ID TMED1_HUMAN Reviewed; 227 AA. AC Q13445; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-JUN-2020, entry version 149. 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=Tp24; DE Short=p24gamma1; DE Flags: Precursor; GN Name=TMED1; Synonyms=IL1RL1L, IL1RL1LG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND POSSIBLE INTERACTION RP WITH IL1RL1. RC TISSUE=Glioblastoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Melanoma; 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 [4] RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 24-43. RC TISSUE=Leukemic T-cell; RX PubMed=19892738; DOI=10.1073/pnas.0908958106; RA Xu G., Shin S.B., Jaffrey S.R.; RT "Global profiling of protease cleavage sites by chemoselective labeling of RT protein N-termini."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009). RN [5] RP SUBCELLULAR LOCATION. RX PubMed=10852829; RA Emery G., Rojo M., Gruenberg J.; RT "Coupled transport of p24 family members."; RL J. Cell Sci. 113:2507-2516(2000). RN [6] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=12237308; DOI=10.1074/jbc.m206989200; RA Jenne N., Frey K., Brugger B., Wieland F.T.; RT "Oligomeric state and stoichiometry of p24 proteins in the early secretory RT pathway."; RL J. Biol. Chem. 277:46504-46511(2002). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-23, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [10] RP VARIANT [LARGE SCALE ANALYSIS] ASN-102. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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. CC -!- SUBUNIT: Homodimer in endoplasmic reticulum, endoplasmic reticulum- CC Golgi intermediate compartment and cis-Golgi network. May interact with CC IL1RL1. {ECO:0000269|PubMed:12237308}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8621446}; CC Single-pass type I membrane protein {ECO:0000255}. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:10852829, CC ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane CC {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308}; Single-pass CC type I membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi CC intermediate compartment membrane {ECO:0000269|PubMed:12237308}; CC Single-pass type I membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8621446}. CC -!- MISCELLANEOUS: Found only in very low concentrations in the endoplasmic CC reticulum, Golgi apparatus and endoplasmic reticulum-Golgi intermediate CC compartment compared to other members of the EMP24/GP25L family. CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U41804; AAC50419.1; -; mRNA. DR EMBL; AC007229; AAD23605.1; -; Genomic_DNA. DR EMBL; BC002443; AAH02443.1; -; mRNA. DR CCDS; CCDS12249.1; -. DR RefSeq; NP_006849.1; NM_006858.3. DR SMR; Q13445; -. DR BioGRID; 116208; 23. DR IntAct; Q13445; 23. DR MINT; Q13445; -. DR STRING; 9606.ENSP00000214869; -. DR TCDB; 9.B.188.1.1; the transmembrane emp24 domain-containing protein (tmed) family. DR iPTMnet; Q13445; -. DR PhosphoSitePlus; Q13445; -. DR SwissPalm; Q13445; -. DR BioMuta; TMED1; -. DR DMDM; 74739789; -. DR EPD; Q13445; -. DR jPOST; Q13445; -. DR MassIVE; Q13445; -. DR MaxQB; Q13445; -. DR PaxDb; Q13445; -. DR PeptideAtlas; Q13445; -. DR PRIDE; Q13445; -. DR ProteomicsDB; 59453; -. DR TopDownProteomics; Q13445; -. DR Antibodypedia; 2281; 190 antibodies. DR DNASU; 11018; -. DR Ensembl; ENST00000214869; ENSP00000214869; ENSG00000099203. DR GeneID; 11018; -. DR KEGG; hsa:11018; -. DR UCSC; uc002mpy.5; human. DR CTD; 11018; -. DR DisGeNET; 11018; -. DR EuPathDB; HostDB:ENSG00000099203.6; -. DR GeneCards; TMED1; -. DR HGNC; HGNC:17291; TMED1. DR HPA; ENSG00000099203; Low tissue specificity. DR MIM; 605395; gene. DR neXtProt; NX_Q13445; -. DR OpenTargets; ENSG00000099203; -. DR PharmGKB; PA134972147; -. DR eggNOG; KOG3287; Eukaryota. DR eggNOG; ENOG410Z18S; LUCA. DR GeneTree; ENSGT00940000158445; -. DR HOGENOM; CLU_066963_0_0_1; -. DR InParanoid; Q13445; -. DR KO; K20348; -. DR OMA; HEADVNN; -. DR OrthoDB; 1292519at2759; -. DR PhylomeDB; Q13445; -. DR TreeFam; TF313000; -. DR BioGRID-ORCS; 11018; 2 hits in 786 CRISPR screens. DR ChiTaRS; TMED1; human. DR GeneWiki; TMED1; -. DR GenomeRNAi; 11018; -. DR Pharos; Q13445; Tdark. DR PRO; PR:Q13445; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q13445; protein. DR Bgee; ENSG00000099203; Expressed in epithelium of bronchus and 219 other tissues. DR ExpressionAtlas; Q13445; baseline and differential. DR Genevisible; Q13445; HS. DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. 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:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. 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 GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR009038; GOLD_dom. DR InterPro; IPR036598; GOLD_dom_sf. DR InterPro; IPR015720; TMP21-related. 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 Cell membrane; Coiled coil; Direct protein sequencing; KW Endoplasmic reticulum; Golgi apparatus; Membrane; Polymorphism; KW Protein transport; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1..23 FT /evidence="ECO:0000244|PubMed:25944712, FT ECO:0000269|PubMed:19892738" FT CHAIN 24..227 FT /note="Transmembrane emp24 domain-containing protein 1" FT /id="PRO_0000248019" FT TOPO_DOM 24..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 VARIANT 102 FT /note="D -> N (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036533" SQ SEQUENCE 227 AA; 25206 MW; 058C5274E05F8575 CRC64; MMAAGAALAL ALWLLMPPVE VGGAGPPPIQ DGEFTFLLPA GRKQCFYQSA PANASLETEY QVIGGAGLDV DFTLESPQGV LLVSESRKAD GVHTVEPTEA GDYKLCFDNS FSTISEKLVF FELIFDSLQD DEEVEGWAEA VEPEEMLDVK MEDIKESIET MRTRLERSIQ MLTLLRAFEA RDRNLQEGNL ERVNFWSAVN VAVLLLVAVL QVCTLKRFFQ DKRPVPT //