MPRIP_RAT
ID MPRIP_RAT Reviewed; 1029 AA.
AC Q9ERE6; Q4KM03;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Myosin phosphatase Rho-interacting protein;
DE AltName: Full=Rho-interacting protein 3;
DE Short=RIP3;
DE AltName: Full=p116Rip;
GN Name=Mprip; Synonyms=Mrip, Rhoip3;
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 [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RA Lanson N.A. Jr., Royals B.A., Claycomb W.C.;
RT "Cloning and sequencing of the rat homologue of p116Rip.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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-226; SER-230; SER-297;
RP SER-622; SER-981 AND SER-997, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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: Targets myosin phosphatase to the actin cytoskeleton.
CC Required for the regulation of the actin cytoskeleton by RhoA and
CC ROCK1. Depletion leads to an increased number of stress fibers in
CC smooth muscle cells through stabilization of actin fibers by
CC phosphorylated myosin. Overexpression of MRIP as well as its F-actin-
CC binding region leads to disassembly of stress fibers in neuronal cells
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent
CC coiled coil domains. Interacts with MYZAP. Binds F-actin through its N-
CC terminus (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Colocalizes with F-actin. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERE6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERE6-2; Sequence=VSP_017301;
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DR EMBL; AF311311; AAG23699.1; -; mRNA.
DR EMBL; BC098911; AAH98911.1; -; mRNA.
DR RefSeq; NP_001029194.1; NM_001034022.1.
DR RefSeq; NP_446266.2; NM_053814.2.
DR AlphaFoldDB; Q9ERE6; -.
DR SMR; Q9ERE6; -.
DR BioGRID; 250473; 1.
DR STRING; 10116.ENSRNOP00000045501; -.
DR CarbonylDB; Q9ERE6; -.
DR iPTMnet; Q9ERE6; -.
DR PhosphoSitePlus; Q9ERE6; -.
DR PaxDb; Q9ERE6; -.
DR PRIDE; Q9ERE6; -.
DR GeneID; 116504; -.
DR KEGG; rno:116504; -.
DR UCSC; RGD:619947; rat. [Q9ERE6-1]
DR CTD; 23164; -.
DR RGD; 619947; Mprip.
DR eggNOG; KOG4807; Eukaryota.
DR InParanoid; Q9ERE6; -.
DR OrthoDB; 428862at2759; -.
DR PRO; PR:Q9ERE6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001725; C:stress fiber; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:RGD.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR CDD; cd13275; PH_M-RIP; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR039597; M-RIP_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1029
FT /note="Myosin phosphatase Rho-interacting protein"
FT /id="PRO_0000097352"
FT DOMAIN 43..150
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 391..487
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..387
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT REGION 152..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..828
FT /note="Interaction with RHOA"
FT /evidence="ECO:0000250"
FT REGION 828..883
FT /note="Interaction with PPP1R12A"
FT /evidence="ECO:0000250"
FT COILED 675..979
FT /evidence="ECO:0000255"
FT COMPBIAS 173..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97434"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 650
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97434"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT VAR_SEQ 352..387
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017301"
FT CONFLICT 886
FT /note="R -> G (in Ref. 2; AAH98911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1029 AA; 117113 MW; 1963C8F11EF58ED4 CRC64;
MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL LLAPDGTDFD
NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM NQCTDVVDGE ARTGQKFSLC
ILTPDKEHFI RAETKEIISG WLEMLMVYPR TNKQNQKKKR KVEPPTPQEP GPAKMAVTSS
SGGSSGSSSS SSSSSIPSAE KVPTTKSTLW QEEMRAKDQP DGTSLSPVQS PSQSQPPAAC
TPRETGLDSK EDENILSGDR VDGGRKVRVE SGYFSLEKAK QDLRAEEQLP PLLSPPSPST
PHSRRSQVIE KFEALDIEKA EHMETNMLIL TTPSSDTRQG RSERRAIPRK RDFASETPTA
PLSDACPLSP HRRAKSLDRR STESSMTPDL LNFKKGWLTK QYEDGQWKKH WFVLADQSLR
YYRDSVAEEA ADLDGEINLS TCYDVTEYPV QRNYGFQIHT KEGEFTLSAM TSGIRRNWIQ
TIMKHVLPTS APDVTSSLPE GKNKSTSFDT CLRPSEKQEA EPGEPDPEQK KSRARERRRE
GRSKTFDWAE FRPIQQALAQ ERASTVGSSD SGDPGCLEAE PGELERERAR RREERRKRFG
MLDTNDGPGM EDTALRMDID RSPGLLGTPD LKTQNVHVEI EQRWHQVETT PLREEKQVPI
APLHLSLEDR SERLSTHELT SLLEKELEQS QKEASDLLEQ NRLLQDQLRV ALGREQSARE
GYVLQATCER GFAAMEETHQ KKIEDLQRQH QRELEKLREE KDRLLAEETA ATISAIEAMK
NAHREEMERE LEKSQRSQIS SINSDIEALR RQYLEELQSV QRELEVLSEQ YSQKCLENAH
LAQALEAERQ ALRQCQRENQ ELNAHNQELN NRLAAEITRL RTLLTREGGG ESTGLPLTQG
KDAYELEVLL RVKESEIQYL KQEISSLKDE LQTALRDKKY ASDKYKDIYT ELSIAKAKAD
CDISRLKEQL KAATEALGEK SPEGTTVSGY DIMKSKSNPD FLKKDRSCVT RQLRNIRSKS
VIEQVSWDN
