RIPR1_MOUSE
ID RIPR1_MOUSE Reviewed; 1223 AA.
AC Q68FE6; G5E8A2; Q80T73; Q8K0T1; Q9D6R4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Rho family-interacting cell polarization regulator 1 {ECO:0000250|UniProtKB:Q6ZS17};
GN Name=Ripor1 {ECO:0000250|UniProtKB:Q6ZS17}; Synonyms=Fam65a, Kiaa1930;
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 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 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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1091-1223.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17251388; DOI=10.1681/asn.2006060675;
RA Patrakka J., Xiao Z., Nukui M., Takemoto M., He L., Oddsson A., Perisic L.,
RA Kaukinen A., Szigyarto C.A.-K., Uhlen M., Jalanko H., Betsholtz C.,
RA Tryggvason K.;
RT "Expression and subcellular distribution of novel glomerulus-associated
RT proteins Dendrin, Ehd3, Sh2d4a, Plekhh2, and 2310066E14Rik.";
RL J. Am. Soc. Nephrol. 18:689-697(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-347; THR-351;
RP SER-468; SER-748; SER-874 AND SER-875, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
CC -!- FUNCTION: Downstream effector protein for Rho-type small GTPases that
CC plays a role in cell polarity and directional migration. Acts as an
CC adapter protein, linking active Rho proteins to STK24 and STK26
CC kinases, and hence positively regulates Golgi reorientation in
CC polarized cell migration upon Rho activation. Involved in the
CC subcellular relocation of STK26 from the Golgi to cytoplasm punctae in
CC a Rho- and PDCD10-dependent manner upon serum stimulation.
CC {ECO:0000250|UniProtKB:Q6ZS17}.
CC -!- SUBUNIT: Interacts (via N-terminus) with RHOA (GTP-bound form); this
CC interaction links active RHOA to STK24 and STK26 kinases. Interacts
CC with RHOB. Interacts with RHOC. Interacts (via C-terminus) with PDCD10;
CC this interaction occurs in a Rho-independent manner. Interacts (via C-
CC terminus) with STK24; this interaction occurs in a PDCD10-dependent and
CC Rho-independent manner. Interacts (via C-terminus) with STK26; this
CC interaction occurs in a PDCD10-dependent and Rho-independent manner.
CC Interacts (via N-terminus) with 14-3-3 proteins; these interactions
CC occur in a Rho-dependent manner. {ECO:0000250|UniProtKB:Q6ZS17}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17251388}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q6ZS17}. Note=Localizes to the
CC podocyte major processes and cell body (PubMed:17251388). Colocalized
CC with STK26 in the Golgi of serum-starved cells and relocated to
CC cytoplasmic punctae, probably vesicular compartments, along with STK26
CC upon serum stimulation in a Rho- and PDCD10-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q6ZS17,
CC ECO:0000269|PubMed:17251388}.
CC -!- TISSUE SPECIFICITY: Expressed in the kidney exclusively by glomerular
CC podocytes. {ECO:0000269|PubMed:17251388}.
CC -!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06820.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH30451.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB26677.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65855.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122573; BAC65855.1; ALT_INIT; mRNA.
DR EMBL; AC127419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11288.1; -; Genomic_DNA.
DR EMBL; BC006820; AAH06820.1; ALT_INIT; mRNA.
DR EMBL; BC030451; AAH30451.1; ALT_INIT; mRNA.
DR EMBL; BC079880; AAH79880.1; -; mRNA.
DR EMBL; AK010063; BAB26677.1; ALT_INIT; mRNA.
DR CCDS; CCDS52660.1; -.
DR RefSeq; NP_001074710.2; NM_001081241.2.
DR RefSeq; XP_006531525.1; XM_006531462.3.
DR AlphaFoldDB; Q68FE6; -.
DR SMR; Q68FE6; -.
DR BioGRID; 217671; 2.
DR STRING; 10090.ENSMUSP00000039966; -.
DR iPTMnet; Q68FE6; -.
DR PhosphoSitePlus; Q68FE6; -.
DR EPD; Q68FE6; -.
DR jPOST; Q68FE6; -.
DR MaxQB; Q68FE6; -.
DR PaxDb; Q68FE6; -.
DR PeptideAtlas; Q68FE6; -.
DR PRIDE; Q68FE6; -.
DR ProteomicsDB; 253293; -.
DR Antibodypedia; 941; 36 antibodies from 13 providers.
DR Ensembl; ENSMUST00000043531; ENSMUSP00000039966; ENSMUSG00000038604.
DR GeneID; 75687; -.
DR KEGG; mmu:75687; -.
DR UCSC; uc009ndj.1; mouse.
