ECM1_HUMAN
ID ECM1_HUMAN Reviewed; 540 AA.
AC Q16610; A8K8S0; B4DW49; B4DY60; O43266; Q5T5G4; Q5T5G5; Q5T5G6; Q8IZ60;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Extracellular matrix protein 1;
DE AltName: Full=Secretory component p85;
DE Flags: Precursor;
GN Name=ECM1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-415.
RX PubMed=9367673; DOI=10.1006/geno.1997.4918;
RA Smits P., Ni J., Feng P., Wauters J., van Hul W., Boutaibi M.E.,
RA Dillon P.J., Merregaert J.;
RT "The human extracellular matrix gene 1 (ECM1): genomic structure, cDNA
RT cloning, expression pattern, and chromosomal localization.";
RL Genomics 45:487-495(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9501329; DOI=10.1016/s0945-053x(97)90017-2;
RA Johnson M.R., Wilkin D.J., Vos H.L., Ortiz de Luna R.I., Dehejia A.M.,
RA Polymeropoulos M.H., Francomano C.A.;
RT "Characterization of the human extracellular matrix protein 1 gene on
RT chromosome 1q21.";
RL Matrix Biol. 16:289-292(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANTS
RP MET-130 AND SER-415.
RC TISSUE=Synovial cell, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-130
RP AND SER-415.
RC TISSUE=Skin;
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 [7]
RP FUNCTION IN BONE FORMATION.
RX PubMed=11165938; DOI=10.1016/s8756-3282(00)00428-2;
RA Deckers M.M.L., Smits P., Karperien M., Ni J., Tylzanowski P., Feng P.,
RA Parmelee D., Zhang J., Bouffard E., Gentz R., Loewik C.W.G.M.,
RA Merregaert J.;
RT "Recombinant human extracellular matrix protein 1 inhibits alkaline
RT phosphatase activity and mineralization of mouse embryonic metatarsals in
RT vitro.";
RL Bone 28:14-20(2001).
RN [8]
RP FUNCTION IN ANGIOGENESIS, AND TISSUE SPECIFICITY.
RX PubMed=11292659; DOI=10.1096/fj.99-0934com;
RA Han Z., Ni J., Smits P., Underhill C.B., Xie B., Chen Y., Liu N.,
RA Tylzanowski P., Parmelee D., Feng P., Ding I., Gao F., Gentz R.,
RA Huylebroeck D., Merregaert J., Zhang L.;
RT "Extracellular matrix protein 1 (ECM1) has angiogenic properties and is
RT expressed by breast tumor cells.";
RL FASEB J. 15:988-994(2001).
RN [9]
RP INVOLVEMENT IN LIPOID PROTEINOSIS.
RX PubMed=11929856; DOI=10.1093/hmg/11.7.833;
RA Hamada T., McLean W.H.I., Ramsay M., Ashton G.H.S., Nanda A., Jenkins T.,
RA Edelstein I., South A.P., Bleck O., Wessagowit V., Mallipeddi R.,
RA Orchard G.E., Wan H., Dopping-Hepenstal P.J.C., Mellerio J.E.,
RA Whittock N.V., Munro C.S., van Steensel M.A.M., Steijlen P.M., Ni J.,
RA Zhang L., Hashimoto T., Eady R.A.E., McGrath J.A.;
RT "Lipoid proteinosis maps to 1q21 and is caused by mutations in the
RT extracellular matrix protein 1 gene (ECM1).";
RL Hum. Mol. Genet. 11:833-840(2002).
RN [10]
RP INTERACTION WITH HSPG2, AND TISSUE SPECIFICITY.
RX PubMed=12604605; DOI=10.1074/jbc.m210529200;
RA Mongiat M., Fu J., Oldershaw R., Greenhalgh R., Gown A.M., Iozzo R.V.;
RT "Perlecan protein core interacts with extracellular matrix protein 1
RT (ECM1), a glycoprotein involved in bone formation and angiogenesis.";
RL J. Biol. Chem. 278:17491-17499(2003).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-444.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP INTERACTION WITH MMP9, AND FUNCTION.
