Full text data of TMED1
TMED1
(IL1RL1L, IL1RL1LG)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Transmembrane emp24 domain-containing protein 1 (Interleukin-1 receptor-like 1 ligand; Putative T1/ST2 receptor-binding protein; p24 family protein gamma-1; Tp24; p24gamma1; Flags: Precursor)
Transmembrane emp24 domain-containing protein 1 (Interleukin-1 receptor-like 1 ligand; Putative T1/ST2 receptor-binding protein; p24 family protein gamma-1; Tp24; p24gamma1; Flags: Precursor)
UniProt
Q13445
ID TMED1_HUMAN Reviewed; 227 AA.
AC Q13445;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 102.
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 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.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential). Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Golgi apparatus, cis-Golgi network
CC membrane; Single-pass type I membrane protein. Endoplasmic
CC reticulum-Golgi intermediate compartment membrane; Single-pass
CC type I membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U41804; AAC50419.1; -; mRNA.
DR EMBL; AC007229; AAD23605.1; -; Genomic_DNA.
DR EMBL; BC002443; AAH02443.1; -; mRNA.
DR RefSeq; NP_006849.1; NM_006858.3.
DR UniGene; Hs.515139; -.
DR ProteinModelPortal; Q13445; -.
DR IntAct; Q13445; 2.
DR MINT; MINT-1180917; -.
DR STRING; 9606.ENSP00000214869; -.
DR DMDM; 74739789; -.
DR PaxDb; Q13445; -.
DR PeptideAtlas; Q13445; -.
DR PRIDE; Q13445; -.
DR DNASU; 11018; -.
DR Ensembl; ENST00000214869; ENSP00000214869; ENSG00000099203.
DR GeneID; 11018; -.
DR KEGG; hsa:11018; -.
DR UCSC; uc002mpy.3; human.
DR CTD; 11018; -.
DR GeneCards; GC19M010943; -.
DR HGNC; HGNC:17291; TMED1.
DR HPA; HPA018507; -.
DR MIM; 605395; gene.
DR neXtProt; NX_Q13445; -.
DR PharmGKB; PA134972147; -.
DR eggNOG; NOG277263; -.
DR HOGENOM; HOG000039809; -.
DR HOVERGEN; HBG000271; -.
DR InParanoid; Q13445; -.
DR OMA; RNLLEDN; -.
DR OrthoDB; EOG7CG716; -.
DR PhylomeDB; Q13445; -.
DR GeneWiki; TMED1; -.
DR GenomeRNAi; 11018; -.
DR NextBio; 41860; -.
DR PRO; PR:Q13445; -.
DR ArrayExpress; Q13445; -.
DR Bgee; Q13445; -.
DR CleanEx; HS_TMED1; -.
DR Genevestigator; Q13445; -.
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 to 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.
DR Pfam; PF01105; 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
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 Helical; (Potential).
FT TOPO_DOM 216 227 Cytoplasmic (Potential).
FT DOMAIN 43 125 GOLD.
FT COILED 145 170 Potential.
FT MOTIF 218 227 COPI vesicle coat-binding (Potential).
FT MOTIF 218 219 COPII vesicle coat-binding (Potential).
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
//
ID TMED1_HUMAN Reviewed; 227 AA.
AC Q13445;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 102.
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 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.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential). Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Golgi apparatus, cis-Golgi network
CC membrane; Single-pass type I membrane protein. Endoplasmic
CC reticulum-Golgi intermediate compartment membrane; Single-pass
CC type I membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U41804; AAC50419.1; -; mRNA.
DR EMBL; AC007229; AAD23605.1; -; Genomic_DNA.
DR EMBL; BC002443; AAH02443.1; -; mRNA.
DR RefSeq; NP_006849.1; NM_006858.3.
DR UniGene; Hs.515139; -.
DR ProteinModelPortal; Q13445; -.
DR IntAct; Q13445; 2.
DR MINT; MINT-1180917; -.
DR STRING; 9606.ENSP00000214869; -.
DR DMDM; 74739789; -.
DR PaxDb; Q13445; -.
DR PeptideAtlas; Q13445; -.
DR PRIDE; Q13445; -.
DR DNASU; 11018; -.
DR Ensembl; ENST00000214869; ENSP00000214869; ENSG00000099203.
DR GeneID; 11018; -.
DR KEGG; hsa:11018; -.
DR UCSC; uc002mpy.3; human.
DR CTD; 11018; -.
DR GeneCards; GC19M010943; -.
DR HGNC; HGNC:17291; TMED1.
DR HPA; HPA018507; -.
DR MIM; 605395; gene.
DR neXtProt; NX_Q13445; -.
DR PharmGKB; PA134972147; -.
DR eggNOG; NOG277263; -.
DR HOGENOM; HOG000039809; -.
DR HOVERGEN; HBG000271; -.
DR InParanoid; Q13445; -.
DR OMA; RNLLEDN; -.
DR OrthoDB; EOG7CG716; -.
DR PhylomeDB; Q13445; -.
DR GeneWiki; TMED1; -.
