Transmembrane protein Tmp21 precursor - Mesocricetus auratus (Golden hamster)

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O35587 (TMEDA_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

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

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 togther 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. Ref.3
Subcellular location	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
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 process	ER-Golgi transport Protein transport Transport
Cellular component	Cell membrane Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane
Domain	Signal Transmembrane Transmembrane helix
PTM	Glycoprotein Methylation
Gene Ontology (GO)
Biological_process	COPI-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_component	COPI-coated vesicle Inferred from sequence or structural similarity. Source: UniProtKB 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell 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
CD59	P13987	5	EBI-4405327,EBI-297972	From a different organism.
TMED2	Q15363	2	EBI-4405327,EBI-998485	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

By similarity

Chain

32 – 219

188

Transmembrane protein Tmp21

PRO_0000010400

Regions

Topological domain

32 – 185

154

Lumenal Potential

Transmembrane

186 – 206

Helical; Potential

Topological domain

207 – 219

Cytoplasmic Potential

Domain

41 – 193

153

GOLD

Region

147 – 178

Required for TMED10 and TMED2 cis-Golgi network localization By similarity

Region

204 – 219

Interaction with COPG1 By similarity

Region

207 – 219

Interaction with ARF1 By similarity

Motif

211 – 219

COPI vesicle coat-binding Potential

Motif

211 – 212

COPII vesicle coat-binding Potential

Amino acid modifications

Modified residue

171

Omega-N-methylated arginine By similarity

Modified residue

176

Omega-N-methylated arginine By similarity

Glycosylation

179

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

O35587 [UniParc].

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

219

24,821

        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

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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.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O35587. 6 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG107275.
Family and domain databases
InterPro	IPR009038. GOLD. [Graphical view]
Pfam	PF01105. EMP24_GP25L. 1 hit. [Graphical view]
PROSITE	PS50866. GOLD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TMEDA_MESAU

Accession

Primary (citable) accession number: O35587

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents