EMIL2_MOUSE
ID EMIL2_MOUSE Reviewed; 1074 AA.
AC Q8K482;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=EMILIN-2;
DE AltName: Full=Basilin;
DE AltName: Full=Elastin microfibril interface-located protein 2;
DE Short=Elastin microfibril interfacer 2;
DE Flags: Precursor;
GN Name=Emilin2;
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], AND CHARACTERIZATION.
RC STRAIN=C57BL/6J; TISSUE=Cochlea;
RX PubMed=12837629; DOI=10.1016/s1044-7431(03)00075-7;
RA Amma L.L., Goodyear R., Faris J.S., Jones I., Ng L., Richardson G.,
RA Forrest D.;
RT "An emilin family extracellular matrix protein identified in the cochlear
RT basilar membrane.";
RL Mol. Cell. Neurosci. 23:460-472(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be responsible for anchoring smooth muscle cells to
CC elastic fibers, and may be involved not only in the formation of the
CC elastic fiber, but also in the processes that regulate vessel assembly.
CC Has cell adhesive capacity. Major component of the cochlear basilar
CC membrane (BM) which may contribute to the developmental assembly or
CC function of the BM.
CC -!- SUBUNIT: Homotrimer associated through a moderately stable interaction
CC of the C-terminal globular C1q domains, allowing the nucleation of the
CC triple helix and then a further quaternary assembly to higher-order
CC polymers via intermolecular disulfide bonds (By similarity). Interacts
CC with EMILIN1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix. Note=Found mainly at the interface between amorphous elastin
CC and microfibrils.
CC -!- TISSUE SPECIFICITY: Highest levels are present in cochlea of P8 pups,
CC followed by modest levels in adult heart and lung, and much lower
CC levels in forebrain, brainstem, cerebellum and hypothalamus. Very low
CC levels detected in muscle, liver, kidney and eye.
CC -!- DEVELOPMENTAL STAGE: Low levels detected in cochlea in neonatal pups at
CC P1. Levels increased 2-fold by P5 and rose further to 16-fold at P13.
CC Expression declined somewhat in adult mice. At 9.5 dpc, as during all
CC stages of development, it is strongly expressed in the neural fold, the
CC limbbuds and the heart. {ECO:0000269|PubMed:12221002}.
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DR EMBL; AF468645; AAM53532.1; -; mRNA.
DR EMBL; BC053753; AAH53753.1; -; mRNA.
DR CCDS; CCDS37686.1; -.
DR RefSeq; NP_660140.1; NM_145158.3.
DR AlphaFoldDB; Q8K482; -.
DR SMR; Q8K482; -.
DR ComplexPortal; CPX-438; EMILIN-2 complex.
DR STRING; 10090.ENSMUSP00000024849; -.
DR GlyGen; Q8K482; 7 sites.
DR iPTMnet; Q8K482; -.
DR PhosphoSitePlus; Q8K482; -.
DR EPD; Q8K482; -.
DR jPOST; Q8K482; -.
DR MaxQB; Q8K482; -.
DR PaxDb; Q8K482; -.
DR PRIDE; Q8K482; -.
DR ProteomicsDB; 277860; -.
DR Antibodypedia; 21912; 57 antibodies from 17 providers.
DR Ensembl; ENSMUST00000233057; ENSMUSP00000156446; ENSMUSG00000024053.
DR GeneID; 246707; -.
DR KEGG; mmu:246707; -.
DR UCSC; uc008dme.1; mouse.
DR CTD; 84034; -.
DR MGI; MGI:2389136; Emilin2.
DR VEuPathDB; HostDB:ENSMUSG00000024053; -.
DR eggNOG; ENOG502QV5P; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR HOGENOM; CLU_011705_0_0_1; -.
DR InParanoid; Q8K482; -.
DR OMA; NIQGKPH; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; Q8K482; -.
DR TreeFam; TF331033; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 246707; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Emilin2; mouse.
DR PRO; PR:Q8K482; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K482; protein.
DR Bgee; ENSMUSG00000024053; Expressed in decidua and 171 other tissues.
DR ExpressionAtlas; Q8K482; baseline and differential.
DR Genevisible; Q8K482; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:1990971; C:EMILIN complex; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:ComplexPortal.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; ISO:MGI.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; ISO:MGI.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF07546; EMI; 1.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Coiled coil; Collagen; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1074
FT /note="EMILIN-2"
FT /id="PRO_0000007818"
FT DOMAIN 47..123
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 852..913
FT /note="Collagen-like"
FT DOMAIN 922..1073
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 121..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..218
FT /evidence="ECO:0000255"
FT COILED 259..345
FT /evidence="ECO:0000255"
FT COILED 374..394
FT /evidence="ECO:0000255"
FT COILED 533..554
FT /evidence="ECO:0000255"
FT COILED 582..620
FT /evidence="ECO:0000255"
FT COMPBIAS 146..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 995
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 77..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 112..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
SQ SEQUENCE 1074 AA; 117310 MW; 4B81728C83CE52A7 CRC64;
MCQETPPRPR APSRWTPALL ALLALGGAGL CHASSQPGYH ARPSARNKNW CAYIVNKNVS
CTVQEGSESF IQAQYNCPWN QMPCPSALVY RVNFRPRFVT RYKIVTQLEW RCCPGFRGPD
CQEGPKDHMK TPRPPSARPK NNLKKATDTD PSQVSQPKKT LSPTNAVEPG QVADAKQGPP
ELQQSKVQVL EEKVVRLTRM VLDLQSTVVG LKENLKHTIQ DDGRKEPDSW LGPLHPQPTP
DSPLAGDAEP SQLPGIPSSK ESGMKDIKSE LAEVKDTLKT KSDKLEELDG KVKGYEGQLK
QLQEAAQGPT VTMTTNELYQ AYVDSKIDAL REELMEGMDR KLADLKNTCE YKLVGLQQQC
DDYGSSYLGV IELIGEKEAS LKKDIADLRA QLQDPVAQPS CCNGQKSSDF GPQIKALDQK
IERVAEATRM LNGRLDNEFD RLSVPEPDAD FDARWTELDA RINVTEKNAE EHCFYIEETL
RGTINGEVDD LRKLLNEKIH SLEDRLGIVL QAANSSDVEL TPMGPALPEQ PGAENEQVLM
ELSRLKDKVQ VVEDFCLQSL PHGIDGALPS VEDLTHVSLS LLESLNDTMH RQFQETSHSI
QKLQEDVNAL HSQLNHSECT GTYLQNGVSD SRTGDSMEAS GFTKTGEQER TVGTVPSPGT
PAAPCCGQLE ERWQKLQNQM LAELDTCKES AHGVQSGVSA IEGRVFQLEQ TCRRLDTISG
SLQRIKEGLG KHVGSLWNCI RQMNGTLKSH SRDISGLKNS VQQFYSHVFQ ISTDLQDLVK
FQPSATEEPS EATEGPSGKT PLESTRPSEE APTEPPRLTP LPEDPAGPPQ TGQQPVLPQR
PLQPPPLPAW PGRTGLPFLP GSSGVIMETG EAGPPGRMGV SGRGLPRGVD GQMGQGPIHS
SEGYAGAPGY PKSPPVTTPG VPLPTLVSFS AGLTQKPFPS DGGVVLFNKV LVNDGDVYNP
NTGIFTAPYD GRYLITATLT PERDTYVEAV LSVSNASVAQ LHTAGYRREF LEYHRPPGAV
HTCGGPGAFH LIVHLKAGDG VNVVVTGGRL AHTDFDEMYS TFSGVFLYPF LSHL
