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Reviewed, UniProtKB/Swiss-Prot Q6WCQ1 (MPRIP_HUMAN)

Last modified November 25, 2008. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Myosin phosphatase Rho-interacting protein
      Short name=M-RIP
Alternative name(s):
    Rho-interacting protein 3
      Short name=RIP3
    p116Rip
Gene names
Name: MPRIP
Synonyms: KIAA0864, MRIP, RHOIP3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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 structure

Binds F-actin through its N-terminus By similarity. Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains.

Subcellular location

Cytoplasmcytoskeleton. Note= Colocalizes with F-actin.

Sequence similarities

Contains 2 PH domains.

Ontologies

Keywords

   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMPhosphoprotein

Gene Ontology (GO)

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6WCQ1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6WCQ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1017-1025: VIEQVSWDT → LKEGLTVQERLKLFESRDLKKD
Isoform 3 (identifier: Q6WCQ1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     346-383: Missing.
     1017-1025: VIEQVSWDT → LKEGLTVQERLKLFESRDLKKD

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain2 – 10251024Myosin phosphatase Rho-interacting protein
PRO_0000223930

Regions

Domain43 – 150108PH 1
Domain387 – 48397PH 2
Region1 – 383383Interaction with F-actin By similarity
Region546 – 824279Interaction with RHOA
Region824 – 87956Interaction with PPP1R12A
Coiled coil673 – 977305 Potential
Compositional bias179 – 25274Ser-rich

Amino acid modifications

Modified residue1811Phosphoserine By similarity
Modified residue1861Phosphoserine By similarity
Modified residue2201Phosphoserine
Modified residue2241Phosphoserine
Modified residue2261Phosphoserine
Modified residue2891Phosphoserine
Modified residue2921Phosphoserine
Modified residue2941Phosphoserine
Modified residue2951Phosphothreonine
Modified residue3201Phosphothreonine By similarity
Modified residue3621Phosphoserine
Modified residue3651Phosphoserine
Modified residue6191Phosphoserine
Modified residue8911Phosphoserine
Modified residue9771Phosphoserine
Modified residue9931Phosphoserine
Modified residue10141Phosphoserine By similarity
Modified residue10161Phosphoserine By similarity

Natural variations

Alternative sequence346 – 38338Missing in isoform 3.
VSP_051947
Alternative sequence1017 – 10259VIEQVSWDT → LKEGLTVQERLKLFESRDLK KD in isoform 2 and isoform 3.
VSP_051948

Experimental info

Sequence conflict311S → P in AAQ63176. Ref.1
Sequence conflict1841S → R in BAD89507. Ref.2
Sequence conflict188 – 1892Missing in BAD89507. Ref.2
Sequence conflict188 – 1892Missing in AAH09982. Ref.6
Sequence conflict1891Missing in AAQ63176. Ref.1
Sequence conflict1891Missing in BAC78198. Ref.3
Sequence conflict1891Missing in CAD39169. Ref.5
Sequence conflict2351S → F in BAD89507. Ref.2
Sequence conflict3271P → Q in BAC78198. Ref.3
Sequence conflict3271P → Q in CAD39169. Ref.5
Sequence conflict3521P → S in BAD89507. Ref.2
Sequence conflict5281R → T in AAQ63176. Ref.1
Sequence conflict5501P → L in BAC78198. Ref.3
Sequence conflict5501P → L in CAD39169. Ref.5
Sequence conflict5781P → S in AAQ63176. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 5B7A30CDB3685E4E

FASTA1,025116,533
        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 
SSSSSSSSSI PSAEKVPTTK STLWQEEMRT KDQPDGSSLS PAQSPSQSQP PAASSLREPG 

       250        260        270        280        290        300 
LESKEEESAM SSDRMDCGRK VRVESGYFSL EKTKQDLKAE EQQLPPPLSP PSPSTPNHRR 

       310        320        330        340        350        360 
SQVIEKFEAL DIEKAEHMET NAVGPSPSSD TRQGRSEKRA FPRKRDFTNE APPAPLPDAS 

       370        380        390        400        410        420 
ASPLSPHRRA KSLDRRSTEP SVTPDLLNFK KGWLTKQYED GQWKKHWFVL ADQSLRYYRD 

       430        440        450        460        470        480 
SVAEEAADLD GEIDLSACYD VTEYPVQRNY GFQIHTKEGE FTLSAMTSGI RRNWIQTIMK 

       490        500        510        520        530        540 
HVHPTTAPDV TSSLPEEKNK SSCSFETCPR PTEKQEAELG EPDPEQKRSR ARERRREGRS 

