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Q5RCJ1

- CIP4_PONAB

UniProt

Q5RCJ1 - CIP4_PONAB

Protein

Cdc42-interacting protein 4

Gene

TRIP10

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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.By similarity

    Sites

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

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. endocytosis Source: UniProtKB-KW

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cdc42-interacting protein 4
    Alternative name(s):
    Thyroid receptor-interacting protein 10
    Short name:
    TR-interacting protein 10
    Short name:
    TRIP-10
    Gene namesi
    Name:TRIP10
    Synonyms:CIP4
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    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.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 601601Cdc42-interacting protein 4PRO_0000261440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei296 – 2961PhosphoserineBy similarity
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei335 – 3351PhosphoserineBy similarity
    Modified residuei351 – 3511PhosphoserineBy similarity
    Modified residuei482 – 4821PhosphoserineBy similarity

    Post-translational modificationi

    Tyrosine phosphorylated. Also phosphorylated by PKA By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ5RCJ1.

    Interactioni

    Subunit structurei

    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.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RCJ1.
    SMRiQ5RCJ1. Positions 10-288, 544-599.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
    BLAST
    Repeati405 – 48177REMAdd
    BLAST
    Domaini540 – 60162SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 288288F-BAR domainBy similarityAdd
    BLAST
    Regioni1 – 117117Required for translocation to the plasma membrane in response to insulin, podosome formation and interaction with AKAP9 and microtubulesBy similarityAdd
    BLAST
    Regioni293 – 601309Interaction with PDE6GBy similarityAdd
    BLAST
    Regioni293 – 537245Interaction with CDC42By similarityAdd
    BLAST
    Regioni471 – 601131Required for interaction with FASLG and localization to lysosomesBy similarityAdd
    BLAST
    Regioni487 – 54155Interaction with DNM2 and WASLBy similarityAdd
    BLAST
    Regioni529 – 60173Interaction with DNM1 and WASLBy similarityAdd
    BLAST
    Regioni538 – 60164Required for podosome formationBy similarityAdd
    BLAST
    Regioni544 – 60158Interaction with WASBy similarityAdd
    BLAST
    Regioni546 – 60156Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili67 – 259193By similarityAdd
    BLAST
    Coiled coili388 – 48194By similarityAdd
    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.By similarity

    Sequence similaritiesi

    Belongs to the FNBP1 family.Curated
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 REM (Hr1) repeat.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    HOVERGENiHBG002489.
    InParanoidiQ5RCJ1.
    KOiK07196.

    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. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5RCJ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV    50
    KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL 100
    ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK 150
    AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD 200
    QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE 250
    GMKVAANAVD PKNDSQVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL 300
    GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP 350
    SPRSGRDPLA ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR 400
    KRLQQQLEER SRELQKEVDQ REALKKMKDV YEKTPQMGDP ASLEPQITET 450
    LSNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPTSAPPDS 500
    SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS PIGHCVAIYH 550
    FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL 600
    N 601
    Length:601
    Mass (Da):68,403
    Last modified:December 21, 2004 - v1
    Checksum:i40CB45B55D79E8FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858279 mRNA. Translation: CAH90516.1.
    RefSeqiNP_001125273.1. NM_001131801.1.
    UniGeneiPab.12665.

    Genome annotation databases

    GeneIDi100172170.
    KEGGipon:100172170.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858279 mRNA. Translation: CAH90516.1 .
    RefSeqi NP_001125273.1. NM_001131801.1.
    UniGenei Pab.12665.

    3D structure databases

    ProteinModelPortali Q5RCJ1.
    SMRi Q5RCJ1. Positions 10-288, 544-599.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5RCJ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100172170.
    KEGGi pon:100172170.

    Organism-specific databases

    CTDi 9322.

    Phylogenomic databases

    HOVERGENi HBG002489.
    InParanoidi Q5RCJ1.
    KOi K07196.

    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. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiCIP4_PONAB
    AccessioniPrimary (citable) accession number: Q5RCJ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3