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

 TMEDA_RAT               Reviewed;         219 AA.
Q63584; Q9R0W6;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
30-AUG-2017, entry version 121.
RecName: Full=Transmembrane emp24 domain-containing protein 10;
AltName: Full=21 kDa transmembrane-trafficking protein;
AltName: Full=Transmembrane protein Tmp21;
AltName: Full=p24 family protein delta-1;
Short=p24delta1;
Flags: Precursor;
Name=Tmed10; Synonyms=Tmp21;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=10376215; DOI=10.3109/10425179909008429;
Hoerer J., Blum R., Feick P., Nastainczyk W., Schulz I.;
"A comparative study of rat and human Tmp21 (p23) reveals the
pseudogene-like features of human Tmp21-II.";
DNA Seq. 10:121-126(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-219.
STRAIN=Wistar; TISSUE=Pancreas;
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).
[3]
PROTEIN SEQUENCE OF 32-47, SUBUNIT, AND SUBCELLULAR LOCATION.
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]
SUBCELLULAR LOCATION, AND INTERACTION WITH TMED2.
PubMed=10214941; DOI=10.1016/S0014-5793(99)00246-X;
Gommel D., Orci L., Emig E.M., Hannah M.J., Ravazzola M., Nickel W.,
Helms J.B., Wieland F.T., Sohn K.;
"p24 and p23, the major transmembrane proteins of COPI-coated
transport vesicles, form hetero-oligomeric complexes and cycle between
the organelles of the early secretory pathway.";
FEBS Lett. 447:179-185(1999).
[5]
INTERACTION WITH KDELR2; TMED2 AND ARF1.
PubMed=11703931; DOI=10.1016/S1534-5807(01)00004-1;
Majoul I., Straub M., Hell S.W., Duden R., Soling H.D.;
"KDEL-cargo regulates interactions between proteins involved in COPI
vesicle traffic: measurements in living cells using FRET.";
Dev. Cell 1:139-153(2001).
[6]
METHYLATION AT ARG-171 AND ARG-176, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15047867; DOI=10.1091/mbc.E04-02-0101;
Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
Yates J.R. III, Howell K.E.;
"Organellar proteomics reveals Golgi arginine dimethylation.";
Mol. Biol. Cell 15:2907-2919(2004).
[7]
SUBCELLULAR LOCATION.
PubMed=15718469; DOI=10.1126/science.1108061;
Malsam J., Satoh A., Pelletier L., Warren G.;
"Golgin tethers define subpopulations of COPI vesicles.";
Science 307:1095-1098(2005).
[8]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 215-LYS-LYS-216.
PubMed=18627576; DOI=10.1111/j.1600-0854.2008.00784.x;
Blum R., Lepier A.;
"The luminal domain of p23 (Tmp21) plays a critical role in p23 cell
surface trafficking.";
Traffic 9:1530-1550(2008).
[9]
INTERACTION WITH STX17.
PubMed=21545355; DOI=10.1042/BC20110006;
Muppirala M., Gupta V., Swarup G.;
"Syntaxin 17 cycles between the ER and ERGIC and is required to
maintain the architecture of ERGIC and Golgi.";
Biol. Cell 103:333-350(2011).
[10]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 12-132, FUNCTION IN
TRANSPORT OF GPI-ANCHORED PROTEINS, AND INTERACTION WITH TMED2.
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. 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,
ECO:0000269|PubMed:27569046}.
-!- 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. {ECO:0000250|UniProtKB:O35587,
ECO:0000250|UniProtKB:P49755, ECO:0000269|PubMed:10214941,
ECO:0000269|PubMed:11703931, ECO:0000269|PubMed:21545355,
ECO:0000269|PubMed:27569046, ECO:0000269|PubMed:9472029}.
-!- INTERACTION:
Q9R064:Gorasp2; NbExp=2; IntAct=EBI-918648, EBI-4422912;
-!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
Single-pass type I membrane protein. Melanosome {ECO:0000250}.
Endoplasmic reticulum membrane; Single-pass type I membrane
protein. Endoplasmic reticulum-Golgi intermediate compartment
membrane; Single-pass type I membrane protein. Cytoplasmic
vesicle, secretory vesicle membrane; Single-pass type I membrane
protein. Cell membrane. 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.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The lumenal domain mediates localization to the plasma
membrane by partially overriding the ER retention by the
cytoplasmic domain.
-!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ004912; CAA06212.1; -; mRNA.
EMBL; X97443; CAA66072.1; -; mRNA.
RefSeq; NP_445919.1; NM_053467.1.
UniGene; Rn.226085; -.
UniGene; Rn.8509; -.
PDB; 5AZX; X-ray; 1.58 A; A/B/C/D=32-132.
