RHPN1_MOUSE
ID RHPN1_MOUSE Reviewed; 643 AA.
AC Q61085; E9QMX9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Rhophilin-1;
DE AltName: Full=GTP-Rho-binding protein 1;
GN Name=Rhpn1; Synonyms=Grbp;
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 FUNCTION.
RC TISSUE=Brain, and Embryo;
RX PubMed=8571126; DOI=10.1126/science.271.5249.645;
RA Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N.,
RA Mukai H., Ono Y., Kakizuka A., Narumiya S.;
RT "Protein kinase N (PKN) and PKN-related protein rhophilin as targets of
RT small GTPase Rho.";
RL Science 271:645-648(1996).
RN [2]
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 [3]
RP INTERACTION WITH ROPN1, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=10591629; DOI=10.1242/jcs.113.1.103;
RA Fujita A., Nakamura K., Kato T., Watanabe N., Ishizaki T., Kimura K.,
RA Mizoguchi A., Narumiya S.;
RT "Ropporin, a sperm-specific binding protein of rhophilin, that is localized
RT in the fibrous sheath of sperm flagella.";
RL J. Cell Sci. 113:103-112(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Has no enzymatic activity. May serve as a target for Rho, and
CC interact with some cytoskeletal component upon Rho binding or relay a
CC Rho signal to other molecules. {ECO:0000269|PubMed:8571126}.
CC -!- SUBUNIT: Binds specifically to GTP-Rho. Interacts with ROPN1.
CC {ECO:0000269|PubMed:10591629}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:10591629}.
CC -!- DOMAIN: The PDZ domain mediates interaction with ROPN1.
CC {ECO:0000269|PubMed:10591629}.
CC -!- SIMILARITY: Belongs to the RHPN family. {ECO:0000305}.
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DR EMBL; U43194; AAC52388.1; -; mRNA.
DR EMBL; AC116393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS27548.1; -.
DR RefSeq; NP_032190.2; NM_008164.2.
DR AlphaFoldDB; Q61085; -.
DR SMR; Q61085; -.
DR BioGRID; 200048; 3.
DR CORUM; Q61085; -.
DR IntAct; Q61085; 1.
DR MINT; Q61085; -.
DR STRING; 10090.ENSMUSP00000113042; -.
DR iPTMnet; Q61085; -.
DR PaxDb; Q61085; -.
DR PRIDE; Q61085; -.
DR ProteomicsDB; 255215; -.
DR Antibodypedia; 7394; 169 antibodies from 25 providers.
DR DNASU; 14787; -.
DR Ensembl; ENSMUST00000023244; ENSMUSP00000023244; ENSMUSG00000022580.
DR GeneID; 14787; -.
DR KEGG; mmu:14787; -.
DR UCSC; uc007whc.2; mouse.
DR CTD; 114822; -.
DR MGI; MGI:1098783; Rhpn1.
DR VEuPathDB; HostDB:ENSMUSG00000022580; -.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT00940000153837; -.
DR HOGENOM; CLU_006514_3_0_1; -.
DR InParanoid; Q61085; -.
DR OrthoDB; 641122at2759; -.
DR Reactome; R-MMU-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 14787; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q61085; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61085; protein.
DR Bgee; ENSMUSG00000022580; Expressed in saccule of membranous labyrinth and 82 other tissues.
DR ExpressionAtlas; Q61085; baseline and differential.
DR Genevisible; Q61085; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:MGI.
DR GO; GO:0003094; P:glomerular filtration; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:MGI.
DR GO; GO:0120039; P:plasma membrane bounded cell projection morphogenesis; IMP:MGI.
DR GO; GO:0097018; P:renal albumin absorption; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09248; BRO1_Rhophilin_1; 1.
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 InterPro; IPR042715; Rhophilin-1_BRO1.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF02185; HR1; 1.
DR Pfam; PF00595; PDZ; 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 Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..643
FT /note="Rhophilin-1"
FT /id="PRO_0000218896"
FT DOMAIN 30..104
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 115..462
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT DOMAIN 500..577
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 509
FT /note="S -> G (in Ref. 1; AAC52388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 71319 MW; 4D964E14069CCA5C CRC64;
MILEERPDGQ GTGEESSRPQ DDGSIRKGYG SFVQNQPGQL QSHRARLHQQ ISKELRMRTG
AENLYRATSN TWVRETVALE LSYVNSNLQL LKEELAELST SVDVDQPEGE GITIPMIPLG
LKETKELDWA TPLKELISEH FGEDGTSFET EIQELEDLRQ ATRTPSRDEA GLDLLAAYYS
QLCFLDARFF SPSRSPGLLF HWYDSLTGVP AQQRALAFEK GSVLFNIGAL HTQIGARQDC
SCTEGTNHAA EAFQRAAGAF RLLRENFSHA PSPDMSAASL SMLEQLMIAQ AQECIFKGLL
LPASATPDIC PDQLQLAQEA AQVATEYGLV HRAMAQPPVR DYLPASWTNL AHVKAEHFCA
LAHYHAAMAL CESHPAKGEL ARQEHVFQPS TPHEPLGPTL PQHPEDRRKL AKAHLKRAIL
GQEEALRLHT LCRVLRKVDL LQVVVTQALR RSLAKYSQLE REDDFFEATE APDIQPKTHQ
TPEGPLSVFS TKNRWQLVGP VHMTRGEGSF GFTLRGDSPV LIAAVVPGGQ AESAGLKEGD
YIVSVNGQPC KWWKHLEVVT QLRSMGEEGV SLQVVSLLPS PEPRGTGPRR AALLWNQREC
GFETPMPTRT RPWPILGWSR KNKQGKTGSH PDPCTNRNCV TCP