RX PubMed=16512877; DOI=10.1111/j.0906-6705.2006.00409.x;
RA Fujimoto N., Terlizzi J., Aho S., Brittingham R., Fertala A., Oyama N.,
RA McGrath J.A., Uitto J.;
RT "Extracellular matrix protein 1 inhibits the activity of matrix
RT metalloproteinase 9 through high-affinity protein/protein interactions.";
RL Exp. Dermatol. 15:300-307(2006).
RN [13]
RP INTERACTION WITH EFEMP1 AND LAMB3.
RX PubMed=19275936; DOI=10.1016/j.matbio.2009.02.003;
RA Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K.,
RA Sasaki T., Oyama N., Merregaert J.;
RT "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through
RT its serum albumin subdomain-like 2 domain.";
RL Matrix Biol. 28:160-169(2009).
RN [14]
RP GLYCOSYLATION AT ASN-444.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP VARIANT LIP ILE-167, AND VARIANTS MET-130 AND SER-415.
RX PubMed=12603844; DOI=10.1046/j.1523-1747.2003.12073.x;
RA Hamada T., Wessagowit V., South A.P., Ashton G.H.S., Chan I., Oyama N.,
RA Siriwattana A., Jewhasuchin P., Charuwichitratana S., Thappa D.M.,
RA Lenane P., Krafchik B., Kulthanan K., Shimizu H., Kaya T.I., Erdal M.E.,
RA Paradisi M., Paller A.S., Seishima M., Hashimoto T., McGrath J.A.;
RT "Extracellular matrix protein 1 gene (ECM1) mutations in lipoid proteinosis
RT and genotype-phenotype correlation.";
RL J. Invest. Dermatol. 120:345-350(2003).
CC -!- FUNCTION: Involved in endochondral bone formation as negative regulator
CC of bone mineralization. Stimulates the proliferation of endothelial
CC cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity.
CC {ECO:0000269|PubMed:11165938, ECO:0000269|PubMed:11292659,
CC ECO:0000269|PubMed:16512877}.
CC -!- SUBUNIT: Interacts (via C-terminus) with HSPG2 (via C-terminus).
CC Interacts with EFEMP1/FBLN3 and LAMB3. Interacts with MMP9.
CC {ECO:0000269|PubMed:12604605, ECO:0000269|PubMed:16512877,
CC ECO:0000269|PubMed:19275936}.
CC -!- INTERACTION:
CC Q16610; Q9NQ94: A1CF; NbExp=3; IntAct=EBI-947964, EBI-2809489;
CC Q16610; Q08043: ACTN3; NbExp=3; IntAct=EBI-947964, EBI-2880652;
CC Q16610; O75934: BCAS2; NbExp=3; IntAct=EBI-947964, EBI-1050106;
CC Q16610; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-947964, EBI-8643161;
CC Q16610; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-947964, EBI-3867333;
CC Q16610; Q86UW9: DTX2; NbExp=3; IntAct=EBI-947964, EBI-740376;
CC Q16610; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-947964, EBI-744099;
CC Q16610; P48023: FASLG; NbExp=3; IntAct=EBI-947964, EBI-495538;
CC Q16610; O75344: FKBP6; NbExp=3; IntAct=EBI-947964, EBI-744771;
CC Q16610; O43559: FRS3; NbExp=3; IntAct=EBI-947964, EBI-725515;
CC Q16610; O75603: GCM2; NbExp=3; IntAct=EBI-947964, EBI-10188645;
CC Q16610; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-947964, EBI-11975289;
CC Q16610; O95872: GPANK1; NbExp=3; IntAct=EBI-947964, EBI-751540;
CC Q16610; P28799: GRN; NbExp=3; IntAct=EBI-947964, EBI-747754;
CC Q16610; P31273: HOXC8; NbExp=3; IntAct=EBI-947964, EBI-1752118;
CC Q16610; P16144-2: ITGB4; NbExp=3; IntAct=EBI-947964, EBI-11051601;
