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Protein

Matrilin-3

Gene

MATN3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.

GO - Molecular functioni

  • extracellular matrix structural constituent Source: ProtInc

GO - Biological processi

  • chondrocyte differentiation Source: InterPro
  • extracellular matrix organization Source: Reactome
  • skeletal system development Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrilin-3
Gene namesi
Name:MATN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6909. MATN3.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Multiple epiphyseal dysplasia 5 (EDM5)7 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal. Multiple epiphyseal dysplasia type 5 is relatively mild and clinically variable. It is primarily characterized by delayed and irregular ossification of the epiphyses and early-onset osteoarthritis.

See also OMIM:607078
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701R → H in EDM5. 1 Publication
VAR_054807
Natural varianti105 – 1051F → S in EDM5. 1 Publication
VAR_020844
Natural varianti120 – 1201T → M in EDM5; retained and accumulates within the cell. 4 Publications
VAR_019882
Natural varianti121 – 1211R → W in EDM5; retained and accumulates within the cell. 5 Publications
VAR_013691
Natural varianti128 – 1281A → P in EDM5; bilateral hereditary microepiphyseal dysplasia. 1 Publication
VAR_019883
Natural varianti134 – 1341E → K in EDM5; retained and accumulates within the cell. 2 Publications
VAR_019884
Natural varianti171 – 1766Missing in EDM5. 1 Publication
VAR_066830
Natural varianti173 – 1731A → D in EDM5. 1 Publication
VAR_066831
Natural varianti192 – 1921I → N in EDM5; retained and accumulates within the cell. 2 Publications
VAR_019885
Natural varianti194 – 1941V → D in EDM5; retained and accumulates within the cell. 2 Publications
VAR_013692
Natural varianti195 – 1951T → K in EDM5. 2 Publications
VAR_054808
Natural varianti209 – 2091R → P in EDM5. 1 Publication
VAR_066832
Natural varianti218 – 2181Y → N in EDM5. 2 Publications
VAR_054809
Natural varianti219 – 2191A → D in EDM5; retained and accumulates within the cell. 3 Publications
Corresponds to variant rs28939677 [ dbSNP | Ensembl ].
VAR_019886
Natural varianti231 – 2311K → N in EDM5. 1 Publication
VAR_066833
Natural varianti245 – 2451V → M in EDM5. 1 Publication
Corresponds to variant rs182164052 [ dbSNP | Ensembl ].
VAR_066834
Spondyloepimetaphyseal dysplasia MATN3-related (SEMD-MATN3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA bone disease characterized by disproportionate early-onset dwarfism, bowing of the lower limbs, lumbar lordosis and normal hands. Skeletal abnormalities include short, wide and stocky long bones with severe epiphyseal and metaphyseal changes, hypoplastic iliac bones and flat, ovoid vertebral bodies.

See also OMIM:608728
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti304 – 3041C → S in SEMD-MATN3. 1 Publication
VAR_019888
Osteoarthritis 2 (OS2)

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. In the hand, osteoarthritis can develop in the distal interphalangeal and the first carpometacarpal (base of thumb) and proximal interphalangeal joints. Patients with osteoarthritis may have one, a few, or all of these sites affected.

See also OMIM:140600

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi140600. phenotype.
607078. phenotype.
608728. phenotype.
Orphaneti93311. Multiple epiphyseal dysplasia type 5.
156728. Spondyloepimetaphyseal dysplasia, matrilin-3 type.
PharmGKBiPA30652.

Polymorphism and mutation databases

BioMutaiMATN3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 486458Matrilin-3PRO_0000007657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi268 ↔ 279PROSITE-ProRule annotation
Disulfide bondi275 ↔ 289PROSITE-ProRule annotation
Disulfide bondi291 ↔ 304PROSITE-ProRule annotation
Disulfide bondi310 ↔ 321PROSITE-ProRule annotation
Disulfide bondi317 ↔ 331PROSITE-ProRule annotation
Disulfide bondi333 ↔ 346PROSITE-ProRule annotation
Disulfide bondi352 ↔ 363PROSITE-ProRule annotation
Disulfide bondi359 ↔ 373PROSITE-ProRule annotation
Disulfide bondi375 ↔ 388PROSITE-ProRule annotation
Disulfide bondi394 ↔ 405PROSITE-ProRule annotation
Disulfide bondi401 ↔ 415PROSITE-ProRule annotation
Disulfide bondi417 ↔ 430PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiO15232.
PaxDbiO15232.
PRIDEiO15232.

PTM databases

PhosphoSiteiO15232.

