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 Q6NS82

Entry ID Method Resolution Chain Position Source
AF-Q6NS82-F1 Predicted AlphaFoldDB

22 variants for Q6NS82

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388478488 91 L>M No EVA
rs3388479413 98 P>L No EVA
rs3388478404 130 E>A No EVA
rs3388479122 130 E>D No EVA
rs585370589 185 G>V No EVA
rs263519159 187 A>S No EVA
rs224418164 188 A>G No EVA
rs251647838 191 V>M No EVA
rs237292059 202 V>I No EVA
rs3388478204 218 V>E No EVA
rs3388479409 228 Y>F No EVA
rs3388479316 330 D>E No EVA
rs3388478224 331 V>F No EVA
rs3388480629 360 L>Q No EVA
rs248233565 384 G>A No EVA
rs224152268 390 A>T No EVA
rs242058132 421 A>G No EVA
rs3388478824 444 P>S No EVA
rs3388478815 457 L>H No EVA
rs255960461 458 S>F No EVA
rs3388479463 482 L>H No EVA
rs3388479127 501 E>* No EVA

No associated diseases with Q6NS82

No regional properties for Q6NS82

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q6NS82

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

2 GO annotations of cellular component

Name Definition
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).
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
endoplasmic reticulum-autophagosome adaptor activity The binding activity of a molecule that brings together an ER membrane and an autophagosome during reticulophagy.

3 GO annotations of biological process

Name Definition
collagen catabolic process The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
endoplasmic reticulum organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
reticulophagy The selective autohagy process in which parts of the endoplasmic reticulum are loaded into autophagosomes, delivered to the vacuole, and degraded in response to changing cellular conditions.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5E9K8 RETREG1 Reticulophagy regulator 1 Bos taurus (Bovine) PR
Q86VR2 RETREG3 Reticulophagy regulator 3 Homo sapiens (Human) PR
Q9H6L5 RETREG1 Reticulophagy regulator 1 Homo sapiens (Human) PR
Q9CQV4 Retreg3 Reticulophagy regulator 3 Mus musculus (Mouse) PR
Q0P4Z1 retreg3 Reticulophagy regulator 3 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MASSGGGNTG AGGTSGLGLG LGLSLGMGEA TGDAEEEAAA AEAVGRLATS LWLRLRGWEA
70 80 90 100 110 120
VLAAAQRLLV WEKPLHSLVT AATLNGLFWL LSSSSLRPFF LLSISLLTYF LLDLWHPRFL
130 140 150 160 170 180
PDVSAPPPEE PHSDSEGAGS GAQPHLLSVP ELCRYLAESW LTFQIHLQEL LQYKRQNPAQ
190 200 210 220 230 240
FCARGCAACA VLAVLGHYVP GVMISYIVLL SILLWPLVVY HELIQRMYTR LEPLLMQLDY
250 260 270 280 290 300
SMKAEADALH HKHDKRKRQG KSAPPAGDEP LAETESESEA ELAGFSPVVD VKKTALALAI
310 320 330 340 350 360
TDSELSDEEA SILESGGFSV SRATTPQLTD VSEDLDQQSL PSEPEEALNR ELGEGEETEL
370 380 390 400 410 420
ASPEDLLSAP PALSKQALDT EEEGAADKEA LLQLSSPLHF VNTHFNGAGS PQDGVKCPPG
430 440 450 460 470 480
APVKTLSPEA VSGDLMAPSS TLSPQLCLAE SGPVTPLSPS VLPSLPQDSP QPLAAPEEEE
490 500 510 520 530 540
ALTTEDFELL DQGELEQLNA ELGLGPEMPP KPPDVLPPPP LGADSHSLVQ SDQEAHAEVE
P