RIPR2_MOUSE
ID RIPR2_MOUSE Reviewed; 1078 AA.
AC Q80U16; A6PW01; A6PW03; Q3TQ58; Q5SY29; Q5SZV4; Q5T0J1; Q8BIM7; Q8BJ19;
AC Q8BJ22; Q8BJ32; Q8BJ54;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Rho family-interacting cell polarization regulator 2 {ECO:0000250|UniProtKB:Q9Y4F9};
GN Name=Ripor2 {ECO:0000250|UniProtKB:Q9Y4F9}; Synonyms=Fam65b, Kiaa0386;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND 7).
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Bone, Cerebellum, Medulla oblongata, Spinal cord, Thymus, and
RC Vein;
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]
RP FUNCTION.
RX PubMed=17150207; DOI=10.1016/j.ydbio.2006.11.002;
RA Yoon S., Molloy M.J., Wu M.P., Cowan D.B., Gussoni E.;
RT "C6ORF32 is upregulated during muscle cell differentiation and induces the
RT formation of cellular filopodia.";
RL Dev. Biol. 301:70-81(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-366 AND SER-582, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
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 INTERACTION WITH DYSF, AND INDUCTION.
RX PubMed=24687993; DOI=10.1096/fj.13-246470;
RA Balasubramanian A., Kawahara G., Gupta V.A., Rozkalne A., Beauvais A.,
RA Kunkel L.M., Gussoni E.;
RT "Fam65b is important for formation of the HDAC6-dysferlin protein complex
RT during myogenic cell differentiation.";
RL FASEB J. 28:2955-2969(2014).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=24958875; DOI=10.1073/pnas.1401950111;
RA Diaz-Horta O., Subasioglu-Uzak A., Grati M., DeSmidt A., Foster J., Cao L.,
RA Bademci G., Tokgoz-Yilmaz S., Duman D., Cengiz F.B., Abad C., Mittal R.,
RA Blanton S., Liu X.Z., Farooq A., Walz K., Lu Z., Tekin M.;
RT "FAM65B is a membrane-associated protein of hair cell stereocilia required
RT for hearing.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9864-9868(2014).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25588844; DOI=10.1242/jcs.161497;
RA Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
RT "Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
RT leading edges polarizes neutrophils.";
RL J. Cell Sci. 128:992-1000(2015).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RHOA AND RHOC, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 176-ARG-LEU-177.
RX PubMed=27269051; DOI=10.7554/elife.14222;
RA Zhao B., Wu Z., Mueller U.;
RT "Murine Fam65b forms ring-like structures at the base of stereocilia
RT critical for mechanosensory hair cell function.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Acts as an inhibitor of the small GTPase RHOA and plays
CC several roles in the regulation of myoblast and hair cell
CC differentiation, lymphocyte T proliferation and neutrophil polarization
CC (PubMed:25588844, PubMed:27269051). Plays a role in fetal mononuclear
CC myoblast differentiation by promoting filopodia and myotube formation
CC (PubMed:17150207). Maintains naive T lymphocytes in a quiescent state
CC and prevents chemokine-induced T lymphocyte responses, such as cell
CC adhesion, polarization and migration (By similarity). Involved also in
CC the regulation of neutrophil polarization, chemotaxis and adhesion
CC (PubMed:25588844). Required for normal development of inner and outer
CC hair cell stereocilia within the cochlea of the inner ear
CC (PubMed:27269051). Plays a role for maintaining the structural
CC organization of the basal domain of stereocilia (PubMed:27269051).
CC Involved in mechanosensory hair cell function (PubMed:27269051).
CC Required for normal hearing (PubMed:27269051).
CC {ECO:0000250|UniProtKB:Q9Y4F9, ECO:0000269|PubMed:17150207,
CC ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27269051}.
