Erlin-2

UniProt data

UniProt name: ERLN2_HUMAN (O94905)

Gene name: ERLIN2; Synonyms=C8orf2, SPFH2; ORFNames=UNQ2441/PRO5003/PRO9924

Organism: Homo sapiens (Human).

Function: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1 (PubMed:19240031, PubMed:17502376). Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex (PubMed:21343306). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (PubMed:24217618). {ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031, ECO:0000269|PubMed:21343306, ECO:0000269|PubMed:24217618}.

Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane.

Transmembrane domains:

  1. 4-24, 21 AA, Helical. {ECO:0000255}.

Sequence: 339 AA

10 20 30 40 50 60 MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK 70 80 90 100 110 120 SVQTTLQTDE VKNVPCGTSG GVMIYFDRIE VVNFLVPNAV YDIVKNYTAD YDKALIFNKI 130 140 150 160 170 180 HHELNQFCSV HTLQEVYIEL FDQIDENLKL ALQQDLTSMA PGLVIQAVRV TKPNIPEAIR 190 200 210 220 230 240 RNYELMESEK TKLLIAAQKQ KVVEKEAETE RKKALIEAEK VAQVAEITYG QKVMEKETEK 250 260 270 280 290 300 KISEIEDAAF LAREKAKADA ECYTAMKIAE ANKLKLTPEY LQLMKYKAIA SNSKIYFGKD 310 320 330 IPNMFMDSAG SVSKQFEGLA DKLSFGLEDE PLETATKEN

CATM prediction

The sequence of ERLN2_HUMAN returned 2 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
           10        20      
    +    |    +    |    +  
(Å) (°) (Å) (°)  
MAQLGAVVAVASSFFCASLFSAVHKIE 7.1 -37.0° 2.2 36.0 -15.8
MAQLGAVVAVASSFFCASLFSAVHKIE 6.5 -51.0° 2.4 45.0 -9.3

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 6, ALA, HA A, 5, GLY, O 3.30Å
A, 6, ALA, HA B, 5, GLY, O 3.30Å