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O08967

- CYH3_MOUSE

UniProt

O08967 - CYH3_MOUSE

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Protein

Cytohesin-3

Gene
Cyth3, Grp1, Pscd3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-trisphosphate
Binding sitei295 – 2951Phosphatidylinositol 3,4,5-trisphosphate
Binding sitei305 – 3051Phosphatidylinositol 3,4,5-trisphosphate
Binding sitei354 – 3541Phosphatidylinositol 3,4,5-trisphosphate

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. regulation of ARF protein signal transduction Source: InterPro
  5. regulation of GTPase activity Source: GOC
Complete GO annotation...

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

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
Complete GO annotation...

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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiO08967.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 206130SEC7Add
BLAST
Domaini264 – 380117PHAdd
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 – 6148 Reviewed predictionAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 SEC7 domain.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 117 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

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