CC -!- SUBUNIT: Homooligomer; homooligomerization is regulated by RHOC and
CC leads to the formation of concatemers through the association of N- and
CC C-termini (PubMed:27269051). Interacts (phosphorylated form) with 14-3-
CC 3 proteins; these interactions occur during myogenic cell
CC differentiation and also induces T cell proliferation arrest (By
CC similarity). Interacts (phosphorylated form) with HDAC6; this
CC interaction occurs during early myogenic differentiation, prevents
CC HDAC6 to deacetylate tubulin and also induces T cell proliferation
CC arrest (By similarity). Interacts with DYSF; this interaction occurs
CC during early myogenic differentiation (PubMed:24687993). Interacts with
CC MYOF (By similarity). Interacts (via active GTP- or inactive GDP-bound
CC forms) with RHOA; this interaction is direct, blocks the loading of GTP
CC to RHOA and decreases upon chemokine CCL19 stimulation in primary T
CC lymphocytes (PubMed:27269051). Interacts with RHOC (PubMed:27269051).
CC Interacts (via phosphorylated form) with YWHAB; this interaction occurs
CC in a chemokine-dependent manner and does not compete for binding of
CC RIPOR2 with RHOA nor blocks inhibition of RIPOR2-mediated RHOA activity
CC (By similarity). Interacts with YWHAE (By similarity). Interacts with
CC YWHAQ (By similarity). {ECO:0000250|UniProtKB:Q9Y4F9,
CC ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:27269051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4F9}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y4F9}. Cell
CC projection, filopodium {ECO:0000250|UniProtKB:Q9Y4F9}. Cell projection,
CC stereocilium {ECO:0000269|PubMed:27269051}. Cell projection,
CC stereocilium membrane {ECO:0000250|UniProtKB:Q7TP54}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q7TP54}. Note=Localized in the
CC cytoplasm in cells undergoing mitosis (By similarity). Colocalized with
CC F-actin (By similarity). Accumulates at the leading edge of polarized
CC neutrophils in a chemokine-dependent manner (By similarity). Localized
CC with RHOC within the basal domain of hair cell stereocilia, near the
CC taper region (PubMed:27269051). Detected in punctate pattern forming a
CC circumferential ring at the stereocilia base (PubMed:27269051).
CC Localized to the apical stereocilia of inner and outer hair cells (By
CC similarity). Not detected as a membrane-associated protein in
CC stereocilia (PubMed:27269051). {ECO:0000250|UniProtKB:Q9Y4F9,
CC ECO:0000269|PubMed:27269051}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q80U16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U16-2; Sequence=VSP_025914, VSP_025917;
CC Name=3;
CC IsoId=Q80U16-3; Sequence=VSP_025910, VSP_025913;
CC Name=4;
CC IsoId=Q80U16-4; Sequence=VSP_025911, VSP_025912;
CC Name=5;
CC IsoId=Q80U16-5; Sequence=VSP_025908, VSP_025909, VSP_025914,
CC VSP_025917;
CC Name=6;
CC IsoId=Q80U16-6; Sequence=VSP_025908, VSP_025909, VSP_025915,
CC VSP_025916;
CC Name=7;
CC IsoId=Q80U16-7; Sequence=VSP_025907, VSP_025909, VSP_025914,
CC VSP_025917;
CC -!- TISSUE SPECIFICITY: Expressed in the cochlea (PubMed:24958875).
CC Expressed in inner hair cells and outer hair cells and Hensen's cells
CC (at protein level) (PubMed:27269051). Expressed in the brain,
CC cerebellum, spinal cord, retina, heart, spleen liver, kidney, bladder,
CC muscle and lung (PubMed:24958875, PubMed:27269051). Expressed in the
CC cochlea of the inner ear (PubMed:24958875, PubMed:27269051).
CC {ECO:0000269|PubMed:24958875, ECO:0000269|PubMed:27269051}.
CC -!- INDUCTION: Up-regulated during regenerating muscle tissue.
CC {ECO:0000269|PubMed:24687993}.
