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Protein

Protein phosphatase 1 regulatory subunit 14A

Gene

CPI17

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Enzyme and pathway databases

ReactomeiR-SSC-5625740. RHO GTPases activate PKNs.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 14A
Alternative name(s):
17 kDa PKC-potentiated inhibitory protein of PP1
Protein kinase C-potentiated inhibitor protein of 17 kDa
Short name:
CPI-17
Gene namesi
Name:CPI17
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 6

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381T → A: Abolishes phosphorylation (in vitro) and strongly reduces inhibitory activity. 3 Publications
Mutagenesisi38 – 381T → E: Reduces inhibitory activity at least 1000-fold. 3 Publications
Mutagenesisi41 – 411Y → A: Promotes dephosphorylation of T-38. Abolishes phosphorylation-dependent increase of inhibitory activity. 1 Publication
Mutagenesisi42 – 421D → A: Strongly reduces inhibitory activity. 1 Publication
Mutagenesisi43 – 431R → A: Strongly reduces inhibitory activity. 1 Publication
Mutagenesisi44 – 441R → A: Reduces inhibitory activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Protein phosphatase 1 regulatory subunit 14APRO_0000071488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei38 – 381Phosphothreonine3 Publications
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei136 – 1361PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation of Thr-38 induces a conformation change.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO18734.

PTM databases

iPTMnetiO18734.

Expressioni

Tissue specificityi

Detected in aorta smooth muscle and bladder.1 Publication

Gene expression databases

GenevisibleiO18734. SS.

Interactioni

Protein-protein interaction databases

DIPiDIP-48426N.
STRINGi9823.ENSSSCP00000021211.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 263Combined sources
Beta strandi34 – 374Combined sources
Beta strandi45 – 473Combined sources
Helixi48 – 6215Combined sources
Helixi65 – 673Combined sources
Turni68 – 703Combined sources
Helixi78 – 814Combined sources
Turni84 – 874Combined sources
Helixi88 – 9811Combined sources
Beta strandi99 – 1024Combined sources
Helixi105 – 11410Combined sources
Turni115 – 1184Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2MNMR-A22-120[»]
1J2NNMR-A22-120[»]
1K5ONMR-A35-120[»]
2RLTNMR-A22-120[»]
ProteinModelPortaliO18734.
SMRiO18734. Positions 22-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO18734.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 12086InhibitoryAdd
BLAST

Sequence similaritiesi

Belongs to the PP1 inhibitor family.Curated

Phylogenomic databases

eggNOGiENOG410IZE6. Eukaryota.
ENOG4111Q1J. LUCA.
GeneTreeiENSGT00390000003608.
HOVERGENiHBG054419.
InParanoidiO18734.
KOiK12328.
OMAiLHKQPGF.
OrthoDBiEOG7RNK21.
TreeFamiTF105546.

Family and domain databases

Gene3Di1.10.150.220. 1 hit.
InterProiIPR008025. PP1_inhibitor.
[Graphical view]
PANTHERiPTHR16188. PTHR16188. 1 hit.
PfamiPF05361. PP1_inhibitor. 1 hit.
[Graphical view]
SUPFAMiSSF81790. SSF81790. 1 hit.

Sequencei

Sequence statusi: Complete.

O18734-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQRLGKRV LSKLQSPSRA RGPGGSPGGL QKRHARVTVK YDRRELQRRL
60 70 80 90 100
DVEKWIDGRL EELYRGREAD MPDEVNIDEL LELESEEERS RKIQGLLKSC
110 120 130 140
TNPTENFVQE LLVKLRGLHK QPGLRQPSPS GDGSLSPRQD RARTAPP
Length:147
Mass (Da):16,672
Last modified:January 1, 1998 - v1
Checksum:i315DAE461CF78BBF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008376 mRNA. Translation: BAA22995.1.
RefSeqiNP_999502.1. NM_214337.1.
UniGeneiSsc.13002.

Genome annotation databases

EnsembliENSSSCT00000029365; ENSSSCP00000021211; ENSSSCG00000023212.
GeneIDi397610.
KEGGissc:397610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008376 mRNA. Translation: BAA22995.1.
RefSeqiNP_999502.1. NM_214337.1.
UniGeneiSsc.13002.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2MNMR-A22-120[»]
1J2NNMR-A22-120[»]
1K5ONMR-A35-120[»]
2RLTNMR-A22-120[»]
ProteinModelPortaliO18734.
SMRiO18734. Positions 22-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48426N.
STRINGi9823.ENSSSCP00000021211.

PTM databases

iPTMnetiO18734.

Proteomic databases

PaxDbiO18734.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000029365; ENSSSCP00000021211; ENSSSCG00000023212.
GeneIDi397610.
KEGGissc:397610.

Organism-specific databases

CTDi94274.

Phylogenomic databases

eggNOGiENOG410IZE6. Eukaryota.
ENOG4111Q1J. LUCA.
GeneTreeiENSGT00390000003608.
HOVERGENiHBG054419.
InParanoidiO18734.
KOiK12328.
OMAiLHKQPGF.
OrthoDBiEOG7RNK21.
TreeFamiTF105546.

Enzyme and pathway databases

ReactomeiR-SSC-5625740. RHO GTPases activate PKNs.

Miscellaneous databases

EvolutionaryTraceiO18734.

Gene expression databases

GenevisibleiO18734. SS.

Family and domain databases

Gene3Di1.10.150.220. 1 hit.
InterProiIPR008025. PP1_inhibitor.
[Graphical view]
PANTHERiPTHR16188. PTHR16188. 1 hit.
PfamiPF05361. PP1_inhibitor. 1 hit.
[Graphical view]
SUPFAMiSSF81790. SSF81790. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI-17) in smooth muscle: its specific localization in smooth muscle."
    Eto M., Senba S., Morita F., Yazawa M.
    FEBS Lett. 410:356-360(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Aorta.
  2. "A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization."
    Eto M., Ohmori T., Suzuki M., Furuya K., Morita F.
    J. Biochem. 118:1104-1107(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 9-71 AND 93-145, FUNCTION, MUTAGENESIS OF THR-38, PHOSPHORYLATION AT THR-38.
  3. Cited for: PHOSPHORYLATION AT THR-38, FUNCTION.
  4. "Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase."
    Koyama M., Ito M., Feng J., Seko T., Shiraki K., Takase K., Hartshorne D.J., Nakano T.
    FEBS Lett. 475:197-200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-38, MUTAGENESIS OF THR-38, FUNCTION.
  5. "Defining the structural determinants and a potential mechanism for inhibition of myosin phosphatase by the protein kinase C-potentiated inhibitor protein of 17 kDa."
    Hayashi Y., Senba S., Yazawa M., Brautigan D.L., Eto M.
    J. Biol. Chem. 276:39858-39863(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-38; TYR-41; ASP-42; ARG-43 AND ARG-44, SUBCELLULAR LOCATION.
  6. "Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation."
    Ohki S.-Y., Eto M., Kariya E., Hayano T., Hayashi Y., Yazawa M., Brautigan D.L., Kainosho M.
    J. Mol. Biol. 314:839-849(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 35-120.
  7. "Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue."
    Ohki S.-Y., Eto M., Shimizu M., Takada R., Brautigan D.L., Kainosho M.
    J. Mol. Biol. 326:1539-1547(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 22-120 OF MUTANT ASP-38.

Entry informationi

Entry nameiPP14A_PIG
AccessioniPrimary (citable) accession number: O18734
Secondary accession number(s): Q9TQZ8
, Q9TQZ9, Q9TR00, Q9TR01, Q9TR02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.