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Q61508 (ECM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extracellular matrix protein 1
Alternative name(s):
Secretory component p85
Gene names
Name:Ecm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity By similarity.

Subunit structure

Interacts (via C-terminus) with HSPG2 (via C-terminus) By similarity. Interacts with EFEMP1/FBLN3 and LAMB3 By similarity. Interacts with MMP9 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Expressed in the connective tissues surronding developing long bones, but not in the cartilage. The long isoform isexpressed in a number of tissues including liver, heart and lungs. The short isoform isexpressed in skin and cartilage-containing tissues such as tail and front paw. No expression is found in brain. Ref.3

Ontologies

Keywords
   Biological processAngiogenesis
Biomineralization
Mineral balance
Osteogenesis
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

biomineral tissue development

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from mutant phenotype PubMed 21217760. Source: MGI

negative regulation of bone mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cytokine-mediated signaling pathway

Inferred from direct assay PubMed 21217760. Source: MGI

negative regulation of peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of T cell migration

Inferred from mutant phenotype PubMed 21217760. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21217760. Source: MGI

regulation of type 2 immune response

Inferred from mutant phenotype PubMed 21217760. Source: MGI

   Cellular_componentextracellular space

Inferred from direct assay PubMed 21217760Ref.1. Source: MGI

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioninterleukin-2 receptor binding

Inferred from physical interaction PubMed 21217760. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q61508-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q61508-2)

The sequence of this isoform differs from the canonical sequence as follows:
     256-380: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.1
Chain20 – 559540Extracellular matrix protein 1
PRO_0000021147

Regions

Repeat170 – 2981291
Repeat302 – 4241232
Region170 – 4242552 X approximate repeats

Amino acid modifications

Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) (high mannose) Ref.4
Glycosylation5351N-linked (GlcNAc...) (high mannose) Ref.4

Natural variations

Alternative sequence256 – 380125Missing in isoform Short.
VSP_004230

Experimental info

Sequence conflict531P → L in AAA37535. Ref.1
Sequence conflict2411R → P in AAA37535. Ref.1
Sequence conflict4661I → V in AAA37535. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F5282E5D7B78E696

FASTA55962,832
        10         20         30         40         50         60 
MGTVSRAALI LACLALASAA SEGAFKASDQ REMTPERLFQ HLHEVGYAAP PSPPQTRRLR 

        70         80         90        100        110        120 
VDHSVTSLHD PPLFEEQREV QPPSSPEDIP VYEEDWPTFL NPNVDKAGPA VPQEAIPLQK 

       130        140        150        160        170        180 
EQPPPQVHIE QKEIDPPAQP QEEIVQKEVK PHTLAGQLPP EPRTWNPARH CQQGRRGVWG 

       190        200        210        220        230        240 
HRLDGFPPGR PSPDNLKQIC LPERQHVIYG PWNLPQTGYS HLSRQGETLN VLETGYSRCC 

       250        260        270        280        290        300 
RCRSDTNRLD CLKLVWEDAM TQFCEAEFSV KTRPHLCCRL RGEERFSCFQ KEAPRPDYLL 

       310        320        330        340        350        360 
RPCPVHQNGM SSGPQLPFPP GLPTPDNVKN ICLLRRFRAV PRNLPATDAI QRQLQALTRL 

       370        380        390        400        410        420 
ETEFQRCCRQ GHNHTCTWKA WEGTLDGYCE RELAIKTHPH SCCHYPPSPA RDECFAHLAP 

       430        440        450        460        470        480 
YPNYDRDILT LDLSRVTPNL MGQLCGSGRV LSKHKQIPGL IQNMTIRCCE LPYPEQACCG 

       490        500        510        520        530        540 
EEEKLAFIEN LCGPRRNSWK DPALCCDLSP EDKQINCFNT NYLRNVALVA GDTGNATGLG 

       550 
EQGPTRGTDA NPAPGSKEE 

« Hide

Isoform Short [UniParc].

Checksum: FB6101384A5F7150
Show »

FASTA43448,357

References

« Hide 'large scale' references
[1]"Molecular cloning, characterization, and genetic mapping of the cDNA coding for a novel secretory protein of mouse. Demonstration of alternative splicing in skin and cartilage."
Bhalerao J., Tylzanowski P., Filie J.D., Kozak C.A., Merregaert J.
J. Biol. Chem. 270:16385-16394(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCE OF 20-37; 71-83 AND 109-112.
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Strain: C57BL/6J.
Tissue: Bone marrow.
[3]"Recombinant human extracellular matrix protein 1 inhibits alkaline phosphatase activity and mineralization of mouse embryonic metatarsals in vitro."
Deckers M.M.L., Smits P., Karperien M., Ni J., Tylzanowski P., Feng P., Parmelee D., Zhang J., Bouffard E., Gentz R., Loewik C.W.G.M., Merregaert J.
Bone 28:14-20(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-463 AND ASN-535.
Tissue: Epidermis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33416 mRNA. Translation: AAA37535.1.
AK153009 mRNA. Translation: BAE31648.1.
AK153471 mRNA. Translation: BAE32022.1.
RefSeqNP_031925.2. NM_007899.2.
UniGeneMm.3433.

3D structure databases

ProteinModelPortalQ61508.
SMRQ61508. Positions 213-299, 365-423, 440-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61508. 1 interaction.

PTM databases

PhosphoSiteQ61508.

Proteomic databases

PaxDbQ61508.
PRIDEQ61508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000117507; ENSMUSP00000112665; ENSMUSG00000028108. [Q61508-1]
GeneID13601.
KEGGmmu:13601.
UCSCuc008qko.2. mouse. [Q61508-1]

Organism-specific databases

CTD1893.
MGIMGI:103060. Ecm1.

Phylogenomic databases

eggNOGNOG45869.
GeneTreeENSGT00390000006215.
HOGENOMHOG000112317.
HOVERGENHBG005561.
InParanoidQ3U5Q5.
OMACCHYPPS.
OrthoDBEOG7KWSHX.
PhylomeDBQ61508.
TreeFamTF330786.

Gene expression databases

ArrayExpressQ61508.
BgeeQ61508.
CleanExMM_ECM1.
GenevestigatorQ61508.

Family and domain databases

InterProIPR008605. ECM1.
IPR020858. Serum_albumin-like.
[Graphical view]
PfamPF05782. ECM1. 1 hit.
[Graphical view]
SUPFAMSSF48552. SSF48552. 2 hits.
ProtoNetSearch...

Other

NextBio284228.
PROQ61508.
SOURCESearch...

Entry information

Entry nameECM1_MOUSE
AccessionPrimary (citable) accession number: Q61508
Secondary accession number(s): Q3U5Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot