Transmembrane protein 119

UniProt data

UniProt name: TM119_HUMAN (Q4V9L6)

Gene name: TMEM119; ORFNames=PSEC0199, UNQ731/PRO1415

Organism: Homo sapiens (Human).

Function: Plays an important role in bone formation and normal bone mineralization. Promotes the differentiation of myoblasts into osteoblasts (PubMed:20025746). May induce the commitment and differentiation of myoblasts into osteoblasts through an enhancement of BMP2 production and interaction with the BMP-RUNX2 pathway. Upregulates the expression of ATF4, a transcription factor which plays a central role in osteoblast differentiation. Essential for normal spermatogenesis and late testicular differentiation (By similarity). {ECO:0000250|UniProtKB:Q8R138, ECO:0000269|PubMed:20025746}.

Subcellular location: Cell membrane {ECO:0000269|PubMed:20025746, ECO:0000269|PubMed:26250788}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8R138}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8R138}.

Transmembrane domains:

  1. 97-117, 21 AA, Helical. {ECO:0000255}.

Sequence: 283 AA

10 20 30 40 50 60 MVSAAAPSLL ILLLLLLGSV PATDARSVPL KATFLEDVAG SGEAEGSSAS SPSLPPPWTP 70 80 90 100 110 120 ALSPTSMGPQ PITLGGPSPP TNFLDGIVDF FRQYVMLIAV VGSLAFLLMF IVCAAVITRQ 130 140 150 160 170 180 KQKASAYYPS SFPKKKYVDQ SDRAGGPRAF SEVPDRAPDS RPEEALDSSR QLQADILAAT 190 200 210 220 230 240 QNLKSPTRAA LGGGDGARMV EGRGAEEEEK GSQEGDQEVQ GHGVPVETPE AQEEPCSGVL 250 260 270 280 EGAVVAGEGQ GELEGSLLLA QEAQGPVGPP ESPCACSSVH PSV

CATM prediction

The sequence of TM119_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
        100       110       1
 +    |    +    |    +    |		 (Å) (°) (Å) (°)  
Model 1 YVMLIAVVGSLAFLLMFIVCAAVITRQ 7.3 -53.1° 3.2 33.6 -3.8

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, 99, ALA, HA A, 98, ILE, O 3.29Å
B, 102, GLY, HA1 A, 99, ALA, O 3.13Å
A, 99, ALA, HA B, 98, ILE, O 3.29Å
A, 102, GLY, HA1 B, 99, ALA, O 3.13Å