CC Q16610; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-947964, EBI-6426443;
CC Q16610; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-947964, EBI-11974251;
CC Q16610; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-947964, EBI-1043191;
CC Q16610; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-947964, EBI-10246607;
CC Q16610; O14910: LIN7A; NbExp=3; IntAct=EBI-947964, EBI-2513988;
CC Q16610; P61968: LMO4; NbExp=3; IntAct=EBI-947964, EBI-2798728;
CC Q16610; Q13064: MKRN3; NbExp=3; IntAct=EBI-947964, EBI-2340269;
CC Q16610; P31323: PRKAR2B; NbExp=3; IntAct=EBI-947964, EBI-2930670;
CC Q16610; Q96NU1: SAMD11; NbExp=3; IntAct=EBI-947964, EBI-14067109;
CC Q16610; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-947964, EBI-744081;
CC Q16610; P09234: SNRPC; NbExp=3; IntAct=EBI-947964, EBI-766589;
CC Q16610; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-947964, EBI-741480;
CC Q16610; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-947964, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=1a;
CC IsoId=Q16610-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=Q16610-2; Sequence=VSP_036414;
CC Name=3;
CC IsoId=Q16610-3; Sequence=VSP_036411, VSP_036412, VSP_036415,
CC VSP_036416;
CC Name=4;
CC IsoId=Q16610-4; Sequence=VSP_036413;
CC -!- TISSUE SPECIFICITY: Expressed in breast cancer tissues. Little or no
CC expression observed in normal breast tissues. Expressed in skin; wide
CC expression is observed throughout the dermis with minimal expression in
CC the epidermis. {ECO:0000269|PubMed:11292659,
CC ECO:0000269|PubMed:12604605}.
CC -!- DISEASE: Lipoid proteinosis (LiP) [MIM:247100]: Rare autosomal
CC recessive disorder characterized by generalized thickening of skin,
CC mucosae and certain viscera. Classical features include beaded eyelid
CC papules and laryngeal infiltration leading to hoarseness.
CC Histologically, there is widespread deposition of hyaline material and
CC disruption/reduplication of basement membrane.
CC {ECO:0000269|PubMed:11929856, ECO:0000269|PubMed:12603844}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ECM1ID40398ch1q21.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U68186; AAB88081.1; -; mRNA.
DR EMBL; U68187; AAB88082.1; -; mRNA.
DR EMBL; U65932; AAB05933.1; -; mRNA.
DR EMBL; U65938; AAB05934.1; -; Genomic_DNA.
DR EMBL; U65933; AAB05934.1; JOINED; Genomic_DNA.
DR EMBL; U65934; AAB05934.1; JOINED; Genomic_DNA.
DR EMBL; U65935; AAB05934.1; JOINED; Genomic_DNA.
DR EMBL; U65936; AAB05934.1; JOINED; Genomic_DNA.
DR EMBL; U65937; AAB05934.1; JOINED; Genomic_DNA.
DR EMBL; AK097046; BAG53412.1; -; mRNA.
DR EMBL; AK292435; BAF85124.1; -; mRNA.
DR EMBL; AK301369; BAG62911.1; -; mRNA.
DR EMBL; AK302279; BAG63622.1; -; mRNA.
DR EMBL; AL356356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53544.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53545.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53546.1; -; Genomic_DNA.
DR EMBL; BC023505; AAH23505.1; -; mRNA.
