TMED9_MOUSE
ID TMED9_MOUSE Reviewed; 235 AA.
AC Q99KF1; Q9CX02;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transmembrane emp24 domain-containing protein 9;
DE AltName: Full=Glycoprotein 25L2;
DE AltName: Full=p24 family protein alpha-2;
DE Short=p24alpha2;
DE Flags: Precursor;
GN Name=Tmed9; Synonyms=Gp25l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-235.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-160, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Appears to be involved in vesicular protein trafficking,
CC mainly in the early secretory pathway. In COPI vesicle-mediated
CC retrograde transport involved in the coatomer recruitment to membranes
CC of the early secretory pathway. Increases coatomer-dependent activity
CC of ARFGAP2. Thought to play a crucial role in the specific retention of
CC p24 complexes in cis-Golgi membranes; specifically contributes to the
CC coupled localization of TMED2 and TMED10 in the cis-Golgi network. May
CC be involved in organization of intracellular membranes, such as of the
CC ER-Golgi intermediate compartment and the Golgi apparatus. Involved in
CC ER localization of PTPN2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer in endoplasmic reticulum. Predominantly
CC monomeric and to lesser extent homodimeric in endoplasmic reticulum-
CC Golgi intermediate compartment and cis-Golgi network. Probably
CC oligomerizes with other members of the EMP24/GP25L family such as
CC TMED2, TMED7 and TMED10. Interacts with TMED5. Interacts (via C-
CC terminus) with COPG1; the interaction involves dimeric TMED9. Interacts
CC with PTPN2 and SPAST. Interacts with STX17; the interaction is direct
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus,
CC cis-Golgi network membrane {ECO:0000250}; Single-pass type I membrane
CC protein {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Cycles between compartments of the early secretatory pathway.
CC {ECO:0000250}.
CC -!- PTM: N-linked glycosylated containing high mannose. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK010259; BAB26802.2; -; mRNA.
DR EMBL; BC004691; AAH04691.1; ALT_INIT; mRNA.
DR CCDS; CCDS49277.1; -.
DR RefSeq; NP_080487.2; NM_026211.3.
DR AlphaFoldDB; Q99KF1; -.
DR SMR; Q99KF1; -.
DR BioGRID; 212239; 6.
DR IntAct; Q99KF1; 2.
DR STRING; 10090.ENSMUSP00000105531; -.
DR GlyConnect; 2784; 11 N-Linked glycans (1 site).
DR GlyGen; Q99KF1; 1 site, 11 N-linked glycans (1 site).
DR iPTMnet; Q99KF1; -.
DR PhosphoSitePlus; Q99KF1; -.
DR EPD; Q99KF1; -.
DR jPOST; Q99KF1; -.
DR MaxQB; Q99KF1; -.
DR PaxDb; Q99KF1; -.
DR PeptideAtlas; Q99KF1; -.
DR PRIDE; Q99KF1; -.
DR ProteomicsDB; 262837; -.
DR TopDownProteomics; Q99KF1; -.
DR Antibodypedia; 29339; 165 antibodies from 24 providers.
DR DNASU; 67511; -.
DR Ensembl; ENSMUST00000109905; ENSMUSP00000105531; ENSMUSG00000058569.
DR GeneID; 67511; -.
DR KEGG; mmu:67511; -.
DR UCSC; uc007qrr.1; mouse.
DR CTD; 54732; -.
DR MGI; MGI:1914761; Tmed9.
DR VEuPathDB; HostDB:ENSMUSG00000058569; -.
DR eggNOG; KOG1690; Eukaryota.
DR GeneTree; ENSGT00940000159747; -.
DR HOGENOM; CLU_066963_2_2_1; -.
DR InParanoid; Q99KF1; -.
DR OMA; MSHRVRM; -.
DR OrthoDB; 1294924at2759; -.
DR PhylomeDB; Q99KF1; -.
DR TreeFam; TF314123; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 67511; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Tmed9; mouse.
DR PRO; PR:Q99KF1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q99KF1; protein.
DR Bgee; ENSMUSG00000058569; Expressed in ascending aorta and 245 other tissues.
DR ExpressionAtlas; Q99KF1; baseline and differential.
DR Genevisible; Q99KF1; MM.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0010638; P:positive regulation of organelle organization; ISS:UniProtKB.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..37
FT /evidence="ECO:0000250"
FT CHAIN 38..235
FT /note="Transmembrane emp24 domain-containing protein 9"
FT /id="PRO_0000010397"
FT TOPO_DOM 38..202
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..145
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 121..160
FT /note="Required for interaction with STX17"
FT /evidence="ECO:0000250"
FT COILED 154..184
FT /evidence="ECO:0000255"
FT MOTIF 228..235
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 228..229
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 160
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 208
FT /note="I -> V (in Ref. 2; AAH04691)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="V -> L (in Ref. 2; AAH04691)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="W -> C (in Ref. 2; AAH04691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 27127 MW; 7B035FB91F1EDEEB CRC64;
MAAVRGVRVV GSSPGLLLGR GMRAFLLLLW LAARGSALYF HIGETEKKCF IEEIPDETMV
IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR QYGSEGRFTF TSHTPGEHQI
CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK
EQNYQRWREE RFRQTSESTN QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV
