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Protein

Cytohesin-1

Gene

Cyth1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Promotes guanine-nucleotide exchange on ARF6. Promotes the activation of ARF6 through replacement of GDP with GTP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei281 – 2811Phosphatidylinositol 3,4,5-trisphosphateBy similarity
Binding sitei292 – 2921Phosphatidylinositol 3,4,5-trisphosphateBy similarity
Binding sitei302 – 3021Phosphatidylinositol 3,4,5-trisphosphateBy similarity
Binding sitei351 – 3511Phosphatidylinositol 3,4,5-trisphosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Lipid-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620397. Cyth1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571E → K: Loss of ARF translocation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Cytohesin-1PRO_0000120196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP97694.
PRIDEiP97694.

PTM databases

iPTMnetiP97694.

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

Protein-protein interaction databases

BioGridi250573. 1 interaction.
STRINGi10116.ENSRNOP00000004196.

Structurei

3D structure databases

ProteinModelPortaliP97694.
SMRiP97694. Positions 58-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 202130SEC7PROSITE-ProRule annotationAdd
BLAST
Domaini260 – 377118PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 2779Phosphatidylinositol 3,4,5-trisphosphate bindingBy similarity
Regioni388 – 3969C-terminal autoinhibitory regionBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili10 – 6758Sequence analysisAdd
BLAST

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

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0930. Eukaryota.
COG5307. LUCA.
HOVERGENiHBG002647.
InParanoidiP97694.
KOiK18441.
PhylomeDBiP97694.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50190. SEC7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Sequence databases

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

Genome annotation databases

GeneIDi116691.
KEGGirno:116691.
UCSCiRGD:620397. rat.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP97694.
SMRiP97694. Positions 58-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250573. 1 interaction.
STRINGi10116.ENSRNOP00000004196.

PTM databases

iPTMnetiP97694.

Proteomic databases

PaxDbiP97694.
PRIDEiP97694.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116691.
KEGGirno:116691.
UCSCiRGD:620397. rat.

Organism-specific databases

CTDi9267.
RGDi620397. Cyth1.

Phylogenomic databases

eggNOGiKOG0930. Eukaryota.
COG5307. LUCA.
HOVERGENiHBG002647.
InParanoidiP97694.
KOiK18441.
PhylomeDBiP97694.

Miscellaneous databases

PROiP97694.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
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.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Rat homologues of yeast sec7p."
    Telemenakis I., Benseler F., Stenius K., Suedhof T.C., Brose N.
    Eur. J. Cell Biol. 74:143-149(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A presynaptic role for the ADP ribosylation factor (ARF)-specific GDP/GTP exchange factor msec7-1."
    Ashery U., Koch H., Scheuss V., Brose N., Rettig J.
    Proc. Natl. Acad. Sci. U.S.A. 96:1094-1099(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-157.
  3. "Localization of mRNAs for subfamily of guanine nucleotide-exchange proteins (GEP) for ARFs (ADP-ribosylation factors) in the brain of developing and mature rats under normal and postaxotomy conditions."
    Suzuki I., Owada Y., Suzuki R., Yoshimoto T., Kondo H.
    Brain Res. Mol. Brain Res. 98:41-50(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiCYH1_RAT
AccessioniPrimary (citable) accession number: P97694
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 96 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.