EMID1_MOUSE
ID EMID1_MOUSE Reviewed; 444 AA.
AC Q91VF5;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=EMI domain-containing protein 1;
DE AltName: Full=Emilin and multimerin domain-containing protein 1;
DE Short=Emu1;
DE Flags: Precursor;
GN Name=Emid1; Synonyms=Emu1;
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 [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12221002; DOI=10.1006/dbio.2002.0764;
RA Leimeister C., Steidl C., Schumacher N., Erhard S., Gessler M.;
RT "Developmental expression and biochemical characterization of Emu family
RT members.";
RL Dev. Biol. 249:204-218(2002).
CC -!- SUBUNIT: Homo- or heteromers.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91VF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91VF5-2; Sequence=VSP_008446;
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc it is expressed in the nephric duct,
CC the dorsal neural tube, the epithelia of the branchial arches, and the
CC optic vesicle. In 14.5 dpc embryos, like in earlier ones, it is
CC expressed in the dorsal spinal cord and the brain, where it is
CC restricted to the proliferating ependymal and cortical cell layers.
CC Expression is also detected in smooth muscles of the digestive tract as
CC well as in the epithelia of the salivary gland, the inner ear, and the
CC developing nephrons of kidney. In early embryos, it is expressed in the
CC epithelium of the branchial arches. At 14.5 dpc, Emu1 is restricted to
CC the epithelium in the advanced developing kidney (at 15.5 dpc and
CC later), transcripts are detected in the epithelium of the developing
CC nephrons and in the collecting duct epithelium.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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DR EMBL; AJ416093; CAC94780.1; -; mRNA.
DR CCDS; CCDS24398.1; -. [Q91VF5-1]
DR CCDS; CCDS88125.1; -. [Q91VF5-2]
DR RefSeq; NP_542162.1; NM_080595.2. [Q91VF5-1]
DR AlphaFoldDB; Q91VF5; -.
DR STRING; 10090.ENSMUSP00000061704; -.
DR GlyConnect; 2282; 1 N-Linked glycan (1 site).
DR GlyGen; Q91VF5; 2 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q91VF5; -.
DR MaxQB; Q91VF5; -.
DR PaxDb; Q91VF5; -.
DR PRIDE; Q91VF5; -.
DR Antibodypedia; 248; 94 antibodies from 21 providers.
DR DNASU; 140703; -.
DR Ensembl; ENSMUST00000062821; ENSMUSP00000061704; ENSMUSG00000034164. [Q91VF5-1]
DR Ensembl; ENSMUST00000163299; ENSMUSP00000131391; ENSMUSG00000034164. [Q91VF5-2]
DR GeneID; 140703; -.
DR KEGG; mmu:140703; -.
DR UCSC; uc007hwg.1; mouse. [Q91VF5-1]
DR CTD; 129080; -.
DR MGI; MGI:2155091; Emid1.
DR VEuPathDB; HostDB:ENSMUSG00000034164; -.
DR eggNOG; ENOG502QSR5; Eukaryota.
DR GeneTree; ENSGT00940000161542; -.
DR HOGENOM; CLU_045268_0_0_1; -.
DR InParanoid; Q91VF5; -.
DR OMA; FVEPRWS; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; Q91VF5; -.
DR TreeFam; TF336589; -.
DR BioGRID-ORCS; 140703; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Emid1; mouse.
DR PRO; PR:Q91VF5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91VF5; protein.
DR Bgee; ENSMUSG00000034164; Expressed in metanephric renal vesicle and 170 other tissues.
DR ExpressionAtlas; Q91VF5; baseline and differential.
DR Genevisible; Q91VF5; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR011489; EMI_domain.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF07546; EMI; 1.
DR PROSITE; PS51041; EMI; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Collagen; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..444
FT /note="EMI domain-containing protein 1"
FT /id="PRO_0000007824"
FT DOMAIN 33..106
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 221..371
FT /note="Collagen-like"
FT REGION 161..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 62..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 95..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT VAR_SEQ 72..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12221002"
FT /id="VSP_008446"
SQ SEQUENCE 444 AA; 45634 MW; 82B3C8C3D27F2C26 CRC64;
MGGPRAWTLL CLGLLLPGGG AAWSVPGARF SGRRNWCSYV VTRTVSCHVQ NGTYLQRVLQ
NCPWPMGCPG NSYRTVVRPL YKVTYKTVTA REWRCCPGHS GVTCEEGSPG LLEPTWTDSG
MRRMAVRPTA LSGCLNCSKV SELTERLKAL EAKVAVLSVT EQTVPSVPAT PEDSALLWGS
PAARGSPGDG SLQDRLDSWG LPGPTGPKGG TDSQSPVRIR GPPGPQGPPG RPGQTGAAGT
PGKMGPPGPP GPPGPPGPPA PVGPPYGQVS LHGDPLLSNT FTEMGSHWPQ GPTGPPGPPG
PPGPMGPPGL PGPMGAPGSP GHMGIPGPSG PKGTSGHPGE KGERGLPGEP GPQGLMGVPG
EPGPKGDPGE KSHWGEGLHQ LREALKILAE RVLILETMIG LYEPDLGSGA GPDGTGTPSL
LRGKRGGHPT NYPIITPRRR SERS
