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Q5RCJ1 (CIP4_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cdc42-interacting protein 4
Alternative name(s):
Thyroid receptor-interacting protein 10
Short name=TR-interacting protein 10
Short name=TRIP-10
Gene names
Name:TRIP10
Synonyms:CIP4
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Also acts as a link between CDC42 signaling and regulation of the actin cytoskeleton. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization in the vicinity of membrane tubules by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization and dynamin may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. May be required for the lysosomal retention of FASLG/FASL By similarity.

Subunit structure

Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, PDE6G, SRC and WAS/WASP. Interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone. May interact with CTNNB1 and HD/HTT By similarity. Interacts specifically with GTP-bound CDC42 and RHOQ. Interacts with DNM2 and WASL By similarity.

Subcellular location

Cytoplasmcytoskeleton By similarity. Cytoplasmcell cortex By similarity. Lysosome By similarity. Golgi apparatus By similarity. Cell membrane By similarity. Cell projectionphagocytic cup By similarity. Note: Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ By similarity.

Domain

The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation By similarity.

Post-translational modification

Tyrosine phosphorylated. Also phosphorylated by PKA By similarity.

Sequence similarities

Belongs to the FNBP1 family.

Contains 1 FCH domain.

Contains 1 REM (Hr1) repeat.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Cdc42-interacting protein 4
PRO_0000261440

Regions

Domain1 – 6565FCH
Repeat405 – 48177REM
Domain540 – 60162SH3
Region1 – 288288F-BAR domain By similarity
Region1 – 117117Required for translocation to the plasma membrane in response to insulin, podosome formation and interaction with AKAP9 and microtubules By similarity
Region293 – 601309Interaction with PDE6G By similarity
Region293 – 537245Interaction with CDC42 By similarity
Region471 – 601131Required for interaction with FASLG and localization to lysosomes By similarity
Region487 – 54155Interaction with DNM2 and WASL By similarity
Region529 – 60173Interaction with DNM1 and WASL By similarity
Region538 – 60164Required for podosome formation By similarity
Region544 – 60158Interaction with WAS By similarity
Region546 – 60156Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2 By similarity
Coiled coil67 – 259193 By similarity
Coiled coil388 – 48194 By similarity

Sites

Site1661Mediates end-to-end attachment of dimers By similarity

Amino acid modifications

Modified residue2961Phosphoserine By similarity
Modified residue2991Phosphoserine By similarity
Modified residue3351Phosphoserine By similarity
Modified residue3511Phosphoserine By similarity
Modified residue4821Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RCJ1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 40CB45B55D79E8FA

FASTA60168,403
        10         20         30         40         50         60 
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV KKYLPKRPAK 

        70         80         90        100        110        120 
DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL ELTKYSQEMK QERKMHFQEG 

       130        140        150        160        170        180 
RRAQQQLENG FKQLENSKRK FERDCREAEK AAQTAERLDQ DINATKADVE KAKQQAHLRS 

       190        200        210        220        230        240 
HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE 

       250        260        270        280        290        300 
VVPIIAKCLE GMKVAANAVD PKNDSQVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL 

       310        320        330        340        350        360 
GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP SPRSGRDPLA 

       370        380        390        400        410        420 
ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR KRLQQQLEER SRELQKEVDQ 

       430        440        450        460        470        480 
REALKKMKDV YEKTPQMGDP ASLEPQITET LSNIERLKLE VQKYEAWLAE AESRVLSNRG 

       490        500        510        520        530        540 
DSLSRHARPP DPPTSAPPDS SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS 

       550        560        570        580        590        600 
PIGHCVAIYH FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL 


N 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858279 mRNA. Translation: CAH90516.1.
RefSeqNP_001125273.1. NM_001131801.1.
UniGenePab.12665.

3D structure databases

ProteinModelPortalQ5RCJ1.
SMRQ5RCJ1. Positions 10-288, 544-599.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RCJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172170.
KEGGpon:100172170.

Organism-specific databases

CTD9322.

Phylogenomic databases

HOVERGENHBG002489.
InParanoidQ5RCJ1.
KOK07196.

Family and domain databases

InterProIPR028498. CIP4.
IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR12602:SF7. PTHR12602:SF7. 1 hit.
PfamPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCIP4_PONAB
AccessionPrimary (citable) accession number: Q5RCJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families