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 Q6FNV5

Entry ID Method Resolution Chain Position Source
AF-Q6FNV5-F1 Predicted AlphaFoldDB

No variants for Q6FNV5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FNV5

No associated diseases with Q6FNV5

7 regional properties for Q6FNV5

Type Name Position InterPro Accession
repeat Sel1-like repeat 107 - 143 IPR006597-1
repeat Sel1-like repeat 147 - 184 IPR006597-2
repeat Sel1-like repeat 185 - 220 IPR006597-3
repeat Sel1-like repeat 372 - 396 IPR006597-4
repeat Sel1-like repeat 577 - 591 IPR006597-5
repeat Sel1-like repeat 592 - 623 IPR006597-6
repeat Sel1-like repeat 624 - 659 IPR006597-7

Functions

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

4 GO annotations of cellular component

Name Definition
Hrd1p ubiquitin ligase ERAD-L complex A multiprotein complex that recognizes and ubiquitinates proteins with misfolded luminal domains during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p.
Hrd1p ubiquitin ligase ERAD-M complex A multiprotein complex that recognizes and ubiquitinates proteins with misfolded membrane domains during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p.
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.
luminal surveillance complex A multiprotein complex that recognizes ERAD-luminal misfolded substrates and brings them to the ubiquitination/extraction machinery. In yeast, this complex consists of Yos9p, Kar2p and Hrd3p proteins.

1 GO annotations of molecular function

Name Definition
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

3 GO annotations of biological process

Name Definition
negative regulation of protein autoubiquitination Any process that stops, prevents or reduces the frequency, rate or extent of protein autoubiquitination.
retrograde protein transport, ER to cytosol The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLLSTYLNWA SVLLTIAGAE SNIDPWDEVS SFLQGKLRKL DVTNPNAYDM NDNEQDATFY
70 80 90 100 110 120
VSMDYHEEEE RSEYESVWQY YNENSDQDWH KSVYDKLQVS ADQFNNTEAM YKLSQINLWG
130 140 150 160 170 180
QYGYPHNKSV AFQYLQKFND MTSYENSSAL FDLAVAYSTG LFGTLPVDVA RGLLYFQRSA
190 200 210 220 230 240
RLGDLKAKQV LAYRYFSGYS VARDVDKALL LYKEIAEEIK KKYSEEQWNM VFPYIESYIV
250 260 270 280 290 300
RIPDFDEGLL GKGLSTVPQS VRRKKTTRPP FAGSSNLKPI GDVGYGEVVM QFKFNAGNGN
310 320 330 340 350 360
PGSFVISDSE HEDRLVELFY TAWDLYKGTY TRGRDCDKAK RLLLQVYKTY DAEVKYMDNL
370 380 390 400 410 420
QKFFYVKSLD LLAHMYFTGE GFERPNVQAA LDLFDRSEKI LEGAEISRTA SEVDKGLISQ
430 440 450 460 470 480
YYFNNTLGAL KHYKKAKESG NAHGILFYQL GKLSEKNPEL KIGDPYLYMQ EASSQQYLPA
490 500 510 520 530 540
QYEFAKMVES NELRKYSVED ITRLYKAFVE ENENIMAPHL RLGFSELLGG SSEVSLYAYA
550 560 570 580 590 600
QAAEQGYEAA QISAAYLLYQ LPYKFDDPPE TTIERKTMAI SYYTRAFKQG NTDAAVVAGD
610 620 630 640 650 660
IYFQMKNYTK ALSLYQSAAL KFSAQALWNI GYMYEHGLGV EKDFHLAKRF YDQILEHNQK
670 680 690 700 710 720
LYFAVKASVM KLQLKSWFMW LNGKELDNIS IDQEQESTVV RPFFDRLVQL LKNLSRETRG
730 740 750 760 770 780
DNKKKNQHRI LKEKKTPSQG IMERFGLQTE DLLTMVCVLI IFAISMFFRT VAPRGQWNVR
790 800 810 820 830
INGVNIAGGN ALGEEGNPEN ENEEDDENDD EGRARARNNF GFGNNFDVQV FAI