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 O13644

Entry ID Method Resolution Chain Position Source
AF-O13644-F1 Predicted AlphaFoldDB

No variants for O13644

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O13644

No associated diseases with O13644

2 regional properties for O13644

Type Name Position InterPro Accession
domain Target SNARE coiled-coil homology domain 213 - 306 IPR000727
domain Syntaxin-5, N-terminal, Sly1p-binding domain 1 - 15 IPR021538

Functions

Description
EC Number
Subcellular Localization
  • Membrane ; Single-pass type IV membrane protein
  • Golgi apparatus membrane ; Single-pass type IV membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cis-Golgi network The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum.
endomembrane system A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
SNARE complex A protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers. One well-characterized example is the neuronal SNARE complex formed of synaptobrevin 2, syntaxin 1a, and SNAP-25.

2 GO annotations of molecular function

Name Definition
SNAP receptor activity Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.
SNARE binding Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.

4 GO annotations of biological process

Name Definition
endoplasmic reticulum to Golgi vesicle-mediated transport The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
intracellular protein transport The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
vesicle docking The initial attachment of a transport vesicle membrane to the target membrane, mediated by proteins protruding from the membrane of the vesicle and the target membrane. Docking requires only that the two membranes come close enough for these proteins to interact and adhere.
vesicle fusion Fusion of the membrane of a transport vesicle with its target membrane.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSFQDRTAEF QACVTKTRSR LRTTTANQAV GGPDQTKHQK SEFTRIAQKI ANQINQTGEK
70 80 90 100 110 120
LQKLSQLAKR KTLFDDRPVE IQELTFQIKQ SLSSLNSDIA SLQQVVKGNR NKPAQMNQHS
130 140 150 160 170 180
ENVVVSLQNS LANTSMTFKD ILEIRTQNMK ASQNRTEKFV ASSSMNANPL INSGNSISPF
190 200 210 220 230 240
ADYNDPKPEA NEDYLSLNLG DGANTRYEQM ALLESQTDTY SQQRMSSIQN IESTITELGG
250 260 270 280 290 300
IFSQLAQMVS EQRETVQRID MHTDDIVSNI GSAQREIVKF YERMSSNRAL LFKIFGIVII
FFLLWVLVT