Q9QX11

SS
Gene name
Cyth1 (Pscd1)
Protein name
Cytohesin-1
Names
PH, SEC7 and coiled-coil domain-containing protein 1 , CLM1 , SEC7 homolog A , mSec7-1
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:19157
EC number
Protein Class

Descriptions

Cytohesin-3 (CYTH3) promotes guanine-nucleotide exchange on Arf1 and Arf6. Cytohesins share a modular architecture consisting of heptad repeats, a Sec7 domain with exchange activity for Arf1 and Arf6, a PH domain that binds phosphatidylinositol (PI) polyphosphates, and a C-terminal helix (CtH) that overlaps with a polybasic region (PBR). Cytohesins are autoinhibited by the Sec7-PH linker (252-264) and CtH/PBR (380-399), which obstruct substrate binding. The autoinhibition can be relieved by Arf6-GTP binding in the presence of the PIP3 head group.

Autoinhibitory domains (AIDs)

248-260 (Sec7-PH linker) SS

Target domain

59-247 (Sec7 domain)

Relief mechanism

Partner binding

Assay

376-395 (C-terminal helix/polybasic region) SS

Target domain

59-247 (Sec7 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9QX11

Entry ID Method Resolution Chain Position Source
AF-Q9QX11-F1 Predicted AlphaFoldDB

19 variants for Q9QX11

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389238052 32 A>D No EVA
rs3389219781 118 E>K No EVA
rs3389226026 121 E>D No EVA
rs3389224225 122 F>V No EVA
rs3389191152 167 A>T No EVA
rs3389196568 173 C>G No EVA
rs3389223070 174 Q>* No EVA
rs3389238108 179 V>G No EVA
rs3389185215 207 D>G No EVA
rs3389196607 223 D>E No EVA
rs3389196617 225 G>E No EVA
rs3389223527 241 N>I No EVA
rs3389183315 302 R>P No EVA
rs3389210755 315 V>M No EVA
rs3402774769 317 D>A No EVA
rs3402841583 317 D>Y No EVA
rs3389210781 320 K>R No EVA
rs3389224163 343 A>* No EVA
rs3389219832 349 E>* No EVA

No associated diseases with Q9QX11

28 regional properties for Q9QX11

Type Name Position InterPro Accession
conserved_site Actinin-type actin-binding domain, conserved site 45 - 54 IPR001589-1
conserved_site Actinin-type actin-binding domain, conserved site 121 - 145 IPR001589-2
domain Calponin homology domain 43 - 149 IPR001715-1
domain Calponin homology domain 166 - 269 IPR001715-2
repeat Filamin/ABP280 repeat-like 276 - 374 IPR017868-1
repeat Filamin/ABP280 repeat-like 376 - 474 IPR017868-2
repeat Filamin/ABP280 repeat-like 475 - 570 IPR017868-3
repeat Filamin/ABP280 repeat-like 571 - 663 IPR017868-4
repeat Filamin/ABP280 repeat-like 667 - 763 IPR017868-5
repeat Filamin/ABP280 repeat-like 764 - 866 IPR017868-6
repeat Filamin/ABP280 repeat-like 867 - 965 IPR017868-7
repeat Filamin/ABP280 repeat-like 966 - 1061 IPR017868-8
repeat Filamin/ABP280 repeat-like 1062 - 1154 IPR017868-9
repeat Filamin/ABP280 repeat-like 1155 - 1249 IPR017868-10
repeat Filamin/ABP280 repeat-like 1250 - 1349 IPR017868-11
repeat Filamin/ABP280 repeat-like 1350 - 1442 IPR017868-12
repeat Filamin/ABP280 repeat-like 1443 - 1539 IPR017868-13
repeat Filamin/ABP280 repeat-like 1540 - 1636 IPR017868-14
repeat Filamin/ABP280 repeat-like 1640 - 1740 IPR017868-15
repeat Filamin/ABP280 repeat-like 1779 - 1860 IPR017868-16
repeat Filamin/ABP280 repeat-like 1860 - 1952 IPR017868-17
repeat Filamin/ABP280 repeat-like 1950 - 2039 IPR017868-18
repeat Filamin/ABP280 repeat-like 2042 - 2134 IPR017868-19
repeat Filamin/ABP280 repeat-like 2132 - 2230 IPR017868-20
repeat Filamin/ABP280 repeat-like 2233 - 2325 IPR017868-21
repeat Filamin/ABP280 repeat-like 2327 - 2420 IPR017868-22
repeat Filamin/ABP280 repeat-like 2424 - 2516 IPR017868-23
repeat Filamin/ABP280 repeat-like 2552 - 2646 IPR017868-24

