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O08967

- CYH3_MOUSE

UniProt

O08967 - CYH3_MOUSE

Protein

Cytohesin-3

Gene

Cyth3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei284 – 2841Phosphatidylinositol 3,4,5-trisphosphate2 Publications
    Binding sitei295 – 2951Phosphatidylinositol 3,4,5-trisphosphate2 Publications
    Binding sitei305 – 3051Phosphatidylinositol 3,4,5-trisphosphate2 Publications
    Binding sitei354 – 3541Phosphatidylinositol 3,4,5-trisphosphate2 Publications

    GO - Molecular functioni

    1. ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
    2. guanyl-nucleotide exchange factor activity Source: MGI
    3. phosphatidylinositol-3,4,5-trisphosphate binding Source: MGI
    4. protein binding Source: MGI

    GO - Biological processi

    1. establishment of epithelial cell polarity Source: MGI
    2. Golgi vesicle transport Source: UniProtKB
    3. positive regulation of cell adhesion Source: MGI
    4. positive regulation of GTPase activity Source: GOC
    5. regulation of ARF protein signal transduction Source: InterPro

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytohesin-3
    Alternative name(s):
    ARF nucleotide-binding site opener 3
    Short name:
    Protein ARNO3
    General receptor of phosphoinositides 1
    Short name:
    Grp1
    PH, SEC7 and coiled-coil domain-containing protein 3
    Short name:
    CLM3
    SEC7 homolog C
    Short name:
    mSec7-3
    Gene namesi
    Name:Cyth3
    Synonyms:Grp1, Pscd3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1335107. Cyth3.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: UniProtKB
    3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    4. plasma membrane Source: MGI
    5. ruffle Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi273 – 2731K → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi277 – 2771R → A or G: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi280 – 2801T → A or G: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi282 – 2821K → A: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi284 – 2841R → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi295 – 2951Y → F: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi305 – 3051R → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi343 – 3431K → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi354 – 3541N → A: Slightly reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi355 – 3551H → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication
    Mutagenesisi388 – 3881L → A: Impairs autoinhibition; when associated with A-392. 1 Publication
    Mutagenesisi392 – 3921K → A: Impairs autoinhibition; when associated with A-388. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 399399Cytohesin-3PRO_0000120201Add
    BLAST

    Proteomic databases

    MaxQBiO08967.
    PaxDbiO08967.
    PRIDEiO08967.

    PTM databases

    PhosphoSiteiO08967.

    Expressioni

    Gene expression databases

    ArrayExpressiO08967.
    BgeeiO08967.
    GenevestigatoriO08967.

    Interactioni

    Subunit structurei

    Interacts with GRASP.5 Publications

    Protein-protein interaction databases

    BioGridi202413. 2 interactions.

    Structurei

    Secondary structure

    1
    399
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 7916
    Helixi81 – 9010
    Helixi98 – 10710
    Helixi113 – 1219
    Helixi125 – 13612
    Helixi145 – 1528
    Helixi162 – 17918
    Beta strandi183 – 1853
    Helixi187 – 20519
    Helixi215 – 2217
    Turni222 – 2254
    Helixi233 – 24513
    Helixi258 – 2603
    Beta strandi266 – 2749
    Beta strandi276 – 2783
    Beta strandi281 – 2899
    Beta strandi292 – 2987
    Beta strandi305 – 3095
    Beta strandi314 – 3185
    Beta strandi324 – 3307
    Beta strandi332 – 3343
    Beta strandi342 – 3443
    Beta strandi350 – 3523
    Beta strandi356 – 3616
    Helixi365 – 38117
    Turni383 – 3864

