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 Q10269

Entry ID Method Resolution Chain Position Source
AF-Q10269-F1 Predicted AlphaFoldDB

5 variants for Q10269

Variant ID(s) Position Change Description Diseaes Association Provenance
I_2306098_A_G 252 T>A No Jeffares_SNPs
I_2306260_A_G 306 N>D No Jeffares_SNPs
I_2306345_A_G 334 H>R No Jeffares_SNPs
I_2306350_A_T 336 M>L No Jeffares_SNPs
I_2306854_C_G 504 Q>E No Jeffares_SNPs

No associated diseases with Q10269

3 regional properties for Q10269

Type Name Position InterPro Accession
conserved_site Fumarate lyase, conserved site 282 - 291 IPR020557
domain Fumarate lyase, N-terminal 13 - 307 IPR022761
domain Argininosuccinate lyase, C-terminal 370 - 439 IPR029419

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cortical endoplasmic reticulum A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of endoplasmic reticulum membrane The component of the endoplasmic reticulum 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.
perinuclear endoplasmic reticulum The portion of endoplasmic reticulum, the intracellular network of tubules and cisternae, that occurs near the nucleus. The lumen of the perinuclear endoplasmic reticulum is contiguous with the nuclear envelope lumen (also called perinuclear space), the region between the inner and outer nuclear membranes.

2 GO annotations of molecular function

Name Definition
ergosterol O-acyltransferase activity Catalysis of the reaction: acyl-CoA + ergosterol = CoA + ergosterol ester.
O-acyltransferase activity Catalysis of the transfer of an acyl group to an oxygen atom on the acceptor molecule.

3 GO annotations of biological process

Name Definition
ergosterol biosynthetic process The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
ergosterol metabolic process The chemical reactions and pathways involving ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds. It is the most important of the D provitamins and is converted to vitamin D2 on irradiation with UV light.
lipid droplet formation A process that results in the assembly, arrangement of constituent parts of a lipid droplet.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTDTPRILIT PSPLSDISTT INKPNVHPSM SLLKALPECR LVVKSKGDKN NANVVEFPLD
70 80 90 100 110 120
RHKQLLIAGK VYHDYKFKPR KSIFDRVTDP NYFAKSEFRG FYVLFWLSMA AWVLQLYARS
130 140 150 160 170 180
YWQRDTLLGL PLARQVFRQF FVLFSSDFLM ICLSFFSYGL QVCIEKNMIR WANLGYTIQT
190 200 210 220 230 240
LWQGFYMVLA VYWVKHRDFP IVQCVFFTLH CAVLIMKQFS YSHHMGYISE IRILHNEYEK
250 260 270 280 290 300
LLKFVRECLN STEKDEKYTF ELTFPNKPAE TISTLQAEEI VALTAKYLSR QMRSEVGNVV
310 320 330 340 350 360
YPDNINFFNY VDYLLVPSLV YSMEFPRVAH FRWHYMAFKA GSTFGLLALT LALVDWYFVP
370 380 390 400 410 420
SAVAVKDLDF IGKLRIAPLL MNKIMFPAII LYLIMFYLIF DCILNAFAEI TKFADRGFYG
430 440 450 460 470 480
AWWNTVTWDE FSREWNKPVH VFLMRHVYHS SISGFKLKKS HAVLLTFLIS ALVHEFVMLL
490 500 510 520 530
ATGKFRCYIL TFQLLQIPLY DLQQMFAFKK RDILGNVFFW IGMFTGPSFL CILYIVF