TMED1_MOUSE
ID TMED1_MOUSE Reviewed; 227 AA.
AC Q3V009; Q3TUX8; Q61073; Q91YK3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transmembrane emp24 domain-containing protein 1;
DE AltName: Full=Interleukin-1 receptor-like 1 ligand;
DE AltName: Full=Putative T1/ST2 receptor-binding protein;
DE AltName: Full=p24 family protein gamma-1;
DE Short=p24gamma1;
DE Flags: Precursor;
GN Name=Tmed1; Synonyms=Il1rl1l;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Ovary, and Uterus;
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 [MRNA] OF 6-227 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Pre-B cell;
RX PubMed=8621446; DOI=10.1074/jbc.271.10.5784;
RA Gayle M.A., Slack J.L., Bonnert T.P., Renshaw B.R., Sonoda G., Taguchi T.,
RA Testa J.R., Dower S.K., Sims J.E.;
RT "Cloning of a putative ligand for the T1/ST2 receptor.";
RL J. Biol. Chem. 271:5784-5789(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, 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: Potential role in vesicular protein trafficking, mainly in
CC the early secretory pathway. May act as a cargo receptor at the lumenal
CC side for incorporation of secretory cargo molecules into transport
CC vesicles and may be involved in vesicle coat formation at the
CC cytoplasmic side. Plays a positive role in IL-33-mediated IL-8 and IL-6
CC production by interacting with interleukin-33 receptor IL1RL1. Plays
CC also a role in the modulation of innate immune signaling through the
CC cGAS-STING pathway by interacting with RNF26.
CC {ECO:0000250|UniProtKB:Q13445}.
CC -!- SUBUNIT: Homodimer in endoplasmic reticulum, endoplasmic reticulum-
CC Golgi intermediate compartment and cis-Golgi network. Interacts with
CC IL1RL1. Interacts with RNF26; this interaction is important to modulate
CC innate immune signaling through the cGAS-STING pathway.
CC {ECO:0000250|UniProtKB:Q13445}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13445};
CC Single-pass type I membrane protein {ECO:0000255}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q13445}; Single-pass type I
CC membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q13445}; Single-pass type I membrane
CC protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q13445}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3V009-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3V009-2; Sequence=VSP_020135, VSP_020136;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8621446}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; AK133513; BAE21696.1; -; mRNA.
DR EMBL; AK160525; BAE35843.1; -; mRNA.
DR EMBL; U41805; AAC52472.1; -; mRNA.
DR CCDS; CCDS22904.1; -. [Q3V009-1]
DR RefSeq; NP_001311439.1; NM_001324510.1.
DR RefSeq; NP_034874.2; NM_010744.4. [Q3V009-1]
DR AlphaFoldDB; Q3V009; -.
DR SMR; Q3V009; -.
DR BioGRID; 201249; 2.
DR IntAct; Q3V009; 1.
DR STRING; 10090.ENSMUSP00000034698; -.
DR PhosphoSitePlus; Q3V009; -.
DR SwissPalm; Q3V009; -.
DR MaxQB; Q3V009; -.
DR PaxDb; Q3V009; -.
DR PeptideAtlas; Q3V009; -.
DR PRIDE; Q3V009; -.
DR ProteomicsDB; 259424; -. [Q3V009-1]
DR ProteomicsDB; 259425; -. [Q3V009-2]
DR Antibodypedia; 2281; 215 antibodies from 25 providers.
DR DNASU; 17083; -.
DR Ensembl; ENSMUST00000034698; ENSMUSP00000034698; ENSMUSG00000032180. [Q3V009-1]
DR GeneID; 17083; -.
DR KEGG; mmu:17083; -.
DR UCSC; uc009olp.1; mouse. [Q3V009-1]
DR CTD; 11018; -.
DR MGI; MGI:106201; Tmed1.
DR VEuPathDB; HostDB:ENSMUSG00000032180; -.
DR eggNOG; KOG3287; Eukaryota.
DR GeneTree; ENSGT00940000158445; -.
DR HOGENOM; CLU_066963_0_0_1; -.
DR InParanoid; Q3V009; -.
DR OMA; EICFDNG; -.
DR PhylomeDB; Q3V009; -.
DR TreeFam; TF313000; -.
DR BioGRID-ORCS; 17083; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Tmed1; mouse.
DR PRO; PR:Q3V009; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3V009; protein.
DR Bgee; ENSMUSG00000032180; Expressed in right kidney and 220 other tissues.
DR ExpressionAtlas; Q3V009; baseline and differential.
DR Genevisible; Q3V009; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..227
FT /note="Transmembrane emp24 domain-containing protein 1"
FT /id="PRO_0000248020"
FT TOPO_DOM 25..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..125
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 145..170
FT /evidence="ECO:0000255"
FT MOTIF 218..227
FT /note="COPI vesicle coat-binding"
FT /evidence="ECO:0000255"
FT MOTIF 218..219
FT /note="COPII vesicle coat-binding"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020135"
FT VAR_SEQ 86..94
FT /note="SRKADGVHT -> MLVLRPSTR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020136"
SQ SEQUENCE 227 AA; 25263 MW; F37FC38E54AB4495 CRC64;
MMAAGAAVAL ALWLLLPAVG VGEAGPPPIQ DGEFTFLLPA GRKQCFYQSA PANASLETEY
QVIGGAGLDV DFTLESPQGV LLVSESRKAD GVHTVEPTEA GDYRLCFDNS FSTISEKLVF
FELIFDSFQD EEEVEGWAEA VEPEEMLDVK MEDIKESIET MRTRLERSIQ MLTLLRAFEA
RDRNLQEDNL ERVNFWSAAN VAVLLLVAVL QVCTLKRFFH DKRPVPT
