Emerin

UniProt data

UniProt name: EMD_HUMAN (P50402)

Gene name: EMD; Synonyms=EDMD, STA

Organism: Homo sapiens (Human).

Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta- catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C. {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649}.

Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:19167377}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non- farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus.

Transmembrane domains:

  1. 223-243, 21 AA, Helical. {ECO:0000255}.

Sequence: 254 AA

10 20 30 40 50 60 MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP PSSSAASSYS 70 80 90 100 110 120 FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF TTRTYGEPES AGPSRAVRQS 130 140 150 160 170 180 VTSFPDADAF HHQVHDDDLL SSSEEECKDR ERPMYGRDSA YQSITHYRPV SASRSSLDLS 190 200 210 220 230 240 YYPTSSSTSF MSSSSSSSSW LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF 250 FIYHFMQAEE GNPF

CATM prediction

The sequence of EMD_HUMAN returned 1 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
  220       230       240    
|    +    |    +    |    + 		 (Å) (°) (Å) (°)  
Model 1 DRQVALWGQLLLFLVFVIVLFFIYHFM 7.3 -53.0° 3.2 33.8 -14.1
Prolines* DRQVPLWGQLLLFLVFVIVLFFIYHFM          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

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, 224, ALA, HA A, 223, VAL, O 3.47Å
B, 227, GLY, HA1 A, 224, ALA, O 3.37Å
B, 228, GLN, HE21 A, 227, GLY, O 2.29Å
A, 224, ALA, HA B, 223, VAL, O 3.47Å
A, 227, GLY, HA1 B, 224, ALA, O 3.37Å
A, 228, GLN, HE21 B, 227, GLY, O 2.29Å