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   24-JAN-2024, entry version 155.
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 surrounding connective tissues of
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   GlyCosmos; Q61508; 3 sites, No reported glycans.
DR   GlyGen; Q61508; 3 sites.
DR   iPTMnet; Q61508; -.
DR   PhosphoSitePlus; Q61508; -.
DR   SwissPalm; Q61508; -.
DR   CPTAC; non-CPTAC-3536; -.
DR   MaxQB; Q61508; -.
DR   PaxDb; 10090-ENSMUSP00000112665; -.
DR   PeptideAtlas; Q61508; -.
DR   ProteomicsDB; 277755; -. [Q61508-1]
DR   ProteomicsDB; 277756; -. [Q61508-2]
DR   Pumba; Q61508; -.
DR   Antibodypedia; 20285; 576 antibodies from 36 providers.
DR   DNASU; 13601; -.
DR   Ensembl; ENSMUST00000117507.10; ENSMUSP00000112665.3; ENSMUSG00000028108.17. [Q61508-1]
DR   GeneID; 13601; -.
DR   KEGG; mmu:13601; -.
DR   UCSC; uc008qko.2; mouse. [Q61508-1]
DR   AGR; MGI:103060; -.
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; CCRCRSH; -.
DR   OrthoDB; 4577436at2759; -.
DR   PhylomeDB; Q61508; -.
DR   TreeFam; TF330786; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   BioGRID-ORCS; 13601; 1 hit in 80 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 63 other cell types or tissues.
DR   ExpressionAtlas; Q61508; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005134; F:interleukin-2 receptor binding; IPI:MGI.
DR   GO; GO:0002020; F:protease 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   Gene3D; 1.10.246.10; -; 2.
DR   InterPro; IPR008605; ECM1.
DR   InterPro; IPR020858; Serum_albumin-like.
DR   PANTHER; PTHR16776; EXTRACELLULAR MATRIX PROTEIN 1; 1.
DR   PANTHER; PTHR16776:SF3; EXTRACELLULAR MATRIX PROTEIN 1; 1.
DR   Pfam; PF05782; ECM1; 1.
DR   SUPFAM; SSF48552; Serum albumin-like; 2.
DR   Genevisible; Q61508; MM.
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
//