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 05-MAY-2009, entry version 58. 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 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 MEDLINE=96215043; 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 IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [5] 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 protein trafficking. CC -!- SUBUNIT: May interact with IL1RL1. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein (Potential). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. CC -!- SIMILARITY: Contains 1 GOLD domain. 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 IPI; IPI00009976; -. DR RefSeq; NP_006849.1; -. DR UniGene; Hs.515139; -. DR PeptideAtlas; Q13445; -. DR PRIDE; Q13445; -. DR Ensembl; ENSG00000099203; Homo sapiens. DR GeneID; 11018; -. DR KEGG; hsa:11018; -. DR GeneCards; GC19M010805; -. DR HGNC; HGNC:17291; TMED1. DR HPA; HPA018507; -. DR MIM; 605395; gene. DR PharmGKB; PA134972147; -. DR HOGENOM; Q13445; -. DR HOVERGEN; Q13445; -. DR OMA; Q13445; GVHTVEP. DR NextBio; 41860; -. DR Bgee; Q13445; -. DR CleanEx; HS_TMED1; -. DR GermOnline; ENSG00000099203; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005102; F:receptor binding; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006810; P:transport; IEA:InterPro. DR InterPro; IPR000348; Emp24_gp25L_p24. DR InterPro; IPR009038; GOLD. DR InterPro; IPR015717; ST2_recp_bnd_rel. DR PANTHER; PTHR22811:SF12; ST2_recp_bnd_rel; 1. DR Pfam; PF01105; EMP24_GP25L; 1. DR PROSITE; PS50866; GOLD; 1. PE 1: Evidence at protein level; KW Cell membrane; Membrane; Polymorphism; Signal; Transmembrane. FT SIGNAL 1 23 Potential. FT CHAIN 24 227 Transmembrane emp24 domain-containing FT protein 1. FT /FTId=PRO_0000248019. FT TOPO_DOM 24 194 Extracellular (Potential). FT TRANSMEM 195 215 Potential. FT TOPO_DOM 216 227 Cytoplasmic (Potential). FT DOMAIN 43 125 GOLD. FT VARIANT 102 102 D -> N (in a breast cancer sample; FT somatic mutation). 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 //