RAB14_RAT
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 03-AUG-2022, entry version 146.
DE RecName: Full=Ras-related protein Rab-14;
GN Name=Rab14;
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: Regulates, together with its guanine nucleotide exchange
CC factor, DENND6A, the specific endocytic transport of ADAM10, N-
CC cadherin/CDH2 shedding and cell-cell adhesion (By similarity). Involved
CC in membrane trafficking between the Golgi complex and endosomes during
CC early embryonic development. Regulates the Golgi to endosome transport
CC of FGFR-containing vesicles during early development, a key process for
CC developing basement membrane and epiblast and primitive endoderm
CC lineages during early postimplantation development. May act by
CC modulating the kinesin KIF16B-cargo association to endosomes.
CC {ECO:0000250, ECO:0000269|PubMed:15004230}.
CC -!- SUBUNIT: Interacts with KIF16B. Interacts with ZFYVE20 (By similarity).
CC {ECO:0000250}.
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. Recruited to phagosomes containing S.aureus or
CC Mycobacterium. {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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M83680; AAA41994.1; -; mRNA.
DR PIR; E42148; E42148.
DR RefSeq; NP_446041.1; NM_053589.1.
DR AlphaFoldDB; P61107; -.
DR SMR; P61107; -.
DR BioGRID; 250177; 5.
DR IntAct; P61107; 7.
DR MINT; P61107; -.
DR STRING; 10116.ENSRNOP00000025649; -.
DR iPTMnet; P61107; -.
DR PhosphoSitePlus; P61107; -.
DR SwissPalm; P61107; -.
DR jPOST; P61107; -.
DR PaxDb; P61107; -.
DR PRIDE; P61107; -.
DR GeneID; 94197; -.
DR KEGG; rno:94197; -.
DR UCSC; RGD:620881; rat.
DR CTD; 51552; -.
DR RGD; 620881; Rab14.
DR eggNOG; KOG0097; Eukaryota.
DR InParanoid; P61107; -.
DR OrthoDB; 1146851at2759; -.
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:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0016324; C:apical plasma membrane; IDA: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; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0005802; C:trans-Golgi network; IEA:InterPro.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
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:0032456; P:endocytic recycling; ISS:UniProtKB.
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:0090387; P:phagolysosome assembly involved in apoptotic cell clearance; 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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030702; Rab14.
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 Acetylation; Cytoplasmic vesicle; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Protein transport; Reference proteome; 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 188..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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
