|TMEDA_HUMAN » Transmembrane emp24 domain-containing protein 10 » 21 kDa transmembrane-trafficking protein;S31III125;S31I125; Tmp-21-I;Transmembrane protein Tmp21;p23;p24 family protein delta-1;p24delta1; p24delta;|
|Hydrophobic Thickness||34.0 ± 1.6 Å|
|Tilt Angle||1 ± 1°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC|
|TM Segments||186-208 (180-215)|
|UniProt annotation for TMEDA_HUMAN » Transmembrane emp24 domain-containing protein 10|
|FUNCTION: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1 (By similarity). In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus. SUBUNIT: Predominantly homodimeric and to lesser extent monomeric in endoplasmic reticulum. Homodimer and monomer 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 TMED9. Interacts with TMED2. Associates with the COPI vesicle coat (coatomer); TMED10:TMED2 heterotetramers are proposed to be involved in coatomer association. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED10. Interacts with ARF1 (GDP- bound); the interaction probably involves a TMED10 oligomer. Interacts with SEC23A; indicative for an association of TMED10 with the COPII vesicle coat. Interacts with CD59, SEC24B, SEC24C and SEC24D (By similarity). Interacts with MPPE1/PGAP5. Interacts with F2LR1. Interacts with KDELR2; the interaction is disrupted by KDELR2 ligand (By similarity). Found in a complex composed at least of SURF4, TMED2 and TMED10. Associates with the presenilin- dependent gamma-secretase complex. Interacts with STX17; the interaction is direct. TISSUE SPECIFICITY: Ubiquitous. DOMAIN: The lumenal domain mediates localization to the plasma membrane by partially overriding the ER retention by the cytoplasmic domain. MISCELLANEOUS: Ectopic expression of TMED10 alone does not result in its proper cis-Golgi network localization. Coexpression of TMED2 is necessary, and coexpression of TMED3 and /or TMED9 is facilitating localization.|
|UniProt features for TMEDA_HUMAN » Transmembrane emp24 domain-containing protein 10|
SIGNAL 1 31 |
CHAIN 32 219 Transmembrane emp24 domain-containing protein 10.
DOMAIN 41 193 GOLD.
REGION 147 178 Required for TMED10 and TMED2 cis-Golgi network localization.
REGION 204 219 Interaction with COPG1.
REGION 207 219 Interaction with ARF1.
MOTIF 211 219 COPI vesicle coat-binding.
MOTIF 211 212 COPII vesicle coat-binding.
|Amino Acid Sequence for TMEDA_HUMAN » Transmembrane emp24 domain-containing protein 10|
|MSGLSGPPAR RGPFPLALLL LFLLGPRLVL AISFHLPINS RKCLREEIHK DLLVTGAYEI SDQSGGAGGL RSHLKITDSA GHILYSKEDA TKGKFAFTTE DYDMFEVCFE SKGTGRIPDQ LVILDMKHGV EAKNYEEIAK VEKLKPLEVE LRRLEDLSES IVNDFAYMKK REEEMRDTNE STNTRVLYFS IFSMFCLIGL ATWQVFYLRR FFKAKKLIE|