RAB14_MOUSE
ID RAB14_MOUSE Reviewed; 215 AA.
AC Q91V41;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ras-related protein Rab-14;
GN Name=Rab14;
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].
RC TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 14-24; 52-59; 62-72; 83-95; 111-125; 133-140 AND
RP 202-210, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 FUNCTION, AND INTERACTION WITH KIF16B.
RX PubMed=21238925; DOI=10.1016/j.devcel.2010.11.008;
RA Ueno H., Huang X., Tanaka Y., Hirokawa N.;
RT "KIF16B/Rab14 molecular motor complex is critical for early embryonic
RT development by transporting FGF receptor.";
RL Dev. Cell 20:60-71(2011).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:21238925}.
CC -!- SUBUNIT: Interacts with ZFYVE20 (By similarity). Interacts with KIF16B.
CC {ECO:0000250, ECO:0000269|PubMed:21238925}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome
CC {ECO:0000250|UniProtKB:P61106}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:P61106}. Note=Recruited to recycling endosomes
CC by DENND6A. Recruited to phagosomes containing S.aureus or
CC M.tuberculosis. {ECO:0000250|UniProtKB:P61106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK002704; BAB22298.1; -; mRNA.
DR EMBL; BC009085; AAH09085.1; -; mRNA.
DR EMBL; BC025139; AAH25139.1; -; mRNA.
DR EMBL; BC056648; AAH56648.1; -; mRNA.
DR CCDS; CCDS15959.1; -.
DR RefSeq; NP_080973.1; NM_026697.3.
DR AlphaFoldDB; Q91V41; -.
DR SMR; Q91V41; -.
DR BioGRID; 212822; 22.
DR IntAct; Q91V41; 7.
DR MINT; Q91V41; -.
DR STRING; 10090.ENSMUSP00000028238; -.
DR iPTMnet; Q91V41; -.
DR PhosphoSitePlus; Q91V41; -.
DR SwissPalm; Q91V41; -.
DR UCD-2DPAGE; Q91V41; -.
DR EPD; Q91V41; -.
DR jPOST; Q91V41; -.
DR MaxQB; Q91V41; -.
DR PaxDb; Q91V41; -.
DR PRIDE; Q91V41; -.
DR ProteomicsDB; 300372; -.
DR Antibodypedia; 15967; 173 antibodies from 31 providers.
DR DNASU; 68365; -.
DR Ensembl; ENSMUST00000028238; ENSMUSP00000028238; ENSMUSG00000026878.
DR GeneID; 68365; -.
DR KEGG; mmu:68365; -.
DR UCSC; uc008jjz.1; mouse.
DR CTD; 51552; -.
DR MGI; MGI:1915615; Rab14.
DR VEuPathDB; HostDB:ENSMUSG00000026878; -.
DR eggNOG; KOG0097; Eukaryota.
DR GeneTree; ENSGT00940000155178; -.
DR InParanoid; Q91V41; -.
DR OMA; TRRITYN; -.
DR OrthoDB; 1146851at2759; -.
DR PhylomeDB; Q91V41; -.
DR TreeFam; TF300032; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 68365; 10 hits in 60 CRISPR screens.
DR ChiTaRS; Rab14; mouse.
DR PRO; PR:Q91V41; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91V41; protein.
DR Bgee; ENSMUSG00000026878; Expressed in metanephric cortical collecting duct and 263 other tissues.
DR ExpressionAtlas; Q91V41; baseline and differential.
DR Genevisible; Q91V41; MM.
DR GO; GO:0097208; C:alveolar lamellar body; ISO:MGI.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IEA:InterPro.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
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:MGI.
DR GO; GO:0045176; P:apical protein localization; ISO:MGI.
DR GO; GO:0007589; P:body fluid secretion; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0090387; P:phagolysosome assembly involved in apoptotic cell clearance; IBA:GO_Central.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS: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; Direct protein sequencing; Endosome;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; 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_0000121186"
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:0000250"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 215 AA; 23897 MW; BC8A8B98FB9944AC CRC64;
MATAPYNYSY IFKYIIIGDM GVGKSCLLHQ FTEKKFMADC PHTIGVEFGT RIIEVSGQKI
KLQIWDTAGQ ERFRAVTRSY YRGAAGALMV YDITRRSTYN HLSSWLTDAR NLTNPNTVII
LIGNKADLEA QRDVTYEEAK QFAEENGLLF LEASAKTGEN VEDAFLEAAK KIYQNIQDGS
LDLNAAESGV QHKPSAPQGG RLTSEPQPQR EGCGC