DR CTD; 79567; -.
DR MGI; MGI:1922937; Ripor1.
DR VEuPathDB; HostDB:ENSMUSG00000038604; -.
DR eggNOG; ENOG502QQ7T; Eukaryota.
DR GeneTree; ENSGT00940000153717; -.
DR HOGENOM; CLU_006211_0_0_1; -.
DR InParanoid; Q68FE6; -.
DR OMA; THKARMS; -.
DR OrthoDB; 1121546at2759; -.
DR PhylomeDB; Q68FE6; -.
DR TreeFam; TF329332; -.
DR BioGRID-ORCS; 75687; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ripor1; mouse.
DR PRO; PR:Q68FE6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q68FE6; protein.
DR Bgee; ENSMUSG00000038604; Expressed in gastrula and 242 other tissues.
DR Genevisible; Q68FE6; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:1990869; P:cellular response to chemokine; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0051683; P:establishment of Golgi localization; ISS:UniProtKB.
DR GO; GO:2001107; P:negative regulation of Rho guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
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; IPR026136; RIPOR3.
DR PANTHER; PTHR15829; PTHR15829; 1.
DR Pfam; PF15903; PL48; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Golgi apparatus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1223
FT /note="Rho family-interacting cell polarization regulator
FT 1"
FT /id="PRO_0000289111"
FT REGION 371..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..112
FT /evidence="ECO:0000255"
FT COMPBIAS 371..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZS17"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU8"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU8"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 580
FT /note="T -> I (in Ref. 4; AAH79880)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="Y -> C (in Ref. 4; AAH30451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1223 AA; 132352 MW; DB34F4C03A86DAB4 CRC64;
MMSLSVRPQR RLLSARVSRS QSFAGVLGSH ERGPRSFTVF SPPGPPRKPL VLSRVSRMFS
VAHPAPKVPQ PERLDLVYTA LKRGLTAYLE VHQQEQEKLQ RQIKESKRNS RLGFLYDLDK
QVKSIERFLR RLEFHASKID ELYEAYCVQR RLRDGAYNMV RAYSTGSPGS REARDSLAEA
TRGHREYTES MCLLENELEA QLGEFHLRMK GLAGFARLCV GDQYEICMKY GRQRWKLRGR
IESSGKQVWD SEETVFLPLL TEFLSIKVTE LKGLANHVVV GSVSCETKDL FAALPQVVAV
DINDLGTIKL SLEVIWSPFD KDDQPSAAST VNKASTVTKR FSTYSQSPPD TPSLREQAFY
NMLRRQEELE NGTAWSLSSE SSDDSSSPQL SGTARHSTPK PLVQQPEPLP VQVAFRRPES
LTSGSMDEEP AMTPSLVNGH APYSRTLSHI SEASVDAALT EAVEAVDSQS PIPGPSPLVY
PDSTHVERVS SVLPVLNNGH SATSPALSTT GPAPTFIDPA PTTQLDLVHK TTDSAPSELP
SITHTTTSSA YSAVSLVNSV PSLTSTTIGS AHTTTPSPLT STGSVPNATD STQATPSPTH
STPSPTHTTI RLTHTTVSPT HSSPSPIHTT PSPTHTTVSP TCTTPSSGHS TTSPTQEAKM
STHTTGAVGP VQTTTSPIST TESPSPSTDV AIISSSSAES TGPGTEPLPC SHPASPPYTK
ADPTASCTSY QSLASSGSKP LTSPAPDSPE QIPKSPSSSP SSSAPEPQHS EHNLAAVAQA
PVPEATGGAG DRRLEEALGT LMSALDDYRG QFPELQGLEQ EVTRLESLLM QRQGLTRSRA
SSLSITVEHA LESFSFLNDD EDEDNDGPGD RHTSSPEVVA EDRLDSSNGQ SLSTGCSALD
ATLVQHLYHC SRLLLKLGTF GPLRCQEAWA LERLLREARV FQEVCERSKL WGNSATSAQE
VVQFSASRPG FLTFWDQCTE GLSPFICSVE RVLLTFCSQY GARLSLRQPG LAEAVCVKFL
EDALGQKLPR RPQPGPGEQF TIFQFWSYVE ALDSPSMDAY VTETAEEVLL VQNLNSDDQA
VVLKALRLAP EGRLRKDGLR ALSSLLVHGN NKVMAAVSTQ LRSLSLGPVF RERALLCFLD
QLEDGDVQTR VAGCLALGCI KAPEGIEPLV YLCQTDTEAV REAARQSLQQ CGEEGQSAHR
QLEESLDALP CIFGPSSMAS TAF
