372165, EBI-5323863;
CC O14966; Q04864-2: REL; NbExp=3; IntAct=EBI-372165, EBI-10829018;
CC O14966; P14373: TRIM27; NbExp=3; IntAct=EBI-372165, EBI-719493;
CC O14966; Q13049: TRIM32; NbExp=3; IntAct=EBI-372165, EBI-742790;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:24788816}. Golgi apparatus
CC {ECO:0000269|PubMed:22042847}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}. Vacuole
CC {ECO:0000269|PubMed:22042847}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22042847}. Note=Colocalizes with LRRK2 along
CC tubular structures emerging from Golgi apparatus (PubMed:29212815).
CC Colocalizes with GM130 at the Golgi apparatus (PubMed:22042847).
CC Colocalizes with dynamic tubules emerging from and retracting to the
CC Golgi apparatus (PubMed:22042847). Colocalizes with TGN46 at the trans-
CC Golgi network (TGN) (PubMed:24788816). In Salmonella enterica serovar
CC Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized
CC with both S.Typhi-containing vacuoles and dynamic tubules as well as
CC those emerging from the vacuole toward the cell periphery
CC (PubMed:22042847). {ECO:0000269|PubMed:22042847,
CC ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14966-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14966-2; Sequence=VSP_043391;
CC Name=3;
CC IsoId=O14966-3; Sequence=VSP_045078;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:24788816}.
CC -!- PTM: In case of Salmonella enterica serovar Typhimurium (S.Typhimurium)
CC infection, is proteolytically cleaved between Gly-41 and Val-42 by the
CC GtgE viral protease encoded on the Gifsy-2 lysogen bacteriophage, which
CC therefore prevents the recruitment of RAB29 to S.Typhimurium-containing
CC vacuoles. In contrast, no proteolytically cleavage is detected in
CC S.Typhi-infected cells (PubMed:22042847).
CC {ECO:0000269|PubMed:22042847}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84488; BAA22160.1; -; mRNA.
DR EMBL; AK308359; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK303879; BAG64815.1; -; mRNA.
DR EMBL; AC119673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002585; AAH02585.1; -; mRNA.
DR CCDS; CCDS1459.1; -. [O14966-1]
DR CCDS; CCDS44301.1; -. [O14966-2]
DR CCDS; CCDS44302.1; -. [O14966-3]
DR RefSeq; NP_001129134.1; NM_001135662.1. [O14966-1]
DR RefSeq; NP_001129135.1; NM_001135663.1. [O14966-2]
DR RefSeq; NP_001129136.1; NM_001135664.1. [O14966-3]
DR RefSeq; NP_003920.1; NM_003929.2. [O14966-1]
DR RefSeq; XP_005245626.1; XM_005245569.1. [O14966-1]
DR RefSeq; XP_005245627.1; XM_005245570.1. [O14966-1]
DR RefSeq; XP_005245628.1; XM_005245571.1. [O14966-1]
DR RefSeq; XP_006711668.1; XM_006711605.3. [O14966-3]
DR RefSeq; XP_006711669.1; XM_006711606.2. [O14966-3]
DR RefSeq; XP_016858237.1; XM_017002748.1. [O14966-2]
DR RefSeq; XP_016858238.1; XM_017002749.1. [O14966-2]
DR RefSeq; XP_016858239.1; XM_017002750.1. [O14966-2]
DR PDB; 6HH2; X-ray; 1.45 A; A=1-177.
DR PDBsum; 6HH2; -.
DR AlphaFoldDB; O14966; -.
DR SMR; O14966; -.
DR BioGRID; 114447; 129.
DR DIP; DIP-31215N; -.
DR IntAct; O14966; 24.
DR MINT; O14966; -.
DR STRING; 9606.ENSP00000356107; -.
DR BindingDB; O14966; -.
DR ChEMBL; CHEMBL3879836; -.
DR iPTMnet; O14966; -.
DR PhosphoSitePlus; O14966; -.
DR BioMuta; RAB29; -.
DR EPD; O14966; -.
DR jPOST; O14966; -.
DR MassIVE; O14966; -.
DR MaxQB; O14966; -.
DR PaxDb; O14966; -.
DR PeptideAtlas; O14966; -.
DR PRIDE; O14966; -.
DR ProteomicsDB; 48340; -. [O14966-1]
DR ProteomicsDB; 48341; -. [O14966-2]
DR ProteomicsDB; 9821; -.
DR Antibodypedia; 20685; 165 antibodies from 27 providers.
DR DNASU; 8934; -.
