ID TMED4_MOUSE Reviewed; 227 AA.
AC Q8R1V4; Q3TY55;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Transmembrane emp24 domain-containing protein 4;
DE AltName: Full=Endoplasmic reticulum stress-response protein 25;
DE Short=ERS25;
DE AltName: Full=p24 family protein alpha-3;
DE Short=p24alpha3;
DE AltName: Full=p26;
DE Flags: Precursor;
GN Name=Tmed4; Synonyms=Ers25;
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 [MRNA].
RA Zhang W., Xie Z., Cao X.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Visual cortex, and Wolffian duct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18326488; DOI=10.1074/jbc.m709656200;
RA Hwang S.O., Boswell S.A., Seo J.-S., Lee S.W.;
RT "Novel oxidative stress-responsive gene ERS25 functions as a regulator of
RT the heat-shock and cell death response.";
RL J. Biol. Chem. 283:13063-13069(2008).
RN [6]
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).
CC -!- FUNCTION: Involved in vesicular protein trafficking, mainly in the
CC early secretory pathway. Involved in the maintenance of the Golgi
CC apparatus. Appears to play a role in the biosynthesis of secreted cargo
CC including processing. Involved in endoplasmic reticulum stress
CC response. May play a role in the regulation of heat-shock response and
CC apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:18326488}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18326488}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18326488}.
CC -!- INDUCTION: By brefeldin A, oxidative stress and heat shock, but not by
CC tunicamycin, hypersomotic stress or serum starvation.
CC {ECO:0000269|PubMed:18326488}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; AF368921; AAM20821.1; -; mRNA.
DR EMBL; AK078425; BAC37268.1; -; mRNA.
DR EMBL; AK158876; BAE34708.1; -; mRNA.
DR EMBL; AL607152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023041; AAH23041.1; -; mRNA.
DR CCDS; CCDS24415.1; -.
DR RefSeq; NP_598781.1; NM_134020.1.
DR AlphaFoldDB; Q8R1V4; -.
DR SMR; Q8R1V4; -.
DR BioGRID; 222141; 3.
DR STRING; 10090.ENSMUSP00000004508; -.
DR GlyConnect; 2783; 6 N-Linked glycans (1 site).
DR GlyCosmos; Q8R1V4; 1 site, 13 glycans.
DR GlyGen; Q8R1V4; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; Q8R1V4; -.
DR PhosphoSitePlus; Q8R1V4; -.
DR SwissPalm; Q8R1V4; -.
DR EPD; Q8R1V4; -.
DR jPOST; Q8R1V4; -.
DR MaxQB; Q8R1V4; -.
DR PaxDb; 10090-ENSMUSP00000004508; -.
DR PeptideAtlas; Q8R1V4; -.
DR ProteomicsDB; 259252; -.
DR Pumba; Q8R1V4; -.
DR Antibodypedia; 13441; 162 antibodies from 25 providers.
DR DNASU; 103694; -.
DR Ensembl; ENSMUST00000004508.13; ENSMUSP00000004508.7; ENSMUSG00000004394.13.
DR GeneID; 103694; -.
DR KEGG; mmu:103694; -.
DR UCSC; uc007hye.1; mouse.
DR AGR; MGI:1915070; -.
DR CTD; 222068; -.
DR MGI; MGI:1915070; Tmed4.
DR VEuPathDB; HostDB:ENSMUSG00000004394; -.
DR eggNOG; KOG1690; Eukaryota.
DR GeneTree; ENSGT00940000159012; -.
DR HOGENOM; CLU_066963_2_2_1; -.
DR InParanoid; Q8R1V4; -.
DR OMA; MRNTNEH; -.
DR OrthoDB; 886406at2759; -.
DR PhylomeDB; Q8R1V4; -.
DR TreeFam; TF314123; -.
DR BioGRID-ORCS; 103694; 3 hits in 77 CRISPR screens.
DR PRO; PR:Q8R1V4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R1V4; Protein.
DR Bgee; ENSMUSG00000004394; Expressed in epithelium of stomach and 270 other cell types or tissues.
DR ExpressionAtlas; Q8R1V4; baseline and differential.
DR Genevisible; Q8R1V4; MM.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR PANTHER; PTHR22811; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22811:SF159; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN 4; 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 Coiled coil; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..227
FT /note="Transmembrane emp24 domain-containing protein 4"
FT /id="PRO_0000010388"
FT TOPO_DOM 30..194
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..137
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 147..176
FT /evidence="ECO:0000255"
FT MOTIF 220..227
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 220..221
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 227 AA; 26022 MW; 38BF0C8475C954BD CRC64;
MAGVGVGPLQ GMVRFGLLVL TVCAACARGL YFHIGETEKR CFIEEIPDET MVIGNYRTQM
WDKQKEVFLP STPGLGMHVE VKDPDGKVVL SRQYGSEGRF TFTSHTPGDH QICLHSNSTR
MALFAGGKLR VHLDIQVGEH ANNYPEIAAK DKLTELQLRA RQLLDQVEQI QKEQDYQRYR
EERFRLTSES TNQRVLWWSI AQTVILILTG IWQMRHLKSF FEAKKLV
//
