RAB13_CANLF
ID RAB13_CANLF Reviewed; 203 AA.
AC F1PTE3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ras-related protein Rab-13;
DE Flags: Precursor;
GN Name=RAB13;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP FUNCTION IN TIGHT JUNCTION ASSEMBLY.
RX PubMed=12058051; DOI=10.1091/mbc.02-02-0029;
RA Marzesco A.M., Dunia I., Pandjaitan R., Recouvreur M., Dauzonne D.,
RA Benedetti E.L., Louvard D., Zahraoui A.;
RT "The small GTPase Rab13 regulates assembly of functional tight junctions in
RT epithelial cells.";
RL Mol. Biol. Cell 13:1819-1831(2002).
RN [3]
RP INTERACTION WITH PRKACA.
RX PubMed=15096524; DOI=10.1083/jcb.200312118;
RA Koehler K., Louvard D., Zahraoui A.;
RT "Rab13 regulates PKA signaling during tight junction assembly.";
RL J. Cell Biol. 165:175-180(2004).
RN [4]
RP FUNCTION.
RX PubMed=18779367; DOI=10.1083/jcb.200802176;
RA Nokes R.L., Fields I.C., Collins R.N., Foelsch H.;
RT "Rab13 regulates membrane trafficking between TGN and recycling endosomes
RT in polarized epithelial cells.";
RL J. Cell Biol. 182:845-853(2008).
RN [5]
RP FUNCTION IN ENDOCYTIC RECYCLING, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP MICALL2.
RX PubMed=18094055; DOI=10.1091/mbc.e07-06-0551;
RA Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.;
RT "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the
RT assembly of tight junctions and adherens junctions.";
RL Mol. Biol. Cell 19:971-983(2008).
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:12058051, ECO:0000269|PubMed:18094055,
CC ECO:0000269|PubMed:18779367}.
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:15096524, ECO:0000269|PubMed:18094055}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18094055};
CC Lipid-anchor {ECO:0000269|PubMed:18094055}; Cytoplasmic side
CC {ECO:0000269|PubMed:18094055}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P51153}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:P51153}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:P51153}. Recycling endosome membrane
CC {ECO:0000269|PubMed:18094055}. 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. Relocalizes to the leading edge of lamellipodia in migrating
CC endothelial cells. {ECO:0000250|UniProtKB:P51153,
CC ECO:0000250|UniProtKB:Q9DD03}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AAEX03005351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001300788.1; NM_001313859.1.
DR AlphaFoldDB; F1PTE3; -.
DR SMR; F1PTE3; -.
DR STRING; 9612.ENSCAFP00000025621; -.
DR PaxDb; F1PTE3; -.
DR PRIDE; F1PTE3; -.
DR Ensembl; ENSCAFT00030041868; ENSCAFP00030036526; ENSCAFG00030022772.
DR Ensembl; ENSCAFT00040005537; ENSCAFP00040004761; ENSCAFG00040002923.
DR Ensembl; ENSCAFT00845028937; ENSCAFP00845022768; ENSCAFG00845016274.
DR GeneID; 612294; -.
DR KEGG; cfa:612294; -.
DR CTD; 5872; -.
DR VEuPathDB; HostDB:ENSCAFG00845016274; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000159989; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; F1PTE3; -.
DR OMA; ENFFLAW; -.
DR OrthoDB; 1426655at2759; -.
DR TreeFam; TF314097; -.
DR Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Proteomes; UP000002254; Chromosome 7.
DR Bgee; ENSCAFG00000017389; Expressed in lymph node and 49 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA: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:0070830; P:bicellular tight junction assembly; IMP: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:0035767; P:endothelial cell chemotaxis; ISS: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:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB.
DR GO; GO:1902463; P:protein localization to cell leading edge; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP: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; IMP: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..200
FT /note="Ras-related protein Rab-13"
FT /id="PRO_0000424142"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424143"
FT REGION 173..203
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 200
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51153"
SQ SEQUENCE 203 AA; 22667 MW; 2D54DE26753C0831 CRC64;
MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DSFNNTYIST IGIDFKIRTV DVEGKKIKLQ
VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ NWMKSIKENA SAGVERLLLG
NKCDMEAKRK VQKEQAIKLA REHGIRFFET SAKSSTNVDE AFSSLARDIL LKSGGRRSGN
SHKAPGTDLK PCDKKNTSKC SLG