CC -!- PTM: Phosphorylated. Chemokine-induced phosphorylation in neutrophils
CC occurs in a PKC- and AKT-dependent manner, resulting in RIPOR2
CC interaction with YWHAB and stabilization. Phosphorylated by PKCA, AKT1
CC and MAPKAPK1A; in vitro. {ECO:0000250|UniProtKB:Q9Y4F9}.
CC -!- DISRUPTION PHENOTYPE: Mice are deaf at 4 weeks of age
CC (PubMed:27269051). Show abnormal hair bundle morphology and polarity
CC and stereociliary growth in the cochlea of the inner ear
CC (PubMed:27269051). Display mislocalization of protein TPRN to the base
CC of stereocilia (PubMed:27269051). Show reduced mechanotransduction
CC currents in hair bundles of outer hair cells (PubMed:27269051). Mice
CC show impaired neutrophil chemotaxis, increased neutrophil adhesion to
CC endothelial cell and reduced neutrophil infiltration into inflamed
CC peritonea (PubMed:25588844). Display increased chemokine-induced RHOA
CC activity and mislocalization of myosin light chain MYL2 in neutrophils
CC (PubMed:25588844). {ECO:0000269|PubMed:25588844,
CC ECO:0000269|PubMed:27269051}.
CC -!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122269; BAC65551.1; ALT_INIT; mRNA.
DR EMBL; AK031928; BAC27606.1; -; mRNA.
DR EMBL; AK036452; BAC29436.1; -; mRNA.
DR EMBL; AK039271; BAC30301.1; -; mRNA.
DR EMBL; AK040887; BAC30732.1; -; mRNA.
DR EMBL; AK041665; BAC31025.1; -; mRNA.
DR EMBL; AK163880; BAE37527.1; -; mRNA.
DR EMBL; AL591851; CAI25708.2; -; Genomic_DNA.
DR EMBL; AL513014; CAI25708.2; JOINED; Genomic_DNA.
DR EMBL; AL513014; CAI25774.2; -; Genomic_DNA.
DR EMBL; AL589699; CAI25774.2; JOINED; Genomic_DNA.
DR EMBL; AL513014; CAI25775.2; -; Genomic_DNA.
DR EMBL; AL591851; CAI25775.2; JOINED; Genomic_DNA.
DR EMBL; AL589699; CAI26080.2; -; Genomic_DNA.
DR EMBL; AL513014; CAI26080.2; JOINED; Genomic_DNA.
DR EMBL; AL513014; CAO77914.1; -; Genomic_DNA.
DR EMBL; AL513014; CAO77916.1; -; Genomic_DNA.
DR EMBL; AL589699; CAO77916.1; JOINED; Genomic_DNA.
DR CCDS; CCDS26377.2; -. [Q80U16-5]
DR CCDS; CCDS36622.1; -. [Q80U16-1]
DR CCDS; CCDS36623.1; -. [Q80U16-2]
DR RefSeq; NP_001073850.1; NM_001080381.1. [Q80U16-2]
DR RefSeq; NP_001273029.1; NM_001286100.1.
DR RefSeq; NP_001273030.1; NM_001286101.1. [Q80U16-7]
DR RefSeq; NP_083955.1; NM_029679.2. [Q80U16-1]
DR RefSeq; NP_848773.3; NM_178658.5. [Q80U16-5]
DR AlphaFoldDB; Q80U16; -.
DR BioGRID; 228735; 2.
DR STRING; 10090.ENSMUSP00000106013; -.
DR iPTMnet; Q80U16; -.
DR PhosphoSitePlus; Q80U16; -.
DR EPD; Q80U16; -.
DR jPOST; Q80U16; -.
DR MaxQB; Q80U16; -.
DR PaxDb; Q80U16; -.
DR PRIDE; Q80U16; -.
