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Protein

Transmembrane emp24 domain-containing protein 10

Gene

Tmed10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • COPI-coated vesicle budding Source: UniProtKB
  • Golgi organization Source: UniProtKB
  • intracellular protein transport Source: HGNC
  • kidney development Source: Ensembl
  • protein oligomerization Source: Ensembl
  • regulated exocytosis Source: HGNC
  • regulation of beta-amyloid formation Source: MGI
  • response to alkaloid Source: Ensembl
  • retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
  • vesicle targeting, to, from or within Golgi Source: HGNC
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.
R-MMU-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane emp24 domain-containing protein 10
Alternative name(s):
21 kDa transmembrane-trafficking protein
Transmembrane protein Tmp21
p24 family protein delta-1
Short name:
p24delta1
Gene namesi
Name:Tmed10
Synonyms:Tmp21
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1915831. Tmed10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 185154LumenalSequence analysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence analysisAdd
BLAST
Topological domaini207 – 21913CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Early embryonic lethal. Decreases the protein but not the mRNA level of Tmed3 and Tmed9. Heterozygous Tmed10 +/- mice are viable but show structural deficits in the Golgi morphology, such as the formation of dilated saccules.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131By similarityAdd
BLAST
Chaini32 – 219188Transmembrane emp24 domain-containing protein 10PRO_0000010401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711Dimethylated arginine; alternateBy similarity
Modified residuei171 – 1711Omega-N-methylated arginine; alternateBy similarity
Modified residuei176 – 1761Dimethylated arginine; alternateBy similarity
Modified residuei176 – 1761Omega-N-methylated arginine; alternateBy similarity
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Methylation

Proteomic databases

EPDiQ9D1D4.
MaxQBiQ9D1D4.
PaxDbiQ9D1D4.
PRIDEiQ9D1D4.

PTM databases

iPTMnetiQ9D1D4.
PhosphoSiteiQ9D1D4.
SwissPalmiQ9D1D4.

Expressioni

Gene expression databases

BgeeiQ9D1D4.
GenevisibleiQ9D1D4. MM.

Interactioni

Subunit structurei

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. Interacts with STX17; the interaction is direct (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212936. 74 interactions.
IntActiQ9D1D4. 77 interactions.
MINTiMINT-1863252.
STRINGi10090.ENSMUSP00000037583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 193153GOLDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 142142Required for interaction with STX17By similarityAdd
BLAST
Regioni147 – 17832Required for TMED10 and TMED2 cis-Golgi network localizationBy similarityAdd
BLAST
Regioni204 – 21916Interaction with COPG1By similarityAdd
BLAST
Regioni207 – 21913Interaction with ARF1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi211 – 2199COPI vesicle coat-bindingSequence analysis
Motifi211 – 2122COPII vesicle coat-bindingSequence analysis

Domaini

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

Sequence similaritiesi

Belongs to the EMP24/GP25L family.Curated
Contains 1 GOLD domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1691. Eukaryota.
ENOG410XTBQ. LUCA.
GeneTreeiENSGT00550000074954.
HOGENOMiHOG000160227.
HOVERGENiHBG107275.
InParanoidiQ9D1D4.
OMAiHTLYSKE.
OrthoDBiEOG7PZRZM.
PhylomeDBiQ9D1D4.
TreeFamiTF313729.

Family and domain databases

InterProiIPR009038. GOLD_dom.
IPR015720. TMP21-related.
[Graphical view]
PANTHERiPTHR22811. PTHR22811. 1 hit.
PfamiPF01105. EMP24_GP25L. 1 hit.
[Graphical view]
SMARTiSM01190. EMP24_GP25L. 1 hit.
[Graphical view]
PROSITEiPS50866. GOLD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D1D4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGLFGPLSR PGPLPSAWLF LLLLGPSSVL GISFHLPVNS RKCLREEIHK
60 70 80 90 100
DLLVTGAYEI TDQSGGAGGL RTHLKITDSA GHILYAKEDA TKGKFAFTTE
110 120 130 140 150
DYDMFEVCFE SKGTGRIPDQ LVILDMKHGV EAKNYEEIAK VEKLKPLEVE
160 170 180 190 200
LRRLEDLSES IVNDFAYMKK REEEMRDTNE STNTRVLYFS IFSMFCLIGL
210
ATWQVFYLRR FFKAKKLIE
Length:219
Mass (Da):24,911
Last modified:June 1, 2001 - v1
Checksum:i206D8CD9FBCC45BB
GO
Isoform 2 (identifier: Q9D1D4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.

