RHPN2_MOUSE
ID RHPN2_MOUSE Reviewed; 686 AA.
AC Q8BWR8; Q9DBN2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Rhophilin-2;
DE AltName: Full=GTP-Rho-binding protein 2;
GN Name=Rhpn2;
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=Liver;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, and Testis;
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 [4]
RP STRUCTURE BY NMR OF 506-603.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of mouse rhophilin-2.";
RL Submitted (AUG-2004) to the PDB data bank.
CC -!- FUNCTION: Binds specifically to GTP-Rho. May function in a Rho pathway
CC to limit stress fiber formation and/or increase the turnover of F-actin
CC structures in the absence of high levels of RhoA activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GTP-bound RhoA and RhoB. Interacts with both
CC GTP- and GDP-bound RhoA. Interacts with KRT18 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RHPN family. {ECO:0000305}.
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DR EMBL; AK004849; BAB23615.1; -; mRNA.
DR EMBL; AK050214; BAC34127.1; -; mRNA.
DR CCDS; CCDS21148.1; -.
DR RefSeq; NP_082173.3; NM_027897.4.
DR PDB; 1VAE; NMR; -; A=506-603.
DR PDBsum; 1VAE; -.
DR AlphaFoldDB; Q8BWR8; -.
DR SMR; Q8BWR8; -.
DR BioGRID; 206579; 3.
DR STRING; 10090.ENSMUSP00000032705; -.
DR iPTMnet; Q8BWR8; -.
DR PhosphoSitePlus; Q8BWR8; -.
DR MaxQB; Q8BWR8; -.
DR PaxDb; Q8BWR8; -.
DR PRIDE; Q8BWR8; -.
DR ProteomicsDB; 253125; -.
DR Antibodypedia; 28974; 142 antibodies from 31 providers.
DR DNASU; 52428; -.
DR Ensembl; ENSMUST00000032705; ENSMUSP00000032705; ENSMUSG00000030494.
DR Ensembl; ENSMUST00000085556; ENSMUSP00000082692; ENSMUSG00000030494.
DR GeneID; 52428; -.
DR KEGG; mmu:52428; -.
DR UCSC; uc009gjs.2; mouse.
DR CTD; 85415; -.
DR MGI; MGI:1289234; Rhpn2.
DR VEuPathDB; HostDB:ENSMUSG00000030494; -.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT00940000153837; -.
DR HOGENOM; CLU_006514_1_1_1; -.
DR InParanoid; Q8BWR8; -.
DR OMA; MICLAYD; -.
DR OrthoDB; 641122at2759; -.
DR PhylomeDB; Q8BWR8; -.
DR TreeFam; TF323502; -.
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 BioGRID-ORCS; 52428; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rhpn2; mouse.
DR EvolutionaryTrace; Q8BWR8; -.
DR PRO; PR:Q8BWR8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BWR8; protein.
DR Bgee; ENSMUSG00000030494; Expressed in secondary oocyte and 231 other tissues.
DR Genevisible; Q8BWR8; MM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003094; P:glomerular filtration; IGI:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.280; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF02185; HR1; 1.
DR SMART; SM01041; BRO1; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46585; SSF46585; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51180; BRO1; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51860; REM_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..686
FT /note="Rhophilin-2"
FT /id="PRO_0000218899"
FT DOMAIN 26..100
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 111..502
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT DOMAIN 515..593
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 46..66
FT /note="Interaction with Rho"
FT /evidence="ECO:0000250"
FT MOD_RES 655
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 55
FT /note="T -> A (in Ref. 1; BAC34127)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="H -> D (in Ref. 1; BAC34127)"
FT /evidence="ECO:0000305"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:1VAE"
FT HELIX 547..551
FT /evidence="ECO:0007829|PDB:1VAE"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:1VAE"
FT HELIX 571..580
FT /evidence="ECO:0007829|PDB:1VAE"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:1VAE"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:1VAE"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:1VAE"
SQ SEQUENCE 686 AA; 76957 MW; BFEBEFB71D04F360 CRC64;
MTDTLLPAAP QPLEKEGDDY FRKGCNPLAQ TGRSKLQNQR AALNQQILKA VRMRTGAENL
LKVATNQKVR EQVRLELSFV NSDLQMLKEE LEGLNISVGV YQGTEEAFTI PLIPLGLKET
KEVDFSIVFK DFILEHYSED SYLYEDDIAD LMDLRQACRT PSRDEAGVEL LMSYFIQLGF
VESRFFPPTR HMGLLFTWYD SFTGVPVSQQ TLLLEKASVL FNIGALYTQI GTRCNRQTQA
GLESAVDAFQ RAAGVLNYLK ETFTHTPSYD MSPAMLSVLV KMMLAQAQES VFEKVCLPGI
QNEFFVLVKV AQEAAKVAEA YRQLHAAMSQ EPVKENIPYS WASVAYVKAY HYGALAHYFA
ATLLIDHQLK PGADEDHQEK CLSQLYDRMP EGMTPLATLK NAGQRVLLGK GHLHRAIGFH
EESLREANLC KKLRDIQVLR DVLSAAHQRT QLKHTQHRED DDLLNLIDAP DVLPKTEREV
KITFPDFSKV TVTDFFQKLG PLSVFSASKR WSPPRGIHFT VEEGDLGFTL RGNTPVQVHF
LDPHCSASLA GAKEGDYIVS IQGVDCKWLT VSEVMKLLKS FGGEEVEMKV VSLLDSTSSM
HNKCATYSVG MQKTYSMICL SMDDDDKADK TKKISKKLSF LSWGTSKNRQ KSASTLCLPE
VGLARSQNKK KLPTPFSLLN SDSSLY
