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Protein

Matrilin-3

Gene

Matn3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.1 Publication

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-3000178. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrilin-3
Gene namesi
Name:Matn3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1328350. Matn3.

Subcellular locationi

GO - Cellular componenti

  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 481454Matrilin-3PRO_0000007658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi263 ↔ 274PROSITE-ProRule annotation
Disulfide bondi270 ↔ 284PROSITE-ProRule annotation
Disulfide bondi286 ↔ 299PROSITE-ProRule annotation
Disulfide bondi305 ↔ 316PROSITE-ProRule annotation
Disulfide bondi312 ↔ 326PROSITE-ProRule annotation
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi328 ↔ 341PROSITE-ProRule annotation
Disulfide bondi347 ↔ 358PROSITE-ProRule annotation
Disulfide bondi354 ↔ 368PROSITE-ProRule annotation
Disulfide bondi370 ↔ 383PROSITE-ProRule annotation
Disulfide bondi389 ↔ 400PROSITE-ProRule annotation
Disulfide bondi396 ↔ 410PROSITE-ProRule annotation
Disulfide bondi412 ↔ 425PROSITE-ProRule annotation
Modified residuei436 – 4361Phosphoserine; by FAM20CBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO35701.
PaxDbiO35701.
PRIDEiO35701.

PTM databases

iPTMnetiO35701.
PhosphoSiteiO35701.

Expressioni

Tissue specificityi

Strongly expressed in growing skeletal tissue such as epiphyseal growth plate or in bone undergoing growth and remodeling. In the bone, actively synthesized in osteoblasts and osteocytes. Expressed in cartilage of sternum, femur, vertebrae, trachea, articular and epiphyseal cartilage, cartilage of developing bones and bones.

Developmental stagei

The earliest expression could be detected in a 12.5 dpc embryo in the cartilage anlage of the developing bones. At 14.5 dpc the primordial skeleton shows a strong expression. At birth present in the developing occipital bones, bones of the nasal cavity, manubrium and corpus of sternum as well as in the cartilage plates of trachea. At no stage of development detected in extraskeletal tissues.

Gene expression databases

BgeeiO35701.
CleanExiMM_MATN3.
GenevisibleiO35701. MM.

Interactioni

Subunit structurei

Can form homooligomers (monomers, dimers, trimers and tetramers) and heterooligomers with matrilin-1. Interacts with COMP (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020899.

Structurei

3D structure databases

ProteinModelPortaliO35701.
SMRiO35701. Positions 77-240, 280-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 253176VWFAPROSITE-ProRule annotationAdd
BLAST
Domaini259 – 30042EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini301 – 34242EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini343 – 38442EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini385 – 42642EGF-like 4PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili451 – 47525Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG4111IJ5. LUCA.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000263415.
HOVERGENiHBG056906.
InParanoidiO35701.
KOiK19467.
OMAiRFQETFC.
OrthoDBiEOG7X9G6P.
TreeFamiTF330078.

Family and domain databases

Gene3Di1.20.5.30. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR030765. Matrilin-3/4.
IPR019466. Matrilin_coiled-coil_trimer.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR11132:SF50. PTHR11132:SF50. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF10393. Matrilin_ccoil. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
SM01279. Matrilin_ccoil. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS50234. VWFA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35701-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSAPLRHL PGLLLLLWPL LLLPSLAAPG RLARASVRRL GTRVPGGSPG
60 70 80 90 100
HLSALATSTR APYSGGRGAG VCKSRPLDLV FIIDSSRSVR PLEFTKVKTF
110 120 130 140 150
VSRIIDTLDI GATDTRVAVV NYASTVKIEF QLNTYSDKQA LKQAVARITP
160 170 180 190 200
LSTGTMSGLA IQTAMEEAFT VEAGARGPMS NIPKVAIIVT DGRPQDQVNE
210 220 230 240 250
VAARARASGI ELYAVGVDRA DMESLKMMAS KPLEEHVFYV ETYGVIEKLS
260 270 280 290 300
ARFQETFCAL DQCMLGTHQC QHVCVSDGDG KHHCECSQGY TLNADGKTCS
310 320 330 340 350
AIDKCALSTH GCEQICVNDR NGSYHCECYG GYALNADRRT CAALDKCASG
360 370 380 390 400
THGCQHICVN DGAGSHHCEC FEGYTLNADK KTCSVRNKCA LGTHGCQHIC
410 420 430 440 450
VSDGAVAYHC DCFPGYTLND DKKTCSDIEE ARSLISIEDA CGCGATLAFQ
460 470 480
EKVSSHLQKL NTKLDNILKK LKVTEYGQVH R
Length:481
Mass (Da):51,845
Last modified:July 27, 2011 - v2
Checksum:iBC82B8A140344CBD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti317 – 3171V → I in CAA71532 (PubMed:9287130).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10521 mRNA. Translation: CAA71532.1.
AJ242929
, AJ242930, AJ242931, AJ242932, AJ242933, AJ242934, AJ242935, AJ242936 Genomic DNA. Translation: CAB72265.1.
AK048456 mRNA. Translation: BAC33343.1.
CCDSiCCDS25806.1.
RefSeqiNP_034900.4. NM_010770.4.
UniGeneiMm.42226.

