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Transmembrane emp24 domain-containing protein 2 (Membrane protein p24A) (p24) (p24 family protein beta-1) (p24beta1)

 TMED2_HUMAN             Reviewed;         201 AA.
Q15363;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 151.
RecName: Full=Transmembrane emp24 domain-containing protein 2;
AltName: Full=Membrane protein p24A;
AltName: Full=p24;
AltName: Full=p24 family protein beta-1;
Short=p24beta1;
Flags: Precursor;
Name=TMED2; Synonyms=RNP24;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8663407; DOI=10.1074/jbc.271.29.17183;
Blum R., Feick P., Puype M., Vandekerckhove J., Klengel R.,
Nastainczyk W., Schulz I.;
"Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal
membranes, are members of a protein family involved in vesicular
trafficking.";
J. Biol. Chem. 271:17183-17189(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH COPI AND COPII VESICLE
COAT.
PubMed=9472029; DOI=10.1083/jcb.140.4.751;
Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A.,
Paccaud J.P., Thomas D.Y., Bergeron J.J., Nilsson T.;
"gp25L/emp24/p24 protein family members of the cis-Golgi network bind
both COP I and II coatomer.";
J. Cell Biol. 140:751-765(1998).
[4]
SUBUNIT.
PubMed=10359607; DOI=10.1091/mbc.10.6.1939;
Fullekrug J., Suganuma T., Tang B.L., Hong W., Storrie B., Nilsson T.;
"Localization and recycling of gp27 (hp24gamma3): complex formation
with other p24 family members.";
Mol. Biol. Cell 10:1939-1955(1999).
[5]
FUNCTION, AND MUTAGENESIS OF 194-PHE-PHE-195 AND 198-ARG-ARG-199.
PubMed=10761932; DOI=10.1016/S0092-8674(00)80703-5;
Goldberg J.;
"Decoding of sorting signals by coatomer through a GTPase switch in
the COPI coat complex.";
Cell 100:671-679(2000).
[6]
SUBCELLULAR LOCATION.
PubMed=10852829;
Emery G., Rojo M., Gruenberg J.;
"Coupled transport of p24 family members.";
J. Cell Sci. 113:2507-2516(2000).
[7]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=12237308; DOI=10.1074/jbc.M206989200;
Jenne N., Frey K., Brugger B., Wieland F.T.;
"Oligomeric state and stoichiometry of p24 proteins in the early
secretory pathway.";
J. Biol. Chem. 277:46504-46511(2002).
[8]
INTERACTION WITH COPG1.
PubMed=16940185; DOI=10.1128/MCB.01055-06;
Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.;
"Coatomer, the coat protein of COPI transport vesicles, discriminates
endoplasmic reticulum residents from p24 proteins.";
Mol. Cell. Biol. 26:8011-8021(2006).
[9]
FUNCTION, AND INTERACTION WITH F2RL1.
PubMed=17693410; DOI=10.1074/jbc.M703205200;
Luo W., Wang Y., Reiser G.;
"p24A, a type I transmembrane protein, controls ARF1-dependent
resensitization of protease-activated receptor-2 by influence on
receptor trafficking.";
J. Biol. Chem. 282:30246-30255(2007).
[10]
INTERACTION WITH ATLA1.
PubMed=17321752; DOI=10.1016/j.mcn.2007.01.012;
Namekawa M., Muriel M.-P., Janer A., Latouche M., Dauphin A.,
Debeir T., Martin E., Duyckaerts C., Prigent A., Depienne C.,
Sittler A., Brice A., Ruberg M.;
"Mutations in the SPG3A gene encoding the GTPase atlastin interfere
with vesicle trafficking in the ER/Golgi interface and Golgi
morphogenesis.";
Mol. Cell. Neurosci. 35:1-13(2007).
[11]
IDENTIFICATION IN A COMPLEX WITH SURF4 AND TMED10.
