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P97531

- CIP4_RAT

UniProt

P97531 - CIP4_RAT

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Protein
Cdc42-interacting protein 4
Gene
Trip10, Cip4, Stp
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei166 – 1661Mediates end-to-end attachment of dimers By similarity

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. endocytosis Source: UniProtKB-KW
  3. hyperosmotic salinity response Source: RGD
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Trip10
Synonyms:Cip4, Stp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621145. Trip10.

Subcellular locationi

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.

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. cell cortex Source: UniProtKB-SubCell
  3. cell projection Source: UniProtKB-KW
  4. cytoskeleton Source: UniProtKB-SubCell
  5. lysosome Source: UniProtKB-SubCell
  6. phagocytic cup Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Cdc42-interacting protein 4
PRO_0000261441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961Phosphoserine By similarity
Modified residuei299 – 2991Phosphoserine By similarity
Modified residuei426 – 4261Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP97531.

PTM databases

PhosphoSiteiP97531.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriP97531.

Interactioni

Subunit structurei

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.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP97531.
SMRiP97531. Positions 10-288, 490-545.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6565FCH
Add
BLAST
Repeati349 – 42577REM
Add
BLAST
Domaini486 – 54762SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 288288F-BAR domain By similarity
Add
BLAST
Regioni1 – 117117Required for translocation to the plasma membrane in response to insulin, podosome formation and interaction with AKAP9 and microtubules By similarity
Add
BLAST
Regioni293 – 547255Interaction with PDE6G
Add
BLAST
Regioni293 – 483191Interaction with CDC42 By similarity
Add
BLAST
Regioni415 – 547133Required for interaction with FASLG and localization to lysosomes By similarity
Add
BLAST
Regioni431 – 48757Interaction with DNM2 and WASL By similarity
Add
BLAST
Regioni476 – 54772Interaction with DNM1 and WASL By similarity
Add
BLAST
Regioni484 – 54764Required for podosome formation By similarity
Add
BLAST
Regioni490 – 54758Interaction with WAS By similarity
Add
BLAST
Regioni492 – 54756Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2 By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili67 – 259193 By similarity
Add
BLAST
Coiled coili332 – 42594 By similarity
Add
BLAST

Domaini

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 similaritiesi

Belongs to the FNBP1 family.
Contains 1 FCH domain.
Contains 1 REM (Hr1) repeat.
Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

HOVERGENiHBG002489.
KOiK07196.
PhylomeDBiP97531.

Family and domain databases

InterProiIPR028498. CIP4.
IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR12602:SF7. PTHR12602:SF7. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97531-1 [UniParc]FASTAAdd to Basket

« Hide

MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERVEVEQ SYAKQLRSLV    50
KKYLPKRPAK DDPEIKFSQQ QSFVQLLQEV NDFAGQRELV AESLGIRVCL 100
ELAKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK 150
AAHTAERLDQ DINATKADVE KAKQQAHLRN HMAEESKNEY AAQLQRFNRD 200
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELQ VVPIIGKCLE 250
GMKVAAESVD AKNDSKVLIE LHKSGFARPG DLEFEDFSQV MNRVPSDSSL 300
GTPDGRPELR AASSRSRAKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ 350
LEERNRELQK EEDQREALKK MKDVYEKTPQ MGDPASLEPR IAETLGNIER 400
LKLEVQKYEA WLAEAESRVL SNRGDSLSRH TRPPDPPTTA PPDSSSSSNN 450
SGSQDNKESS EEPPSEEGQD TPIYTEFDED FEEPASPIGQ CVAIYHFEGS 500
SEGTVSMSEG EDLSLMEEDK GDGWTRVRRK QGGEGYVPTS YLRVTLN 547
Length:547
Mass (Da):62,799
Last modified:November 28, 2006 - v3
Checksum:iEE995A691E661DE5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4032KL → NV in BAA22191. 1 Publication
Sequence conflicti417 – 4171S → T in BAA22191. 1 Publication
Sequence conflicti457 – 4571K → M in BAA22191. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006914 mRNA. Translation: BAA22191.1.
BC061840 mRNA. Translation: AAH61840.1.
PIRiJC5261.
RefSeqiNP_446372.1. NM_053920.1.
UniGeneiRn.10814.

Genome annotation databases

GeneIDi116717.
KEGGirno:116717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006914 mRNA. Translation: BAA22191.1 .
BC061840 mRNA. Translation: AAH61840.1 .
PIRi JC5261.
RefSeqi NP_446372.1. NM_053920.1.
UniGenei Rn.10814.

3D structure databases

ProteinModelPortali P97531.
SMRi P97531. Positions 10-288, 490-545.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei P97531.

Proteomic databases

PRIDEi P97531.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 116717.
KEGGi rno:116717.

Organism-specific databases

CTDi 9322.
RGDi 621145. Trip10.

Phylogenomic databases

HOVERGENi HBG002489.
KOi K07196.
PhylomeDBi P97531.

Miscellaneous databases

NextBioi 619616.
PROi P97531.

Gene expression databases

Genevestigatori P97531.

Family and domain databases

InterProi IPR028498. CIP4.
IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR12602:SF7. PTHR12602:SF7. 1 hit.
Pfami PF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
SMARTi SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 2 hits.
PROSITEi PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCIP4_RAT
AccessioniPrimary (citable) accession number: P97531
Secondary accession number(s): Q6P744
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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