EMIL2_HUMAN
ID EMIL2_HUMAN Reviewed; 1053 AA.
AC Q9BXX0; B2RMY3; Q8NBH3; Q96JQ4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=EMILIN-2;
DE AltName: Full=Elastin microfibril interface-located protein 2;
DE Short=Elastin microfibril interfacer 2;
DE AltName: Full=Protein FOAP-10;
DE Flags: Precursor;
GN Name=EMILIN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-903.
RC TISSUE=Kidney;
RX PubMed=11278945; DOI=10.1074/jbc.m011591200;
RA Doliana R., Bot S., Mungiguerra G., Canton A., Cilli S.P., Colombatti A.;
RT "Isolation and characterization of EMILIN-2, a new component of the growing
RT EMILINs family and a member of the EMI domain-containing superfamily.";
RL J. Biol. Chem. 276:12003-12011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-1053.
RC TISSUE=Adrenal gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 846-1053.
RC TISSUE=Macrophage;
RA Fujii Y., Takayama K., Tsuritani K., Yajima Y., Amemiya T., Ukai Y.,
RA Naito K., Kawaguchi A.;
RT "Homo sapiens mRNA for FOAP-10 protein, partial cds.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-616.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
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.
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 fetal heart and adult
CC lung. Intermediate levels in peripheral leukocytes, placenta, and
CC spinal cord and low expression in fetal brain, spleen, thymus, and lung
CC and in adult heart, aorta, testis, bone marrow, small intestine,
CC thymus, lymph node, and appendix.
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DR EMBL; AF270513; AAK37963.1; -; mRNA.
DR EMBL; AP000919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01690.1; -; Genomic_DNA.
DR EMBL; BC136541; AAI36542.1; -; mRNA.
DR EMBL; AK090519; BAC03470.1; -; mRNA.
DR EMBL; AB026706; BAB61020.1; -; mRNA.
DR CCDS; CCDS11828.1; -.
DR RefSeq; NP_114437.2; NM_032048.2.
DR AlphaFoldDB; Q9BXX0; -.
DR SMR; Q9BXX0; -.
DR BioGRID; 123848; 26.
DR ComplexPortal; CPX-436; EMILIN-2 complex.
DR IntAct; Q9BXX0; 11.
DR STRING; 9606.ENSP00000254528; -.
DR GlyGen; Q9BXX0; 23 sites, 3 O-linked glycans (13 sites).
DR iPTMnet; Q9BXX0; -.
DR PhosphoSitePlus; Q9BXX0; -.
DR BioMuta; EMILIN2; -.
DR DMDM; 296439365; -.
DR EPD; Q9BXX0; -.
DR jPOST; Q9BXX0; -.
DR MassIVE; Q9BXX0; -.
DR MaxQB; Q9BXX0; -.
DR PaxDb; Q9BXX0; -.
DR PeptideAtlas; Q9BXX0; -.
DR PRIDE; Q9BXX0; -.
DR ProteomicsDB; 79535; -.
DR Antibodypedia; 21912; 57 antibodies from 17 providers.
DR DNASU; 84034; -.
DR Ensembl; ENST00000254528.4; ENSP00000254528.3; ENSG00000132205.11.
DR GeneID; 84034; -.
DR KEGG; hsa:84034; -.
DR MANE-Select; ENST00000254528.4; ENSP00000254528.3; NM_032048.3; NP_114437.2.
DR UCSC; uc002kln.4; human.
DR CTD; 84034; -.
DR DisGeNET; 84034; -.
DR GeneCards; EMILIN2; -.
DR HGNC; HGNC:19881; EMILIN2.
DR HPA; ENSG00000132205; Tissue enhanced (parathyroid).
DR MIM; 608928; gene.
DR neXtProt; NX_Q9BXX0; -.
DR OpenTargets; ENSG00000132205; -.
DR PharmGKB; PA134880588; -.
DR VEuPathDB; HostDB:ENSG00000132205; -.
DR eggNOG; ENOG502QV5P; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR HOGENOM; CLU_011705_0_0_1; -.
DR InParanoid; Q9BXX0; -.
DR OMA; NIQGKPH; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; Q9BXX0; -.
DR TreeFam; TF331033; -.
DR PathwayCommons; Q9BXX0; -.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; Q9BXX0; -.
DR BioGRID-ORCS; 84034; 8 hits in 1066 CRISPR screens.