PubMed=18287528; DOI=10.1091/mbc.E07-10-0989;
Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.;
"The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate
compartment (ERGIC)-53, and p25 are required to maintain the
architecture of ERGIC and Golgi.";
Mol. Biol. Cell 19:1976-1990(2008).
[12]
FUNCTION, INTERACTION WITH CASR, AND MUTAGENESIS OF 194-PHE-PHE-195.
PubMed=20361938; DOI=10.1016/j.bbrc.2010.03.156;
Stepanchick A., Breitwieser G.E.;
"The cargo receptor p24A facilitates calcium sensing receptor
maturation and stabilization in the early secretory pathway.";
Biochem. Biophys. Res. Commun. 395:136-140(2010).
[13]
FUNCTION, AND INTERACTION WITH CD59; SEC24A; SEC24B; SEC24C AND
SEC24D.
PubMed=20427317; DOI=10.1242/jcs.062950;
Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
"Selective export of human GPI-anchored proteins from the endoplasmic
reticulum.";
J. Cell Sci. 123:1705-1715(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION, AND INTERACTION WITH F2R; P2RY4; P2RY11 AND OPRM1.
PubMed=21219331; DOI=10.1111/j.1471-4159.2011.07173.x;
Luo W., Wang Y., Reiser G.;
"Proteinase-activated receptors, nucleotide P2Y receptors, and mu-
opioid receptor-1B are under the control of the type I transmembrane
proteins p23 and p24A in post-Golgi trafficking.";
J. Neurochem. 117:71-81(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 19-114, AND INTERACTION WITH
TMED10.
PubMed=27569046; DOI=10.1016/j.jmb.2016.08.023;
Nagae M., Hirata T., Morita-Matsumoto K., Theiler R., Fujita M.,
Kinoshita T., Yamaguchi Y.;
"3D structure and interaction of p24beta and p24delta golgi dynamics
domains: implication for p24 complex formation and cargo transport.";
J. Mol. Biol. 428:4087-4099(2016).
-!- FUNCTION: Involved in vesicular protein trafficking. Mainly
functions in the early secretory pathway but also in post-Golgi
membranes. 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 TMED10 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 inhibits the GTPase-
activating activity of ARFGAP1 towards ARF1 thus preventing
immature uncoating and allowing cargo selection to take place.
Involved in trafficking of G protein-coupled receptors (GPCRs).
Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the
Golgi to the plasma membrane thus contributing to receptor
resensitization. Facilitates CASR maturation and stabilization in
the early secretory pathway and increases CASR plasma membrane
targeting. Proposed to be involved in organization of
intracellular membranes such as the maintenance of the Golgi
apparatus. May also play a role in the biosynthesis of secreted
cargo such as eventual processing. {ECO:0000269|PubMed:10761932,
ECO:0000269|PubMed:17693410, ECO:0000269|PubMed:20361938,
ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:21219331}.
-!- SUBUNIT: Monomer and homodimer in the endoplasmic reticulum,
endoplasmic reticulum-Golgi intermediate compartment and Golgi.
Probably oligomerizes with other members of the EMP24/GP25L family
such as TMED7, TMED9 and TMED10. Interacts (via GOLD domain) with
TMED10 (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 TMED2. Interacts with
SEC23A; indicative for an association of TMED2 with the COPII
vesicle coat. Interacts with ARF1 and ARFGAP1 (By similarity).
Interacts with CD59, SEC24A, SEC24B, SEC24C, SEC24D and ATLA1.
Interacts with KDELR1; the interaction is decreased by KDEL ligand
(By similarity). Interacts with F2RL1; the interaction occurs at
the Golgi apparatus. Interacts with CASR (immaturely glycosylated
form); the interaction occurs in the endoplasmic reticulum-Golgi
intermediate compartment or cis-Golgi. Interacts with F2RL1; the
interaction occurs at the Golgi apparatus. Interacts with GORASP1
and GORASP2 (By similarity). Found in a complex composed at least
of SURF4, TMED2 and TMED10. {ECO:0000250|UniProtKB:Q63524,
ECO:0000269|PubMed:10359607, ECO:0000269|PubMed:12237308,
ECO:0000269|PubMed:16940185, ECO:0000269|PubMed:17321752,
ECO:0000269|PubMed:17693410, ECO:0000269|PubMed:18287528,
ECO:0000269|PubMed:20361938, ECO:0000269|PubMed:20427317,
ECO:0000269|PubMed:21219331, ECO:0000269|PubMed:27569046}.