Miscellaneous databases

PMAP-CutDBO15232.

Expressioni

Tissue specificityi

Expressed only in cartilaginous tissues, such as vertebrae, ribs and shoulders.

Gene expression databases

BgeeiO15232.
CleanExiHS_MATN3.
GenevisibleiO15232. HS.

Interactioni

Subunit structurei

Can form homooligomers (monomers, dimers, trimers and tetramers) and heterooligomers with matrilin-1 (By similarity). Interacts with COMP.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KRTAP10-8P604103EBI-6262458,EBI-10171774
NOTCH2NLQ7Z3S93EBI-6262458,EBI-945833
TCF4P158843EBI-6262458,EBI-533224

Protein-protein interaction databases

BioGridi110318. 7 interactions.
IntActiO15232. 4 interactions.
STRINGi9606.ENSP00000383894.

Structurei

3D structure databases

ProteinModelPortaliO15232.
SMRiO15232. Positions 82-245, 255-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 258176VWFAPROSITE-ProRule annotationAdd
BLAST
Domaini264 – 30542EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini306 – 34742EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini348 – 38942EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini390 – 43142EGF-like 4PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili456 – 48025By similarityAdd
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

eggNOGiNOG300624.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000263415.
HOVERGENiHBG056906.
InParanoidiO15232.
OMAiRFQETFC.
OrthoDBiEOG7X9G6P.
PhylomeDBiO15232.
TreeFamiTF330078.

Family and domain databases

Gene3Di1.20.5.30. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR030746. Matrilin-3.
IPR019466. Matrilin_coiled-coil_trimer.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR22992:SF15. PTHR22992:SF15. 1 hit.
PfamiPF10393. Matrilin_ccoil. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15232-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPRPAPARRL PGLLLLLWPL LLLPSAAPDP VARPGFRRLE TRGPGGSPGR
60 70 80 90 100
RPSPAAPDGA PASGTSEPGR ARGAGVCKSR PLDLVFIIDS SRSVRPLEFT
110 120 130 140 150
KVKTFVSRII DTLDIGPADT RVAVVNYAST VKIEFQLQAY TDKQSLKQAV
160 170 180 190 200
GRITPLSTGT MSGLAIQTAM DEAFTVEAGA REPSSNIPKV AIIVTDGRPQ
210 220 230 240 250
DQVNEVAARA QASGIELYAV GVDRADMASL KMMASEPLEE HVFYVETYGV
260 270 280 290 300
IEKLSSRFQE TFCALDPCVL GTHQCQHVCI SDGEGKHHCE CSQGYTLNAD
310 320 330 340 350
KKTCSALDRC ALNTHGCEHI CVNDRSGSYH CECYEGYTLN EDRKTCSAQD
360 370 380 390 400
KCALGTHGCQ HICVNDRTGS HHCECYEGYT LNADKKTCSV RDKCALGSHG
410 420 430 440 450
CQHICVSDGA ASYHCDCYPG YTLNEDKKTC SATEEARRLV STEDACGCEA
460 470 480
TLAFQDKVSS YLQRLNTKLD DILEKLKINE YGQIHR
Length:486
Mass (Da):52,817
Last modified:May 1, 1999 - v2
Checksum:i688847BCC791B331
GO
Isoform 2 (identifier: O15232-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     266-307: Missing.

Show »
Length:444
Mass (Da):48,317
Checksum:i86E2198CA1627B15
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111P → S.1 Publication
VAR_019881
Natural varianti70 – 701R → H in EDM5. 1 Publication
VAR_054807
Natural varianti105 – 1051F → S in EDM5. 1 Publication
VAR_020844
Natural varianti120 – 1201T → M in EDM5; retained and accumulates within the cell. 4 Publications
VAR_019882
Natural varianti121 – 1211R → W in EDM5; retained and accumulates within the cell. 5 Publications
VAR_013691
Natural varianti128 – 1281A → P in EDM5; bilateral hereditary microepiphyseal dysplasia. 1 Publication
VAR_019883
Natural varianti134 – 1341E → K in EDM5; retained and accumulates within the cell. 2 Publications
VAR_019884
Natural varianti171 – 1766Missing in EDM5. 1 Publication
VAR_066830
Natural varianti173 – 1731A → D in EDM5. 1 Publication
VAR_066831
Natural varianti192 – 1921I → N in EDM5; retained and accumulates within the cell. 2 Publications
VAR_019885
Natural varianti194 – 1941V → D in EDM5; retained and accumulates within the cell. 2 Publications
VAR_013692
Natural varianti195 – 1951T → K in EDM5. 2 Publications
VAR_054808
Natural varianti209 – 2091R → P in EDM5. 1 Publication
VAR_066832
Natural varianti218 – 2181Y → N in EDM5. 2 Publications
VAR_054809
Natural varianti219 – 2191A → D in EDM5; retained and accumulates within the cell. 3 Publications
Corresponds to variant rs28939677 [ dbSNP | Ensembl ].
VAR_019886
Natural varianti231 – 2311K → N in EDM5. 1 Publication
VAR_066833
Natural varianti245 – 2451V → M in EDM5. 1 Publication
Corresponds to variant rs182164052 [ dbSNP | Ensembl ].
VAR_066834
Natural varianti252 – 2521E → K Secreted normally as the wild-type. 3 Publications
Corresponds to variant rs52826764 [ dbSNP | Ensembl ].
VAR_019887
Natural varianti303 – 3031T → M.3 Publications
Corresponds to variant rs28939676 [ dbSNP | Ensembl ].
VAR_015852
Natural varianti304 – 3041C → S in SEMD-MATN3. 1 Publication
VAR_019888

