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P97531 (CIP4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cdc42-interacting protein 4
Alternative name(s):
Salt tolerant protein
Thyroid receptor-interacting protein 10
Short name=TR-interacting protein 10
Short name=TRIP-10
Gene names
Name:Trip10
Synonyms:Cip4, Stp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 specifically with GTP-bound CDC42 and RHOQ. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, FASLG/FASL, GAPVD1, LYN, microtubules, SRC, WAS/WASP and WASL/N-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 with PDE6G. Ref.4

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.

Tissue specificity

Expressed in adrenal gland, aorta, brain, heart, kidney, liver, skeletal muscle and spleen. Ref.1

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.

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 – 547547Cdc42-interacting protein 4
PRO_0000261441

Regions

Domain1 – 6565FCH
Repeat349 – 42577REM
Domain486 – 54762SH3
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 – 547255Interaction with PDE6G
Region293 – 483191Interaction with CDC42 By similarity
Region415 – 547133Required for interaction with FASLG and localization to lysosomes By similarity
Region431 – 48757Interaction with DNM2 and WASL By similarity
Region476 – 54772Interaction with DNM1 and WASL By similarity
Region484 – 54764Required for podosome formation By similarity
Region490 – 54758Interaction with WAS By similarity
Region492 – 54756Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2 By similarity
Coiled coil67 – 259193 By similarity
Coiled coil332 – 42594 By similarity

Sites

Site1661Mediates end-to-end attachment of dimers By similarity

Amino acid modifications

Modified residue2961Phosphoserine By similarity
Modified residue2991Phosphoserine By similarity
Modified residue4261Phosphoserine By similarity

Experimental info

Sequence conflict402 – 4032KL → NV in BAA22191. Ref.1
Sequence conflict4171S → T in BAA22191. Ref.1
Sequence conflict4571K → M in BAA22191. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P97531 [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: EE995A691E661DE5

FASTA54762,799
        10         20         30         40         50         60 
MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERVEVEQ SYAKQLRSLV KKYLPKRPAK 

        70         80         90        100        110        120 
DDPEIKFSQQ QSFVQLLQEV NDFAGQRELV AESLGIRVCL ELAKYSQEMK QERKMHFQEG 

       130        140        150        160        170        180 
RRAQQQLENG FKQLENSKRK FERDCREAEK AAHTAERLDQ DINATKADVE KAKQQAHLRN 

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

       250        260        270        280        290        300 
VVPIIGKCLE GMKVAAESVD AKNDSKVLIE LHKSGFARPG DLEFEDFSQV MNRVPSDSSL 

       310        320        330        340        350        360 
GTPDGRPELR AASSRSRAKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ LEERNRELQK 

       370        380        390        400        410        420 
EEDQREALKK MKDVYEKTPQ MGDPASLEPR IAETLGNIER LKLEVQKYEA WLAEAESRVL 

       430        440        450        460        470        480 
SNRGDSLSRH TRPPDPPTTA PPDSSSSSNN SGSQDNKESS EEPPSEEGQD TPIYTEFDED 

       490        500        510        520        530        540 
FEEPASPIGQ CVAIYHFEGS SEGTVSMSEG EDLSLMEEDK GDGWTRVRRK QGGEGYVPTS 


YLRVTLN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a novel rat salt-tolerant protein by functional complementation in yeast."
Tsuji E., Tsuji Y., Misumi Y., Fujita A., Sasaguri M., Ideishi M., Arakawa K.
Biochem. Biophys. Res. Commun. 229:134-138(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: Wistar.
Tissue: Kidney.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]Lubec G., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 391-402, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]"A proline-rich domain in the gamma subunit of phosphodiesterase 6 mediates interaction with SH3-containing proteins."
Morin F., Vannier B., Houdart F., Regnacq M., Berges T., Voisin P.
Mol. Vis. 9:449-459(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDE6G.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006914 mRNA. Translation: BAA22191.1.
BC061840 mRNA. Translation: AAH61840.1.
PIRJC5261.
RefSeqNP_446372.1. NM_053920.1.
UniGeneRn.10814.

3D structure databases

ProteinModelPortalP97531.
SMRP97531. Positions 10-288, 490-545.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP97531.

Proteomic databases

PRIDEP97531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116717.
KEGGrno:116717.

Organism-specific databases

CTD9322.
RGD621145. Trip10.

Phylogenomic databases

HOVERGENHBG002489.
KOK07196.
PhylomeDBP97531.

Gene expression databases

GenevestigatorP97531.

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. 2 hits.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619616.
PROP97531.

Entry information

Entry nameCIP4_RAT
AccessionPrimary (citable) accession number: P97531
Secondary accession number(s): Q6P744
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 80 of the entry and version 3 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