DR ProteomicsDB; 253316; -. [Q80U16-1]
DR ProteomicsDB; 253317; -. [Q80U16-2]
DR ProteomicsDB; 253318; -. [Q80U16-3]
DR ProteomicsDB; 253319; -. [Q80U16-4]
DR ProteomicsDB; 253320; -. [Q80U16-5]
DR ProteomicsDB; 253321; -. [Q80U16-6]
DR ProteomicsDB; 253322; -. [Q80U16-7]
DR Antibodypedia; 25358; 175 antibodies from 26 providers.
DR Ensembl; ENSMUST00000038477; ENSMUSP00000043663; ENSMUSG00000036006. [Q80U16-2]
DR Ensembl; ENSMUST00000058009; ENSMUSP00000051342; ENSMUSG00000036006. [Q80U16-3]
DR Ensembl; ENSMUST00000091694; ENSMUSP00000089286; ENSMUSG00000036006. [Q80U16-5]
DR Ensembl; ENSMUST00000110384; ENSMUSP00000106013; ENSMUSG00000036006. [Q80U16-1]
DR GeneID; 193385; -.
DR KEGG; mmu:193385; -.
DR UCSC; uc007pwa.2; mouse. [Q80U16-6]
DR UCSC; uc007pwb.2; mouse. [Q80U16-5]
DR UCSC; uc007pwc.1; mouse. [Q80U16-4]
DR UCSC; uc007pwd.1; mouse. [Q80U16-2]
DR UCSC; uc007pwe.1; mouse. [Q80U16-1]
DR UCSC; uc011yxo.2; mouse. [Q80U16-7]
DR CTD; 9750; -.
DR MGI; MGI:2444879; Ripor2.
DR VEuPathDB; HostDB:ENSMUSG00000036006; -.
DR eggNOG; ENOG502QQ7T; Eukaryota.
DR GeneTree; ENSGT00940000153717; -.
DR HOGENOM; CLU_432085_0_0_1; -.
DR InParanoid; Q80U16; -.
DR OMA; HENEQSR; -.
DR OrthoDB; 1121546at2759; -.
DR PhylomeDB; Q80U16; -.
DR TreeFam; TF329332; -.
DR BioGRID-ORCS; 193385; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Fam65b; mouse.
DR PRO; PR:Q80U16; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q80U16; protein.
DR Bgee; ENSMUSG00000036006; Expressed in lateral septal nucleus and 233 other tissues.
DR ExpressionAtlas; Q80U16; baseline and differential.
DR Genevisible; Q80U16; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR GO; GO:0060171; C:stereocilium membrane; ISO:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IMP:UniProtKB.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:1903904; P:negative regulation of establishment of T cell polarity; ISS:UniProtKB.
DR GO; GO:1905872; P:negative regulation of protein localization to cell leading edge; IMP:UniProtKB.
DR GO; GO:2001107; P:negative regulation of Rho guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:2000405; P:negative regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR031780; FAM65_N.
DR InterPro; IPR033035; FAM65B.
DR InterPro; IPR026136; RIPOR3.
DR PANTHER; PTHR15829; PTHR15829; 1.
DR PANTHER; PTHR15829:SF2; PTHR15829:SF2; 1.
