[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R12A AND RHOA. TISSUE=Aorta; DOI=10.1074/jbc.M305622200; PubMed=14506264 [NCBI, ExPASy, EBI, Israel, Japan] Surks H.K., Richards C.T., Mendelsohn M.E.; "Myosin phosphatase-Rho interacting protein. A new member of the myosin phosphatase complex that directly binds RhoA."; J. Biol. Chem. 278:51484-51493(2003).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH PPP1R12A. DOI=10.1074/jbc.M410909200; PubMed=15545284 [NCBI, ExPASy, EBI, Israel, Japan] Koga Y., Ikebe M.; "p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA."; J. Biol. Chem. 280:4983-4991(2005).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Inazawa J., Imoto I.; "Cloning of human orthologue RHOIP3 of Mus Rhoip3."; Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1024 (ISOFORM 1). TISSUE=Melanoma; The German cDNA consortium; Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-1024 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-1024 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-1024 (ISOFORM 2). TISSUE=Brain, Lymph, and Muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R12A AND F-ACTIN. DOI=10.1074/jbc.M506863200; PubMed=16257966 [NCBI, ExPASy, EBI, Israel, Japan] Surks H.K., Riddick N., Ohtani K.; "M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells."; J. Biol. Chem. 280:42543-42551(2005).
[7]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-223; SER-364; SER-618 AND SER-992, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-992, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).

Comments

FUNCTION: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells.
SUBUNIT: Binds F-actin through its N-terminus (By similarity). Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains.
INTERACTION:
P31946:YWHAB; NbExp=1; IntAct=EBI-1022605, EBI-359815;
P61981:YWHAG; NbExp=1; IntAct=EBI-1022605, EBI-359832;
P27348:YWHAQ; NbExp=1; IntAct=EBI-1022605, EBI-359854;
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes with F-actin.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q6WCQ1-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q6WCQ1-2
Features which should be applied to build the isoform sequence: VSP_051948.

Name	3
Isoform ID	Q6WCQ1-3
Features which should be applied to build the isoform sequence: VSP_051947, VSP_051948.

SIMILARITY: Contains 2 PH domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY296247; AAQ63176.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB189741; BAD89507.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB098507; BAC78198.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL834513; CAD39169.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009982; AAH09982.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC075847; AAH75847.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105987; AAI05988.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_055949.2; -.
NP_958431.2; -.

UniGene

Hs.462341

3D structure databases

HSSP

Q9UN19; 1FAO. [HSSP ENTRY / PDB]

ModBase

Q6WCQ1.

Protein-protein interaction databases

IntAct

Q6WCQ1; -.

PTM databases

PhosphoSite

Q6WCQ1; -.

Organism-specific databases

HIX0013577; -.

HGNC:30321; MPRIP.

Gene expression databases

ArrayExpress

Q6WCQ1; -.

GermOnline

ENSG00000133030; Homo sapiens.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR001849; PH.
IPR011993; PH_type.
Graphical view of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 2.

Pfam

PF00169; PH; 2.
Pfam graphical view of domain structure.

SMART

SM00233; PH; 2.
SMART graphical view of domain structure.

PROSITE

PS50003; PH_DOMAIN; 2.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q6WCQ1.

Genome annotation databases

Ensembl

ENSG00000133030; Homo sapiens. [Contig view]

GeneID

23164; -.

KEGG

hsa:23164; -.

Phylogenomic databases

HOVERGEN

Q6WCQ1; -.