Genome annotation databases

EnsembliENSMUST00000020899; ENSMUSP00000020899; ENSMUSG00000020583.
GeneIDi17182.
KEGGimmu:17182.
UCSCiuc007nag.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10521 mRNA. Translation: CAA71532.1.
AJ242929
, AJ242930, AJ242931, AJ242932, AJ242933, AJ242934, AJ242935, AJ242936 Genomic DNA. Translation: CAB72265.1.
AK048456 mRNA. Translation: BAC33343.1.
CCDSiCCDS25806.1.
RefSeqiNP_034900.4. NM_010770.4.
UniGeneiMm.42226.

3D structure databases

ProteinModelPortaliO35701.
SMRiO35701. Positions 77-240, 280-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020899.

PTM databases

iPTMnetiO35701.
PhosphoSiteiO35701.

Proteomic databases

MaxQBiO35701.
PaxDbiO35701.
PRIDEiO35701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020899; ENSMUSP00000020899; ENSMUSG00000020583.
GeneIDi17182.
KEGGimmu:17182.
UCSCiuc007nag.2. mouse.

Organism-specific databases

CTDi4148.
MGIiMGI:1328350. Matn3.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG4111IJ5. LUCA.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000263415.
HOVERGENiHBG056906.
InParanoidiO35701.
KOiK19467.
OMAiRFQETFC.
OrthoDBiEOG7X9G6P.
TreeFamiTF330078.

Enzyme and pathway databases

ReactomeiR-MMU-3000178. ECM proteoglycans.

Miscellaneous databases

NextBioi291502.
PROiO35701.
SOURCEiSearch...

Gene expression databases

BgeeiO35701.
CleanExiMM_MATN3.
GenevisibleiO35701. MM.

Family and domain databases

Gene3Di1.20.5.30. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR030765. Matrilin-3/4.
IPR019466. Matrilin_coiled-coil_trimer.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR11132:SF50. PTHR11132:SF50. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF10393. Matrilin_ccoil. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
SM01279. Matrilin_ccoil. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of matrilin-3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand factor."
    Wagener R., Kobbe B., Paulsson M.
    FEBS Lett. 413:129-134(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  2. "Structure and mapping of the mouse matrilin-3 gene (Matn3), a member of a gene family containing a U12-type AT-AC intron."
    Wagener R., Kobbe B., Aszodi A., Liu Z., Beier D.R., Paulsson M.
    Mamm. Genome 11:85-90(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
    Tissue: Liver.
  3. "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.
    , 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: Head.
  4. "Molecular structure and tissue distribution of matrilin-3, a filament-forming extracellular matrix protein expressed during skeletal development."
    Klatt A.R., Nitsche D.P., Kobbe B., Morgelin M., Paulsson M., Wagener R.
    J. Biol. Chem. 275:3999-4006(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, CHARACTERIZATION, FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMATN3_MOUSE
AccessioniPrimary (citable) accession number: O35701
Secondary accession number(s): Q543Q2, Q9JHM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.