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Protein

PDZ and LIM domain protein 4

Gene

Pdlim4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • actinin binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • actin cytoskeleton organization Source: RGD
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
PDZ and LIM domain protein 4
Alternative name(s):
H-REV18
LIM protein RIL
RIT-18
Reversion-induced LIM protein
Gene namesi
Name:Pdlim4
Synonyms:Ril
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3575. Pdlim4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330PDZ and LIM domain protein 4PRO_0000075875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111PhosphoserineCombined sources
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei119 – 1191PhosphoserineCombined sources
Modified residuei124 – 1241PhosphoserineCombined sources
Modified residuei134 – 1341PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on tyrosine residue(s). Can be dephosphorylated by PTPN13 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP36202.
PRIDEiP36202.

PTM databases

PhosphoSiteiP36202.

Expressioni

Tissue specificityi

Detected in several tissues, most prominent in brain and heart of adults.

Interactioni

Subunit structurei

Interacts with the LIM domain with the second and fourth PDZ domains of PTPN13.By similarity

GO - Molecular functioni

  • actinin binding Source: RGD

Protein-protein interaction databases

IntActiP36202. 1 interaction.
STRINGi10116.ENSRNOP00000064261.

Structurei

3D structure databases

ProteinModelPortaliP36202.
SMRiP36202. Positions 1-87, 244-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8484PDZPROSITE-ProRule annotationAdd
BLAST
Domaini255 – 30551LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
HOVERGENiHBG061371.
InParanoidiP36202.
PhylomeDBiP36202.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR031847. DUF4749.
IPR001478. PDZ.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF15936. DUF4749. 1 hit.
PF00412. LIM. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHAVTLRGP SPWGFRLVGG RDFSAPLTIS RVHAGSKAAL AALCPGDSIQ
60 70 80 90 100
AINGESTELM THLEAQNRIK GCHDHLTLSV SRPENKNWPS SPNDKAQAHR
110 120 130 140 150
IHIDPEAQDG SPATSRRSSI SGISLEDNRS GLGSPYGQPP RLPVPHNGSS
160 170 180 190 200
NEVTLPSQMS ALHVSPPPSA DTPRILPRNR DCRVDLGSEV YRMLREPAEP
210 220 230 240 250
AASEPKQSGS FRYLQGMLEA GEGGDRPGSG GSRNLKPAAS KLGAPLSGLQ
260 270 280 290 300
GLPECTRCGH GIVGTIVKAR DKLYHPECFM CSDCGLNLKQ RGYFFLDERL
310 320 330
YCENHAKARV KPPEGYDVVA VYPNAKVELV
Length:330
Mass (Da):35,521
Last modified:October 1, 1996 - v2
Checksum:i84BEB1E629ADA584
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76454 mRNA. Translation: CAA53992.1.
PIRiS71828.
RefSeqiNP_058758.1. NM_017062.2.
UniGeneiRn.34221.

Genome annotation databases

GeneIDi24915.
KEGGirno:24915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76454 mRNA. Translation: CAA53992.1.
PIRiS71828.
RefSeqiNP_058758.1. NM_017062.2.
UniGeneiRn.34221.

3D structure databases

ProteinModelPortaliP36202.
SMRiP36202. Positions 1-87, 244-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP36202. 1 interaction.
STRINGi10116.ENSRNOP00000064261.

PTM databases

PhosphoSiteiP36202.

Proteomic databases

PaxDbiP36202.
PRIDEiP36202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24915.
KEGGirno:24915.

Organism-specific databases

CTDi8572.
RGDi3575. Pdlim4.

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
HOVERGENiHBG061371.
InParanoidiP36202.
PhylomeDBiP36202.

Miscellaneous databases

NextBioi604841.
PROiP36202.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR031847. DUF4749.
IPR001478. PDZ.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF15936. DUF4749. 1 hit.
PF00412. LIM. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of ril, a novel LIM domain gene, is down-regulated in Hras-transformed cells and restored in phenotypic revertants."
    Kiess M., Scharm B., Aguzzi A., Hajnal A., Klemenz R., Schwarte-Waldhoff I., Schaefer R.
    Oncogene 10:61-68(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-119; SER-124 AND SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDLI4_RAT
AccessioniPrimary (citable) accession number: P36202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.