Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5FW85 (ECM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extracellular matrix protein 2
Alternative name(s):
Tenonectin
Gene names
Name:Ecm2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length670 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes matrix assembly and cell adhesiveness. Ref.3

Subunit structure

Interacts with numerous extracellular matrix proteins. Ref.3

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.3.

Developmental stage

At E16.5, present in periosteum of ribs. At P0, present in tendons connecting the scapula and humerus to muscles (at protein level). Ref.3

Sequence similarities

Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily.

Contains 13 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Contains 1 VWFC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 670651Extracellular matrix protein 2
PRO_0000287728

Regions

Domain96 – 15358VWFC
Domain278 – 31538LRRNT
Repeat339 – 35921LRR 1
Repeat365 – 38622LRR 2
Repeat387 – 40721LRR 3
Repeat410 – 43021LRR 4
Repeat436 – 45621LRR 5
Repeat457 – 47822LRR 6
Repeat481 – 50121LRR 7
Repeat507 – 52822LRR 8
Repeat529 – 54921LRR 9
Repeat553 – 57321LRR 10
Repeat580 – 60122LRR 11
Repeat603 – 62422LRR 12
Repeat632 – 65524LRR 13
Motif266 – 2683Cell attachment site Potential
Compositional bias181 – 26282Glu-rich

Amino acid modifications

Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Glycosylation4771N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5FW85 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 025BE9522417F5E3

FASTA67076,676
        10         20         30         40         50         60 
MKLAVLFCFI LLIVLQTDCE RGTRRQRRRM HQRRLRKSSS FHLRANRQLE VQQTTAAPDA 

        70         80         90        100        110        120 
RLPTANSDYS VEENIESLLS NLGVESSYSV LPGKKGYCFV KGMIMYNKAV WSPEPCTTCL 

       130        140        150        160        170        180 
CSNGRVLCDE TECHPKACPY TIKPEGECCP ICSDAEQESI NKLHKQVPPP QMEMDQVAIK 

       190        200        210        220        230        240 
EALQSEEDEE IAEGHKEHKK ETSVPTKIHG DGERTERKLR PEKEGRSAHQ PLYHGRREEE 

       250        260        270        280        290        300 
ESKEETEREG EEEEEEEEEE EEDAIRGDVF RMSSRVIPGT PRGRPRLPRS CSLSYRTISC 

       310        320        330        340        350        360 
VHADFTEIPP ITAPEVTNLE LVGNSIISIP DEAFNGLPNL ERLDLSRNNI TSSGIGPKAF 

       370        380        390        400        410        420 
KSLKKLMRLN MDGNNLVHIP SDLPSTLEEL KINDNNLQAI DEKSLSDLNQ LVTLELEGNN 

       430        440        450        460        470        480 
LSEINVDPLA FQSLESLSYL RLGRNKFRII PQGLPASTEE LYLENNQIEE ITEICFNHTR 

       490        500        510        520        530        540 
KITMIILRYN KIEESRIAPL AWINQENLES IDLSYNKLYH VPSYLPKSLL HLVLIGNQID 

       550        560        570        580        590        600 
RIPGYVFGHM QPGLEYLYLS FNRLSDDGVD LVSFYGAYHS LRELFLDHND FKSIPPGIQD 

       610        620        630        640        650        660 
MKALHFLRLN NNKIRNIHPE QICNAEEDED SALEHLHLEN NYIRTREISS YAFSCIRLYS 

       670 
SIVLKPQHIK 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: C57BL/6J.
Tissue: Hypothalamus and Medulla oblongata.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"Transcriptome-based systematic identification of extracellular matrix proteins."
Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C., Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D., Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J. expand/collapse author list , Sugiura N., Kimata K., Hayashizaki Y., Sekiguchi K.
Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK038812 mRNA. Translation: BAE20541.1.
AK040995 mRNA. Translation: BAE20587.1.
AK134746 mRNA. Translation: BAE22265.1.
BC065151 mRNA. Translation: AAH65151.1.
BC089559 mRNA. Translation: AAH89559.1.
RefSeqNP_001012324.1. NM_001012324.2.
UniGeneMm.386931.

3D structure databases

ProteinModelPortalQ5FW85.
SMRQ5FW85. Positions 94-152, 288-645.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ5FW85.

Proteomic databases

PRIDEQ5FW85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051504; ENSMUSP00000060402; ENSMUSG00000043631.
GeneID407800.
KEGGmmu:407800.
UCSCuc007qjl.1. mouse.

Organism-specific databases

CTD1842.
MGIMGI:3039578. Ecm2.

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00730000110250.
HOGENOMHOG000112319.
HOVERGENHBG031529.
InParanoidQ5FW85.
KOK08119.
OMAAVWSPKP.
OrthoDBEOG773XGV.
PhylomeDBQ5FW85.
TreeFamTF330031.

Gene expression databases

BgeeQ5FW85.
GenevestigatorQ5FW85.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR026906. LRR_5.
IPR001007. VWF_C.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF13306. LRR_5. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
SMARTSM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 13 hits.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio407225.
PROQ5FW85.
SOURCESearch...

Entry information

Entry nameECM2_MOUSE
AccessionPrimary (citable) accession number: Q5FW85
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2005
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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