Note: No experimental confirmation available.
Show »
Length:94
Mass (Da):11,334
Checksum:i557FA4D72F8D6895
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961C → Y in AAH64755 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 125125Missing in isoform 2. 1 PublicationVSP_013582Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003676 mRNA. Translation: BAB22932.1.
AK084117 mRNA. Translation: BAC39119.1.
AK150605 mRNA. Translation: BAE29697.1.
AK152643 mRNA. Translation: BAE31382.1.
AK152656 mRNA. Translation: BAE31393.1.
BC006774 mRNA. Translation: AAH06774.1.
BC064755 mRNA. Translation: AAH64755.1.
BC085097 mRNA. Translation: AAH85097.1.
CCDSiCCDS36498.1. [Q9D1D4-1]
RefSeqiNP_081051.1. NM_026775.4. [Q9D1D4-1]
UniGeneiMm.379159.
Mm.472063.
Mm.483371.

Genome annotation databases

EnsembliENSMUST00000040766; ENSMUSP00000037583; ENSMUSG00000021248. [Q9D1D4-1]
GeneIDi68581.
KEGGimmu:68581.
UCSCiuc007ogy.1. mouse. [Q9D1D4-2]
uc007ogz.1. mouse. [Q9D1D4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003676 mRNA. Translation: BAB22932.1.
AK084117 mRNA. Translation: BAC39119.1.
AK150605 mRNA. Translation: BAE29697.1.
AK152643 mRNA. Translation: BAE31382.1.
AK152656 mRNA. Translation: BAE31393.1.
BC006774 mRNA. Translation: AAH06774.1.
BC064755 mRNA. Translation: AAH64755.1.
BC085097 mRNA. Translation: AAH85097.1.
CCDSiCCDS36498.1. [Q9D1D4-1]
RefSeqiNP_081051.1. NM_026775.4. [Q9D1D4-1]
UniGeneiMm.379159.
Mm.472063.
Mm.483371.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212936. 74 interactions.
IntActiQ9D1D4. 77 interactions.
MINTiMINT-1863252.
STRINGi10090.ENSMUSP00000037583.

PTM databases

iPTMnetiQ9D1D4.
PhosphoSiteiQ9D1D4.
SwissPalmiQ9D1D4.

Proteomic databases

EPDiQ9D1D4.
MaxQBiQ9D1D4.
PaxDbiQ9D1D4.
PRIDEiQ9D1D4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040766; ENSMUSP00000037583; ENSMUSG00000021248. [Q9D1D4-1]
GeneIDi68581.
KEGGimmu:68581.
UCSCiuc007ogy.1. mouse. [Q9D1D4-2]
uc007ogz.1. mouse. [Q9D1D4-1]

Organism-specific databases

CTDi10972.
MGIiMGI:1915831. Tmed10.

Phylogenomic databases

eggNOGiKOG1691. Eukaryota.
ENOG410XTBQ. LUCA.
GeneTreeiENSGT00550000074954.
HOGENOMiHOG000160227.
HOVERGENiHBG107275.
InParanoidiQ9D1D4.
OMAiHTLYSKE.
OrthoDBiEOG7PZRZM.
PhylomeDBiQ9D1D4.
TreeFamiTF313729.

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.
R-MMU-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

ChiTaRSiTmed10. mouse.
NextBioi327496.
PROiQ9D1D4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1D4.
GenevisibleiQ9D1D4. MM.

Family and domain databases

InterProiIPR009038. GOLD_dom.
IPR015720. TMP21-related.
[Graphical view]
PANTHERiPTHR22811. PTHR22811. 1 hit.
PfamiPF01105. EMP24_GP25L. 1 hit.
[Graphical view]
SMARTiSM01190. EMP24_GP25L. 1 hit.
[Graphical view]
PROSITEiPS50866. GOLD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and Czech II.
    Tissue: Bone marrow, Embryo and Embryonic spinal cord.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NMRI.
    Tissue: Blastocyst and Mammary tumor.
  3. "The p24 family member p23 is required for early embryonic development."
    Denzel A., Otto F., Girod A., Pepperkok R., Watson R., Rosewell I., Bergeron J.J., Solari R.C., Owen M.J.
    Curr. Biol. 10:55-58(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  4. "A subset of p23 localized on secretory granules in pancreatic beta-cells."
    Hosaka M., Watanabe T., Yamauchi Y., Sakai Y., Suda M., Mizutani S., Takeuchi T., Isobe T., Izumi T.
    J. Histochem. Cytochem. 55:235-245(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTMEDA_MOUSE
AccessioniPrimary (citable) accession number: Q9D1D4
Secondary accession number(s): Q3U7I7, Q6P227, Q922U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.