RIPR1_RAT
ID RIPR1_RAT Reviewed; 1217 AA.
AC Q4FZU8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Rho family-interacting cell polarization regulator 1 {ECO:0000312|RGD:1307772};
GN Name=Ripor1 {ECO:0000312|RGD:1307772}; Synonyms=Fam65a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-1217.
RC TISSUE=Placenta;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-347; SER-452; SER-455
RP AND SER-742, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:Q6ZS17}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q6ZS17}. Note=Localizes to the
CC podocyte major processes and cell body. Colocalized with STK26 in the
CC Golgi of serum-starved cells and relocated to cytoplasmic punctae,
CC probably vesicular compartments, along with STK26 upon serum
CC stimulation in a Rho- and PDCD10-dependent manner.
CC {ECO:0000250|UniProtKB:Q68FE6, ECO:0000250|UniProtKB:Q6ZS17}.
CC -!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
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DR EMBL; AABR03114145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099098; AAH99098.1; -; mRNA.
DR RefSeq; NP_001094130.1; NM_001100660.1.
DR AlphaFoldDB; Q4FZU8; -.
DR SMR; Q4FZU8; -.
DR STRING; 10116.ENSRNOP00000023710; -.
DR iPTMnet; Q4FZU8; -.
DR PhosphoSitePlus; Q4FZU8; -.
DR jPOST; Q4FZU8; -.
DR PaxDb; Q4FZU8; -.
DR PRIDE; Q4FZU8; -.
DR Ensembl; ENSRNOT00000023710; ENSRNOP00000023710; ENSRNOG00000017604.
DR GeneID; 291974; -.
DR KEGG; rno:291974; -.
DR UCSC; RGD:1307772; rat.
DR CTD; 79567; -.
DR RGD; 1307772; Ripor1.
DR eggNOG; ENOG502QQ7T; Eukaryota.
DR GeneTree; ENSGT00940000153717; -.
DR HOGENOM; CLU_006211_0_0_1; -.
DR InParanoid; Q4FZU8; -.
DR OrthoDB; 1121546at2759; -.
DR PhylomeDB; Q4FZU8; -.
DR TreeFam; TF329332; -.
DR PRO; PR:Q4FZU8; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000017604; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q4FZU8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS: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:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0051683; P:establishment of Golgi localization; ISS:UniProtKB.
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..1217
FT /note="Rho family-interacting cell polarization regulator
FT 1"
FT /id="PRO_0000289112"
FT REGION 371..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..112
FT /evidence="ECO:0000255"
FT COILED 786..828
FT /evidence="ECO:0000255"
FT COMPBIAS 371..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZS17"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE6"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE6"
SQ SEQUENCE 1217 AA; 131731 MW; FBF69A045AA54388 CRC64;
MMSLSVRPQR RLLSARVSRS QSFAGVLGSQ ERGPRNFTVF SPPGPQRKPL VLSRVSRMFS
VAHPAPKVPQ PERLDLVYAA 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 SGTARYSSTP KPLVQQPEPL PVQVTFRRPE
SLSSGSMDEE PPLTPALVNG HAPYSRTLSH ISEASVDAAL TEAMEAVDLK CPAPGPSPLV
YPESTHVEHV SSVPPVADNG RSATSPALST AGPAPTFIDP ASSTQLDLVH KATDSGSSEL
PSITHTMASS TYSAVSPINS VPGLTSTTVG STHKPMPSPL TSTGSIPSVT DSIQTTTSPT
HTTPSPTHTT VSPTHSTPSP THTTVSPSNA ALSPSNATPS LSHSTTSPTQ KATMSTHTTS
AVGPVQTTTS PISTTVSPSP SVDTAIISSS SAVPSVPGPE ARPCSHPTST PYTKADPTAA
CTSSPSLASS GPKPLTSPAP DSLEQILKSP SSSPSSIVPE PQRSELSLAL VAQAPVPEAT
GGAGDRRLEE ALRTLMAALD DYRGQFPELQ GLEQEVTRLE SLLMQRQGLT RSRASSLSIT
VEHALESFSF LNDDEDEDND SPGDRPTSSP EVVAEERLDS SNAQCLSTGC SALDATLVQH
LYHCSCLLLK LGTFGPLRCQ EAWALERLLR EARVLQEVCE HSKLWGNAVT SAQEVVQFSA
SRPGFLTFWD QCTEGLNPFL CPVEQVLLTF CSQYGARLSL RQPGLAEAVC VKFLEDALGQ
KLPRRPHSGP GEQLTIFQFW SYVEVLDSPS MEAYVTETAE EVLLVQNLNS DDQAVVLKAL
RLAPEGRLRK DGLRALSSLL VHGNSKVMAA VSTQLRSLSL GPVFRERALL CFLDQLEDED
VQTRVAGCLA LGCIKAPEGI EPLVYLCQTD TEAVREAARQ SLQQCGEEGQ SAHRQLEESL
DALPCLFGPS SMASTAF
