Search TCDB: (?)
TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


3.A.16.1.1
Mammalian ER retrotranslocon. The Grp170 protein plays a role during ERAD, positioning this client-release factor at the retrotranslocation site, allowing a mechanism to couple client release from BiP and retrotranslocation (Inoue and Tsai, 2016). The cryo-EM structure of the ERAD protein channel, formed by tetrameric human Derlin-1, has been solved (Rao et al. 2021).  The structure shows that Derlin-1 forms a homotetramer that encircles a large tunnel traversing the ER membrane. The tunnel has a diameter of about 12 to 15 angstroms, large enough to allow an α-helix to pass through. The structure shows a lateral gate within the membrane, providing access of transmembrane proteins to the tunnel. Thus, Derlin-1 forms a protein channel for translocation of misfolded proteins. This structure is different from the monomeric yeast Derlin structure previously reported, which forms a semichannel with another protein (Rao et al. 2021).

Accession Number:Q8TAT6
Protein Name:Npl4
Length:608
Molecular Weight:68120.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate

Cross database links:

RefSeq: NP_060391.2   
Entrez Gene ID: 55666   
Pfam: PF05021    PF05020   
OMIM: 606590  gene
KEGG: hsa:55666   

Gene Ontology

GO:0005829 C:cytosol
GO:0005783 C:endoplasmic reticulum
GO:0042175 C:nuclear membrane-endoplasmic reticulum network
GO:0005634 C:nucleus
GO:0005515 F:protein binding
GO:0008270 F:zinc ion binding
GO:0006944 P:cellular membrane fusion
GO:0030433 P:ER-associated protein catabolic process
GO:0007030 P:Golgi organization

References (7)

[1] “Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.”  Nagase T.et.al.   10819331
[2] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.”  Gevaert K.et.al.   12665801
[5] “The full-ORF clone resource of the German cDNA consortium.”  Bechtel S.et.al.   17974005
[6] “Cloning and characterization of the gene encoding human NPL4, a protein interacting with the ubiquitin fusion-degradation protein (UFD1L).”  Botta A.et.al.   11574150
[7] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence 
1:	MAESIIIRVQ SPDGVKRITA TKRETAATFL KKVAKEFGFQ NNGFSVYINR NKTGEITASS 
61:	NKSLNLLKIK HGDLLFLFPS SLAGPSSEME TSVPPGFKVF GAPNVVEDEI DQYLSKQDGK 
121:	IYRSRDPQLC RHGPLGKCVH CVPLEPFDED YLNHLEPPVK HMSFHAYIRK LTGGADKGKF 
181:	VALENISCKI KSGCEGHLPW PNGICTKCQP SAITLNRQKY RHVDNIMFEN HTVADRFLDF 
241:	WRKTGNQHFG YLYGRYTEHK DIPLGIRAEV AAIYEPPQIG TQNSLELLED PKAEVVDEIA 
301:	AKLGLRKVGW IFTDLVSEDT RKGTVRYSRN KDTYFLSSEE CITAGDFQNK HPNMCRLSPD 
361:	GHFGSKFVTA VATGGPDNQV HFEGYQVSNQ CMALVRDECL LPCKDAPELG YAKESSSEQY 
421:	VPDVFYKDVD KFGNEITQLA RPLPVEYLII DITTTFPKDP VYTFSISQNP FPIENRDVLG 
481:	ETQDFHSLAT YLSQNTSSVF LDTISDFHLL LFLVTNEVMP LQDSISLLLE AVRTRNEELA 
541:	QTWKRSEQWA TIEQLCSTVG GQLPGLHEYG AVGGSTHTAT AAMWACQHCT FMNQPGTGHC 
601:	EMCSLPRT