RND2_HUMAN
ID RND2_HUMAN Reviewed; 227 AA.
AC P52198; A8K2D4; O00690; O00734; Q5U0P6; Q99535;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Rho-related GTP-binding protein RhoN;
DE AltName: Full=Rho family GTPase 2;
DE AltName: Full=Rho-related GTP-binding protein Rho7;
DE AltName: Full=Rnd2;
DE Flags: Precursor;
GN Name=RND2; Synonyms=ARHN, RHO7;
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].
RC TISSUE=Brain;
RX PubMed=9531558; DOI=10.1083/jcb.141.1.187;
RA Nobes C.D., Lauritzen I., Mattei M.-G., Paris S., Hall A., Chardin P.;
RT "A new member of the Rho family, Rnd1, promotes disassembly of actin
RT filament structures and loss of cell adhesion.";
RL J. Cell Biol. 141:187-197(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8938427; DOI=10.1101/gr.6.11.1029;
RA Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M., Hood L.,
RA King M.-C.;
RT "Complete genomic sequence and analysis of 117 kb of human DNA containing
RT the gene BRCA1.";
RL Genome Res. 6:1029-1049(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 [8]
RP INTERACTION WITH RACGAP1, AND SUBCELLULAR LOCATION.
RX PubMed=12590651; DOI=10.1042/bj20021652;
RA Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D.,
RA Chardin P., Gacon G.;
RT "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male
RT germ cells.";
RL Biochem. J. 372:105-112(2003).
RN [9]
RP INTERACTION WITH UBXD5.
RX PubMed=11940653; DOI=10.1128/mcb.22.9.2952-2964.2002;
RA Katoh H., Harada A., Mori K., Negishi M.;
RT "Socius is a novel Rnd GTPase-interacting protein involved in disassembly
RT of actin stress fibers.";
RL Mol. Cell. Biol. 22:2952-2964(2002).
CC -!- FUNCTION: May be specifically involved in neuronal and hepatic
CC functions. Is a C3 toxin-insensitive member of the Rho subfamily (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the Rho-GAP domain of RACGAP1
CC (PubMed:12590651). Interacts with UBXD5 (PubMed:11940653). Interacts
CC with PRAG1 (By similarity). {ECO:0000250|UniProtKB:Q5HZE6,
CC ECO:0000269|PubMed:11940653, ECO:0000269|PubMed:12590651}.
CC -!- INTERACTION:
CC P52198; O43157: PLXNB1; NbExp=2; IntAct=EBI-1111436, EBI-1111488;
CC P52198; O15031: PLXNB2; NbExp=2; IntAct=EBI-1111436, EBI-722004;
CC P52198; Q8R511: Fnbp1; Xeno; NbExp=2; IntAct=EBI-1111436, EBI-1111424;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Note=Colocalizes with RACGAP1 in Golgi-derived
CC proacrosomal vesicles and the acrosome. {ECO:0000269|PubMed:12590651}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; X95456; CAA64726.1; -; mRNA.
DR EMBL; L78833; AAC37595.1; -; Genomic_DNA.
DR EMBL; AF498968; AAM21115.1; -; mRNA.
DR EMBL; BT019394; AAV38201.1; -; mRNA.
DR EMBL; AK290199; BAF82888.1; -; mRNA.
DR EMBL; CH471152; EAW60920.1; -; Genomic_DNA.
DR EMBL; BC094842; AAH94842.1; -; mRNA.
DR EMBL; BC104986; AAI04987.1; -; mRNA.
DR EMBL; BC104990; AAI04991.1; -; mRNA.
DR CCDS; CCDS11452.1; -.
DR RefSeq; NP_005431.1; NM_005440.4.
DR AlphaFoldDB; P52198; -.
DR SMR; P52198; -.
DR BioGRID; 113810; 434.
DR IntAct; P52198; 4.
DR STRING; 9606.ENSP00000466680; -.
DR iPTMnet; P52198; -.
DR PhosphoSitePlus; P52198; -.
DR BioMuta; RND2; -.
DR DMDM; 2507301; -.
DR EPD; P52198; -.
DR jPOST; P52198; -.
DR MassIVE; P52198; -.
DR PaxDb; P52198; -.
DR PeptideAtlas; P52198; -.
DR PRIDE; P52198; -.
DR ProteomicsDB; 56471; -.
DR Antibodypedia; 29498; 124 antibodies from 26 providers.
DR DNASU; 8153; -.
DR Ensembl; ENST00000587250.4; ENSP00000466680.1; ENSG00000108830.10.
DR GeneID; 8153; -.
DR KEGG; hsa:8153; -.
DR MANE-Select; ENST00000587250.4; ENSP00000466680.1; NM_005440.5; NP_005431.1.
DR UCSC; uc002icn.4; human.
DR CTD; 8153; -.
DR DisGeNET; 8153; -.
DR GeneCards; RND2; -.
DR HGNC; HGNC:18315; RND2.
DR HPA; ENSG00000108830; Group enriched (brain, choroid plexus, testis).
DR MIM; 601555; gene.
DR neXtProt; NX_P52198; -.
DR OpenTargets; ENSG00000108830; -.
DR PharmGKB; PA134936989; -.
DR VEuPathDB; HostDB:ENSG00000108830; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000157020; -.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; P52198; -.
DR OMA; QMPSRTN; -.
DR OrthoDB; 1283783at2759; -.
DR PhylomeDB; P52198; -.
DR PathwayCommons; P52198; -.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; P52198; -.
DR BioGRID-ORCS; 8153; 26 hits in 1065 CRISPR screens.
DR ChiTaRS; RND2; human.
DR GeneWiki; Rnd2; -.
DR GenomeRNAi; 8153; -.
DR Pharos; P52198; Tbio.
DR PRO; PR:P52198; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P52198; protein.
DR Bgee; ENSG00000108830; Expressed in C1 segment of cervical spinal cord and 159 other tissues.
DR Genevisible; P52198; HS.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
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:0005769; C:early endosome; IEA:Ensembl.
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:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
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:0048672; P:positive regulation of collateral sprouting; IEA:Ensembl.
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:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd04173; Rnd2_Rho7; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041842; RhoN.
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 Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..224
FT /note="Rho-related GTP-binding protein RhoN"
FT /id="PRO_0000198876"
FT PROPEP 225..227
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281228"
FT REGION 187..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 210..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 224
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 224
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 25369 MW; DB2127B97B468F86 CRC64;
MEGQSGRCKI VVVGDAECGK TALLQVFAKD AYPGSYVPTV FENYTASFEI DKRRIELNMW
DTSGSSYYDN VRPLAYPDSD AVLICFDISR PETLDSVLKK WQGETQEFCP NAKVVLVGCK
LDMRTDLATL RELSKQRLIP VTHEQGTVLA KQVGAVSYVE CSSRSSERSV RDVFHVATVA
SLGRGHRQLR RTDSRRGMQR SAQLSGRPDR GNEGEIHKDR AKSCNLM