DR ChiTaRS; EMILIN2; human.
DR GenomeRNAi; 84034; -.
DR Pharos; Q9BXX0; Tbio.
DR PRO; PR:Q9BXX0; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9BXX0; protein.
DR Bgee; ENSG00000132205; Expressed in decidua and 136 other tissues.
DR Genevisible; Q9BXX0; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; NAS:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IC:ComplexPortal.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:ComplexPortal.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ComplexPortal.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:ComplexPortal.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:ComplexPortal.
DR GO; GO:0008217; P:regulation of blood pressure; IC:ComplexPortal.
DR GO; GO:0042127; P:regulation of cell population proliferation; IC:ComplexPortal.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1053
FT /note="EMILIN-2"
FT /id="PRO_0000007817"
FT DOMAIN 44..120
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 840..892
FT /note="Collagen-like"
FT DOMAIN 901..1052
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 120..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..215
FT /evidence="ECO:0000255"
FT COILED 253..340
FT /evidence="ECO:0000255"
FT COILED 369..389
FT /evidence="ECO:0000255"
FT COILED 578..634
FT /evidence="ECO:0000255"
FT COMPBIAS 143..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 74..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 109..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT VARIANT 215
FT /note="A -> T (in dbSNP:rs16943977)"
FT /id="VAR_057528"
FT VARIANT 259
FT /note="M -> V (in dbSNP:rs35267664)"
FT /id="VAR_057529"
FT VARIANT 903
FT /note="P -> S (in dbSNP:rs56288451)"
FT /evidence="ECO:0000269|PubMed:11278945"
FT /id="VAR_062003"
FT CONFLICT 545
FT /note="K -> G (in Ref. 1; AAK37963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1053 AA; 115687 MW; 9F2895AB0AC5E8EF CRC64;
MWQPRRPWPR VPWRWALALL ALVGAGLCHA GPQPGYPARP SARNKNWCAY IVNKNVSCSV
LEGSESFIQA QYNCAWNQMP CPSALVYRVN FRPRYVTRYK TVTQLEWRCC PGFRGGDCQE
GPKDPVKTLR PTPARPRNSL KKATDNEPSQ FSEPRKTLSP TGTAQPSWGV DPKEGPQELQ
EKKIQVLEEK VLRLTRTVLD LQSSLAGVSE NLKHATQDDA SRTRAPGLSS QHPKPDTTVS
GDTETGQSPG VFNTKESGMK DIKSELAEVK DTLKNKSDKL EELDGKVKGY EGQLRQLQEA
AQGPTVTMTT NELYQAYVDS KIDALREELM EGMDRKLADL KNSCEYKLTG LQQQCDDYGS
SYLGVIELIG EKETSLRKEI NNLRARLQEP SAQANCCDSE KNGDIGQQIK TLDQKIERVA
EATRMLNGRL DNEFDRLIVP EPDVDFDAKW NELDARINVT EKNAEEHCFY IEETLRGAIN
GEVGDLKQLV DQKIQSLEDR LGSVLLQMTN NTGAELSPPG AAALPGVSGS GDERVMMELN
HLKDKVQVVE DICLLNIQGK PHGMEGALPN REDRAVRDSL HLLKSLNDTM HRKFQETEQT
IQKLQQDFSF LYSQLNHTEN DVTHLQKEMS NCRAGENAGM GRFTKVGEQE RTVDTLPSPQ
HPVAHCCSQL EERWQRLQSQ VISELDACKE CTQGVQREVS MVEGRVSHME KTCSKLDSIS
GNLQRIKEGL NKHVSSLWNC VRQMNGTLRS HSRDISGLKN SVQQFYSHVF QISTDLQDLV
KFQPSAKAPS PPPPAEAPKE PLQPEPAPPR PSGPATAEDP GRRPVLPQRP PEERPPQPPG
STGVIAETGQ AGPPAGAGVS GRGLPRGVDG QTGSGTVPGA EGFAGAPGYP KSPPVASPGA
PVPSLVSFSA GLTQKPFPSD GGVVLFNKVL VNDGDVYNPS TGVFTAPYDG RYLITATLTP
ERDAYVEAVL SVSNASVAQL HTAGYRREFL EYHRPPGALH TCGGPGAFHL IVHLKAGDAV
NVVVTGGKLA HTDFDEMYST FSGVFLYPFL SHL
