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 11-MAY-2016, entry version 122. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND POSSIBLE RP INTERACTION 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., RA Taguchi T., 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., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA 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 RT project: 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 RT labeling of 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 RT secretory 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., RA Buerckstuemmer T., 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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., RA Ayoub D., 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., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Potential role in vesicular protein trafficking, mainly CC in the early secretory pathway. May act as a cargo receptor at the CC lumenal side for incorporation of secretory cargo molecules into CC transport vesicles and may be involved in vesicle coat formation CC at the cytoplasmic side. CC -!- SUBUNIT: Homodimer in endoplasmic reticulum, endoplasmic CC reticulum-Golgi intermediate compartment and cis-Golgi network. CC May interact with 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}; CC Single-pass type I membrane protein {ECO:0000255}. Endoplasmic CC reticulum-Golgi intermediate compartment membrane CC {ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Widely expressed. CC {ECO:0000269|PubMed:8621446}. CC -!- MISCELLANEOUS: Found only in very low concentrations in the CC endoplasmic reticulum, Golgi apparatus and endoplasmic reticulum- CC Golgi intermediate compartment compared to other members of the CC EMP24/GP25L family. CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GOLD domain. {ECO:0000255|PROSITE- CC ProRule:PRU00096}. 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 UniGene; Hs.211463; -. DR UniGene; Hs.515139; -. DR UniGene; Hs.661691; -. DR ProteinModelPortal; Q13445; -. DR BioGrid; 116208; 16. DR IntAct; Q13445; 6. DR MINT; MINT-1180917; -. DR STRING; 9606.ENSP00000214869; -. DR TCDB; 9.B.188.1.1; the transmembrane emp24 domain-containing protein (tmed) family. DR SwissPalm; Q13445; -. DR DMDM; 74739789; -. DR EPD; Q13445; -. DR MaxQB; Q13445; -. DR PaxDb; Q13445; -. DR PeptideAtlas; Q13445; -. DR PRIDE; Q13445; -. DR TopDownProteomics; Q13445; -. DR DNASU; 11018; -. DR Ensembl; ENST00000214869; ENSP00000214869; ENSG00000099203. DR GeneID; 11018; -. DR KEGG; hsa:11018; -. DR UCSC; uc002mpy.5; human. DR CTD; 11018; -. DR GeneCards; TMED1; -. DR HGNC; HGNC:17291; TMED1. DR HPA; HPA018507; -. DR MIM; 605395; gene. DR neXtProt; NX_Q13445; -. DR PharmGKB; PA134972147; -. DR eggNOG; KOG3287; Eukaryota. DR eggNOG; ENOG410Z18S; LUCA. DR GeneTree; ENSGT00670000097656; -. DR HOGENOM; HOG000039809; -. DR HOVERGEN; HBG000271; -. DR InParanoid; Q13445; -. DR OMA; RSRQMQT; -. DR OrthoDB; EOG7CG716; -. DR PhylomeDB; Q13445; -. DR TreeFam; TF313000; -. DR GeneWiki; TMED1; -. DR GenomeRNAi; 11018; -. DR NextBio; 41860; -. DR PRO; PR:Q13445; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; Q13445; -. DR CleanEx; HS_TMED1; -. DR ExpressionAtlas; Q13445; baseline and differential. DR Genevisible; Q13445; HS. 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:receptor binding; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR009038; GOLD_dom. 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; Complete proteome; KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus; KW Membrane; Polymorphism; Protein transport; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1 23 {ECO:0000244|PubMed:25944712, FT ECO:0000269|PubMed:19892738}. FT CHAIN 24 227 Transmembrane emp24 domain-containing FT protein 1. FT /FTId=PRO_0000248019. FT TOPO_DOM 24 194 Extracellular. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TOPO_DOM 216 227 Cytoplasmic. {ECO:0000255}. FT DOMAIN 43 125 GOLD. {ECO:0000255|PROSITE- FT ProRule:PRU00096}. FT COILED 145 170 {ECO:0000255}. FT MOTIF 218 227 COPI vesicle coat-binding. {ECO:0000255}. FT MOTIF 218 219 COPII vesicle coat-binding. FT {ECO:0000255}. FT VARIANT 102 102 D -> N (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=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 //