EMIL3_MOUSE
ID EMIL3_MOUSE Reviewed; 758 AA.
AC P59900;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=EMILIN-3;
DE AltName: Full=EMILIN-5;
DE AltName: Full=Elastin microfibril interface located protein 5;
DE Short=Elastin microfibril interfacer 5;
DE AltName: Full=Elastin microfibril interface-located protein 3;
DE Short=Elastin microfibril interfacer 3;
DE Flags: Precursor;
GN Name=Emilin3; Synonyms=Emilin5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP DEVELOPMENTAL STAGE.
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).
RN [3]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14706625; DOI=10.1016/j.bbrc.2003.11.181;
RA Doi M., Nagano A., Nakamura Y.;
RT "Molecular cloning and characterization of a novel gene, EMILIN-5, and its
RT possible involvement in skeletal development.";
RL Biochem. Biophys. Res. Commun. 313:888-893(2004).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:14706625}.
CC Note=According to PubMed:14706625 it is cytoplasmic.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, expression is only observed in the
CC tailbud and the hindgut. At 11.5 dpc the expression is found at sites
CC of bone formation, i.e. surrounding mesenchymal condensates in the
CC fore- and hindlimbs, the nose, the maxilla, and the other parts of the
CC jaw. At 13.5 dpc, detected in perichondrium and around developing
CC skeletons, but barely detectable in mature osteoblasts. At 14.5 dpc it
CC is strongly expressed in the enteric nerves of the digestive tract and
CC the bladder. Expression is also observed surrounding the main branches
CC of the alveoli and surrounding sites of bone formation in skull and
CC trunk. {ECO:0000269|PubMed:12221002, ECO:0000269|PubMed:14706625}.
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DR EMBL; BC054738; AAH54738.1; -; mRNA.
DR EMBL; BC057619; AAH57619.1; -; mRNA.
DR CCDS; CCDS16999.1; -.
DR RefSeq; NP_001278074.1; NM_001291145.1.
DR RefSeq; NP_878260.1; NM_182840.2.
DR AlphaFoldDB; P59900; -.
DR BioGRID; 235029; 1.
DR GlyGen; P59900; 5 sites.
DR PhosphoSitePlus; P59900; -.
DR PaxDb; P59900; -.
DR PRIDE; P59900; -.
DR ProteomicsDB; 277790; -.
DR Antibodypedia; 57328; 79 antibodies from 17 providers.
DR Ensembl; ENSMUST00000057169; ENSMUSP00000059732; ENSMUSG00000050700.
DR GeneID; 280635; -.
DR KEGG; mmu:280635; -.
DR UCSC; uc008nrk.2; mouse.
DR CTD; 90187; -.
DR MGI; MGI:2389142; Emilin3.
DR VEuPathDB; HostDB:ENSMUSG00000050700; -.
DR eggNOG; ENOG502QV8J; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR InParanoid; P59900; -.
DR OMA; FMTIVGE; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; P59900; -.
DR TreeFam; TF331033; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 280635; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mmrn2; mouse.
DR PRO; PR:P59900; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P59900; protein.
DR Bgee; ENSMUSG00000050700; Expressed in ureter smooth muscle and 101 other tissues.
DR ExpressionAtlas; P59900; baseline and differential.
DR Genevisible; P59900; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR InterPro; IPR011489; EMI_domain.
DR Pfam; PF07546; EMI; 1.
DR PROSITE; PS51041; EMI; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..758
FT /note="EMILIN-3"
FT /id="PRO_0000007820"
FT DOMAIN 54..130
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT REGION 131..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..401
FT /evidence="ECO:0000255"
FT COILED 460..483
FT /evidence="ECO:0000255"
FT COILED 528..567
FT /evidence="ECO:0000255"
FT COILED 642..677
FT /evidence="ECO:0000255"
FT COILED 720..753
FT /evidence="ECO:0000255"
FT COMPBIAS 142..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 85..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 119..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
SQ SEQUENCE 758 AA; 82396 MW; 71153567BB41D66E CRC64;
MGRRLSVWLC TVAALLSGAQ AKGTPLLARP AQPSASRYSL YTTGWRPRLR PGPHKSLCAY
VVHRNVTCVL QEGAESYIKA EYRNCGWGPN CPSTVRYRTV FRPRYKIGYK TVTDLAWRCC
PGLTGESCPE HLTDHGATPP HQEPEPQIPL GQLGPGPRPS PYSREAPRPR GRKGQGPFGE
RLEQRLSQAY GTLSGLVASH ENPNRITGDS RAPVVPIGFG VIPEGLVAPE DRGRGPLIPP
LSEILSKVTE VSNTLQTKVQ LLDEVRGLAL GHEAHLQRLR EAPPSPLTSL ALLEEYVDQR
LQRLWGSLLD GFEQKLQGVQ SECDLRVQEV RQQCEEGQAA SQRLHQSLDG RELALRRELS
QLGTQLQGLT LTGGGTCCSQ LALISARVDS LERNLQAVTE TQGGPGTLAA DELARLSAAM
LQGGVDGLLE GLETINGTEN GARGCCLRME VGGWGVGGFG STLEQRVQSL EERLATLTGE
LSPESAIPDR SARPLVHSEL AVLEQRLVSL ETSCTPSTTT AILDNLVAEV KAWQSRSEAL
LHQVARHTAL LQQLNGTVAE VQGQLAEGTG SSLQGEITLL KVNLNSVSKS LTGLSDSVSQ
YSDAFSAANT SLDERERRVE AEVHTIQEQI SSQGSRLQAG HRQVLNLRGE LEQLKAGMAN
VARGLSRCRD TAQELQHTVG HFDQRVAQVE GACERLGLLA THLNSLPTEQ LRSREGLWGH
IDKLNHTLAQ HTQDIARLRD DLLDCRAQLA EVRPGRAD