DR Ensembl; ENST00000235932.8; ENSP00000235932.4; ENSG00000117280.13. [O14966-1]
DR Ensembl; ENST00000367139.8; ENSP00000356107.3; ENSG00000117280.13. [O14966-1]
DR Ensembl; ENST00000414729.1; ENSP00000402910.1; ENSG00000117280.13. [O14966-1]
DR Ensembl; ENST00000437324.6; ENSP00000416613.2; ENSG00000117280.13. [O14966-3]
DR Ensembl; ENST00000446390.6; ENSP00000389899.2; ENSG00000117280.13. [O14966-2]
DR GeneID; 8934; -.
DR KEGG; hsa:8934; -.
DR MANE-Select; ENST00000367139.8; ENSP00000356107.3; NM_003929.3; NP_003920.1.
DR UCSC; uc009xbp.4; human. [O14966-1]
DR CTD; 8934; -.
DR DisGeNET; 8934; -.
DR GeneCards; RAB29; -.
DR HGNC; HGNC:9789; RAB29.
DR HPA; ENSG00000117280; Tissue enhanced (kidney).
DR MIM; 603949; gene.
DR neXtProt; NX_O14966; -.
DR OpenTargets; ENSG00000117280; -.
DR PharmGKB; PA34151; -.
DR VEuPathDB; HostDB:ENSG00000117280; -.
DR eggNOG; KOG4423; Eukaryota.
DR GeneTree; ENSGT00940000159363; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; O14966; -.
DR OMA; SACIIMF; -.
DR PhylomeDB; O14966; -.
DR TreeFam; TF324491; -.
DR PathwayCommons; O14966; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; O14966; -.
DR BioGRID-ORCS; 8934; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; RAB29; human.
DR GenomeRNAi; 8934; -.
DR Pharos; O14966; Tchem.
DR PRO; PR:O14966; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O14966; protein.
DR Bgee; ENSG00000117280; Expressed in nephron tubule and 197 other tissues.
DR ExpressionAtlas; O14966; baseline and differential.
DR Genevisible; O14966; HS.
DR GO; GO:0005801; C:cis-Golgi network; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0097708; C:intracellular vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042470; C:melanosome; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
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; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005773; C:vacuole; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070840; F:dynein complex binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019003; F:GDP binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007030; P:Golgi organization; IMP: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; IMP:ParkinsonsUK-UCL.
DR GO; GO:0044788; P:modulation by host of viral process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903441; P:protein localization to ciliary membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0072657; P:protein localization to membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901214; P:regulation of neuron death; ISS:ParkinsonsUK-UCL.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042110; P:T cell activation; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901998; P:toxin transport; IMP:ParkinsonsUK-UCL.
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 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW Differentiation; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..203
FT /note="Ras-related protein Rab-7L1"
FT /id="PRO_0000121127"
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 SITE 41..42
FT /note="Cleavage; by S.Typhimurium viral protease GtgE"
FT MOD_RES 71
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29212815"
FT MOD_RES 72
FT /note="Phosphoserine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29212815"
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 VAR_SEQ 1..72
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045078"
FT VAR_SEQ 42..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043391"
FT MUTAGEN 71
FT /note="T->A: Loss of phosphorylation by LRRK2."
FT /evidence="ECO:0000269|PubMed:29212815"
FT MUTAGEN 71
FT /note="T->E: Loss of phosphorylation by LRRK2. Does not
FT stimulate LRRK2 kinase activity; when associated with E-
FT 72."
FT /evidence="ECO:0000269|PubMed:29212815"
FT MUTAGEN 72
FT /note="S->A: Loss of phosphorylation by LRRK2."
FT /evidence="ECO:0000269|PubMed:29212815"
FT MUTAGEN 72
FT /note="S->E: Loss of phosphorylation by LRRK2. Does not
FT stimulate LRRK2 kinase activity; when associated with E-
FT 71."
FT /evidence="ECO:0000269|PubMed:29212815"
FT MUTAGEN 73
FT /note="M->S: Loss of LRRK2 binding. Does not stimulate
FT LRRK2 kinase activity. Localized to the cytosol."
FT /evidence="ECO:0000269|PubMed:29212815"
FT MUTAGEN 75
FT /note="R->S: Loss of LRRK2 binding. Does not stimulate
FT LRRK2 kinase activity. Localized to the cytosol."
FT /evidence="ECO:0000269|PubMed:29212815"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:6HH2"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:6HH2"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6HH2"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:6HH2"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:6HH2"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:6HH2"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:6HH2"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6HH2"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:6HH2"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:6HH2"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:6HH2"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6HH2"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:6HH2"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6HH2"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:6HH2"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:6HH2"
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
