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Protein

Cytohesin-1

Gene

Cyth1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei281Phosphatidylinositol 3,4,5-trisphosphateBy similarity1
Binding sitei292Phosphatidylinositol 3,4,5-trisphosphateBy similarity1
Binding sitei302Phosphatidylinositol 3,4,5-trisphosphateBy similarity1
Binding sitei351Phosphatidylinositol 3,4,5-trisphosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGuanine-nucleotide releasing factor
LigandLipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytohesin-1
Alternative name(s):
PH, SEC7 and coiled-coil domain-containing protein 1
SEC7 homolog A
Short name:
rSec7-1
Gene namesi
Name:Cyth1
Synonyms:Pscd1, Sec7a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620397 Cyth1

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
Mutagenesisi157E → K: Loss of ARF translocation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001201961 – 398Cytohesin-1Add BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Post-translational modificationi

Ubiquitinated by SCF(FBXW11) E3 ubiquitin-protein ligase complex. Ubiquitination induces proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

PaxDbiP97694
PRIDEiP97694

PTM databases

iPTMnetiP97694
PhosphoSitePlusiP97694

Expressioni

Tissue specificityi

Present in all tissues tested, with highest protein levels in brain and adrenal.

Developmental stagei

On embryonic days 15 (E15) and E18, expression is seen in the mantle and ventricular germinal zones throughout the neuraxis. On postnatal days 0 (P0) and P7, expression is seen in the cerebral neocortex, olfactory mitral and granule cell layers, hippocampal pyramidal and dentate granule cells and the striatum. A lower expression is seen in gray matter in di-, mes- and met-encephali. In the cerebellum, the expression is evident in the external and internal granule cell layers and Purkinje cell layer. On P14, a decreased expression is seen in the di-, mes- and met-encephali. On P21 and thereafter, expression is seen in the olfactory mitral and granule cells, dentate granule cells and the cerebellar granule cells and Purkinje cells.1 Publication

Interactioni

Subunit structurei

Interacts with TRIM23 and CYTIP (By similarity). Interacts (via coiled-coil domain) with FRMD4A (via coiled-coil domain) (By similarity). Interacts with FRMD4B (By similarity). Found in a complex with PARD3, CYTH1 and FRMD4A (By similarity). Interacts (via N-terminal domain) with INAVA (via N-terminal domain) (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250573, 1 interactor
STRINGi10116.ENSRNOP00000004196

Structurei

3D structure databases

ProteinModelPortaliP97694
SMRiP97694
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini73 – 202SEC7PROSITE-ProRule annotationAdd BLAST130
Domaini260 – 377PHPROSITE-ProRule annotationAdd BLAST118

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 277Phosphatidylinositol 3,4,5-trisphosphate bindingBy similarity9
Regioni388 – 396C-terminal autoinhibitory regionBy similarity9

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili10 – 67Sequence analysisAdd BLAST58

Domaini

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0930 Eukaryota
COG5307 LUCA
HOVERGENiHBG002647
InParanoidiP97694
KOiK18441
PhylomeDBiP97694

Family and domain databases

CDDicd00171 Sec7, 1 hit
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

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

P97694-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEDDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKEE IAEVANEIES
60 70 80 90 100
LGSTEERKNM QRNKQVAMGR KKFNMDPKKG IQFLIENGLL KNTCEDIAQF
110 120 130 140 150
LYKGEGLNKT AIGDYLGERD EFSIQVLHAF VELHEFTDLN LVQALRQFLW
160 170 180 190 200
SFRLPGEAQK IDRMMEAFAQ RYCQCNTGVF QSTDTCYVLS FAIIMLNTSL
210 220 230 240 250
HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK NEPFKIPEDD
260 270 280 290 300
GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
310 320 330 340 350
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG
360 370 380 390
NHTVYRISAP TPEEKEDWIK CIKAAISRDP FYEMLAARKK KVSSTKRH
Length:398
Mass (Da):46,274
Last modified:May 1, 1997 - v1
Checksum:i79E06E2364282E85
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B2GUV0B2GUV0_RAT
Cyth1 protein
Cyth1 Usp36
397Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83895 mRNA Translation: AAB41443.1
RefSeqiNP_446362.1, NM_053910.1
UniGeneiRn.10672
Rn.188834

Genome annotation databases

GeneIDi116691
KEGGirno:116691
UCSCiRGD:620397 rat

Similar proteinsi

Entry informationi

Entry nameiCYH1_RAT
AccessioniPrimary (citable) accession number: P97694
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1997
Last modified: September 12, 2018
This is version 112 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

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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