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O35587 (TMEDA_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transmembrane protein Tmp21
Alternative name(s):
21 kDa transmembrane-trafficking protein
Integral membrane protein p23
p24 family protein delta-1
Short name=p24delta1
Gene names
Name:TMED10
Synonyms:TMP21
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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.

Subunit structure

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

Subcellular location

Golgi apparatuscis-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 vesiclesecretory vesicle membrane; Single-pass type I membrane protein By similarity. Cell membrane By similarity. Golgi apparatustrans-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

Domain

The lumenal domain mediates localization to the plasma membrane by partially overriding the ER retention by the cytoplasmic domain By similarity.

Sequence similarities

Belongs to the EMP24/GP25L family.

Contains 1 GOLD domain.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentCell membrane
Cytoplasmic vesicle
Endoplasmic reticulum
Golgi apparatus
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Methylation
Gene Ontology (GO)
   Biological_processCOPI-coated vesicle budding

Inferred from sequence or structural similarity. Source: UniProtKB

beta-amyloid formation

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

retrograde vesicle-mediated transport, Golgi to ER

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCOPI-coated vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from sequence or structural similarity. Source: GOC

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

gamma-secretase complex

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network transport vesicle

Inferred from direct assay Ref.2. Source: UniProtKB

transport vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CD59P139875EBI-4405327,EBI-297972From a different organism.
TMED2Q153632EBI-4405327,EBI-998485From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 By similarity
Chain32 – 219188Transmembrane protein Tmp21
PRO_0000010400

Regions

Topological domain32 – 185154Lumenal Potential
Transmembrane186 – 20621Helical; Potential
Topological domain207 – 21913Cytoplasmic Potential
Domain41 – 193153GOLD
Region1 – 142142Required for interaction with STX17 By similarity
Region147 – 17832Required for TMED10 and TMED2 cis-Golgi network localization By similarity
Region204 – 21916Interaction with COPG1 By similarity
Region207 – 21913Interaction with ARF1 By similarity
Motif211 – 2199COPI vesicle coat-binding Potential
Motif211 – 2122COPII vesicle coat-binding Potential

Amino acid modifications

Modified residue1711Omega-N-methylated arginine By similarity
Modified residue1761Omega-N-methylated arginine By similarity
Glycosylation1791N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O35587 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1FCF2E49ABB565EB

FASTA21924,821
        10         20         30         40         50         60 
MSGSSGPLSW PGPRPCALLF LLLLGPSSVL AISFHLPVNS RKCLREEIHK DLLVTGAYEI 

        70         80         90        100        110        120 
TDQSGGAGGL RTHLKITDSA GHILYAKEDA TKGKFAFTTE DYDMFEVCFE SKGTGRIPDQ 

       130        140        150        160        170        180 
LVILDMKHGV EAKNYEEIAK VEKLKPLEVE LRRLEDLSES IVNDFAYMKK REEEMRDTNE 

       190        200        210 
STNTRVLYFS IFSMLCLIGL ATWQVFYLRR FFKAKKLIE 

« Hide

References

[1]"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].
[2]"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.
[3]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001513 mRNA. Translation: CAA04796.1.
RefSeqNP_001268617.1. NM_001281688.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35587. 6 interactions.
MINTMINT-4996182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101832157.

Phylogenomic databases

HOVERGENHBG107275.

Family and domain databases

InterProIPR009038. GOLD.
[Graphical view]
PfamPF01105. EMP24_GP25L. 1 hit.
[Graphical view]
PROSITEPS50866. GOLD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTMEDA_MESAU
AccessionPrimary (citable) accession number: O35587
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families