       550        560        570        580        590        600 
KTFDWAEFRP IQQALAQERV GGVGPADTHE PLRPEAEPGE LERERARRRE ERRKRFGMLD 

       610        620        630        640        650        660 
ATDGPGTEDA ALRMEVDRSP GLPMSDLKTH NVHVEIEQRW HQVETTPLRE EKQVPIAPVH 

       670        680        690        700        710        720 
LSSEDGGDRL STHELTSLLE KELEQSQKEA SDLLEQNRLL QDQLRVALGR EQSAREGYVL 

       730        740        750        760        770        780 
QATCERGFAA MEETHQKKIE DLQRQHQREL EKLREEKDRL LAEETAATIS AIEAMKNAHR 

       790        800        810        820        830        840 
EEMERELEKS QRSQISSVNS DVEALRRQYL EELQSVQREL EVLSEQYSQK CLENAHLAQA 

       850        860        870        880        890        900 
LEAERQALRQ CQRENQELNA HNQELNNRLA AEITRLRTLL TGDGGGEATG SPLAQGKDAY 

       910        920        930        940        950        960 
ELEVLLRVKE SEIQYLKQEI SSLKDELQTA LRDKKYASDK YKDIYTELSI AKAKADCDIS 

       970        980        990       1000       1010       1020 
RLKEQLKAAT EALGEKSPDS ATVSGYDIMK SKSNPDFLKK DRSCVTRQLR NIRSKSVIEQ 


VSWDT 

« Hide

Isoform 2 [UniParc].

Checksum: EE674842C8133516
Show »

1,038118,103
Isoform 3 [UniParc].

Checksum: FCFDB3210A73EEF9
Show »

1,000114,049

References

« Hide 'large scale' references
[1]"Myosin phosphatase-Rho interacting protein. A new member of the myosin phosphatase complex that directly binds RhoA."
Surks H.K., Richards C.T., Mendelsohn M.E.
J. Biol. Chem. 278:51484-51493(2003) [PubMed: 14506264] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PPP1R12A AND RHOA.
Tissue: Aorta.
[2]"p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA."
Koga Y., Ikebe M.
J. Biol. Chem. 280:4983-4991(2005) [PubMed: 15545284] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PPP1R12A.
[3]"Cloning of human orthologue RHOIP3 of Mus Rhoip3."
Inazawa J., Imoto I.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]The German cDNA consortium
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1025 (ISOFORM 1).
Tissue: Melanoma.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-1025 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1025 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 377-1025 (ISOFORM 2).
Tissue: Brain, Lymph and Muscle.
[7]"M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells."
Surks H.K., Riddick N., Ohtani K.
J. Biol. Chem. 280:42543-42551(2005) [PubMed: 16257966] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1R12A AND F-ACTIN.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-224; SER-365; SER-619 AND SER-993, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-993, MASS SPECTROMETRY.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-224; SER-226; SER-289; SER-292; SER-294; THR-295; SER-362; SER-365; SER-619; SER-891 AND SER-977, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY296247 mRNA. Translation: AAQ63176.1.
AB189741 mRNA. Translation: BAD89507.1.
AB098507 mRNA. Translation: BAC78198.1.
AC079111 Genomic DNA. No translation available.
AC055811 Genomic DNA. No translation available.
AL834513 mRNA. Translation: CAD39169.1.
BC009982 mRNA. Translation: AAH09982.2.
BC075847 mRNA. Translation: AAH75847.1.
BC105987 mRNA. Translation: AAI05988.1.
RefSeqNP_055949.2.
NP_958431.2.
UniGeneHs.462341

3D structure databases

HSSPHSSP built from PDB template 1FAO based on UniProtKB Q9UN19.
ModBaseSearch...

Protein-protein interaction databases

IntActQ6WCQ1.

PTM databases

PhosphoSiteQ6WCQ1.

Genome annotation databases

EnsemblENSG00000133030. Homo sapiens. [Contig view]
GeneID23164.
KEGGhsa:23164.

Organism-specific databases

H-InvDBHIX0013577.
HGNCHGNC:30321. MPRIP.
HUGESearch...
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ6WCQ1.

Gene expression databases

ArrayExpressQ6WCQ1.
GermOnlineENSG00000133030. Homo sapiens.

Family and domain databases

InterProIPR001849. PH.
IPR011993. PH_type.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 2 hits.
PfamPF00169. PH. 2 hits.
[Graphical view]
SMARTSM00233. PH. 2 hits.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio44551.

Entry information

Entry nameMPRIP_HUMAN
AccessionPrimary (citable) accessio