Other

ProtoNet

Q6WCQ1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1024`	`1024`	`Myosin phosphatase Rho-interacting protein.`	`PRO_0000223930`
`DOMAIN`	`43 150`	`108`	`PH 1.`
`DOMAIN`	`386 482`	`97`	`PH 2.`
`REGION`	`1 382`	`382`	`Interaction with F-actin (By similarity).`
`REGION`	`545 823`	`279`	`Interaction with RHOA.`
`REGION`	`823 878`	`56`	`Interaction with PPP1R12A.`
`COILED`	`672 976`	`305`	`Potential.`
`COMPBIAS`	`179 188`	`10`	`Poly-Ser.`
`MOD_RES`	`180 180`		`Phosphoserine (By similarity).`
`MOD_RES`	`185 185`		`Phosphoserine (By similarity).`
`MOD_RES`	`219 219`		`Phosphoserine.`
`MOD_RES`	`223 223`		`Phosphoserine.`
`MOD_RES`	`225 225`		`Phosphoserine (By similarity).`
`MOD_RES`	`319 319`		`Phosphothreonine (By similarity).`
`MOD_RES`	`364 364`		`Phosphoserine.`
`MOD_RES`	`618 618`		`Phosphoserine.`
`MOD_RES`	`992 992`		`Phosphoserine.`
`MOD_RES`	`1013 1013`		`Phosphoserine (By similarity).`
`MOD_RES`	`1015 1015`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`345 382`		`Missing (in isoform 3).`	`VSP_051947`
`VAR_SEQ`	`1016 1024`		`VIEQVSWDT -> LKEGLTVQERLKLFESRDLKKD (in isoform 2 and isoform 3).`	`VSP_051948`
`CONFLICT`	`31 31`		`S -> P (in Ref. 1; AAQ63176).`
`CONFLICT`	`179 179`		`Missing (in Ref. 2; BAD89507 and 5; AAH09982).`
`CONFLICT`	`183 183`		`S -> R (in Ref. 2; BAD89507).`
`CONFLICT`	`234 234`		`S -> F (in Ref. 2; BAD89507).`
`CONFLICT`	`326 326`		`P -> Q (in Ref. 3; BAC78198 and 4; CAD39169).`
`CONFLICT`	`351 351`		`P -> S (in Ref. 2; BAD89507).`
`CONFLICT`	`527 527`		`R -> T (in Ref. 1; AAQ63176).`
`CONFLICT`	`549 549`		`P -> L (in Ref. 3; BAC78198 and 4; CAD39169).`
`CONFLICT`	`577 577`		`P -> S (in Ref. 1; AAQ63176).`

Sequence information

Length: 1024 AA [This is the length of the unprocessed precursor]

Molecular weight: 116446 Da [This is the MW of the unprocessed precursor]

CRC64: CAF217DDA1F27F1E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL LLAPDGTDFD 

        70         80         90        100        110        120 
NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM NQCTDVVDGE GRTGQKFSLC 

       130        140        150        160        170        180 
ILTPEKEHFI RAETKEIVSG WLEMLMVYPR TNKQNQKKKR KVEPPTPQEP GPAKVAVTSS 

       190        200        210        220        230        240 
SSSSSSSSIP SAEKVPTTKS TLWQEEMRTK DQPDGSSLSP AQSPSQSQPP AASSLREPGL 

       250        260        270        280        290        300 
ESKEEESAMS SDRMDCGRKV RVESGYFSLE KTKQDLKAEE QQLPPPLSPP SPSTPNHRRS 

       310        320        330        340        350        360 
QVIEKFEALD IEKAEHMETN AVGPSPSSDT RQGRSEKRAF PRKRDFTNEA PPAPLPDASA 

       370        380        390        400        410        420 
SPLSPHRRAK SLDRRSTEPS VTPDLLNFKK GWLTKQYEDG QWKKHWFVLA DQSLRYYRDS 

       430        440        450        460        470        480 
VAEEAADLDG EIDLSACYDV TEYPVQRNYG FQIHTKEGEF TLSAMTSGIR RNWIQTIMKH 

       490        500        510        520        530        540 
VHPTTAPDVT SSLPEEKNKS SCSFETCPRP TEKQEAELGE PDPEQKRSRA RERRREGRSK 

       550        560        570        580        590        600 
TFDWAEFRPI QQALAQERVG GVGPADTHEP LRPEAEPGEL ERERARRREE RRKRFGMLDA 

       610        620        630        640        650        660 
TDGPGTEDAA LRMEVDRSPG LPMSDLKTHN VHVEIEQRWH QVETTPLREE KQVPIAPVHL 

       670        680        690        700        710        720 
SSEDGGDRLS THELTSLLEK ELEQSQKEAS DLLEQNRLLQ DQLRVALGRE QSAREGYVLQ 

       730        740        750        760        770        780 
ATCERGFAAM EETHQKKIED LQRQHQRELE KLREEKDRLL AEETAATISA IEAMKNAHRE 

       790        800        810        820        830        840 
EMERELEKSQ RSQISSVNSD VEALRRQYLE ELQSVQRELE VLSEQYSQKC LENAHLAQAL 

       850        860        870        880        890        900 
EAERQALRQC QRENQELNAH NQELNNRLAA EITRLRTLLT GDGGGEATGS PLAQGKDAYE 

       910        920        930        940        950        960 
LEVLLRVKES EIQYLKQEIS SLKDELQTAL RDKKYASDKY KDIYTELSIA KAKADCDISR 

       970        980        990       1000       1010       1020 
LKEQLKAATE ALGEKSPDSA TVSGYDIMKS KSNPDFLKKD RSCVTRQLRN IRSKSVIEQV 


SWDT

Q6WCQ1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools