RTKN_MOUSE
ID RTKN_MOUSE Reviewed; 564 AA.
AC Q8C6B2; E9QM24; Q61192; Q8VIG7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Rhotekin;
GN Name=Rtkn {ECO:0000312|MGI:MGI:107371};
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] {ECO:0000305, ECO:0000312|EMBL:AAC52605.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RHOA; RHOB AND
RP RHOC, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000312|EMBL:AAC52605.1};
RX PubMed=8662891; DOI=10.1074/jbc.271.23.13556;
RA Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N.,
RA Fujisawa K., Morii N., Madaule P., Narumiya S.;
RT "Rhotekin, a new putative target for Rho bearing homology to a
RT serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.";
RL J. Biol. Chem. 271:13556-13560(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC36222.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36222.1};
RC TISSUE=Head {ECO:0000312|EMBL:BAC36222.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH13820.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH13820.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH13820.1};
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Lung;
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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may confer
CC increased resistance to apoptosis to cells in gastric tumorigenesis.
CC May play a novel role in the organization of septin structures (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts via its C-terminal region with the TAX1BP3 PDZ
CC domain. This interaction facilitates Rho-mediated activation of the c-
CC Fos serum response element (SRE). Interacts with SEPT9 (By similarity).
CC Specifically binds to GTP-bound RHOA, RHOB and RHOC and inhibits their
CC GTPase activity. {ECO:0000250|UniProtKB:Q9BST9,
CC ECO:0000269|PubMed:8662891}.
CC -!- INTERACTION:
CC Q8C6B2; Q9QUI0: Rhoa; NbExp=3; IntAct=EBI-1162441, EBI-643583;
CC Q8C6B2; P61586: RHOA; Xeno; NbExp=4; IntAct=EBI-1162441, EBI-446668;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C6B2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8662891};
CC IsoId=Q8C6B2-2; Sequence=VSP_052006;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain and kidney. Weakly
CC expressed in lung, testis, skeletal muscle, heart and thymus.
CC {ECO:0000269|PubMed:8662891}.
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DR EMBL; U54638; AAC52605.1; -; mRNA.
DR EMBL; AK076155; BAC36222.1; -; mRNA.
DR EMBL; AC104324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013820; AAH13820.1; -; mRNA.
DR CCDS; CCDS20274.1; -. [Q8C6B2-2]
DR CCDS; CCDS51817.1; -. [Q8C6B2-1]
DR RefSeq; NP_001129699.1; NM_001136227.1. [Q8C6B2-1]
DR RefSeq; NP_033132.2; NM_009106.2. [Q8C6B2-2]
DR RefSeq; NP_598396.2; NM_133641.2. [Q8C6B2-2]
DR AlphaFoldDB; Q8C6B2; -.
DR SMR; Q8C6B2; -.
DR BioGRID; 203032; 6.
DR DIP; DIP-29983N; -.
DR IntAct; Q8C6B2; 5.
DR MINT; Q8C6B2; -.
DR STRING; 10090.ENSMUSP00000065571; -.
DR iPTMnet; Q8C6B2; -.
DR PhosphoSitePlus; Q8C6B2; -.
DR jPOST; Q8C6B2; -.
DR MaxQB; Q8C6B2; -.
DR PaxDb; Q8C6B2; -.
DR PeptideAtlas; Q8C6B2; -.
DR PRIDE; Q8C6B2; -.
DR ProteomicsDB; 257053; -. [Q8C6B2-1]
DR ProteomicsDB; 257054; -. [Q8C6B2-2]
DR Antibodypedia; 31499; 255 antibodies from 31 providers.
DR Ensembl; ENSMUST00000065512; ENSMUSP00000065571; ENSMUSG00000034930. [Q8C6B2-1]
DR Ensembl; ENSMUST00000087938; ENSMUSP00000085249; ENSMUSG00000034930. [Q8C6B2-2]
DR Ensembl; ENSMUST00000121093; ENSMUSP00000112501; ENSMUSG00000034930. [Q8C6B2-2]
DR GeneID; 20166; -.
DR KEGG; mmu:20166; -.
DR UCSC; uc009cms.2; mouse. [Q8C6B2-1]
DR UCSC; uc009cmt.2; mouse. [Q8C6B2-2]
DR CTD; 6242; -.
DR MGI; MGI:107371; Rtkn.
DR VEuPathDB; HostDB:ENSMUSG00000034930; -.
DR eggNOG; ENOG502QRWR; Eukaryota.
DR GeneTree; ENSGT00940000158491; -.
DR HOGENOM; CLU_025066_1_0_1; -.
DR InParanoid; Q8C6B2; -.
DR OMA; KGLPRTW; -.
DR OrthoDB; 497196at2759; -.
DR PhylomeDB; Q8C6B2; -.
DR TreeFam; TF331476; -.
DR Reactome; R-MMU-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 20166; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8C6B2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8C6B2; protein.
DR Bgee; ENSMUSG00000034930; Expressed in superior frontal gyrus and 233 other tissues.
DR ExpressionAtlas; Q8C6B2; baseline and differential.
DR Genevisible; Q8C6B2; MM.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005095; F:GTPase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0031106; P:septin ring organization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR InterPro; IPR012966; AHD.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR030471; RTKN.
DR PANTHER; PTHR21538:SF19; PTHR21538:SF19; 1.
DR Pfam; PF08174; Anillin; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS51860; REM_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; GTP-binding; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..564
FT /note="Rhotekin"
FT /id="PRO_0000233941"
FT DOMAIN 17..98
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 309..416
FT /note="PH"
FT /evidence="ECO:0000255"
FT REGION 518..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 230
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BST9"
FT VAR_SEQ 1..36
FT /note="MFSRNHRSRITVARGSALEMEFKRGRFRLSFFSESP -> MQDRLRILEDLN
FT MLYIRQMALSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8662891"
FT /id="VSP_052006"
FT CONFLICT 67
FT /note="Q -> L (in Ref. 2; BAC36222)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="R -> G (in Ref. 4; AAH13820)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="A -> V (in Ref. 1; AAC52605 and 4; AAH13820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 63013 MW; 0934EEBF09B12A3E CRC64;
MFSRNHRSRI TVARGSALEM EFKRGRFRLS FFSESPEDTE LQRKLDHEIR MRDGACKLLA
ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLEK TGRRPSDSVQ PAQHSPCRGR
VCISDLRIPL MWKDTEYFKN KGDLHRWAVF LLLQIGEQIQ DTEMVLVDRT LTDISFQNNV
LFAEAEPDFE LRLELYGACV EEEGALAGAP KRLATKLSSS LGRSSGKRVR ASLDSAGASG
NSPVLLPTPA VGGPRFHLLA HTTLTLEEVQ DGFRTHDLTL TSHEENPAWL PLYGSVCCRL
AAQPLCMIQP TASGALRVQQ AGELQNGTLV HGVLKGTNLF CYWRSEDADT GQEPLFTIVI
NKETRVRAGE LEQAPEWPFT LSISNKYGDD EVTNTLQLES REALQNWMEA LWQLFFDMSQ
WRHCCDEVMK IETPAPRKPP QALAKQGSLY HEMAIEPLDD IAAVTDILAQ REGTRLEPSP
PWLAMFTDQP ALPSSCSPAS VAPVPTWMQP LPWGRPRTFS LDAAPADHSL GPSRSVAPLP
PQRSPKSRGF YSKSQLGPWL QSPV