DR CCDS; CCDS55632.1; -. [Q16610-4]
DR CCDS; CCDS953.1; -. [Q16610-1]
DR CCDS; CCDS954.1; -. [Q16610-2]
DR RefSeq; NP_001189787.1; NM_001202858.1. [Q16610-4]
DR RefSeq; NP_004416.2; NM_004425.3. [Q16610-1]
DR RefSeq; NP_073155.2; NM_022664.2. [Q16610-2]
DR AlphaFoldDB; Q16610; -.
DR BioGRID; 108222; 153.
DR IntAct; Q16610; 73.
DR MINT; Q16610; -.
DR STRING; 9606.ENSP00000358045; -.
DR GlyConnect; 1228; 20 N-Linked glycans (4 sites), 1 O-Linked glycan (1 site).
DR GlyGen; Q16610; 12 sites, 21 N-linked glycans (4 sites), 3 O-linked glycans (6 sites).
DR iPTMnet; Q16610; -.
DR PhosphoSitePlus; Q16610; -.
DR BioMuta; ECM1; -.
DR DMDM; 48429255; -.
DR EPD; Q16610; -.
DR jPOST; Q16610; -.
DR MassIVE; Q16610; -.
DR MaxQB; Q16610; -.
DR PaxDb; Q16610; -.
DR PeptideAtlas; Q16610; -.
DR PRIDE; Q16610; -.
DR ProteomicsDB; 60944; -. [Q16610-1]
DR ProteomicsDB; 60945; -. [Q16610-2]
DR ProteomicsDB; 60946; -. [Q16610-3]
DR ProteomicsDB; 60947; -. [Q16610-4]
DR Antibodypedia; 20285; 509 antibodies from 36 providers.
DR DNASU; 1893; -.
DR Ensembl; ENST00000346569.6; ENSP00000271630.6; ENSG00000143369.15. [Q16610-2]
DR Ensembl; ENST00000369047.9; ENSP00000358043.4; ENSG00000143369.15. [Q16610-1]
DR Ensembl; ENST00000369049.8; ENSP00000358045.4; ENSG00000143369.15. [Q16610-4]
DR GeneID; 1893; -.
DR KEGG; hsa:1893; -.
DR MANE-Select; ENST00000369047.9; ENSP00000358043.4; NM_004425.4; NP_004416.2.
DR UCSC; uc001eus.4; human. [Q16610-1]
DR CTD; 1893; -.
DR DisGeNET; 1893; -.
DR GeneCards; ECM1; -.
DR GeneReviews; ECM1; -.
DR HGNC; HGNC:3153; ECM1.
DR HPA; ENSG00000143369; Tissue enhanced (epididymis, esophagus).
DR MalaCards; ECM1; -.
DR MIM; 247100; phenotype.
DR MIM; 602201; gene.
DR neXtProt; NX_Q16610; -.
DR OpenTargets; ENSG00000143369; -.
DR Orphanet; 530; Lipoid proteinosis.
DR PharmGKB; PA27598; -.
DR VEuPathDB; HostDB:ENSG00000143369; -.
DR eggNOG; ENOG502RY3T; Eukaryota.
DR GeneTree; ENSGT00390000006215; -.
DR HOGENOM; CLU_038587_0_0_1; -.
DR InParanoid; Q16610; -.
DR OMA; QTNCFNI; -.
DR OrthoDB; 509393at2759; -.
DR PhylomeDB; Q16610; -.
DR TreeFam; TF330786; -.
DR PathwayCommons; Q16610; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q16610; -.
DR SIGNOR; Q16610; -.
DR BioGRID-ORCS; 1893; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; ECM1; human.
DR GeneWiki; ECM1; -.
DR GenomeRNAi; 1893; -.
DR Pharos; Q16610; Tbio.
DR PRO; PR:Q16610; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16610; protein.
DR Bgee; ENSG00000143369; Expressed in lower esophagus mucosa and 176 other tissues.
DR ExpressionAtlas; Q16610; baseline and differential.
DR Genevisible; Q16610; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005134; F:interleukin-2 receptor binding; IEA:Ensembl.