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei266 – 30742Missing in isoform 2. 1 PublicationVSP_054374Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224741 mRNA. Translation: CAA12110.1.
EU541440 mRNA. Translation: ACB29772.1.
AC079145 Genomic DNA. Translation: AAX88937.1.
CH471053 Genomic DNA. Translation: EAX00837.1.
BC139907 mRNA. Translation: AAI39908.1.
AJ001047 mRNA. Translation: CAA04501.1.
Y13341 mRNA. Translation: CAA73785.1.
CCDSiCCDS46226.1. [O15232-1]
RefSeqiNP_002372.1. NM_002381.4. [O15232-1]
UniGeneiHs.656199.

Genome annotation databases

EnsembliENST00000407540; ENSP00000383894; ENSG00000132031. [O15232-1]
ENST00000421259; ENSP00000398753; ENSG00000132031. [O15232-2]
GeneIDi4148.
KEGGihsa:4148.
UCSCiuc002rdl.3. human. [O15232-1]
uc010exu.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224741 mRNA. Translation: CAA12110.1.
EU541440 mRNA. Translation: ACB29772.1.
AC079145 Genomic DNA. Translation: AAX88937.1.
CH471053 Genomic DNA. Translation: EAX00837.1.
BC139907 mRNA. Translation: AAI39908.1.
AJ001047 mRNA. Translation: CAA04501.1.
Y13341 mRNA. Translation: CAA73785.1.
CCDSiCCDS46226.1. [O15232-1]
RefSeqiNP_002372.1. NM_002381.4. [O15232-1]
UniGeneiHs.656199.

3D structure databases

ProteinModelPortaliO15232.
SMRiO15232. Positions 82-245, 255-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110318. 7 interactions.
IntActiO15232. 4 interactions.
STRINGi9606.ENSP00000383894.

PTM databases

PhosphoSiteiO15232.

Polymorphism and mutation databases

BioMutaiMATN3.

Proteomic databases

MaxQBiO15232.
PaxDbiO15232.
PRIDEiO15232.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000407540; ENSP00000383894; ENSG00000132031. [O15232-1]
ENST00000421259; ENSP00000398753; ENSG00000132031. [O15232-2]
GeneIDi4148.
KEGGihsa:4148.
UCSCiuc002rdl.3. human. [O15232-1]
uc010exu.1. human.

Organism-specific databases

CTDi4148.
GeneCardsiGC02M020191.
GeneReviewsiMATN3.
HGNCiHGNC:6909. MATN3.
MIMi140600. phenotype.
602109. gene.
607078. phenotype.
608728. phenotype.
neXtProtiNX_O15232.
Orphaneti93311. Multiple epiphyseal dysplasia type 5.
156728. Spondyloepimetaphyseal dysplasia, matrilin-3 type.
PharmGKBiPA30652.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300624.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000263415.
HOVERGENiHBG056906.
InParanoidiO15232.
OMAiRFQETFC.
OrthoDBiEOG7X9G6P.
PhylomeDBiO15232.
TreeFamiTF330078.

Enzyme and pathway databases

ReactomeiREACT_163906. ECM proteoglycans.

Miscellaneous databases

GeneWikiiMATN3.
GenomeRNAii4148.
NextBioi16298.
PMAP-CutDBO15232.
PROiO15232.
SOURCEiSearch...

