Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q20678

Entry ID Method Resolution Chain Position Source
AF-Q20678-F1 Predicted AlphaFoldDB

No variants for Q20678

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q20678

No associated diseases with Q20678

2 regional properties for Q20678

Type Name Position InterPro Accession
domain Exocyst complex component Sec3, C-terminal 187 - 825 IPR019160
domain Exocyst complex component Sec3, PIP2-binding N-terminal domain 33 - 124 IPR028258

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
exocyst A protein complex peripherally associated with the plasma membrane that determines where vesicles dock and fuse. At least eight complex components are conserved between yeast and mammals.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

1 GO annotations of molecular function

Name Definition
phosphatidylinositol-4,5-bisphosphate binding Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.

4 GO annotations of biological process

Name Definition
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
Golgi to plasma membrane transport The directed movement of substances from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane, where they fuse and release their contents by exocytosis.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
vesicle tethering involved in exocytosis The initial, indirect interaction between a secretory vesicle membrane and a site of exocytosis in the plasma membrane. This interaction is mediated by tethering factors (or complexes), which interact with both membranes. Interaction can occur via direct binding to membrane phospholipids or membrane proteins, or via binding to vesicle coat proteins. This process is distinct from and prior to docking and fusion.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NV70 EXOC1 Exocyst complex component 1 Homo sapiens (Human) PR
Q8R3S6 Exoc1 Exocyst complex component 1 Mus musculus (Mouse) PR
10 20 30 40 50 60
MSAIRKIIQR QLFQKDDERI QAIVNVSKLD GKKKKNQTLL CLAVTIEHPI AVRLYFVKGE
70 80 90 100 110 120
KDDTFKKKDR FNLREVREID GINPKKASPE FHITIGDHQY VILAGSAEEK DEFIRELYKL
130 140 150 160 170 180
SCQYLPVQMP DFCNFSLPQL ESETSIIPIE LPEHDMAMQS DYQPISNKED ADFRKLIARA
190 200 210 220 230 240
NLTIGEAHIF AEMLTEQLQS LDGANINSMM DSENSVNQLL SSIDAALTGV ESVEKELDRC
250 260 270 280 290 300
DDILAFVRNS IELIEEKDSL SVVERKNKQR LNEEIVSFVN SLQAVTDSHI ETLKQANFSN
310 320 330 340 350 360
PESVQRCTDA ARAVAQFWHG RISKPMLQMK AYQDRNDELT AVDVFVDRLM SHLSALFSNL
370 380 390 400 410 420
NDLSLDHEWH ELCIPKQSQR FRALSPLSDL INWLKTNRPK ACNLVLQKYI DSTNLLYKRL
430 440 450 460 470 480
FDNFFETLIN KVPKANSSEK KSKANESANI SLRSDNQSFL STSSEIDTEV LPQLIETVLA
490 500 510 520 530 540
ELSAVIDAEQ KFVVRFFHIN SELLAQFDTT STGSGDSSSL GGRSMEKHMN EQVRHVMGNL
550 560 570 580 590 600
FDSLNIHLDS FCRAVCRHNP SNVLLLFVIM SKKVLLPQDP SSYFSITFGS LVVLIKRQFD
610 620 630 640 650 660
AFIQMECSQY SEVRIAKKTR IGILPSIFRF ANFVRRAEII FENAERRTDL EKAYFNLCRA
670 680 690 700 710 720
VCDGIQKAAA NQYSKSPSSV VKFENYHELY LTLSELKISC LDQQRKDAKA LKEEHIDAYV
730 740 750 760 770 780
KEFMGRPLKE IQTFFDNVNN FIETRGIRPD EISYQQQFSR IELKKVISQH PGKEVKKGLE
790 800 810 820 830 840
QLYKKIEKNL VANSSLLQVV WRDMQEQFVK QIAEYNKLIL TCYPGSKIEL EVSTDTVLQF
FSEIAQQH