ID   RAB13_RAT               Reviewed;         203 AA.
AC   P35286; Q8K3X5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   04-NOV-2026, entry version 192.
DE   RecName: Full=Ras-related protein Rab-13;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:Q9DD03};
DE   Flags: Precursor;
GN   Name=Rab13 {ECO:0000312|RGD:620880};
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;
RX   PubMed=19074001; DOI=10.1095/biolreprod.108.071647;
RA   Mruk D.D., Lau A.S.;
RT   "RAB13 participates in ectoplasmic specialization dynamics in the rat
RT   testis.";
RL   Biol. Reprod. 80:590-601(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 40-203.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=1313420; DOI=10.1016/s0021-9258(18)42619-1;
RA   Elferink L.A., Anzai K., Scheller R.H.;
RT   "Rab15, a novel low molecular weight GTP-binding protein specifically
RT   expressed in rat brain.";
RL   J. Biol. Chem. 267:5768-5775(1992).
RN   [3]
RP   FUNCTION IN NEURITE OUTGROWTH.
RX   PubMed=20008558; DOI=10.1128/mcb.01067-09;
RA   Sakane A., Honda K., Sasaki T.;
RT   "Rab13 regulates neurite outgrowth in PC12 cells through its effector
RT   protein, JRAB/MICAL-L2.";
RL   Mol. Cell. Biol. 30:1077-1087(2010).
RN   [4]
RP   FUNCTION IN EXOCYTOSIS, AND ACTIVITY REGULATION.
RX   PubMed=21041651; DOI=10.1073/pnas.1009523107;
RA   Sun Y., Bilan P.J., Liu Z., Klip A.;
RT   "Rab8A and Rab13 are activated by insulin and regulate GLUT4 translocation
RT   in muscle cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:19909-19914(2010).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=22562557; DOI=10.1369/0022155412448069;
RA   Hirvonen M.J., Mulari M.T., Bueki K.G., Vihko P., Haerkoenen P.L.,
RA   Vaeaenaenen H.K.;
RT   "Rab13 is upregulated during osteoclast differentiation and associates with
RT   small vesicles revealing polarized distribution in resorbing cells.";
RL   J. Histochem. Cytochem. 60:537-549(2012).
RN   [6]
RP   INTERACTION WITH LEPROT AND LEPROTL1.
RX   PubMed=23772379; DOI=10.1016/j.fob.2013.01.004;
RA   Hirvonen M.J., Bueki K.G., Sun Y., Mulari M.T., Haerkoenen P.L.,
RA   Vaeaenaenen K.H.;
RT   "Novel interaction of Rab13 and Rab8 with endospanins.";
RL   FEBS Open Bio 3:83-88(2013).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH PRKACA.
RX   PubMed=23419316; DOI=10.1530/jme-13-0011;
RA   Su W., Liu X.;
RT   "RAB13 regulates Sertoli cell permeability barrier dynamics through protein
RT   kinase A.";
RL   J. Mol. Endocrinol. 50:305-318(2013).
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. RAB13 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:20008558, ECO:0000269|PubMed:21041651,
CC       ECO:0000269|PubMed:23419316}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P51153};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P51153};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P62820};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) including DENND1C, which promote the exchange of bound GDP for
CC       free GTP. Regulated by GTPase activating proteins (GAPs) which increase
CC       the GTP hydrolysis activity. Inhibited by GDP dissociation inhibitors
CC       (GDIs) (By similarity). Activated in response to insulin
CC       (PubMed:21041651). {ECO:0000250|UniProtKB:P51153,
CC       ECO:0000269|PubMed:21041651}.
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:23419316, ECO:0000269|PubMed:23772379}.
CC   -!- INTERACTION:
CC       P35286; Q6PDU4: Leprotl1; NbExp=3; IntAct=EBI-917332, EBI-8702651;
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   -!- TISSUE SPECIFICITY: Highest levels found in lung, kidney, whole brain
CC       and spinal cord. Expressed in all tissues tested including Sertoli and
CC       germ cells (at protein level). Also detected in osteoclasts.
CC       {ECO:0000269|PubMed:19074001, ECO:0000269|PubMed:22562557}.
