O35587 (TMEDA_MESAU) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 77. History...
Names and origin
|Protein names||Recommended name:|
Transmembrane protein Tmp21
21 kDa transmembrane-trafficking protein
Integral membrane protein p23
p24 family protein delta-1
|Organism||Mesocricetus auratus (Golden hamster)|
|Taxonomic identifier||10036 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus|
|Sequence length||219 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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. 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 By similarity.
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. Interacts with MPPE1/PGAP5. Interacts with F2LR1. Interacts with KDELR2; the interaction is disrupted by KDELR2 ligand. Found in a complex composed at least of SURF4, TMED2 and TMED10. Associates with the presenilin-dependent gamma-secretase complex By similarity. Interacts with STX17; the interaction is direct By similarity. Ref.3
Golgi apparatus › cis-Golgi network membrane; Single-pass type I membrane protein By similarity. Melanosome By similarity. Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity. Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein By similarity. Cytoplasmic vesicle › secretory vesicle membrane; Single-pass type I membrane protein By similarity. Cell membrane By similarity. Golgi apparatus › trans-Golgi network membrane; Single-pass type I membrane protein. Note: Cycles between compartments of the early secretatory pathway By similarity. Is one of the most abundant proteins in the cis-Golgi network. Detected in trans-Golgi network-derived transport vesicles. Ref.2
The lumenal domain mediates localization to the plasma membrane by partially overriding the ER retention by the cytoplasmic domain By similarity.
Belongs to the EMP24/GP25L family.
Contains 1 GOLD domain.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Signal peptide||1 – 31||31||By similarity|
|Chain||32 – 219||188||Transmembrane protein Tmp21||PRO_0000010400|
|Topological domain||32 – 185||154||Lumenal Potential|
|Transmembrane||186 – 206||21||Helical; Potential|
|Topological domain||207 – 219||13||Cytoplasmic Potential|
|Domain||41 – 193||153||GOLD|
|Region||1 – 142||142||Required for interaction with STX17 By similarity|
|Region||147 – 178||32||Required for TMED10 and TMED2 cis-Golgi network localization By similarity|
|Region||204 – 219||16||Interaction with COPG1 By similarity|
|Region||207 – 219||13||Interaction with ARF1 By similarity|
|Motif||211 – 219||9||COPI vesicle coat-binding Potential|
|Motif||211 – 212||2||COPII vesicle coat-binding Potential|
Amino acid modifications
|Modified residue||171||1||Omega-N-methylated arginine By similarity|
|Modified residue||176||1||Omega-N-methylated arginine By similarity|
|Glycosylation||179||1||N-linked (GlcNAc...) Potential|
|||"Involvement of the transmembrane protein p23 in biosynthetic protein transport."|
Rojo M., Pepperkok R., Emery G., Kellner R., Stang E., Parton R.G., Gruenberg J.
J. Cell Biol. 139:1119-1135(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
|||"Identification of components of trans-Golgi network-derived transport vesicles and detergent-insoluble complexes by nanoelectrospray tandem mass spectrometry."|
Shevchenko A., Keller P., Scheiffele P., Mann M., Simons K.
Electrophoresis 18:2591-2600(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
|||"Selective export of human GPI-anchored proteins from the endoplasmic reticulum."|
Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.
J. Cell Sci. 123:1705-1715(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD59; SEC24B; SEC24C AND SEC24D.
|AJ001513 mRNA. Translation: CAA04796.1.|
|RefSeq||NP_001268617.1. NM_001281688.1. |
3D structure databases
Protein-protein interaction databases
|IntAct||O35587. 6 interactions.|
Protocols and materials databases
Genome annotation databases
Family and domain databases
|InterPro||IPR009038. GOLD. |
|Pfam||PF01105. EMP24_GP25L. 1 hit. |
|PROSITE||PS50866. GOLD. 1 hit. |
|Accession||Primary (citable) accession number: O35587|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families