PDB; 5AZY; X-ray; 1.80 A; A/B=32-132.
PDBsum; 5AZX; -.
PDBsum; 5AZY; -.
SMR; Q63584; -.
BioGrid; 250029; 1.
IntAct; Q63584; 7.
MINT; MINT-4579083; -.
STRING; 10116.ENSRNOP00000010512; -.
iPTMnet; Q63584; -.
PhosphoSitePlus; Q63584; -.
SwissPalm; Q63584; -.
PaxDb; Q63584; -.
PRIDE; Q63584; -.
Ensembl; ENSRNOT00000010512; ENSRNOP00000010512; ENSRNOG00000007901.
GeneID; 84599; -.
KEGG; rno:84599; -.
UCSC; RGD:620970; rat.
CTD; 10972; -.
RGD; 620970; Tmed10.
eggNOG; KOG1691; Eukaryota.
eggNOG; ENOG410XTBQ; LUCA.
GeneTree; ENSGT00550000074954; -.
HOVERGEN; HBG107275; -.
InParanoid; Q63584; -.
KO; K20352; -.
OMA; FSMCCLI; -.
OrthoDB; EOG091G0O9D; -.
PhylomeDB; Q63584; -.
Reactome; R-RNO-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-RNO-5694530; Cargo concentration in the ER.
Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
PRO; PR:Q63584; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000007901; -.
Genevisible; Q63584; RN.
GO; GO:0005801; C:cis-Golgi network; IDA:HGNC.
GO; GO:0030137; C:COPI-coated vesicle; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:RGD.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0070765; C:gamma-secretase complex; IDA:RGD.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IDA:HGNC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA: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:0042589; C:zymogen granule membrane; IDA:HGNC.
GO; GO:0032403; F:protein complex binding; IDA:RGD.
GO; GO:0019905; F:syntaxin binding; IEA:Ensembl.
GO; GO:0035964; P:COPI-coated vesicle budding; ISS:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:RGD.
GO; GO:0006886; P:intracellular protein transport; TAS:HGNC.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0051259; P:protein oligomerization; IDA:RGD.
GO; GO:0045055; P:regulated exocytosis; IEP:HGNC.
GO; GO:1902003; P:regulation of amyloid-beta formation; ISS:UniProtKB.
GO; GO:0043279; P:response to alkaloid; IEP:RGD.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISS:UniProtKB.
GO; GO:0006903; P:vesicle targeting; NAS:HGNC.
GO; GO:0048199; P:vesicle targeting, to, from or within Golgi; IEP:HGNC.
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;
Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
Glycoprotein; Golgi apparatus; Membrane; Methylation;
Protein transport; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 31 {ECO:0000250}.
CHAIN 32 219 Transmembrane emp24 domain-containing
protein 10.
/FTId=PRO_0000010404.
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-
ProRule:PRU00096}.
REGION 1 142 Required for interaction with STX17.
{ECO:0000250}.
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.
{ECO:0000255}.
MOD_RES 171 171 Dimethylated arginine.
{ECO:0000269|PubMed:15047867}.
MOD_RES 176 176 Dimethylated arginine.
{ECO:0000269|PubMed:15047867}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 215 216 KK->SS: Reduced localization to COPI-
coated vesicles and endoplasmic
reticulum-Golgi intermediate compartment.
{ECO:0000269|PubMed:18627576}.
STRAND 32 36 {ECO:0000244|PDB:5AZX}.
STRAND 41 47 {ECO:0000244|PDB:5AZX}.
STRAND 53 61 {ECO:0000244|PDB:5AZX}.
HELIX 67 69 {ECO:0000244|PDB:5AZX}.
STRAND 71 78 {ECO:0000244|PDB:5AZX}.
STRAND 83 89 {ECO:0000244|PDB:5AZX}.
STRAND 91 98 {ECO:0000244|PDB:5AZX}.
STRAND 104 112 {ECO:0000244|PDB:5AZX}.
STRAND 120 128 {ECO:0000244|PDB:5AZX}.
SEQUENCE 219 AA; 24858 MW; 51FC99ECB6D47ADE CRC64;
MSGLSGPLSW PGPLLSALLF LFLLGPSSVL GISFHLPVNS RKCLREEIHK DLLVTGAYEI
TDQSGGAGGL RTHLKITDSA GHILYAKEDA TKGKFAFTTE DYDMFEVCFE SKGTGRIPDQ
LVILDMKHGV EAKNYEEIAK VEKLKPLEVE LRRLEDLSES IVNDFAYMKK REEEMRDTNE
STNTRVLYFS IFSMFCLIGL ATWQVFYLRR FFKAKKLIE


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