-!- INTERACTION:
P41180:CASR; NbExp=3; IntAct=EBI-998485, EBI-4400127;
P13987:CD59; NbExp=4; IntAct=EBI-998485, EBI-297972;
P55085:F2RL1; NbExp=6; IntAct=EBI-998485, EBI-4303189;
O35587:TMED10 (xeno); NbExp=2; IntAct=EBI-998485, EBI-4405327;
P49755:TMED10; NbExp=7; IntAct=EBI-998485, EBI-998422;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic
vesicle, COPI-coated vesicle membrane
{ECO:0000269|PubMed:9472029}; Single-pass type I membrane protein
{ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
{ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308};
Single-pass type I membrane protein {ECO:0000255}. Golgi
apparatus, Golgi stack membrane {ECO:0000269|PubMed:10852829,
ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein
{ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308};
Single-pass type I membrane protein {ECO:0000255}. Endoplasmic
reticulum-Golgi intermediate compartment membrane
{ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein
{ECO:0000255}. Note=Cycles between compartments of the early
secretatory pathway. {ECO:0000269|PubMed:12237308}.
-!- MISCELLANEOUS: Ectopic expression of TMED2 alone does not result
in its proper cis-Golgi network localization. Coexpression of
TMED10 is necessary, and coexpression of TMED3 and/or TMED9 is
facilitating localization. Down-regulation of TMED10 expression
reduces TMED2 protein level.
-!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X92098; CAA63069.1; -; mRNA.
EMBL; BC025957; AAH25957.1; -; mRNA.
CCDS; CCDS9250.1; -.
RefSeq; NP_001308374.1; NM_001321445.1.
RefSeq; NP_006806.1; NM_006815.3.
UniGene; Hs.733403; -.
PDB; 5AZW; X-ray; 1.50 A; A/B=19-114.
PDBsum; 5AZW; -.
ProteinModelPortal; Q15363; -.
SMR; Q15363; -.
BioGrid; 116158; 51.
ELM; Q15363; -.
IntAct; Q15363; 36.
MINT; MINT-5000229; -.
STRING; 9606.ENSP00000262225; -.
TCDB; 9.B.188.1.2; the transmembrane emp24 domain-containing protein (tmed) family.
iPTMnet; Q15363; -.
PhosphoSitePlus; Q15363; -.
BioMuta; TMED2; -.
DMDM; 3914237; -.
EPD; Q15363; -.
PaxDb; Q15363; -.
PeptideAtlas; Q15363; -.
PRIDE; Q15363; -.
TopDownProteomics; Q15363; -.
DNASU; 10959; -.
Ensembl; ENST00000262225; ENSP00000262225; ENSG00000086598.
GeneID; 10959; -.
KEGG; hsa:10959; -.
CTD; 10959; -.
DisGeNET; 10959; -.
EuPathDB; HostDB:ENSG00000086598.10; -.
GeneCards; TMED2; -.
HGNC; HGNC:16996; TMED2.
HPA; HPA014060; -.
neXtProt; NX_Q15363; -.
OpenTargets; ENSG00000086598; -.
PharmGKB; PA142670796; -.
eggNOG; KOG1692; Eukaryota.
eggNOG; ENOG410XQCK; LUCA.
GeneTree; ENSGT00670000097656; -.
HOGENOM; HOG000160229; -.
HOVERGEN; HBG105106; -.
InParanoid; Q15363; -.
KO; K20347; -.
OMA; YTYCFGN; -.
OrthoDB; EOG091G0L5D; -.
PhylomeDB; Q15363; -.
