Cdc42-interacting protein 4 - Rattus norvegicus (Rat)

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P97531 (CIP4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton By similarity. Cytoplasm › cell cortex By similarity. Lysosome By similarity. Golgi apparatus By similarity. Cell membrane By similarity. Cell projection › phagocytic 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.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Golgi apparatus Lysosome Membrane
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW hyperosmotic salinity response Inferred from direct assay Ref.1. Source: RGD
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic cup Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 547

547

Cdc42-interacting protein 4

PRO_0000261441

Regions

Domain

1 – 65

FCH

Repeat

349 – 425

REM

Domain

486 – 547

SH3

Region

1 – 288

288

F-BAR domain By similarity

Region

1 – 117

117

Required for translocation to the plasma membrane in response to insulin, podosome formation and interaction with AKAP9 and microtubules By similarity

Region

293 – 547

255

Interaction with PDE6G

Region

293 – 483

191

Interaction with CDC42 By similarity

Region

415 – 547

133

Required for interaction with FASLG and localization to lysosomes By similarity

Region

431 – 487

Interaction with DNM2 and WASL By similarity

Region

476 – 547

Interaction with DNM1 and WASL By similarity

Region

484 – 547

Required for podosome formation By similarity

Region

490 – 547

Interaction with WAS By similarity

Region

492 – 547

Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2 By similarity

Coiled coil

67 – 259

193

By similarity

Coiled coil

332 – 425

By similarity

Sites

Site

166

Mediates end-to-end attachment of dimers By similarity

Amino acid modifications

Modified residue

296

Phosphoserine By similarity

Modified residue

299

Phosphoserine By similarity

Modified residue

426

Phosphoserine By similarity

Experimental info

Sequence conflict

402 – 403

KL → NV in BAA22191. Ref.1

Sequence conflict

417

S → T in BAA22191. Ref.1

Sequence conflict

457

K → M in BAA22191. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P97531 [UniParc].

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

FASTA

547

62,799

        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' referencesShow '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, 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.
IPI	IPI00205459.
PIR	JC5261.
RefSeq	NP_446372.1. NM_053920.1.
UniGene	Rn.10814.
3D structure databases
HSSP	HSSP built from PDB template 2CT4 based on UniProtKB Q15642.
ProteinModelPortal	P97531.
SMR	P97531. Positions 10-288, 490-545.
ModBase	Search...
PTM databases
PhosphoSite	P97531.
Proteomic databases
PRIDE	P97531.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	116717.
KEGG	rno:116717.
Organism-specific databases
CTD	9322.
RGD	621145. Trip10.
Phylogenomic databases
HOVERGEN	HBG002489.
KO	K07196.
Gene expression databases
Genevestigator	P97531.
Family and domain databases
InterPro	IPR001060. FCH_dom. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00611. FCH. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
SMART	SM00055. FCH. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50133. FCH. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	619616.

Entry information

Entry name

CIP4_RAT

Accession

Primary (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:	May 1, 2013
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents