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 Q08967

Entry ID Method Resolution Chain Position Source
AF-Q08967-F1 Predicted AlphaFoldDB

13 variants for Q08967

Variant ID(s) Position Change Description Diseaes Association Provenance
s16-133197 52 D>E No SGRP
s16-133288 83 I>V No SGRP
s16-133302 87 N>K No SGRP
s16-133306 89 D>N No SGRP
s16-133366 109 D>N No SGRP
s16-133387 116 Q>E No SGRP
s16-133387 116 Q>K No SGRP
s16-135050 670 R>P No SGRP
s16-135193 718 K>E No SGRP
s16-135273 744 Q>H No SGRP
s16-135327 762 M>I No SGRP
s16-135325 762 M>V No SGRP
s16-135335 765 M>T No SGRP

No associated diseases with Q08967

24 regional properties for Q08967

Type Name Position InterPro Accession
domain F-box domain 1 - 50 IPR001810
repeat Parallel beta-helix repeat 198 - 217 IPR006626-1
repeat Parallel beta-helix repeat 238 - 260 IPR006626-2
repeat Parallel beta-helix repeat 423 - 444 IPR006626-3
repeat Parallel beta-helix repeat 467 - 489 IPR006626-4
repeat Parallel beta-helix repeat 490 - 512 IPR006626-5
repeat Parallel beta-helix repeat 513 - 535 IPR006626-6
repeat Parallel beta-helix repeat 536 - 558 IPR006626-7
repeat Parallel beta-helix repeat 559 - 581 IPR006626-8
repeat Parallel beta-helix repeat 582 - 604 IPR006626-9
repeat Parallel beta-helix repeat 605 - 627 IPR006626-10
repeat Parallel beta-helix repeat 628 - 650 IPR006626-11
repeat Parallel beta-helix repeat 651 - 673 IPR006626-12
repeat Parallel beta-helix repeat 713 - 735 IPR006626-13
repeat Parallel beta-helix repeat 736 - 758 IPR006626-14
repeat Parallel beta-helix repeat 760 - 782 IPR006626-15
repeat Parallel beta-helix repeat 783 - 805 IPR006626-16
repeat Parallel beta-helix repeat 828 - 850 IPR006626-17
domain Carbohydrate-binding/sugar hydrolysis domain 337 - 511 IPR006633-1
domain Carbohydrate-binding/sugar hydrolysis domain 536 - 672 IPR006633-2
domain Carbohydrate-binding/sugar hydrolysis domain 681 - 804 IPR006633-3
domain Periplasmic copper-binding protein NosD, beta helix domain 719 - 868 IPR007742
repeat Parallel beta-helix repeat-2 530 - 569 IPR022441
domain Right handed beta helix domain 423 - 568 IPR039448

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
cellular bud neck The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
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.
fungal-type vacuole A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
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.

1 GO annotations of molecular function

Name Definition
FAD transmembrane transporter activity Enables the directed movement of flavin-adenine dinucleotide (FAD) from one side of a membrane to the other. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form.

5 GO annotations of biological process

Name Definition
FAD transport The directed movement of flavin-adenine dinucleotide (FAD) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form.
fungal-type cell wall biogenesis A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
sphingolipid biosynthetic process The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P53121 FLC3 Putative flavin carrier protein 3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P39719 FLC2 Flavin carrier protein 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MQVLVTLWCL ICTCLVLPVA AKKRTLTASS LVTCMENSQL SANSFDVSFS PDDRSLHYDL
70 80 90 100 110 120
DMTTQIDSYI YAYVDVYAYG FKIITENFDV CSMGWKQFCP VHPGNIQIDS IEYIAQKYVK
130 140 150 160 170 180
MIPGIAYQVP DIDAYVRLNI YNNVSENLAC IQVFFSNGKT VSQIGVKWVT AVIAGIGLLT
190 200 210 220 230 240
SAVLSTFGNS TAASHISANT MSLFLYFQSV AVVAMQHVDS VPPIAAAWSE NLAWSMGLIR
250 260 270 280 290 300
ITFMQKIFRW YVEATGGSAS LYLTATTMSV LTQRGLDYLK NTSVYKRAEN VLYGNSNTLI
310 320 330 340 350 360
FRGIKRMGYR MKIENTAIVC TGFTFFVLCG YFLAGFIMAC KYSIELCIRC GWMRSDRFYQ
370 380 390 400 410 420
FRKNWRSVLK GSLLRYIYIG FTQLTILSFW EFTERDSAGV IVIACLFIVL SCGLMAWAAY
430 440 450 460 470 480
RTIFFASKSV EMYNNPAALL YGDEYVLNKY GFFYTMFNAK HYWWNALLTT YILVKALFVG
490 500 510 520 530 540
FAQASGKTQA LAIFIIDLAY FVAIIRYKPY LDRPTNIVNI FICTVTLVNS FLFMFFSNLF
550 560 570 580 590 600
NQKYAVSAIM GWVFFIMNAA FSLLLLLMIL AFTTIILFSK NPDSRFKPAK DDRASFQKHA
610 620 630 640 650 660
IPHEGALNKS VANELMALGN VAKDHTENWE YELKSQEGKS EDNLFGVEYD DEKTGTNSEN
670 680 690 700 710 720
AESSSKETTR PTFSEKVLRS LSIKRNKSKL GSFKRSAPDK ITQQEVSPDR ASSSPNSKSY
730 740 750 760 770 780
PGVSHTRQES EANNGLINAY EDEQFSLMEP SILEDAASST QMHAMPARDL SLSSVANAQD
790
VTKKANILDP DYL