DR GenomeRNAi; 11018; -.
DR NextBio; 41860; -.
DR PRO; PR:Q13445; -.
DR ArrayExpress; Q13445; -.
DR Bgee; Q13445; -.
DR CleanEx; HS_TMED1; -.
DR Genevestigator; Q13445; -.
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 to 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.
DR Pfam; PF01105; 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
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 Helical; (Potential).
FT TOPO_DOM 216 227 Cytoplasmic (Potential).
FT DOMAIN 43 125 GOLD.
FT COILED 145 170 Potential.
FT MOTIF 218 227 COPI vesicle coat-binding (Potential).
FT MOTIF 218 219 COPII vesicle coat-binding (Potential).
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
//
MIM
605395
*RECORD*
*FIELD* NO
605395
*FIELD* TI
*605395 TRANSMEMBRANE EMP24 TRANSPORT DOMAIN-CONTAINING PROTEIN 1; TMED1
;;INTERLEUKIN 1 RECEPTOR-LIKE 1 LIGAND; IL1RL1LG;;
read moreIL1RL1-BINDING PROTEIN
*FIELD* TX
CLONING
The T1/ST2 receptor, also called IL1RL1 (601203), is a member of the
interleukin-1 receptor family. Gayle et al. (1996) determined that none
of the 3 interleukin-1 species (IL1A (147760), IL1B (147720), or IL1RA
(IL1RN; 147679)) binds to IL1RL1. By flow cytometry, they found that
several cell lines bind specifically to IL1RL1. Using expression
cloning, Gayle et al. (1996) isolated a cDNA encoding IL1RL1 ligand, or
IL1RL1LG. Sequence analysis predicted that the 227-amino acid, type I
transmembrane protein, which lacks any similarity to any of the IL1
types, contains a 170-amino acid extracellular region between the signal
peptide and the transmembrane domain as well as a 12-amino acid
cytoplasmic tail. Northern blot analysis detected wide expression of a
1.5-kb transcript. Functional analysis failed to show that the
interaction of IL1RL1LG and IL1RL1 leads to the activation of DNA
binding by nuclear factor kappa-B (NFKB; 164011) or transcription from
the IL8 (146930) promoter. The authors concluded that other proteins
must interact with IL1RL1 in order for these functions to occur.
MAPPING
Using FISH, Gayle et al. (1996) mapped the IL1RL1LG gene to 19p13.2.
*FIELD* RF
1. Gayle, M. A.; Slack, J. L.; Bonnert, T. P.; Renshaw, B. R.; Sonoda,
G.; Taguchi, T.; Testa, J. R.; Dower, S. K.; Sims, J. E.: Cloning
of a putative ligand for the T1/ST2 receptor. J. Biol. Chem. 271:
5784-5789, 1996.
*FIELD* CD
Paul J. Converse: 11/9/2000
*FIELD* ED
alopez: 05/23/2006
mgross: 11/9/2000
*RECORD*
*FIELD* NO
605395
*FIELD* TI
*605395 TRANSMEMBRANE EMP24 TRANSPORT DOMAIN-CONTAINING PROTEIN 1; TMED1
;;INTERLEUKIN 1 RECEPTOR-LIKE 1 LIGAND; IL1RL1LG;;
read moreIL1RL1-BINDING PROTEIN
*FIELD* TX
CLONING
The T1/ST2 receptor, also called IL1RL1 (601203), is a member of the
interleukin-1 receptor family. Gayle et al. (1996) determined that none
of the 3 interleukin-1 species (IL1A (147760), IL1B (147720), or IL1RA
(IL1RN; 147679)) binds to IL1RL1. By flow cytometry, they found that
several cell lines bind specifically to IL1RL1. Using expression
cloning, Gayle et al. (1996) isolated a cDNA encoding IL1RL1 ligand, or
IL1RL1LG. Sequence analysis predicted that the 227-amino acid, type I
transmembrane protein, which lacks any similarity to any of the IL1
types, contains a 170-amino acid extracellular region between the signal
peptide and the transmembrane domain as well as a 12-amino acid
cytoplasmic tail. Northern blot analysis detected wide expression of a
1.5-kb transcript. Functional analysis failed to show that the
interaction of IL1RL1LG and IL1RL1 leads to the activation of DNA
binding by nuclear factor kappa-B (NFKB; 164011) or transcription from
the IL8 (146930) promoter. The authors concluded that other proteins
must interact with IL1RL1 in order for these functions to occur.
MAPPING
Using FISH, Gayle et al. (1996) mapped the IL1RL1LG gene to 19p13.2.
*FIELD* RF
1. Gayle, M. A.; Slack, J. L.; Bonnert, T. P.; Renshaw, B. R.; Sonoda,
G.; Taguchi, T.; Testa, J. R.; Dower, S. K.; Sims, J. E.: Cloning
of a putative ligand for the T1/ST2 receptor. J. Biol. Chem. 271:
5784-5789, 1996.
*FIELD* CD
Paul J. Converse: 11/9/2000
*FIELD* ED
alopez: 05/23/2006
mgross: 11/9/2000