DR Pfam; PF15903; PL48; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Chemotaxis; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Hearing;
KW Membrane; Myogenesis; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..1078
FT /note="Rho family-interacting cell polarization regulator
FT 2"
FT /id="PRO_0000289115"
FT REGION 80..138
FT /note="Involved in cell filopodia formation"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F9"
FT REGION 488..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..137
FT /evidence="ECO:0000255"
FT COMPBIAS 488..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F9"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025907"
FT VAR_SEQ 1..16
FT /note="MPPGTKRLRALGAFSA -> MQFLDPEDLLDEEDDIFGE (in isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025908"
FT VAR_SEQ 385..426
FT /note="Missing (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025909"
FT VAR_SEQ 385..389
FT /note="RWLRL -> VGNGT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025910"
FT VAR_SEQ 385..388
FT /note="RWLR -> VSSV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025911"
FT VAR_SEQ 389..1078
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025912"
FT VAR_SEQ 390..1078
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025913"
FT VAR_SEQ 650..672
FT /note="CKPAGSRSRSSSLSLTVESALES -> DAKHLEDQRLNDAASRMEITEGE
FT (in isoform 2, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025914"
FT VAR_SEQ 650..668
FT /note="CKPAGSRSRSSSLSLTVES -> VSTFLGKKKKSDLVWKNAS (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025915"
FT VAR_SEQ 669..1078
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025916"
FT VAR_SEQ 673..1078
FT /note="Missing (in isoform 2, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025917"
FT MUTAGEN 176..177
FT /note="RL->AA: Inhibits interaction with RHOC. Reduces
FT homooligomerization activity. Inhibits RHOC-dependent
FT homooligomerization activity. Abolishes ability to rescue
FT the morphological hair bundle defect in hair cell of
FT RIPOR2-deficient mice."
FT /evidence="ECO:0000269|PubMed:27269051"
FT CONFLICT 534
FT /note="R -> S (in Ref. 1; BAC65551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1078 AA; 118970 MW; 207E1F6172144E2C CRC64;
MPPGTKRLRA LGAFSAGLPT RLPEIMLVGS QSFSPGGPNG IIRSQSFAGF SGLQERRSRC
NSFIENASAL KKPQAKLKKM HNLGHKNNNT PKEPQPKRVE EVYRALKNGL DEYLEFHQTE
LDKLTAQLKD MKRNSRLGVL YDLDKQIKTI ERYMRRLEFH ISKVDELYEA YCIQRRLQDG
ASKMKQAFAT SPASKAARES LSEINRSYKE YTENMCAIEA ELESLLGEFS IKMKGLAGFA
RLCPGDQYEI FMKYGRQRWK LKGKIEVNGK QSWDGAETVF LPLIVGFISI KVTELKGLAT
HILVGSVTCE TKELFAARPQ VVAVDINDLG TIKLNLEITW YPFDVEDTTP SSGPGNKTAA
LQRRMSMYSQ GTPETPTFKD QSFFRWLRLS VLSALRDTFF ATLHHNHSVG DLPSLSLNPK
ALLEFYSNLP DDIFESGKAA EEKRPLSLSF SDLQDGDCVF TSSSATSPSS SHSAHPEITI
TPAELTHSSL SSQNEGTEDS SSASSRNSLG EDHEPKSHPK SDTVEPGKPG VATRSGTESL
FLESSVAEAL LQESDEASEL KPVELDTFEG NITKQLVKRL TSAEGPVTTD KLFFEGSVGS
ESEAGRSFLD GSLEDAFNGL FLALDPHKKQ YKEFQDLNQE VTHLDDVLKC KPAGSRSRSS
SLSLTVESAL ESFDFLNTSD FDEEEEDGDD VCHVGGGADS VFSDTETEKS GYRSVHPEAR
GHLSEALTED TGVGTSVAGS PLPLTTGNES LDITIVKHLQ YCTQLIQQIV FSSKTPFVAR
SLLEKLSRQV LVMQKLAAVS DENLGNITSV VEAIPEFHKK LSLLAFWTKC CSPSGVYHSS
AARLIKQLEA SFARSINKDY PGLAEPVFRT LVSQILDRAE PLLSSSLSSE VITVFQYYSF
FTSHGVSDLE TYLGQLTRQV AMVQTLQSLR DEKLLQTMSD LAPSNLPAQQ EVLRTLALLL
TRDDNEVSEA VTLYLAAASK NEHFREKALL YYCEALTKAN LQLQKAACLA LKSLEATESI
KMLVTLCQSD TEEIRTVASE TLLSLGEDGR LAYEQLDKFP RDCVKVGGRH GTEVATAF