CC   -!- DOMAIN: Switch 1, switch 2 and the interswitch regions are
CC       characteristic of Rab GTPases and mediate the interactions with Rab
CC       downstream effectors. The switch regions undergo conformational changes
CC       upon nucleotide binding which drive interaction with specific sets of
CC       effector proteins, with most effectors only binding to GTP-bound Rab.
CC       {ECO:0000250|UniProtKB:P62820}.
CC   -!- PTM: Ubiquitinated via 'Lys-11'-linked ubiquitination on Lys-46 and
CC       Lys-58; impairing the recruitment of guanosine diphosphate (GDP)
CC       dissociation inhibitor 1/GDI1. {ECO:0000250|UniProtKB:P51153}.
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; AF525280; AAM82588.1; -; mRNA.
DR   EMBL; M83678; AAA41993.1; -; mRNA.
DR   PIR; D42148; D42148.
DR   RefSeq; NP_112354.1; NM_031092.2.
DR   AlphaFoldDB; P35286; -.
DR   SMR; P35286; -.
DR   FunCoup; P35286; 1095.
DR   IntAct; P35286; 4.
DR   STRING; 10116.ENSRNOP00000071741; -.
DR   iPTMnet; P35286; -.
DR   PhosphoSitePlus; P35286; -.
DR   jPOST; P35286; -.
DR   PaxDb; 10116-ENSRNOP00000071741; -.
DR   GeneID; 81756; -.
DR   KEGG; rno:81756; -.
DR   UCSC; RGD:620880; rat.
DR   AGR; RGD:620880; -.
DR   CTD; 5872; -.
DR   RGD; 620880; Rab13.
DR   VEuPathDB; HostDB:ENSRNOG00000016733; -.
DR   eggNOG; KOG0078; Eukaryota.
DR   HOGENOM; CLU_041217_10_7_1; -.
DR   InParanoid; P35286; -.
DR   OMA; AEDNFNH; -.
DR   OrthoDB; 37757at9989; -.
DR   PhylomeDB; P35286; -.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:P35286; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000016733; Expressed in ovary and 20 other cell types or tissues.
DR   GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
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; ISS:UniProtKB.
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:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:RGD.
DR   GO; GO:0003925; F:G protein activity; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:UniProtKB.
DR   GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR   GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0097368; P:establishment of Sertoli cell barrier; IMP:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IC:UniProtKB.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:RGD.
DR   GO; GO:0141162; P:negative regulation of cAMP/PKA signal transduction; IMP:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR   GO; GO:0046326; P:positive regulation of D-glucose import across plasma membrane; IC:UniProtKB.
DR   GO; GO:1902463; P:protein localization to cell leading edge; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0044795; P:trans-Golgi network to recycling endosome transport; ISS:UniProtKB.
DR   CDD; cd01867; Rab8_Rab10_Rab13_like; 1.
DR   FunFam; 3.40.50.300:FF:000363; Secretion related GTPase srgA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR050305; Small_GTPase_Rab.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Hydrolase; Isopeptide bond;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Reference proteome; Tight junction; Transport; Ubl conjugation.
FT   CHAIN           1..200
FT                   /note="Ras-related protein Rab-13"
FT                   /id="PRO_0000121184"
FT   PROPEP          201..203
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370759"
FT   REGION          173..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           31..45
FT                   /note="Switch 1"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   MOTIF           63..80
FT                   /note="Switch 2"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   COMPBIAS        178..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         63
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         153
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"
FT   CROSSLNK        46
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P51153"
FT   CROSSLNK        58
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P51153"
FT   CONFLICT        76
FT                   /note="A -> S (in Ref. 2; AAA41993)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="G -> E (in Ref. 2; AAA41993)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  22901 MW;  B6687462C6EA95A4 CRC64;
     MAKAYDHLFK LLLIGDSGVG KTCLIIRFAE DNFNSTYIST IGIDFKIRTV EIEGKRIKLQ
     VWDTAGQERF KTITTAYYRG AMGIILVYDI TDEKSFENIQ NWMKSIKENA SAGVERLLLG
     NKCDMEAKRK VQREQAERLA REHRIRFFET SAKSSVNVDE AFSSLARDIL LKTGGRRSGN
     SSKPSSTDLK VSDKKNSNKC SLG
//