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FGYX-ray1.50A261-387[»]
    1FGZX-ray2.05A261-387[»]
    1FHWX-ray1.90A/B264-391[»]
    1FHXX-ray2.50A/B264-391[»]
    1U2BX-ray1.80A261-387[»]
    2R09X-ray1.90A/B63-399[»]
    2R0DX-ray2.04A/B63-399[»]
    ProteinModelPortaliO08967.
    SMRiO08967. Positions 63-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO08967.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini77 – 206130SEC7PROSITE-ProRule annotationAdd
    BLAST
    Domaini264 – 380117PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni273 – 2808Phosphatidylinositol 3,4,5-trisphosphate binding
    Regioni391 – 3999C-terminal autoinhibitory region

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili14 – 6148Sequence AnalysisAdd
    BLAST

    Domaini

    Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate.
    Autoinhibited by its C-terminal basic region.

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 SEC7 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5307.
    HOGENOMiHOG000253023.
    HOVERGENiHBG002647.
    InParanoidiO08967.
    OMAiNLTCVEE.
    OrthoDBiEOG7RBZ9C.
    PhylomeDBiO08967.
    TreeFamiTF352091.

    Family and domain databases

    Gene3Di1.10.1000.11. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR023394. Sec7_alpha_orthog.
    IPR000904. Sec7_dom.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF01369. Sec7. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00222. Sec7. 1 hit.
    [Graphical view]
    SUPFAMiSSF48425. SSF48425. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50190. SEC7. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O08967-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEGGGGEGG SVPEDLSLEE REELLDIRRR KKELIDDIER LKYEIAEVMT    50
    EIDNLTSVEE SKTTQRNKQI AMGRKKFNMD PKKGIQFLIE NDLLQSSPED 100
    VAQFLYKGEG LNKTVIGDYL GERDDFNIKV LQAFVELHEF ADLNLVQALR 150
    QFLWSFRLPG EAQKIDRMME AFASRYCLCN PGVFQSTDTC YVLSFAIIML 200
    NTSLHNHNVR DKPTAERFIT MNRGINEGGD LPEELLRNLY ESIKNEPFKI 250
    PEDDGNDLTH TFFNPDREGW LLKLGGRVKT WKRRWFILTD NCLYYFEYTT 300
    DKEPRGIIPL ENLSIREVED PRKPNCFELY NPSHKGQVIK ACKTEADGRV 350
    VEGNHVVYRI SAPSPEEKEE WMKSIKASIS RDPFYDMLAT RKRRIANKK 399
    Length:399
    Mass (Da):46,280
    Last modified:July 1, 1997 - v1
    Checksum:i00F7FEB9C3849157
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001871 Genomic DNA. Translation: AAB60876.1.
    AB013470 mRNA. Translation: BAA33433.1.
    AF084221 mRNA. Translation: AAF23858.1.
    BC035296 mRNA. Translation: AAH35296.2.
    CCDSiCCDS19845.1.
    RefSeqiNP_035312.3. NM_011182.4.
    UniGeneiMm.281003.

    Genome annotation databases

    EnsembliENSMUST00000116456; ENSMUSP00000112157; ENSMUSG00000018001.
    GeneIDi19159.
    KEGGimmu:19159.
    UCSCiuc009ako.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001871 Genomic DNA. Translation: AAB60876.1 .
    AB013470 mRNA. Translation: BAA33433.1 .
    AF084221 mRNA. Translation: AAF23858.1 .
    BC035296 mRNA. Translation: AAH35296.2 .
    CCDSi CCDS19845.1.
    RefSeqi NP_035312.3. NM_011182.4.
    UniGenei Mm.281003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FGY X-ray 1.50 A 261-387 [» ]
    1FGZ X-ray 2.05 A 261-387 [» ]
    1FHW X-ray 1.90 A/B 264-391 [» ]
    1FHX X-ray 2.50 A/B 264-391 [» ]
    1U2B X-ray 1.80 A 261-387 [» ]
    2R09 X-ray 1.90 A/B 63-399 [» ]
    2R0D X-ray 2.04 A/B 63-399 [» ]
    ProteinModelPortali O08967.
    SMRi O08967. Positions 63-397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202413. 2 interactions.

