RHOF_HUMAN
ID RHOF_HUMAN Reviewed; 211 AA.
AC Q9HBH0; Q8WVB1; Q9NXH6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Rho-related GTP-binding protein RhoF;
DE AltName: Full=Rho family GTPase Rif;
DE AltName: Full=Rho in filopodia;
DE Flags: Precursor;
GN Name=RHOF; Synonyms=ARHF, RIF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11084341; DOI=10.1016/s0960-9822(00)00777-6;
RA Ellis S., Mellor H.;
RT "The novel Rho-family GTPase rif regulates coordinated actin-based membrane
RT rearrangements.";
RL Curr. Biol. 10:1387-1390(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HBH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HBH0-2; Sequence=VSP_013571, VSP_013572;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AF239923; AAG24952.1; -; mRNA.
DR EMBL; AK000254; BAA91034.1; -; mRNA.
DR EMBL; BC018208; AAH18208.1; -; mRNA.
DR CCDS; CCDS9222.1; -. [Q9HBH0-1]
DR RefSeq; NP_061907.2; NM_019034.2. [Q9HBH0-1]
DR AlphaFoldDB; Q9HBH0; -.
DR SMR; Q9HBH0; -.
DR BioGRID; 120004; 676.
DR IntAct; Q9HBH0; 11.
DR STRING; 9606.ENSP00000267205; -.
DR GlyGen; Q9HBH0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HBH0; -.
DR PhosphoSitePlus; Q9HBH0; -.
DR BioMuta; RHOF; -.
DR DMDM; 13633711; -.
DR EPD; Q9HBH0; -.
DR jPOST; Q9HBH0; -.
DR MassIVE; Q9HBH0; -.
DR MaxQB; Q9HBH0; -.
DR PaxDb; Q9HBH0; -.
DR PeptideAtlas; Q9HBH0; -.
DR PRIDE; Q9HBH0; -.
DR ProteomicsDB; 81548; -. [Q9HBH0-1]
DR ProteomicsDB; 81549; -. [Q9HBH0-2]
DR Antibodypedia; 31593; 250 antibodies from 27 providers.
DR DNASU; 54509; -.
DR Ensembl; ENST00000267205.7; ENSP00000267205.2; ENSG00000139725.8. [Q9HBH0-1]
DR Ensembl; ENST00000537171.5; ENSP00000477391.1; ENSG00000139725.8. [Q9HBH0-2]
DR GeneID; 54509; -.
DR KEGG; hsa:54509; -.
DR MANE-Select; ENST00000267205.7; ENSP00000267205.2; NM_019034.3; NP_061907.2.
DR UCSC; uc001ubb.4; human. [Q9HBH0-1]
DR CTD; 54509; -.
DR DisGeNET; 54509; -.
DR GeneCards; RHOF; -.
DR HGNC; HGNC:15703; RHOF.
DR HPA; ENSG00000139725; Low tissue specificity.
DR MIM; 618867; gene.
DR neXtProt; NX_Q9HBH0; -.
DR OpenTargets; ENSG00000139725; -.
DR PharmGKB; PA24954; -.
DR VEuPathDB; HostDB:ENSG00000139725; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000158903; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q9HBH0; -.
DR OMA; ECSAKHQ; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q9HBH0; -.
DR TreeFam; TF331746; -.
DR PathwayCommons; Q9HBH0; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9HBH0; -.
DR BioGRID-ORCS; 54509; 37 hits in 1067 CRISPR screens.
DR ChiTaRS; RHOF; human.
DR GenomeRNAi; 54509; -.
DR Pharos; Q9HBH0; Tbio.
DR PRO; PR:Q9HBH0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9HBH0; protein.
DR Bgee; ENSG00000139725; Expressed in granulocyte and 153 other tissues.
DR ExpressionAtlas; Q9HBH0; baseline and differential.
DR Genevisible; Q9HBH0; HS.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
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:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
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; Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Reference proteome.
FT CHAIN 1..208
FT /note="Rho-related GTP-binding protein RhoF"
FT /id="PRO_0000198865"
FT PROPEP 209..211
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000281216"
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:0007744|PubMed:22814378"
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"
FT VAR_SEQ 158..170
FT /note="GLSACEQIRAALY -> VGRGQDPGAQPWL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013571"
FT VAR_SEQ 171..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013572"
FT CONFLICT 142
FT /note="L -> P (in Ref. 2; BAA91034)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> P (in Ref. 2; BAA91034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 23625 MW; AF82AE0CEDC34FAD CRC64;
MDAPGALAQT AAPGPGRKEL KIVIVGDGGC GKTSLLMVYS QGSFPEHYAP SVFEKYTASV
TVGSKEVTLN LYDTAGQEDY DRLRPLSYQN THLVLICYDV MNPTSYDNVL IKWFPEVTHF
CRGIPMVLIG CKTDLRKDKE QLRKLRAAQL EPITYMQGLS ACEQIRAALY LECSAKFREN
VEDVFREAAK VALSALKKAQ RQKKRRLCLL L
