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O08967

- CYH3_MOUSE

UniProt

O08967 - CYH3_MOUSE

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Protein

Cytohesin-3

Gene

Cyth3

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-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

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
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 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
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

BgeeiO08967.
ExpressionAtlasiO08967. baseline and differential.
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 – 7916Combined sources
Helixi81 – 9010Combined sources
Helixi98 – 10710Combined sources
Helixi113 – 1219Combined sources
Helixi125 – 13612Combined sources
Helixi145 – 1528Combined sources
Helixi162 – 17918Combined sources
Beta strandi183 – 1853Combined sources
Helixi187 – 20519Combined sources
Helixi215 – 2217Combined sources
Turni222 – 2254Combined sources
Helixi233 – 24513Combined sources
Helixi258 – 2603Combined sources
Beta strandi266 – 2749Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi281 – 2899Combined sources
Beta strandi292 – 2987Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi314 – 3185Combined sources
Beta strandi324 – 3307Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi356 – 3616Combined sources
Helixi365 – 38117Combined sources
Turni383 – 3864Combined sources

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.
KOiK18441.
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

        10         20         30         40         50
MDEGGGGEGG SVPEDLSLEE REELLDIRRR KKELIDDIER LKYEIAEVMT
60 70 80 90 100
EIDNLTSVEE SKTTQRNKQI AMGRKKFNMD PKKGIQFLIE NDLLQSSPED
110 120 130 140 150
VAQFLYKGEG LNKTVIGDYL GERDDFNIKV LQAFVELHEF ADLNLVQALR
160 170 180 190 200
QFLWSFRLPG EAQKIDRMME AFASRYCLCN PGVFQSTDTC YVLSFAIIML
210 220 230 240 250
NTSLHNHNVR DKPTAERFIT MNRGINEGGD LPEELLRNLY ESIKNEPFKI
260 270 280 290 300
PEDDGNDLTH TFFNPDREGW LLKLGGRVKT WKRRWFILTD NCLYYFEYTT
310 320 330 340 350
DKEPRGIIPL ENLSIREVED PRKPNCFELY NPSHKGQVIK ACKTEADGRV
360 370 380 390
VEGNHVVYRI SAPSPEEKEE WMKSIKASIS RDPFYDMLAT RKRRIANKK
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.
KOi K18441.
OMAi NLTCVEE.
OrthoDBi EOG7RBZ9C.
PhylomeDBi O08967.
TreeFami TF352091.

Miscellaneous databases

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

Gene expression databases

Bgeei O08967.
ExpressionAtlasi O08967. baseline and differential.
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: October 29, 2014
This is version 119 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