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Q8CJ53 (CIP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length603 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. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization 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. May be required for the lysosomal retention of FASLG/FASL By similarity. Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. Ref.2 Ref.7

Subunit structure

Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures By similarity. 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. Ref.2 Ref.7 Ref.8

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcell cortex. Lysosome. Golgi apparatus By similarity. Cell membrane. 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 By similarity. Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ. Ref.2 Ref.6 Ref.7

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.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CJ53-1)

Also known as: Cip4/2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8CJ53-2)

Also known as: H;

The sequence of this isoform differs from the canonical sequence as follows:
     515-515: Missing.
Isoform 3 (identifier: Q8CJ53-3)

The sequence of this isoform differs from the canonical sequence as follows:
     329-384: Missing.
Isoform 4 (identifier: Q8CJ53-4)

The sequence of this isoform differs from the canonical sequence as follows:
     329-384: Missing.
     515-515: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Cdc42-interacting protein 4
PRO_0000261439

Regions

Domain1 – 6565FCH
Repeat405 – 48177REM
Domain542 – 60362SH3
Region1 – 288288F-BAR domain By similarity
Region1 – 117117Required for podosome formation and interaction with AKAP9 and microtubules By similarity
Region1 – 117117Required for translocation to the plasma membrane in response to insulin
Region293 – 603311Interaction with PDE6G By similarity
Region293 – 539247Interaction with CDC42 By similarity
Region471 – 603133Required for interaction with FASLG and localization to lysosomes By similarity
Region487 – 54357Interaction with DNM2 and WASL
Region532 – 60372Interaction with DNM1 and WASL By similarity
Region540 – 60364Required for podosome formation By similarity
Region546 – 60358Interaction with WAS By similarity
Region548 – 60356Interaction 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

Natural variations

Alternative sequence329 – 38456Missing in isoform 3 and isoform 4.
VSP_021722
Alternative sequence5151Missing in isoform 2 and isoform 4.
VSP_021723

Experimental info

Mutagenesis4541I → S: Impairs interaction with CDC42 and RHOQ and reduces insulin-stimulated translocation to the plasma membrane. Ref.2
Sequence conflict3211W → C in AAN38709. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Cip4/2) [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: DDA6271D5FD515AC

FASTA60368,489
        10         20         30         40         50         60 
MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERAEVEQ AYAKQLRSLV KKYLPKRPTK 

        70         80         90        100        110        120 
DDPEVKFSQQ 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 AKNDSQVLIE LHKSGFARPG DLEFEDFSQV INRVPSDSSL 

       310        320        330        340        350        360 
GTPDGRPELR AASSRSRAKR WPFGKKNKPR PPSLSLLGGH LPSTLSDGPS SPRSGRDPLA 

       370        380        390        400        410        420 
ILSEISKSVK PRLASFRSFR GGRGTVATED FSHLPPEQQR KRLQQQLEER NRELQKEEDQ 

       430        440        450        460        470        480 
REALKKMKDV YEKTPQMGDP ASLEPRIAET LGNIERLKLE VQKYEAWLAE AESRVLSNRG 

       490        500        510        520        530        540 
DSLSRHARPP DPPTTAPPDS SSSSTNSGSQ DNKESSSEEP PSEGQDTPIY TEFDEDFEEP 

       550        560        570        580        590        600 
ASPIGQCVAI YHFEGSSEGT VSMSEGEDLS LMEEDKGDGW TRVRRKQGAE GYVPTSYLRV 


TLN 

« Hide

Isoform 2 (H) [UniParc].

Checksum: 165D63A9EC6CD884
Show »

FASTA60268,402
Isoform 3 [UniParc].

Checksum: 5DE65DB3D6C9B8E2
Show »

FASTA54762,654
Isoform 4 [UniParc].

Checksum: 8627CD20F0C19667
Show »

FASTA54662,567

References

« Hide 'large scale' references
[1]"Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms."
Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., Deng X., Whitcomb D., Corey S.J.
Biochem. Biophys. Res. Commun. 293:1426-1430(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Heart.
[2]"The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes."
Chang L., Adams R.D., Saltiel A.R.
Proc. Natl. Acad. Sci. U.S.A. 99:12835-12840(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC42 AND RHOQ, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-454.
Tissue: Adipocyte.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow and Thymus.
[4]"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] (ISOFORM 3).
Strain: FVB/N.
Tissue: Mammary gland.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 98-104, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle."
Archila S., King M.A., Carlson G.M., Rice N.A.
Biochem. Biophys. Res. Commun. 345:1592-1599(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis."
Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.
J. Cell Biol. 172:269-279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION.
[8]"Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4 trafficking in adipocytes."
Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M., Pessin J.E., Saltiel A.R.
Cell Metab. 5:59-72(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAPVD1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY081142 mRNA. Translation: AAL89589.1.
AF502565 mRNA. Translation: AAN38709.1.
AK088909 mRNA. Translation: BAC40648.1.
AK149902 mRNA. Translation: BAE29155.1.
BC003249 mRNA. Translation: AAH03249.1.
CCDSCCDS28930.1. [Q8CJ53-3]
RefSeqNP_001229318.1. NM_001242389.1. [Q8CJ53-1]
NP_001229319.1. NM_001242390.1. [Q8CJ53-2]
NP_001229320.1. NM_001242391.1. [Q8CJ53-4]
NP_598886.1. NM_134125.4. [Q8CJ53-3]
UniGeneMm.37368.

3D structure databases

ProteinModelPortalQ8CJ53.
SMRQ8CJ53. Positions 10-288, 384-481, 546-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223098. 1 interaction.

PTM databases

PhosphoSiteQ8CJ53.

Proteomic databases

MaxQBQ8CJ53.
PaxDbQ8CJ53.
PRIDEQ8CJ53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019631; ENSMUSP00000019631; ENSMUSG00000019487. [Q8CJ53-3]
GeneID106628.
KEGGmmu:106628.
UCSCuc008dej.2. mouse. [Q8CJ53-3]
uc008dek.2. mouse. [Q8CJ53-1]
uc008del.2. mouse. [Q8CJ53-2]
uc008dem.2. mouse. [Q8CJ53-4]

Organism-specific databases

CTD9322.
MGIMGI:2146901. Trip10.

Phylogenomic databases

eggNOGNOG323796.
GeneTreeENSGT00510000046403.
HOGENOMHOG000231767.
HOVERGENHBG002489.
InParanoidQ8CJ53.
KOK07196.
OMASPKFGRD.
OrthoDBEOG780RQK.
PhylomeDBQ8CJ53.
TreeFamTF351162.

Gene expression databases

BgeeQ8CJ53.
CleanExMM_TRIP10.
GenevestigatorQ8CJ53.

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

NextBio358316.
PROQ8CJ53.
SOURCESearch...

Entry information

Entry nameCIP4_MOUSE
AccessionPrimary (citable) accession number: Q8CJ53
Secondary accession number(s): Q8BTR8, Q8R433, Q99LI0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 83 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot