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Protein

Transmembrane emp24 domain-containing protein 9

Gene

Tmed9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane emp24 domain-containing protein 9
Alternative name(s):
p24 family protein alpha-2
Short name:
p24alpha2
Gene namesi
Name:Tmed9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1307627. Tmed9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 202165LumenalSequence analysisAdd
BLAST
Transmembranei203 – 22220HelicalSequence analysisAdd
BLAST
Topological domaini223 – 23513CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 235198Transmembrane emp24 domain-containing protein 9PRO_0000413988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence analysis
Modified residuei160 – 1601N6-acetyllysineBy similarity

Post-translational modificationi

N-linked glycosylated containing high mannose.By similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PaxDbiQ5I0E7.
PRIDEiQ5I0E7.

Expressioni

Gene expression databases

GenevisibleiQ5I0E7. RN.

Interactioni

Subunit structurei

Monomer and homodimer in endoplasmic reticulum. Predominantly monomeric and to lesser extent homodimeric 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 TMED10. Interacts with TMED5. Interacts (via C-terminus) with COPG1; the interaction involves dimeric TMED9. Interacts with PTPN2 and SPAST (By similarity). Interacts with STX17; the interaction is direct.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Gorasp2Q9R0643EBI-920903,EBI-4422912

Protein-protein interaction databases

BioGridi262515. 5 interactions.
IntActiQ5I0E7. 4 interactions.
MINTiMINT-4655706.
STRINGi10116.ENSRNOP00000030668.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 14599GOLDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni121 – 16040Required for interaction with STX17By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili154 – 18431Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi228 – 2358COPI vesicle coat-bindingSequence analysis
Motifi228 – 2292COPII vesicle coat-bindingSequence analysis

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1690. Eukaryota.
ENOG410XPUW. LUCA.
GeneTreeiENSGT00430000030848.
HOGENOMiHOG000160228.
HOVERGENiHBG105357.
InParanoidiQ5I0E7.
OMAiCASALYF.
OrthoDBiEOG74BJT2.
PhylomeDBiQ5I0E7.
TreeFamiTF314123.

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]

Sequencei

Sequence statusi: Complete.

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

Q5I0E7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVRGVRVV GTSPGLLLGR GMRAFLLLLC LAARGGALYF HIGETEKKCF
60 70 80 90 100
IEEIPDETMV IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR
110 120 130 140 150
QYGSEGRFTF TSHTPGEHQI CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN
160 170 180 190 200
DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK EQNYQRWREE RFRQTSESTN
210 220 230
QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV
Length:235
Mass (Da):27,028
Last modified:February 15, 2005 - v1
Checksum:i32F0D1DCC9EFBA6E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381L → I AA sequence (PubMed:9472029).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474032 Genomic DNA. Translation: EDL93964.1.
BC088422 mRNA. Translation: AAH88422.1.
RefSeqiNP_001009703.1. NM_001009703.1.
UniGeneiRn.9386.

Genome annotation databases

EnsembliENSRNOT00000036140; ENSRNOP00000030668; ENSRNOG00000021882.
GeneIDi361207.
KEGGirno:361207.
UCSCiRGD:1307627. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474032 Genomic DNA. Translation: EDL93964.1.
BC088422 mRNA. Translation: AAH88422.1.
RefSeqiNP_001009703.1. NM_001009703.1.
UniGeneiRn.9386.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi262515. 5 interactions.
IntActiQ5I0E7. 4 interactions.
MINTiMINT-4655706.
STRINGi10116.ENSRNOP00000030668.

Proteomic databases

PaxDbiQ5I0E7.
PRIDEiQ5I0E7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000036140; ENSRNOP00000030668; ENSRNOG00000021882.
GeneIDi361207.
KEGGirno:361207.
UCSCiRGD:1307627. rat.

Organism-specific databases

CTDi54732.
RGDi1307627. Tmed9.

Phylogenomic databases

eggNOGiKOG1690. Eukaryota.
ENOG410XPUW. LUCA.
GeneTreeiENSGT00430000030848.
HOGENOMiHOG000160228.
HOVERGENiHBG105357.
InParanoidiQ5I0E7.
OMAiCASALYF.
OrthoDBiEOG74BJT2.
PhylomeDBiQ5I0E7.
TreeFamiTF314123.

Enzyme and pathway databases

ReactomeiR-RNO-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

NextBioi675552.
PROiQ5I0E7.

Gene expression databases

GenevisibleiQ5I0E7. RN.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "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].
    Strain: Brown Norway.
    Tissue: Lung.
  4. "gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer."
    Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A., Paccaud J.P., Thomas D.Y., Bergeron J.J., Nilsson T.
    J. Cell Biol. 140:751-765(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-64, SIGNAL SEQUENCE CLEAVAGE SITE, SUBUNIT, SUBCELLULAR LOCATION.
  5. "Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi."
    Muppirala M., Gupta V., Swarup G.
    Biol. Cell 103:333-350(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX17.

Entry informationi

Entry nameiTMED9_RAT
AccessioniPrimary (citable) accession number: Q5I0E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: February 15, 2005
Last modified: May 11, 2016
This is version 86 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.