    PTM databases

    PhosphoSitei O08967.

    Proteomic databases

    MaxQBi O08967.
    PaxDbi O08967.
    PRIDEi O08967.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000116456 ; ENSMUSP00000112157 ; ENSMUSG00000018001 .
    GeneIDi 19159.
    KEGGi mmu:19159.
    UCSCi uc009ako.2. mouse.

    Organism-specific databases

    CTDi 9265.
    MGIi MGI:1335107. Cyth3.

    Phylogenomic databases

    eggNOGi COG5307.
    HOGENOMi HOG000253023.
    HOVERGENi HBG002647.
    InParanoidi O08967.
    OMAi NLTCVEE.
    OrthoDBi EOG7RBZ9C.
    PhylomeDBi O08967.
    TreeFami TF352091.

    Miscellaneous databases

    ChiTaRSi CYTH3. mouse.
    EvolutionaryTracei O08967.
    NextBioi 295818.
    PROi O08967.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08967.
    Bgeei O08967.
    Genevestigatori O08967.

    Family and domain databases

    Gene3Di 1.10.1000.11. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR023394. Sec7_alpha_orthog.
    IPR000904. Sec7_dom.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF01369. Sec7. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00222. Sec7. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48425. SSF48425. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50190. SEC7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains."
      Klarlund J.K., Guilherme A., Holik J.J., Virbasius J.V., Chawla A., Czech M.P.
      Science 275:1927-1930(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complex regulation of multiple cytohesin-like genes in murine tissues and cells."
      Kim H.-S., Chen Y., Lonai P.
      FEBS Lett. 433:312-316(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Anergic T lymphocytes selectively express an integrin regulatory protein of the cytohesin family."
      Korthauer U., Nagel W., Davis E.M., Le Beau M.M., Menon R.S., Mitchell E.O., Kozak C.A., Kolanus W., Bluestone J.A.
      J. Immunol. 164:308-318(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NIH Swiss.
    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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    5. "Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors."
      Nevrivy D.J., Peterson V.J., Avram D., Ishmael J.E., Hansen S.G., Dowell P., Hruby D.E., Dawson M.I., Leid M.
      J. Biol. Chem. 275:16827-16836(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRASP.
    6. "Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains."
      Ferguson K.M., Kavran J.M., Sankaran V.G., Fournier E., Isakoff S.J., Skolnik E.Y., Lemmon M.A.
      Mol. Cell 6:373-384(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 264-391 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE, LIPID-BINDING, DOMAIN.
    7. "Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains."
      Lietzke S.E., Bose S., Cronin T., Klarlund J., Chawla A., Czech M.P., Lambright D.G.
      Mol. Cell 6:385-394(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 261-387 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 1,3,4,5-TETRAPHOSPHATE, DOMAIN, LIPID-BINDING.
    8. "Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains."
      Cronin T.C., DiNitto J.P., Czech M.P., Lambright D.G.
      EMBO J. 23:3711-3720(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 261-387 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE, LIPID-BINDING, DOMAIN, MUTAGENESIS OF LYS-273; ARG-277; THR-280; LYS-282; ARG-284; TYR-295; ARG-305; LYS-343; ASN-354 AND HIS-355.
    9. "Structural basis and mechanism of autoregulation in 3-phosphoinositide-dependent Grp1 family Arf GTPase exchange factors."
      DiNitto J.P., Delprato A., Gabe Lee M.T., Cronin T.C., Huang S., Guilherme A., Czech M.P., Lambright D.G.
      Mol. Cell 28:569-583(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 63-399 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 1,3,4,5-TETRAPHOSPHATE, FUNCTION, DOMAIN, AUTOINHIBITORY REGION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-388 AND LYS-392, LIPID-BINDING.

    Entry informationi

    Entry nameiCYH3_MOUSE
    AccessioniPrimary (citable) accession number: O08967
    Secondary accession number(s): Q8CI93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3