Gene expression databases

BgeeiO15232.
CleanExiHS_MATN3.
GenevisibleiO15232. HS.

Family and domain databases

Gene3Di1.20.5.30. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR030746. Matrilin-3.
IPR019466. Matrilin_coiled-coil_trimer.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR22992:SF15. PTHR22992:SF15. 1 hit.
PfamiPF10393. Matrilin_ccoil. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
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. "Characterization of human matrilin-3 (MATN3)."
    Belluoccio D., Schenker T., Baici A., Trueb B.
    Genomics 53:391-394(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Cartilage.
  2. "Matrilin-3 increases not only upon osteoarthritis but also in cartilage-forming tumors and down-regulates SOX9 via EGF domain 1-dependent signaling."
    Vincourt J.-B., Takigawa M.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 184-486 (ISOFORM 1).
  7. "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] OF 177-486 (ISOFORM 1).
  8. "Interactions between the cartilage oligomeric matrix protein and matrilins. Implications for matrix assembly and the pathogenesis of chondrodysplasias."
    Mann H.H., Oezbek S., Engel J., Paulsson M., Wagener R.
    J. Biol. Chem. 279:25294-25298(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COMP.
  9. "Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia."
    Chapman K.L., Mortier G.R., Chapman K., Loughlin J., Grant M.E., Briggs M.D.
    Nat. Genet. 28:393-396(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDM5 TRP-121 AND ASP-194.
  10. Cited for: VARIANT MET-303, ASSOCIATION WITH OS2.
  11. "Familial multiple epiphyseal dysplasia due to a matrilin-3 mutation: further delineation of the phenotype including 40 years follow-up."
    Mostert A.K., Dijkstra P.F., Jansen B.R.H., van Horn J.R., de Graaf B., Heutink P., Lindhout D.
    Am. J. Med. Genet. A 120:490-497(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EDM5 PRO-128.
  12. "Novel and recurrent mutations clustered in the von Willebrand factor A domain of MATN3 in multiple epiphyseal dysplasia."
    Mabuchi A., Haga N., Maeda K., Nakashima E., Manabe N., Hiraoka H., Kitoh H., Kosaki R., Nishimura G., Ohashi H., Ikegawa S.
    Hum. Mutat. 24:439-440(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDM5 SER-105; MET-120 AND TRP-121, VARIANTS SER-11; LYS-252 AND MET-303.
  13. "Missense mutations in the beta strands of the single A-domain of matrilin-3 result in multiple epiphyseal dysplasia."
    Jackson G.C., Barker F.S., Jakkula E., Czarny-Ratajczak M., Maekitie O., Cole W.G., Wright M.J., Smithson S.F., Suri M., Rogala P., Mortier G.R., Baldock C., Wallace A., Elles R., Ala-Kokko L., Briggs M.D.
    J. Med. Genet. 41:52-59(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDM5 MET-120; TRP-121; LYS-134; ASN-192 AND ASP-219, VARIANTS LYS-252 AND MET-303.
  14. "Spondylo-epi-metaphyseal dysplasia (SEMD) matrilin 3 type: homozygote matrilin 3 mutation in a novel form of SEMD."
    Borochowitz Z.U., Scheffer D., Adir V., Dagoneau N., Munnich A., Cormier-Daire V.
    J. Med. Genet. 41:366-372(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SEMD-MATN3 SER-304.
  15. "Mutation in the von Willebrand factor-A domain is not a prerequisite for the MATN3 mutation in multiple epiphyseal dysplasia."
    Maeda K., Nakashima E., Horikoshi T., Mabuchi A., Ikegawa S.
    Am. J. Med. Genet. A 136:285-286(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EDM5 HIS-70.
  16. "Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3."
    Cotterill S.L., Jackson G.C., Leighton M.P., Wagener R., Maekitie O., Cole W.G., Briggs M.D.
    Hum. Mutat. 26:557-565(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDM5 TRP-121; LYS-195 AND ASN-218, VARIANT LYS-252, CHARACTERIZATION OF VARIANTS MET-120; TRP-121; LYS-134; ASN-192; ASP-194 AND ASP-219, CHARACTERIZATION OF VARIANT LYS-252.
  17. "Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
    Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
    Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDM5 MET-120; TRP-121; 171-ASP--VAL-176 DEL; ASP-173; LYS-195; PRO-209; ASN-218; ASP-219; ASN-231 AND MET-245.

Entry informationi

Entry nameiMATN3_HUMAN
AccessioniPrimary (citable) accession number: O15232
Secondary accession number(s): B2CPU0, Q4ZG02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.