Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytohesin-3

Gene

Cyth3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Play a role in the epithelial polarization (PubMed:20080746).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei284Phosphatidylinositol 3,4,5-trisphosphate2 Publications1
Binding sitei295Phosphatidylinositol 3,4,5-trisphosphate2 Publications1
Binding sitei305Phosphatidylinositol 3,4,5-trisphosphate2 Publications1
Binding sitei354Phosphatidylinositol 3,4,5-trisphosphate2 Publications1

GO - Molecular functioni

  • ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
  • guanyl-nucleotide exchange factor activity Source: MGI
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: MGI

GO - Biological processi

  • establishment of epithelial cell polarity Source: MGI
  • Golgi vesicle transport Source: UniProtKB
  • positive regulation of cell adhesion Source: MGI
  • regulation of ARF protein signal transduction Source: InterPro

Keywordsi

Molecular functionGuanine-nucleotide releasing factor
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-6811438 Intra-Golgi traffic

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1335107 Cyth3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi161E → K: Impairs epithelium polarization. 1 Publication1
Mutagenesisi273K → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi277R → A or G: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi280T → A or G: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi282K → A: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi284R → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi295Y → F: Reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi305R → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi343K → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi354N → A: Slightly reduces phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi355H → A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding. 1 Publication1
Mutagenesisi388L → A: Impairs autoinhibition; when associated with A-392. 1 Publication1
Mutagenesisi392K → A: Impairs autoinhibition; when associated with A-388. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3763004

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001202011 – 399Cytohesin-3Add BLAST399

Proteomic databases

PaxDbiO08967
PRIDEiO08967

PTM databases

iPTMnetiO08967
PhosphoSitePlusiO08967

Expressioni

Gene expression databases

BgeeiENSMUSG00000018001
ExpressionAtlasiO08967 baseline and differential
GenevisibleiO08967 MM

Interactioni

Subunit structurei

Interacts with GRASP. Interacts with FRMD4A (PubMed:20080746). Interacts with FRMD4B (PubMed:20080746).6 Publications

GO - Molecular functioni

  • ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
  • guanyl-nucleotide exchange factor activity Source: MGI

Protein-protein interaction databases

BioGridi202413, 5 interactors
IntActiO08967, 3 interactors
STRINGi10090.ENSMUSP00000112157

Structurei

Secondary structure

1399
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi64 – 79Combined sources16
Helixi81 – 90Combined sources10
Helixi98 – 107Combined sources10
Helixi113 – 121Combined sources9
Helixi125 – 136Combined sources12
Helixi145 – 152Combined sources8
Helixi162 – 179Combined sources18
Beta strandi183 – 185Combined sources3
Helixi187 – 205Combined sources19
Helixi215 – 221Combined sources7
Turni222 – 225Combined sources4
Helixi233 – 245Combined sources13
Helixi258 – 260Combined sources3
Beta strandi266 – 274Combined sources9
Beta strandi276 – 278Combined sources3
Beta strandi281 – 289Combined sources9
Beta strandi292 – 298Combined sources7
Beta strandi305 – 309Combined sources5
Beta strandi314 – 318Combined sources5
Beta strandi324 – 330Combined sources7
Beta strandi332 – 334Combined sources3
Beta strandi342 – 344Combined sources3
Beta strandi350 – 352Combined sources3
Beta strandi356 – 361Combined sources6
Helixi365 – 381Combined sources17
Turni383 – 386Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
6BBPelectron microscopy35.00A63-399[»]
6BBQelectron microscopy35.00A63-399[»]
ProteinModelPortaliO08967
SMRiO08967
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08967

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 206SEC7PROSITE-ProRule annotationAdd BLAST130
Domaini264 – 380PHPROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni273 – 280Phosphatidylinositol 3,4,5-trisphosphate binding8
Regioni391 – 399C-terminal autoinhibitory region9

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili14 – 61Sequence analysisAdd BLAST48

Domaini

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0930 Eukaryota
COG5307 LUCA
GeneTreeiENSGT00760000119036
HOGENOMiHOG000253023
HOVERGENiHBG002647
InParanoidiO08967
KOiK18441
OMAiFTSTDTC
OrthoDBiEOG091G0RZS
PhylomeDBiO08967
TreeFamiTF352091

Family and domain databases

Gene3Di1.10.1000.11, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR023394 Sec7_C_sf
IPR000904 Sec7_dom
IPR035999 Sec7_dom_sf
PfamiView protein in Pfam
PF00169 PH, 1 hit
PF01369 Sec7, 1 hit
SMARTiView protein in SMART
SM00233 PH, 1 hit
SM00222 Sec7, 1 hit
SUPFAMiSSF48425 SSF48425, 1 hit
PROSITEiView protein in PROSITE
PS50003 PH_DOMAIN, 1 hit
PS50190 SEC7, 1 hit

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:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiCYH3_MOUSE
AccessioniPrimary (citable) accession number: O08967
Secondary accession number(s): Q8CI93
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 1, 1997
Last modified: March 28, 2018
This is version 148 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health