ID RAB14_RAT Reviewed; 215 AA. AC P61107; P35287; Q969L0; Q9UI11; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 161. DE RecName: Full=Ras-related protein Rab-14; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61106}; GN Name=Rab14 {ECO:0000312|RGD:620881}; 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]. 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 [2] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-25; GLN-70 AND RP ASN-124. RX PubMed=15004230; DOI=10.1091/mbc.e03-10-0777; RA Junutula J.R., De Maziere A.M., Peden A.A., Ervin K.E., Advani R.J., RA van Dijk S.M., Klumperman J., Scheller R.H.; RT "Rab14 is involved in membrane trafficking between the Golgi complex and RT endosomes."; RL Mol. Biol. Cell 15:2218-2229(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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 set of downstream effectors directly responsible for vesicle CC formation, movement, tethering and fusion (By similarity). RAB14 is CC involved in membrane trafficking between the Golgi complex and CC endosomes during early embryonic development (PubMed:15004230). CC Regulates the Golgi to endosome transport of FGFR-containing vesicles CC during early development, a key process for developing basement CC membrane and epiblast and primitive endoderm lineages during early CC postimplantation development. May act by modulating the kinesin KIF16B- CC cargo association to endosomes (By similarity). Regulates, together CC with its guanine nucleotide exchange factor DENND6A, the specific CC endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell CC adhesion. Mediates endosomal tethering and fusion through the CC interaction with RUFY1 and RAB4B (By similarity). Interaction with CC RAB11FIP1 may function in the process of neurite formation (By CC similarity). {ECO:0000250|UniProtKB:P61106, CC ECO:0000250|UniProtKB:Q91V41, ECO:0000269|PubMed:15004230}. 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:P61106}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P61106}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P61106}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) including DENND6A and DENND6B which promote the exchange of CC bound GDP for free GTP. Regulated by GTPase activating proteins (GAPs) CC which increase the GTP hydrolysis activity. Inhibited by GDP CC dissociation inhibitors (GDIs) which prevent Rab-GDP dissociation. CC {ECO:0000250|UniProtKB:P61106}. CC -!- SUBUNIT: Interacts with ZFYVE20. Interacts with KIF16B. Interacts (GTP- CC bound form) with RUFY1; the interaction recruits RUFY1 onto endosomal CC membranes. Interacts (GTP-bound form) with RAB11FIP1 (via its C- CC terminus); the interaction does not mediate RAB11FIP1 recruitment to CC membranes (By similarity). Interacts with RAB11FIP2 (By similarity). CC {ECO:0000250|UniProtKB:P61106}. CC -!- INTERACTION: CC P61107; Q9Y2I1: NISCH; Xeno; NbExp=9; IntAct=EBI-917845, EBI-2688731; CC -!- SUBCELLULAR LOCATION: Recycling endosome CC {ECO:0000250|UniProtKB:P61106}. Early endosome membrane CC {ECO:0000269|PubMed:15004230}; Lipid-anchor CC {ECO:0000305|PubMed:15004230}; Cytoplasmic side CC {ECO:0000305|PubMed:15004230}. Golgi apparatus membrane CC {ECO:0000269|PubMed:15004230}; Lipid-anchor CC {ECO:0000305|PubMed:15004230}; Cytoplasmic side CC {ECO:0000305|PubMed:15004230}. Golgi apparatus, trans-Golgi network CC membrane {ECO:0000269|PubMed:15004230}; Lipid-anchor CC {ECO:0000305|PubMed:15004230}; Cytoplasmic side CC {ECO:0000305|PubMed:15004230}. Cytoplasmic vesicle, phagosome CC {ECO:0000250|UniProtKB:P61106}. Note=Recruited to recycling endosomes CC by DENND6A. {ECO:0000250|UniProtKB:P61106}. CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Highest levels CC found in whole brain, spinal cord, heart, kidney and lung. CC -!- DOMAIN: Switch I, switch II 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 drives interaction with specific sets of CC effector proteins, with most effectors only binding to GTP-bound Rab. CC {ECO:0000250|UniProtKB:P61106}. 