ECM1_MOUSE
ID ECM1_MOUSE Reviewed; 559 AA.
AC Q61508; Q3U5Q5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Extracellular matrix protein 1;
DE AltName: Full=Secretory component p85;
DE Flags: Precursor;
GN Name=Ecm1;
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 LONG AND SHORT), AND PROTEIN SEQUENCE
RP OF 20-37; 71-83 AND 109-112.
RC STRAIN=BALB/cJ;
RX PubMed=7608209; DOI=10.1074/jbc.270.27.16385;
RA Bhalerao J., Tylzanowski P., Filie J.D., Kozak C.A., Merregaert J.;
RT "Molecular cloning, characterization, and genetic mapping of the cDNA
RT coding for a novel secretory protein of mouse. Demonstration of alternative
RT splicing in skin and cartilage.";
RL J. Biol. Chem. 270:16385-16394(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY.
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-463 AND ASN-535.
RC TISSUE=Epidermis;
RX PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA Nishimura S.;
RT "High throughput quantitative glycomics and glycoform-focused proteomics of
RT murine dermis and epidermis.";
RL Mol. Cell. Proteomics 4:1977-1989(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
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: 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with HSPG2 (via C-terminus).
CC Interacts with EFEMP1/FBLN3 and LAMB3. Interacts with MMP9.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q61508-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q61508-2; Sequence=VSP_004230;
CC -!- TISSUE SPECIFICITY: Expressed in the connective tissues surronding
CC developing long bones, but not in the cartilage. The long isoform is
CC expressed in a number of tissues including liver, heart and lungs. The
CC short isoform is expressed in skin and cartilage-containing tissues
CC such as tail and front paw. No expression is found in brain.
CC {ECO:0000269|PubMed:11165938}.
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DR EMBL; L33416; AAA37535.1; -; mRNA.
DR EMBL; AK153009; BAE31648.1; -; mRNA.
DR EMBL; AK153471; BAE32022.1; -; mRNA.
DR CCDS; CCDS17619.1; -. [Q61508-1]
DR RefSeq; NP_031925.2; NM_007899.2. [Q61508-1]
DR AlphaFoldDB; Q61508; -.
DR BioGRID; 199366; 4.
DR IntAct; Q61508; 1.
DR STRING; 10090.ENSMUSP00000112665; -.
DR GlyGen; Q61508; 3 sites.
DR iPTMnet; Q61508; -.
DR PhosphoSitePlus; Q61508; -.
DR SwissPalm; Q61508; -.
DR CPTAC; non-CPTAC-3536; -.
DR MaxQB; Q61508; -.
DR PaxDb; Q61508; -.
DR PeptideAtlas; Q61508; -.
DR PRIDE; Q61508; -.
DR ProteomicsDB; 277755; -. [Q61508-1]
DR ProteomicsDB; 277756; -. [Q61508-2]
DR Antibodypedia; 20285; 509 antibodies from 36 providers.
DR DNASU; 13601; -.
DR Ensembl; ENSMUST00000117507; ENSMUSP00000112665; ENSMUSG00000028108. [Q61508-1]
DR GeneID; 13601; -.
DR KEGG; mmu:13601; -.
DR UCSC; uc008qko.2; mouse. [Q61508-1]
DR CTD; 1893; -.
DR MGI; MGI:103060; Ecm1.
DR VEuPathDB; HostDB:ENSMUSG00000028108; -.
DR eggNOG; ENOG502RY3T; Eukaryota.
DR GeneTree; ENSGT00390000006215; -.
DR HOGENOM; CLU_038587_0_0_1; -.
DR InParanoid; Q61508; -.
DR OMA; QTNCFNI; -.
DR OrthoDB; 509393at2759; -.
DR PhylomeDB; Q61508; -.
DR TreeFam; TF330786; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 13601; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Ecm1; mouse.
DR PRO; PR:Q61508; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61508; protein.
DR Bgee; ENSMUSG00000028108; Expressed in esophagus and 60 other tissues.
DR ExpressionAtlas; Q61508; baseline and differential.
DR Genevisible; Q61508; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005134; F:interleukin-2 receptor binding; IPI:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0003416; P:endochondral bone growth; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0010466; P:negative regulation of peptidase activity; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:MGI.
DR GO; GO:2000404; P:regulation of T cell migration; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0002828; P:regulation of type 2 immune response; IMP:MGI.
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;
KW Direct protein sequencing; Extracellular matrix; Glycoprotein;
KW Mineral balance; Osteogenesis; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:7608209"
FT CHAIN 20..559
FT /note="Extracellular matrix protein 1"
FT /id="PRO_0000021147"
FT REPEAT 170..298
FT /note="1"
FT REPEAT 302..424
FT /note="2"
FT REGION 170..424
FT /note="2 X approximate repeats"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62894"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT VAR_SEQ 256..380
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7608209"
FT /id="VSP_004230"
FT CONFLICT 53
FT /note="P -> L (in Ref. 1; AAA37535)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="R -> P (in Ref. 1; AAA37535)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="I -> V (in Ref. 1; AAA37535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 62832 MW; F5282E5D7B78E696 CRC64;
MGTVSRAALI LACLALASAA SEGAFKASDQ REMTPERLFQ HLHEVGYAAP PSPPQTRRLR
VDHSVTSLHD PPLFEEQREV QPPSSPEDIP VYEEDWPTFL NPNVDKAGPA VPQEAIPLQK
EQPPPQVHIE QKEIDPPAQP QEEIVQKEVK PHTLAGQLPP EPRTWNPARH CQQGRRGVWG
HRLDGFPPGR PSPDNLKQIC LPERQHVIYG PWNLPQTGYS HLSRQGETLN VLETGYSRCC
RCRSDTNRLD CLKLVWEDAM TQFCEAEFSV KTRPHLCCRL RGEERFSCFQ KEAPRPDYLL
RPCPVHQNGM SSGPQLPFPP GLPTPDNVKN ICLLRRFRAV PRNLPATDAI QRQLQALTRL
ETEFQRCCRQ GHNHTCTWKA WEGTLDGYCE RELAIKTHPH SCCHYPPSPA RDECFAHLAP
YPNYDRDILT LDLSRVTPNL MGQLCGSGRV LSKHKQIPGL IQNMTIRCCE LPYPEQACCG
EEEKLAFIEN LCGPRRNSWK DPALCCDLSP EDKQINCFNT NYLRNVALVA GDTGNATGLG
EQGPTRGTDA NPAPGSKEE