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein
  • Cytoplasm, cytosol
  • Cell junction, tight junction
  • Cell junction, adherens junction
  • Colocalized with TJP1 during epithelial polarization (PubMed:20080746)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
adherens junction A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules.
bicellular tight junction An occluding cell-cell junction that is composed of a branching network of sealing strands that completely encircles the apical end of each cell in an epithelial sheet; the outer leaflets of the two interacting plasma membranes are seen to be tightly apposed where sealing strands are present. Each sealing strand is composed of a long row of transmembrane adhesion proteins embedded in each of the two interacting plasma membranes.
cytoplasmic side of plasma membrane The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
extrinsic component of presynaptic membrane The component of the presynaptic membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
neuromuscular junction The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
lipid binding Binding to a lipid.

3 GO annotations of biological process

Name Definition
establishment of epithelial cell polarity The specification and formation of anisotropic intracellular organization of an epithelial cell.
presynaptic modulation of chemical synaptic transmission Any process, acting in the presynapse that results in modulation of chemical synaptic transmission.
regulation of ARF protein signal transduction Any process that modulates the frequency, rate or extent of ARF protein signal transduction.

16 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q2KI41 CYTH2 Cytohesin-2 Bos taurus (Bovine) SS
O43739 CYTH3 Cytohesin-3 Homo sapiens (Human) EV
Q99418 CYTH2 Cytohesin-2 Homo sapiens (Human) SS
Q9UIA0 CYTH4 Cytohesin-4 Homo sapiens (Human) SS
Q15438 CYTH1 Cytohesin-1 Homo sapiens (Human) SS
A2A5R2 Arfgef2 Brefeldin A-inhibited guanine nucleotide-exchange protein 2 Mus musculus (Mouse) PR
G3X9K3 Arfgef1 Brefeldin A-inhibited guanine nucleotide-exchange protein 1 Mus musculus (Mouse) PR
Q3TES0 Iqsec3 IQ motif and SEC7 domain-containing protein 3 Mus musculus (Mouse) SS
Q8R0S2 Iqsec1 IQ motif and SEC7 domain-containing protein 1 Mus musculus (Mouse) SS
P63034 Cyth2 Cytohesin-2 Mus musculus (Mouse) SS
Q80YW0 Cyth4 Cytohesin-4 Mus musculus (Mouse) SS
O08967 Cyth3 Cytohesin-3 Mus musculus (Mouse) EV
Q5DU25 Iqsec2 IQ motif and SEC7 domain-containing protein 2 Mus musculus (Mouse) SS
P97696 Cyth3 Cytohesin-3 Rattus norvegicus (Rat) SS
P63035 Cyth2 Cytohesin-2 Rattus norvegicus (Rat) SS
P97694 Cyth1 Cytohesin-1 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MEDDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKEE IAEVANEIES LGSTEERKNM
70 80 90 100 110 120
QRNKQVAMGR KKFNMDPKKG IQFLIENGLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD
130 140 150 160 170 180
EFSIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNTGVF
190 200 210 220 230 240
QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK
250 260 270 280 290 300
NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
310 320 330 340 350 360
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP
370 380 390
TPEEKEDWIK CIKAAISRDP FYEMLAARKK KVSSTKRH