TreeFam; TF313000; -.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
ChiTaRS; TMED2; human.
GeneWiki; TMED2; -.
GenomeRNAi; 10959; -.
PRO; PR:Q15363; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000086598; -.
CleanEx; HS_TMED2; -.
ExpressionAtlas; Q15363; baseline and differential.
Genevisible; Q15363; HS.
GO; GO:0030137; C:COPI-coated vesicle; ISS:UniProtKB.
GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; ISS:HGNC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0042589; C:zymogen granule membrane; ISS:HGNC.
GO; GO:0035459; P:cargo loading into vesicle; TAS:UniProtKB.
GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:UniProtKB.
GO; GO:0048208; P:COPII vesicle coating; TAS:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
GO; GO:0032525; P:somite rostral/caudal axis specification; IEA:Ensembl.
InterPro; IPR009038; GOLD_dom.
InterPro; IPR036598; GOLD_dom_sf.
InterPro; IPR015720; TMP21-related.
PANTHER; PTHR22811; PTHR22811; 1.
Pfam; PF01105; EMP24_GP25L; 1.
SMART; SM01190; EMP24_GP25L; 1.
SUPFAM; SSF101576; SSF101576; 1.
PROSITE; PS50866; GOLD; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Cytoplasmic vesicle;
Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
Protein transport; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 201 Transmembrane emp24 domain-containing
protein 2.
/FTId=PRO_0000010381.
TOPO_DOM 21 168 Lumenal. {ECO:0000255}.
TRANSMEM 169 189 Helical. {ECO:0000255}.
TOPO_DOM 190 201 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 112 GOLD. {ECO:0000255|PROSITE-
ProRule:PRU00096}.
REGION 1 181 Interaction with F2RL1.
{ECO:0000269|PubMed:17693410}.
REGION 118 157 Required for TMED10 and TMED2 cis-Golgi
network localization.
COILED 117 167 {ECO:0000255}.
MOTIF 194 201 COPI vesicle coat-binding. {ECO:0000255}.
MOTIF 194 195 COPII vesicle coat-binding.
{ECO:0000255}.
MUTAGEN 194 195 FF->AA: Disrupts association with
coatomer; when associated with S-198-199-
S. {ECO:0000269|PubMed:10761932,
ECO:0000269|PubMed:20361938}.
MUTAGEN 194 195 FF->AA: Reduced surface and total
expression of CASR.
{ECO:0000269|PubMed:10761932,
ECO:0000269|PubMed:20361938}.
MUTAGEN 198 199 RR->SS: Disrupts association with
coatomer; when associated with A-194-195-
A. {ECO:0000269|PubMed:10761932}.
MUTAGEN 198 199 RR->SS: No inhibition of coatomer-
dependent GTP hydrolysis.
{ECO:0000269|PubMed:10761932}.
STRAND 22 25 {ECO:0000244|PDB:5AZW}.
STRAND 29 37 {ECO:0000244|PDB:5AZW}.
STRAND 42 49 {ECO:0000244|PDB:5AZW}.
STRAND 51 53 {ECO:0000244|PDB:5AZW}.
STRAND 57 62 {ECO:0000244|PDB:5AZW}.
STRAND 68 83 {ECO:0000244|PDB:5AZW}.
STRAND 85 96 {ECO:0000244|PDB:5AZW}.
STRAND 104 112 {ECO:0000244|PDB:5AZW}.
SEQUENCE 201 AA; 22761 MW; C452370E459DC894 CRC64;
MVTLAELLVL LAALLATVSG YFVSIDAHAE ECFFERVTSG TKMGLIFEVA EGGFLDIDVE
ITGPDNKGIY KGDRESSGKY TFAAHMDGTY KFCFSNRMST MTPKIVMFTI DIGEAPKGQD
METEAHQNKL EEMINELAVA MTAVKHEQEY MEVRERIHRA INDNTNSRVV LWSFFEALVL
VAMTLGQIYY LKRFFEVRRV V


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