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Protein

Cytohesin-1

Gene

Cyth1

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

Functioni

Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP.1 Publication

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

  • ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

  • establishment of epithelial cell polarity Source: MGI
  • positive regulation of GTPase activity Source: MGI
  • regulation of cell adhesion Source: GO_Central
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
Short name:
CLM1
SEC7 homolog A
Short name:
mSec7-1
Gene namesi
Name:Cyth1
Synonyms:Pscd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1334257. Cyth1.

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: MGI
  • cytosol Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3851L → A: Impairs autoinhibition; when associated with A-389. Impairs translocation to the cell membrane. 1 Publication
Mutagenesisi389 – 3891K → A: Impairs autoinhibition; when associated with A-385. Impairs translocation to the cell membrane. 1 Publication
Mutagenesisi394 – 3941S → E: Increases guanine exchange factor activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Cytohesin-1PRO_0000120195Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9QX11.
PaxDbiQ9QX11.
PRIDEiQ9QX11.

PTM databases

PhosphoSiteiQ9QX11.

Expressioni

Gene expression databases

BgeeiQ9QX11.
ExpressionAtlasiQ9QX11. baseline and differential.
GenevisibleiQ9QX11. MM.

Interactioni

Subunit structurei

Interacts with TRIM23 and CYTIP.By similarity

Protein-protein interaction databases

IntActiQ9QX11. 1 interaction.
STRINGi10090.ENSMUSP00000101909.

Structurei

3D structure databases

ProteinModelPortaliQ9QX11.
SMRiQ9QX11. 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.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00760000119036.
HOVERGENiHBG002647.
InParanoidiQ9QX11.
KOiK18441.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QX11-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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:July 27, 2011 - v2
Checksum:i79E06E2364282E85
GO
Isoform 2 (identifier: Q9QX11-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     273-273: Missing.

Show »
Length:397
Mass (Da):46,217
Checksum:i75F3183266EC695A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31D → E in AAC71694 (PubMed:9745014).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei273 – 2731Missing in isoform 2. 1 PublicationVSP_006035

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013464 mRNA. Translation: BAA33428.1.
AF051337 mRNA. Translation: AAC71694.1.
AB035538 mRNA. Translation: BAB13509.1.
CCDSiCCDS48996.1. [Q9QX11-1]
CCDS48997.1. [Q9QX11-2]
RefSeqiNP_001106169.1. NM_001112699.1. [Q9QX11-2]
NP_035310.2. NM_011180.3. [Q9QX11-1]
UniGeneiMm.86413.

Genome annotation databases

EnsembliENSMUST00000017276; ENSMUSP00000017276; ENSMUSG00000017132. [Q9QX11-2]
ENSMUST00000106305; ENSMUSP00000101912; ENSMUSG00000017132. [Q9QX11-1]
GeneIDi19157.
KEGGimmu:19157.
UCSCiuc011yil.1. mouse. [Q9QX11-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013464 mRNA. Translation: BAA33428.1.
AF051337 mRNA. Translation: AAC71694.1.
AB035538 mRNA. Translation: BAB13509.1.
CCDSiCCDS48996.1. [Q9QX11-1]
CCDS48997.1. [Q9QX11-2]
RefSeqiNP_001106169.1. NM_001112699.1. [Q9QX11-2]
NP_035310.2. NM_011180.3. [Q9QX11-1]
UniGeneiMm.86413.

3D structure databases

ProteinModelPortaliQ9QX11.
SMRiQ9QX11. Positions 58-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QX11. 1 interaction.
STRINGi10090.ENSMUSP00000101909.

PTM databases

PhosphoSiteiQ9QX11.

Proteomic databases

MaxQBiQ9QX11.
PaxDbiQ9QX11.
PRIDEiQ9QX11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017276; ENSMUSP00000017276; ENSMUSG00000017132. [Q9QX11-2]
ENSMUST00000106305; ENSMUSP00000101912; ENSMUSG00000017132. [Q9QX11-1]
GeneIDi19157.
KEGGimmu:19157.
UCSCiuc011yil.1. mouse. [Q9QX11-1]

Organism-specific databases

CTDi9267.
MGIiMGI:1334257. Cyth1.

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00760000119036.
HOVERGENiHBG002647.
InParanoidiQ9QX11.
KOiK18441.
TreeFamiTF352091.

Miscellaneous databases

ChiTaRSiCyth1. mouse.
NextBioi295810.
PROiQ9QX11.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QX11.
ExpressionAtlasiQ9QX11. baseline and differential.
GenevisibleiQ9QX11. MM.

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]
ProtoNetiSearch...

Publicationsi

  1. "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] (ISOFORM 2).
    Tissue: Brain.
  2. "Cloning and sequencing of cDNA encoding mouse cytohesin-1."
    O'Rourke A.M., Escuro G., Feeney A.J.
    Immunogenetics 48:354-355(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: B10D2/NSNJ.
    Tissue: Lymph node.
  3. "Cloning and characterization of the promoter of murine cytohesin-1 gene."
    Goda N., Tanoue A., Kikuchi S., Tsujimoto G.
    Biochim. Biophys. Acta 1493:195-199(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AUTOINHIBITION, MUTAGENESIS OF LEU-385; LYS-389 AND SER-394.

Entry informationi

Entry nameiCYH1_MOUSE
AccessioniPrimary (citable) accession number: Q9QX11
Secondary accession number(s): O88817, Q76MU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 114 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.