E3 ubiquitin-protein ligase ZNRF4 {ECO:0000305}

UniProt data

UniProt name: ZNRF4_HUMAN (Q8WWF5)

Gene name: ZNRF4 {ECO:0000312|HGNC:HGNC:17726}

Organism: Homo sapiens (Human).

Function: E3 ubiquitin-protein ligase which specifically induces ubiquitination and proteasomal degradation of CANX within the endoplasmic reticulum (PubMed:21205830). Could have a role in spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q9DAH2, ECO:0000269|PubMed:21205830}.

Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21205830}; Single-pass type I membrane protein {ECO:0000305}.

Transmembrane domains:

  1. 251-271, 21 AA, Helical. {ECO:0000255}.

Sequence: 429 AA

10 20 30 40 50 60 MPLCRPEHLM PRASRVPVAA SLPLSHAVIP TQLPSRPGHR PPGRPRRCPK ASCLPPPVGP 70 80 90 100 110 120 SSTQTAKRVT MGWPRPGRAL VAVKALLVLS LLQVPAQAVV RAVLEDNSSS VDFADLPALF 130 140 150 160 170 180 GVPLAPEGIR GYLMEVKPAN ACHPIEAPRL GNRSLGAIVL IRRYDCTFDL KVLNAQRAGF 190 200 210 220 230 240 EAAIVHNVHS DDLVSMTHVY EDLRGQIAIP SVFVSEAASQ DLRVILGCNK SAHALLLPDD 250 260 270 280 290 300 PPCHDLGCHP VLTVSWVLGC TLALVVSAFF VLNHLWLWAQ ACCSHRRPVK TSTCQKAQVR 310 320 330 340 350 360 TFTWHNDLCA ICLDEYEEGD QLKILPCSHT YHCKCIDPWF SQAPRRSCPV CKQSVAATED 370 380 390 400 410 420 SFDSTTYSFR DEDPSLPGHR PPIWAIQVQL RSRRLELLGR ASPHCHCSTT SLEAEYTTVS SAPPEAPGQ

CATM prediction

The sequence of ZNRF4_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
    250       260       270  
  |    +    |    +    |    
(Å) (°) (Å) (°)  
CHAVLTVSWVLGCTLALVVSAFFVLNH 7.1 -51.8° 0.6 48.1 -17.7
CHPVLTVSWVLGCTLALVVSAFFVLNH          

* 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:


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Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 259, GLY, HA1 A, 256, TRP, O 3.21Å
B, 260, CYS, HA A, 259, GLY, O 3.21Å
A, 259, GLY, HA1 B, 256, TRP, O 3.21Å
A, 260, CYS, HA B, 259, GLY, O 3.21Å