RHOF_MOUSE
ID RHOF_MOUSE Reviewed; 211 AA.
AC Q8BYP3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Rho-related GTP-binding protein RhoF;
DE Flags: Precursor;
GN Name=Rhof; Synonyms=Arhf;
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=Hypothalamus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and an inactive GDP-bound state. Causes the
CC formation of thin, actin-rich surface projections called filopodia.
CC Functions cooperatively with CDC42 and Rac to generate additional
CC structures, increasing the diversity of actin-based morphology (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AK038837; BAC30145.1; -; mRNA.
DR CCDS; CCDS39263.1; -.
DR RefSeq; NP_780301.1; NM_175092.3.
DR AlphaFoldDB; Q8BYP3; -.
DR SMR; Q8BYP3; -.
DR STRING; 10090.ENSMUSP00000031401; -.
DR PhosphoSitePlus; Q8BYP3; -.
DR EPD; Q8BYP3; -.
DR MaxQB; Q8BYP3; -.
DR PaxDb; Q8BYP3; -.
DR PRIDE; Q8BYP3; -.
DR ProteomicsDB; 254879; -.
DR Antibodypedia; 31593; 250 antibodies from 27 providers.
DR DNASU; 23912; -.
DR Ensembl; ENSMUST00000031401; ENSMUSP00000031401; ENSMUSG00000029449.
DR Ensembl; ENSMUST00000160479; ENSMUSP00000124866; ENSMUSG00000029449.
DR Ensembl; ENSMUST00000186469; ENSMUSP00000140177; ENSMUSG00000029449.
DR GeneID; 23912; -.
DR KEGG; mmu:23912; -.
DR UCSC; uc008zne.1; mouse.
DR CTD; 54509; -.
DR MGI; MGI:1345629; Rhof.
DR VEuPathDB; HostDB:ENSMUSG00000029449; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000158903; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q8BYP3; -.
DR OMA; ECSAKHQ; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q8BYP3; -.
DR TreeFam; TF331746; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 23912; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rhof; mouse.
DR PRO; PR:Q8BYP3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BYP3; protein.
DR Bgee; ENSMUSG00000029449; Expressed in granulocyte and 130 other tissues.
DR ExpressionAtlas; Q8BYP3; baseline and differential.
DR Genevisible; Q8BYP3; MM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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 InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Cytoskeleton; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..208
FT /note="Rho-related GTP-binding protein RhoF"
FT /id="PRO_0000198866"
FT PROPEP 209..211
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000281217"
FT MOTIF 48..56
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 73..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH0"
FT MOD_RES 208
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 211 AA; 23577 MW; 825722E91A631D18 CRC64;
MDAPGAPAPA AAPSSARKEL KIVIVGDGGC GKTSLLMVYC QGSFPEHYAP SVFEKYTASV
TVGNKEVTLN LYDTAGQEDY DRLRPLSYQN THLVLICYDV MNPTSYDNVL IKWFPEVTHF
CRGIPTVLIG CKTDLRKDKE QLRKLRAAQL EPITYTQGLN ACEQMRGALY LECSAKFREN
VEDVFREAAK VALSALKKAQ RQKKHRICLL L
