RAB13_MOUSE
ID RAB13_MOUSE Reviewed; 202 AA.
AC Q9DD03;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ras-related protein Rab-13;
DE Flags: Precursor;
GN Name=Rab13;
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=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP INTERACTION WITH MICALL2.
RX PubMed=16525024; DOI=10.1091/mbc.e05-09-0826;
RA Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT endocytic recycling of occludin.";
RL Mol. Biol. Cell 17:2465-2475(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
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 [5]
RP INTERACTION WITH BICDL2.
RX PubMed=20360680; DOI=10.1038/emboj.2010.51;
RA Schlager M.A., Kapitein L.C., Grigoriev I., Burzynski G.M., Wulf P.S.,
RA Keijzer N., de Graaff E., Fukuda M., Shepherd I.T., Akhmanova A.,
RA Hoogenraad C.C.;
RT "Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related
RT protein 1 (BICDR-1) regulates neuritogenesis.";
RL EMBO J. 29:1637-1651(2010).
RN [6]
RP FUNCTION IN ANGIOGENESIS, SUBCELLULAR LOCATION, AND INTERACTION WITH GRB2.
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 is involved in
CC endocytic recycling and regulates the transport to the plasma membrane
CC of transmembrane proteins like the tight junction protein
CC OCLN/occludin. Thereby, it regulates the assembly and the activity of
CC tight junctions. Moreover, it may also regulate tight junction assembly
CC by activating the PKA signaling pathway and by reorganizing the actin
CC cytoskeleton through the activation of the downstream effectors PRKACA
CC and MICALL2 respectively. Through its role in tight junction assembly,
CC may play a role in the establishment of Sertoli cell barrier. Plays
CC also a role in angiogenesis through regulation of endothelial cells
CC chemotaxis. Also involved in neurite outgrowth. Has also been proposed
CC to play a role in post-Golgi membrane trafficking from the TGN to the
CC recycling endosome. Finally, it has been involved in insulin-induced
CC transport to the plasma membrane of the glucose transporter GLUT4 and
CC therefore may play a role in glucose homeostasis.
CC {ECO:0000269|PubMed:21543326}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). That Rab may be
CC activated by DENND1C, a guanine exchange factor. Activated in response
CC to insulin (By similarity). {ECO:0000250|UniProtKB:P51153}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with MICALL2; competes with RAB8A
CC and is involved in tight junctions assembly. Interacts (GTP-bound form)
CC with MICALL1. Interacts (GTP-bound form) with MICAL1, MICAL3, MICALCL,
CC EHBP1 and EHBP1L1; ternary complexes of RAB8A, RAB13 and either MICAL1
CC or EHBP1L1 are possible. Interacts with PRKACA; downstream effector of
CC RAB13 involved in tight junction assembly. Interacts with GRB2; may
CC recruit RAB13 to the leading edge of migrating endothelial cells where
CC it can activate RHOA. Interacts (isoprenylated form) with PDE6D;
CC dissociates RAB13 from membranes. Interacts with BICDL2/BICDR2.
CC Interacts with LEPROT and LEPROTL1. {ECO:0000250|UniProtKB:P51153,
CC ECO:0000269|PubMed:16525024, ECO:0000269|PubMed:20360680,
CC 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:0000269|PubMed:21543326}. 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 (PubMed:21543326).
CC {ECO:0000250|UniProtKB:P51153, ECO:0000269|PubMed:21543326}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK002303; BAB22000.1; -; mRNA.
DR EMBL; BC027214; AAH27214.1; -; mRNA.
DR CCDS; CCDS17522.1; -.
DR RefSeq; NP_080953.1; NM_026677.4.
DR AlphaFoldDB; Q9DD03; -.
DR SMR; Q9DD03; -.
DR BioGRID; 212806; 5.
DR IntAct; Q9DD03; 20.
DR MINT; Q9DD03; -.
DR STRING; 10090.ENSMUSP00000070588; -.
DR iPTMnet; Q9DD03; -.
DR PhosphoSitePlus; Q9DD03; -.
DR EPD; Q9DD03; -.
DR jPOST; Q9DD03; -.
DR MaxQB; Q9DD03; -.
DR PaxDb; Q9DD03; -.
DR PRIDE; Q9DD03; -.
DR ProteomicsDB; 300287; -.
DR DNASU; 68328; -.
DR Ensembl; ENSMUST00000065418; ENSMUSP00000070588; ENSMUSG00000027935.
DR GeneID; 68328; -.
DR KEGG; mmu:68328; -.
DR UCSC; uc008qbm.2; mouse.
DR CTD; 5872; -.
DR MGI; MGI:1927232; Rab13.
DR VEuPathDB; HostDB:ENSMUSG00000027935; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000159989; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q9DD03; -.
DR OMA; ENFFLAW; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; Q9DD03; -.
DR TreeFam; TF314097; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 68328; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rab13; mouse.
DR PRO; PR:Q9DD03; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9DD03; protein.
DR Bgee; ENSMUSG00000027935; Expressed in ectoplacental cone and 232 other tissues.
DR ExpressionAtlas; Q9DD03; baseline and differential.
DR Genevisible; Q9DD03; MM.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; TAS:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
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; IDA: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; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISS:UniProtKB.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
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; IMP: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..199
FT /note="Ras-related protein Rab-13"
FT /id="PRO_0000121183"
FT PROPEP 200..202
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370758"
FT REGION 174..202
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 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51153"
FT MOD_RES 199
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51153"
SQ SEQUENCE 202 AA; 22770 MW; 5DF599432E228AC0 CRC64;
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNSTYIST IGIDFKIRTV DIEGKRIKLQ
VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ NWMKSIKENA SAGVERLLLG
NKCDMEAKRQ VQREQAEKLA REHRIRFFET SAKSSVNVDE AFSSLARDIL LKTGGRRSGT
NSKPSSTGLK TSDKKKNKCL LG