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; M83680; AAA41994.1; -; mRNA. DR PIR; E42148; E42148. DR RefSeq; NP_446041.2; NM_053589.3. DR AlphaFoldDB; P61107; -. DR SMR; P61107; -. DR BioGRID; 250177; 5. DR FunCoup; P61107; 3486. DR IntAct; P61107; 8. DR STRING; 10116.ENSRNOP00000025649; -. DR GlyGen; P61107; 1 site. DR iPTMnet; P61107; -. DR PhosphoSitePlus; P61107; -. DR SwissPalm; P61107; -. DR jPOST; P61107; -. DR PaxDb; 10116-ENSRNOP00000025649; -. DR GeneID; 94197; -. DR KEGG; rno:94197; -. DR UCSC; RGD:620881; rat. DR AGR; RGD:620881; -. DR CTD; 51552; -. DR RGD; 620881; Rab14. DR eggNOG; KOG0097; Eukaryota. DR InParanoid; P61107; -. DR OMA; ADISWHY; -. DR OrthoDB; 9989112at2759; -. DR PhylomeDB; P61107; -. DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-8873719; RAB geranylgeranylation. DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs. DR PRO; PR:P61107; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0097208; C:alveolar lamellar body; IDA:RGD. DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; EXP:UniProtKB. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; EXP:UniProtKB. DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB. DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO. DR GO; GO:0005802; C:trans-Golgi network; IEA:InterPro. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB. DR GO; GO:0003925; F:G protein activity; ISS:UniProtKB. DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0031489; F:myosin V binding; ISO:RGD. DR GO; GO:0045176; P:apical protein localization; IDA:RGD. DR GO; GO:0007589; P:body fluid secretion; IMP:RGD. DR GO; GO:0042742; P:defense response to bacterium; IEA:InterPro. DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:RGD. DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB. DR GO; GO:0034058; P:endosomal vesicle fusion; ISO:RGD. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0046907; P:intracellular transport; NAS:UniProtKB. DR GO; GO:0001845; P:phagolysosome assembly; IBA:GO_Central. DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; IDA:RGD. DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB. DR CDD; cd04122; Rab14; 1. DR FunFam; 3.40.50.300:FF:000344; Ras-related protein Rab-14; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR030702; Rab14. DR InterPro; IPR050209; Rab_GTPases_membrane_traffic. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47979; DRAB11-RELATED; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. 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 Acetylation; Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding; KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation; KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P61106" FT CHAIN 2..215 FT /note="Ras-related protein Rab-14" FT /id="PRO_0000121187" FT REGION 38..46 FT /note="Switch-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 69..85 FT /note="Switch-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 188..215 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 25 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 25 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 38 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 39 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 42 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 43 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 66 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 124 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 127 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 155 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT BINDING 156 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61106" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P61106" FT MOD_RES 215 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250" FT LIPID 213 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 215 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT MUTAGEN 25 FT /note="S->N: Mimicks the GTP-bound state and is enriched in FT the Golgi region." FT /evidence="ECO:0000269|PubMed:15004230" FT MUTAGEN 70 FT /note="Q->L: Mimicks the GDP-bound state." FT /evidence="ECO:0000269|PubMed:15004230" FT MUTAGEN 124 FT /note="N->I: Enriched in the Golgi region." FT /evidence="ECO:0000269|PubMed:15004230" SQ SEQUENCE 215 AA; 23927 MW; B435AAC6F562B007 CRC64; MATTPYNYSY IFKYIIIGDM GVGKSCLLHQ FTEKKFMADC PHTIGVEFGT RIIEVSGQKI KLQIWDTAGQ ERFRAVTRSY YRGAAGALMV YDITRRSTYN HLSSWLTDAR NLTNPNTVII LIGNKADLEA QRDVTYEEAK QFAEENGLLF LEASAKTGEN VEDAFLEAAK KIYQNIQDGS LDLNAAESGV QHKPSAPQGG RLTSEPQPQR EGCGC //