DR GO; GO:0043236; F:laminin binding; IPI:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR GO; GO:0003416; P:endochondral bone growth; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IDA:UniProtKB.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0030500; P:regulation of bone mineralization; IBA:GO_Central.
DR GO; GO:2000404; P:regulation of T cell migration; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0002828; P:regulation of type 2 immune response; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR008605; ECM1.
DR InterPro; IPR020858; Serum_albumin-like.
DR PANTHER; PTHR16776; PTHR16776; 1.
DR Pfam; PF05782; ECM1; 1.
DR SUPFAM; SSF48552; SSF48552; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Biomineralization; Disease variant;
KW Extracellular matrix; Glycoprotein; Mineral balance; Osteogenesis;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:Q62894"
FT CHAIN 20..540
FT /note="Extracellular matrix protein 1"
FT /id="PRO_0000021146"
FT REPEAT 150..279
FT /note="1"
FT REPEAT 283..405
FT /note="2"
FT REGION 41..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..405
FT /note="2 X approximate repeats"
FT REGION 515..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036411"
FT VAR_SEQ 72..81
FT /note="QSQVQPPPSQ -> MALPLRDRVK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036412"
FT VAR_SEQ 74
FT /note="Q -> GKEGRGPRPHSQPWLGERVGCSHIPPSI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036413"
FT VAR_SEQ 237..361
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9367673"
FT /id="VSP_036414"
FT VAR_SEQ 237..241
FT /note="WEEAM -> VRLGS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036415"
FT VAR_SEQ 242..540
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036416"
FT VARIANT 130
FT /note="T -> M (in dbSNP:rs3737240)"
FT /evidence="ECO:0000269|PubMed:12603844,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_018690"
FT VARIANT 167
FT /note="F -> I (in LiP; dbSNP:rs121909116)"
FT /evidence="ECO:0000269|PubMed:12603844"
FT /id="VAR_018691"
FT VARIANT 415
FT /note="G -> S (in dbSNP:rs13294)"
FT /evidence="ECO:0000269|PubMed:12603844,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9367673"
FT /id="VAR_014761"
FT VARIANT 528
FT /note="G -> R (in dbSNP:rs1050901)"
FT /id="VAR_014762"
FT VARIANT 535
FT /note="S -> F (in dbSNP:rs1050904)"
FT /id="VAR_014763"
FT CONFLICT 78..84
FT /note="Missing (in Ref. 3; BAG63622)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="Q -> R (in Ref. 3; BAF85124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 60674 MW; EA575895CDE068BE CRC64;
MGTTARAALV LTYLAVASAA SEGGFTATGQ RQLRPEHFQE VGYAAPPSPP LSRSLPMDHP
DSSQHGPPFE GQSQVQPPPS QEATPLQQEK LLPAQLPAEK EVGPPLPQEA VPLQKELPSL
QHPNEQKEGT PAPFGDQSHP EPESWNAAQH CQQDRSQGGW GHRLDGFPPG RPSPDNLNQI
CLPNRQHVVY GPWNLPQSSY SHLTRQGETL NFLEIGYSRC CHCRSHTNRL ECAKLVWEEA
MSRFCEAEFS VKTRPHWCCT RQGEARFSCF QEEAPQPHYQ LRACPSHQPD ISSGLELPFP
PGVPTLDNIK NICHLRRFRS VPRNLPATDP LQRELLALIQ LEREFQRCCR QGNNHTCTWK
AWEDTLDKYC DREYAVKTHH HLCCRHPPSP TRDECFARRA PYPNYDRDIL TIDIGRVTPN
LMGHLCGNQR VLTKHKHIPG LIHNMTARCC DLPFPEQACC AEEEKLTFIN DLCGPRRNIW
RDPALCCYLS PGDEQVNCFN INYLRNVALV SGDTENAKGQ GEQGSTGGTN ISSTSEPKEE
