ECM1_RAT
ID ECM1_RAT Reviewed; 562 AA.
AC Q62894; Q5U2S9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Extracellular matrix protein 1;
DE AltName: Full=Secretory component p85;
DE Flags: Precursor;
GN Name=Ecm1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 261-325.
RC STRAIN=Wistar Kyoto; TISSUE=Heart;
RA Csikos T., Gallinat S., Stoll M., Unger T.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
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.
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DR EMBL; BC085879; AAH85879.1; -; mRNA.
DR EMBL; U42581; AAA84385.1; -; mRNA.
DR RefSeq; NP_446334.1; NM_053882.1.
DR AlphaFoldDB; Q62894; -.
DR STRING; 10116.ENSRNOP00000028740; -.
DR GlyGen; Q62894; 3 sites.
DR iPTMnet; Q62894; -.
DR PhosphoSitePlus; Q62894; -.
DR PaxDb; Q62894; -.
DR PRIDE; Q62894; -.
DR GeneID; 116662; -.
DR KEGG; rno:116662; -.
DR UCSC; RGD:620357; rat.
DR CTD; 1893; -.
DR RGD; 620357; Ecm1.
DR VEuPathDB; HostDB:ENSRNOG00000021166; -.
DR eggNOG; ENOG502RY3T; Eukaryota.
DR HOGENOM; CLU_038587_0_0_1; -.
DR InParanoid; Q62894; -.
DR OMA; QTNCFNI; -.
DR OrthoDB; 509393at2759; -.
DR PhylomeDB; Q62894; -.
DR TreeFam; TF330786; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:Q62894; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000021166; Expressed in esophagus and 18 other tissues.
DR Genevisible; Q62894; RN.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0005134; F:interleukin-2 receptor binding; ISO:RGD.
DR GO; GO:0043236; F:laminin binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0003416; P:endochondral bone growth; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISO:RGD.
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; ISO:RGD.
DR GO; GO:2000404; P:regulation of T cell migration; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0002828; P:regulation of type 2 immune response; ISO:RGD.
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 Angiogenesis; Biomineralization; Extracellular matrix; Glycoprotein;
KW Mineral balance; Osteogenesis; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:26479776"
FT CHAIN 20..562
FT /note="Extracellular matrix protein 1"
FT /id="PRO_0000043411"
FT REPEAT 172..301
FT /note="1"
FT REPEAT 305..427
FT /note="2"
FT REGION 46..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..427
FT /note="2 X approximate repeats"
FT REGION 539..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 562 AA; 63249 MW; 41968A0E036EB64A CRC64;
MGTIRSSALI LACLALASAA SEGAFKVSDQ REMKPEHLFQ HLHEVGYAAP PSPPQTRRLQ
VHHSETSPHD PPLFEEQKEV QPPSSPEDIP VYEEEWLTFL NPNVGKVDPA LPQEAIPLQK
EQPPPRIPIE QKEIDPPVQH QEEIVQSRQK EEKPPTLTGQ HPPEPRTWNP ARHCQQGRRG
IWGHRLDGFP PGRPSPDNLK QICLPERQHV VYGPWNLPQT GYSHLSRQGE ALNLLETGYS
RCCRCRSDTN RLDCVKLVWE DAMTQFCEAE FSVKTRPHLC CKQRGEERFS CFQKEAPRPD
YLLRPCPIHQ TGISSGTQLP FPPGLPTPDN VKNICLLRRF RSVPRNLPAT DAIQRQLQAL
TRLETEFQRC CRQGHNHTCT WKAWEDTLDG YCDRELAIKT HPHSCCHYPP SPARDECFAH
LAPYPNYDRD LLTVDLSRVT PNLMDHLCGN GRVLSKHKQI PGLIQNMTVR CCELPYPEQA
CCGEEEKLAF IEDLCGPRRN SWKDPALCCT LSPGDKQANC FNTNYLRNVA LVAGDTGNAT
GLGQQGPTGG TNVGPAPGSK EE
