RHBT3_MOUSE
ID RHBT3_MOUSE Reviewed; 611 AA.
AC Q9CTN4; Q05DP2; Q3UTS4; Q80X55; Q9CVT0;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Rho-related BTB domain-containing protein 3;
DE EC=3.6.1.-;
GN Name=Rhobtb3; Synonyms=Kiaa0878;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12426103; DOI=10.1016/s0378-1119(02)00980-0;
RA Ramos S., Khademi F., Somesh B.P., Rivero F.;
RT "Genomic organization and expression profile of the small GTPases of the
RT RhoBTB family in human and mouse.";
RL Gene 298:147-157(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Retina, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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).
CC -!- FUNCTION: Rab9-regulated ATPase required for endosome to Golgi
CC transport. Involved in transport vesicle docking at the Golgi complex,
CC possibly by participating in release M6PRBP1/TIP47 from vesicles to
CC permit their efficient docking and fusion at the Golgi. Specifically
CC binds Rab9, but not other Rab proteins. Has low intrinsic ATPase
CC activity due to autoinhibition, which is relieved by Rab9 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAB9A and RAB9B (at lower level compared to
CC RAB9A-binding). Interacts with M6PRBP1/TIP47 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05664.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC98044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129234; BAC98044.1; ALT_INIT; mRNA.
DR EMBL; AK020938; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK006650; BAB24689.1; -; mRNA.
DR EMBL; AK139158; BAE23906.1; -; mRNA.
DR EMBL; CH466563; EDL37111.1; -; Genomic_DNA.
DR EMBL; BC005664; AAH05664.1; ALT_SEQ; mRNA.
DR EMBL; BC050836; AAH50836.1; -; mRNA.
DR CCDS; CCDS26652.1; -.
DR RefSeq; NP_082769.1; NM_028493.2.
DR AlphaFoldDB; Q9CTN4; -.
DR SMR; Q9CTN4; -.
DR BioGRID; 215902; 3.
DR STRING; 10090.ENSMUSP00000022078; -.
DR iPTMnet; Q9CTN4; -.
DR PhosphoSitePlus; Q9CTN4; -.
DR MaxQB; Q9CTN4; -.
DR PaxDb; Q9CTN4; -.
DR PRIDE; Q9CTN4; -.
DR ProteomicsDB; 254862; -.
DR Antibodypedia; 636; 136 antibodies from 26 providers.
DR Ensembl; ENSMUST00000022078; ENSMUSP00000022078; ENSMUSG00000021589.
DR GeneID; 73296; -.
DR KEGG; mmu:73296; -.
DR UCSC; uc007rfy.1; mouse.
DR CTD; 22836; -.
DR MGI; MGI:1920546; Rhobtb3.
DR VEuPathDB; HostDB:ENSMUSG00000021589; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00850000132411; -.
DR HOGENOM; CLU_029897_0_0_1; -.
DR InParanoid; Q9CTN4; -.
DR OMA; MSVNIVA; -.
DR OrthoDB; 338031at2759; -.
DR PhylomeDB; Q9CTN4; -.
DR TreeFam; TF323347; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-9706019; RHOBTB3 ATPase cycle.
DR BioGRID-ORCS; 73296; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rhobtb3; mouse.
DR PRO; PR:Q9CTN4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9CTN4; protein.
DR Bgee; ENSMUSG00000021589; Expressed in manus and 223 other tissues.
DR ExpressionAtlas; Q9CTN4; baseline and differential.
DR Genevisible; Q9CTN4; MM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
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:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
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:0008584; P:male gonad development; IMP:MGI.
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:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.30.710.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031260; RhoBTB3.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR PANTHER; PTHR24072:SF139; PTHR24072:SF139; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54695; SSF54695; 2.
DR PROSITE; PS50097; BTB; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Golgi apparatus; Hydrolase; Nucleotide-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..611
FT /note="Rho-related BTB domain-containing protein 3"
FT /id="PRO_0000198965"
FT DOMAIN 254..356
FT /note="BTB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 420..487
FT /note="BTB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..175
FT /note="Rho-like"
FT REGION 420..611
FT /note="Interaction with Rab9"
FT /evidence="ECO:0000250"
FT CONFLICT 588
FT /note="N -> H (in Ref. 3; BAB24689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 69208 MW; F053962BD8CA1CDF CRC64;
MSIHIVALGN EGDTFHQDNR PSGLIRTYLG RSPLVSGDES SLLLNAASTV ARPVFTEYQA
SAFGNVKLVV HDCPVWDIFD SDWYTSRNLI GGADIIVIKY NVNDKFSFHE VKDNYIPVIK
RASNSVPVII AAVGTRQNEE LPCTCPLCTS DRGSCVTTTE GIQLAKELGA TYLELHSLDD
FYIGKYFGGV LEYFMIQALN QKTSEKMKKR KMTSSFHGIR PPQLEQPEKM PVLKAEASHY
HSDLNNLLLC CQCVDVVFYH PEVTGVVEAH KIVLCSVSHV FMLLFNVKSP ADIQDSSIIR
TTQDLFAINR DAVLPGASQE APSNPPLPVI VKDALFCSCL SDILRFIYSG AFQWEELEED
VRRKLKDSGD VSDIIEKVKC ILKTPGKINC LRNCKTYQAR KPLWFYNTSL KFFLNKPMLA
DVVFEIQGAT VPAHRAILVA RCEVMAAMFN GNYMEAKSVL IPVYGVSKET FLSFLEYLYT
DSCCPAGIFQ AMCLLICAEM YQVSRLQHIC ELFIITQLQS MPSRELASMN LDIVDLLKKA
KFHHSDCLST WLLHFIATNY LIFSQKPEFQ DLSVEERSFV EKHRWPSNMY LKQLAEYRKY
IHSRKCRCLV M
