|TMED9_HUMAN » Transmembrane emp24 domain-containing protein 9 » GMP25;Glycoprotein 25L2;p24 family protein alpha-2;p24alpha2; p25;|
|Hydrophobic Thickness||32.0 ± 1.4 Å|
|Tilt Angle||2 ± 0°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC|
|TM Segments||203-225 (197-232)|
|UniProt annotation for TMED9_HUMAN » Transmembrane emp24 domain-containing protein 9|
|FUNCTION: Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer- dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB. SUBUNIT: Monomer and homodimer in endoplasmic reticulum. Predominantly monomeric and to lesser extent homodimeric in endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. Probably oligomerizes with other members of the EMP24/GP25L family such as TMED2, TMED7 and TMED10. Interacts with TMED5. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED9. Interacts with PTPN2 and SPAST. Interacts with STX17; the interaction is direct.|
|UniProt features for TMED9_HUMAN » Transmembrane emp24 domain-containing protein 9|
SIGNAL 1 37 By similarity. |
CHAIN 38 235 Transmembrane emp24 domain-containing protein 9.
DOMAIN 47 145 GOLD.
COILED 154 184 Potential.
MOTIF 228 235 COPI vesicle coat-binding (Potential).
MOTIF 228 229 COPII vesicle coat-binding (Potential).
|Amino Acid Sequence for TMED9_HUMAN » Transmembrane emp24 domain-containing protein 9|
|MAVELGVLLV RPRPGTGLGR VMRTLLLVLW LATRGSALYF HIGETEKKCF IEEIPDETMV IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR QYGSEGRFTF TSHTPGEHQI CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK EQNYQRWREE RFRQTSESTN QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV|