RAB13_DANRE
ID RAB13_DANRE Reviewed; 200 AA.
AC Q7T3A4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ras-related protein Rab-13;
DE Flags: Precursor;
GN Name=rab13;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=21543326; DOI=10.1074/jbc.m111.245209;
RA Wu C., Agrawal S., Vasanji A., Drazba J., Sarkaria S., Xie J., Welch C.M.,
RA Liu M., Anand-Apte B., Horowitz A.;
RT "Rab13-dependent trafficking of RhoA is required for directional migration
RT and angiogenesis.";
RL J. Biol. Chem. 286:23511-23520(2011).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab may be involved in
CC endocytic recycling and may regulate the transport to the plasma
CC membrane of transmembrane proteins. May regulate the assembly and the
CC activity of tight junctions. May play a role in angiogenesis through
CC regulation of endothelial cells chemotaxis. May be involved in neurite
CC outgrowth. Has also been proposed to play a role in post-Golgi membrane
CC trafficking from the TGN to the recycling endosome. Finally, it has
CC been involved in insulin-induced transport to the plasma membrane of
CC glucose transporters. {ECO:0000269|PubMed:21543326}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51153};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P51153}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:P51153}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:P51153}. Recycling endosome
CC membrane {ECO:0000250|UniProtKB:P51153}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9DD03}. Note=Tight junctions or associated with
CC vesicles scattered throughout the cytoplasm in cells lacking tight
CC junctions (By similarity). Relocalizes to the leading edge of
CC lamellipodia in migrating endothelial cells (By similarity).
CC {ECO:0000250|UniProtKB:P51153, ECO:0000250|UniProtKB:Q9DD03}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BX004983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053195; AAH53195.1; -; mRNA.
DR RefSeq; NP_958486.1; NM_201329.1.
DR AlphaFoldDB; Q7T3A4; -.
DR SMR; Q7T3A4; -.
DR STRING; 7955.ENSDARP00000046921; -.
DR PaxDb; Q7T3A4; -.
DR Ensembl; ENSDART00000046922; ENSDARP00000046921; ENSDARG00000034771.
DR GeneID; 373105; -.
DR KEGG; dre:373105; -.
DR CTD; 5872; -.
DR ZFIN; ZDB-GENE-030826-30; rab13.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000159989; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q7T3A4; -.
DR OMA; ENFFLAW; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; Q7T3A4; -.
DR TreeFam; TF314097; -.
DR Reactome; R-DRE-8873719; RAB geranylgeranylation.
DR Reactome; R-DRE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q7T3A4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000034771; Expressed in cleaving embryo and 31 other tissues.
DR ExpressionAtlas; Q7T3A4; baseline.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR GO; GO:1902463; P:protein localization to cell leading edge; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0044795; P:trans-Golgi network to recycling endosome transport; ISS:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Tight junction; Transport.
FT CHAIN 1..197
FT /note="Ras-related protein Rab-13"
FT /id="PRO_0000424144"
FT PROPEP 198..200
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424145"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 197
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 197
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51153"
SQ SEQUENCE 200 AA; 22458 MW; FA177CEDAEF2820C CRC64;
MAKKYDFLFK LLLIGDSGVG KTCLIIRFAE DNFNSTYIST IGIDFKVKTI EVEGKKVKLQ
VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSYENIQ NWMKSIKENA SAGVSRMLLG
NKCDIEAKRK VSKETGEKLA KEHGIRFFET SAKSSINVEE SFTSLARDIL LKSNKKPGPS
GREVKLTSTE KKSSSKCLLL
