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Transmembrane emp24 domain-containing protein 10 (21 kDa transmembrane-trafficking protein) (Integral membrane protein p23) (Transmembrane protein Tmp21) (p24 family protein delta-1) (p24delta1)

 TMEDA_RABIT             Reviewed;         219 AA.
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 120.
RecName: Full=Transmembrane emp24 domain-containing protein 10;
AltName: Full=21 kDa transmembrane-trafficking protein;
AltName: Full=Integral membrane protein p23;
AltName: Full=Transmembrane protein Tmp21;
AltName: Full=p24 family protein delta-1;
Flags: Precursor;
Name=TMED10; Synonyms=TMP21;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
STRAIN=New Zealand white; TISSUE=Liver;
PubMed=8947548; DOI=10.1083/jcb.135.5.1239;
Sohn K., Orci L., Ravazzola M., Amherdt M., Bremser M., Lottspeich F.,
Fiedler K., Helms J.B., Wieland F.T.;
"A major transmembrane protein of Golgi-derived COPI-coated vesicles
involved in coatomer binding.";
J. Cell Biol. 135:1239-1248(1996).
PubMed=9990005; DOI=10.1073/pnas.96.4.1224;
Reinhard C., Harter C., Bremser M., Brugger B., Sohn K., Helms J.B.,
Wieland F.T.;
"Receptor-induced polymerization of coatomer.";
Proc. Natl. Acad. Sci. U.S.A. 96:1224-1228(1999).
PubMed=9813083; DOI=10.1083/jcb.143.3.601;
Majoul I., Sohn K., Wieland F.T., Pepperkok R., Pizza M.,
Hillemann J., Soling H.D.;
"KDEL receptor (Erd2p)-mediated retrograde transport of the cholera
toxin A subunit from the Golgi involves COPI, p23, and the COOH
terminus of Erd2p.";
J. Cell Biol. 143:601-612(1998).
PubMed=18182008; DOI=10.1111/j.1600-0854.2007.00697.x;
Langer J.D., Roth C.M., Bethune J., Stoops E.H., Brugger B.,
Herten D.P., Wieland F.T.;
"A conformational change in the alpha-subunit of coatomer induced by
ligand binding to gamma-COP revealed by single-pair FRET.";
Traffic 9:597-607(2008).
PubMed=10799309; DOI=10.1006/bbrc.2000.2511;
Weidler M., Reinhard C., Friedrich G., Wieland F.T., Rosch P.;
"Structure of the cytoplasmic domain of p23 in solution: implications
for the formation of COPI vesicles.";
Biochem. Biophys. Res. Commun. 271:401-408(2000).
-!- 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). {ECO:0000250,
-!- 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 (via GOLD domain) with
TMED2 (via GOLD domain). 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).
{ECO:0000250|UniProtKB:O35587, ECO:0000250|UniProtKB:P49755,
-!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Melanosome {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Endoplasmic reticulum-Golgi intermediate compartment membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}. Cell membrane
{ECO:0000250}. Golgi apparatus, trans-Golgi network membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Note=Cycles between compartments of the early secretatory pathway.
-!- DOMAIN: The lumenal domain mediates localization to the plasma
membrane by partially overriding the ER retention by the
cytoplasmic domain. {ECO:0000250}.
-!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; X98303; CAA66947.1; -; mRNA.
RefSeq; NP_001075877.1; NM_001082408.1.
RefSeq; XP_008270117.1; XM_008271895.2.
UniGene; Ocu.1770; -.
PDB; 1M23; NMR; -; A=207-219.
PDB; 1P23; NMR; -; A/B/C/D=207-219.
PDBsum; 1M23; -.
PDBsum; 1P23; -.
SMR; Q28735; -.
BioGrid; 1172317; 1.
ELM; Q28735; -.
IntAct; Q28735; 1.
STRING; 9986.ENSOCUP00000004033; -.
PRIDE; Q28735; -.
GeneID; 100009296; -.
KEGG; ocu:100009296; -.
CTD; 10972; -.
eggNOG; KOG1691; Eukaryota.
HOGENOM; HOG000160227; -.
HOVERGEN; HBG107275; -.
InParanoid; Q28735; -.
KO; K20352; -.
EvolutionaryTrace; Q28735; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0030137; C:COPI-coated vesicle; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0070765; C:gamma-secretase complex; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0035964; P:COPI-coated vesicle budding; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:1902003; P:regulation of amyloid-beta formation; ISS:UniProtKB.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:UniProtKB.
InterPro; IPR009038; GOLD_dom.
InterPro; IPR015720; TMP21-related.
PANTHER; PTHR22811; PTHR22811; 1.
Pfam; PF01105; EMP24_GP25L; 1.
SMART; SM01190; EMP24_GP25L; 1.
PROSITE; PS50866; GOLD; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasmic vesicle;
Endoplasmic reticulum; ER-Golgi transport; Glycoprotein;
Golgi apparatus; Membrane; Methylation; Protein transport;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
SIGNAL 1 31 {ECO:0000250}.
CHAIN 32 219 Transmembrane emp24 domain-containing
protein 10.
TOPO_DOM 32 185 Lumenal. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
TOPO_DOM 207 219 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 193 GOLD. {ECO:0000255|PROSITE-
REGION 1 142 Required for interaction with STX17.
REGION 147 178 Required for TMED10 and TMED2 cis-Golgi
network localization. {ECO:0000250}.
REGION 204 219 Interaction with COPG1. {ECO:0000250}.
REGION 207 219 Interaction with ARF1. {ECO:0000250}.
MOTIF 211 219 COPI vesicle coat-binding. {ECO:0000255}.
MOTIF 211 212 COPII vesicle coat-binding.
MOD_RES 171 171 Dimethylated arginine; alternate.
MOD_RES 171 171 Omega-N-methylated arginine; alternate.
MOD_RES 176 176 Dimethylated arginine; alternate.
MOD_RES 176 176 Omega-N-methylated arginine; alternate.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
MUTAGEN 211 212 FF->AA: Impairs association with
coatomer; when associated with 215-S-S-
216. {ECO:0000269|PubMed:9990005}.
MUTAGEN 215 216 KK->SS: Impairs association with
coatomer; when associated with 211-A-A-
212. {ECO:0000269|PubMed:9990005}.
HELIX 208 218 {ECO:0000244|PDB:1M23}.
SEQUENCE 219 AA; 24914 MW; 5AFA700D0A4DAB4C CRC64;

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