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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

  • calcium ion binding Source: InterPro
  • extracellular matrix structural constituent Source: ProtInc

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-3000178. ECM proteoglycans.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-HSA-8957275. Post-translational protein phosphorylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrilin-3
Gene namesi
Name:MATN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6909. MATN3.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: Reactome
  • proteinaceous extracellular matrix Source: ProtInc

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05480770R → H in EDM5. 1 PublicationCorresponds to variant dbSNP:rs104893640Ensembl.1
Natural variantiVAR_020844105F → S in EDM5. 1 Publication1
Natural variantiVAR_019882120T → M in EDM5; retained and accumulates within the cell. 4 PublicationsCorresponds to variant dbSNP:rs397515546Ensembl.1
Natural variantiVAR_013691121R → W in EDM5; retained and accumulates within the cell. 5 PublicationsCorresponds to variant dbSNP:rs104893637Ensembl.1
Natural variantiVAR_019883128A → P in EDM5; bilateral hereditary microepiphyseal dysplasia. 1 PublicationCorresponds to variant dbSNP:rs104893641Ensembl.1
Natural variantiVAR_019884134E → K in EDM5; retained and accumulates within the cell. 2 Publications1
Natural variantiVAR_066830171 – 176Missing in EDM5. 1 Publication6
Natural variantiVAR_066831173A → D in EDM5. 1 Publication1
Natural variantiVAR_019885192I → N in EDM5; retained and accumulates within the cell. 2 Publications1
Natural variantiVAR_013692194V → D in EDM5; retained and accumulates within the cell. 2 PublicationsCorresponds to variant dbSNP:rs104893645Ensembl.1
Natural variantiVAR_054808195T → K in EDM5. 2 Publications1
Natural variantiVAR_066832209R → P in EDM5. 1 PublicationCorresponds to variant dbSNP:rs749845872Ensembl.1
Natural variantiVAR_054809218Y → N in EDM5. 2 Publications1
Natural variantiVAR_019886219A → D in EDM5; retained and accumulates within the cell. 3 PublicationsCorresponds to variant dbSNP:rs28939677Ensembl.1
Natural variantiVAR_066833231K → N in EDM5. 1 PublicationCorresponds to variant dbSNP:rs773642745Ensembl.1
Natural variantiVAR_066834245V → M in EDM5. 1 PublicationCorresponds to variant dbSNP:rs182164052Ensembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_019888304C → S in SEMD-MATN3. 1 PublicationCorresponds to variant dbSNP:rs104893639Ensembl.1
Osteoarthritis 2 (OS2)1 Publication
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

DisGeNETi4148.
GeneReviewsiMATN3.
MalaCardsiMATN3.
MIMi140600. phenotype.
607078. phenotype.
608728. phenotype.
OpenTargetsiENSG00000132031.
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000765729 – 486Matrilin-3Add BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198Omega-N-methylarginineBy similarity1
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
Modified residuei441Phosphoserine; by FAM20C1 Publication1
Modified residuei442Phosphothreonine; by FAM20C1 Publication1

Keywords - PTMi

Disulfide bond, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO15232.
PaxDbiO15232.
PeptideAtlasiO15232.
PRIDEiO15232.

PTM databases

iPTMnetiO15232.
PhosphoSitePlusiO15232.

Miscellaneous databases

PMAP-CutDBiO15232.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000132031.
CleanExiHS_MATN3.
GenevisibleiO15232. HS.

Organism-specific databases

HPAiHPA051250.

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

Show more details

Protein-protein interaction databases

BioGridi110318. 7 interactors.
IntActiO15232. 5 interactors.
STRINGi9606.ENSP00000383894.

Structurei

3D structure databases

ProteinModelPortaliO15232.
SMRiO15232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini83 – 258VWFAPROSITE-ProRule annotationAdd BLAST176
Domaini264 – 305EGF-like 1PROSITE-ProRule annotationAdd BLAST42
Domaini306 – 347EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini348 – 389EGF-like 3PROSITE-ProRule annotationAdd BLAST42
Domaini390 – 431EGF-like 4PROSITE-ProRule annotationAdd BLAST42

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili456 – 480By similarityAdd BLAST25

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG4111IJ5. LUCA.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000263415.
HOVERGENiHBG056906.
InParanoidiO15232.
KOiK19467.
OMAiRFQETFC.
OrthoDBiEOG091G04O4.
PhylomeDBiO15232.
TreeFamiTF330078.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiView protein in InterPro
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR030765. Matrilin_3.
IPR019466. Matrilin_coiled-coil_trimer.
IPR002035. VWF_A.
PANTHERiPTHR11132:SF154. PTHR11132:SF154. 1 hit.
PfamiView protein in Pfam
PF07645. EGF_CA. 1 hit.
PF10393. Matrilin_ccoil. 1 hit.
PF00092. VWA. 1 hit.
SMARTiView protein in SMART
SM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
SM01279. Matrilin_ccoil. 1 hit.
SM00327. VWA. 1 hit.
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF57184. SSF57184. 1 hit.
SSF58002. SSF58002. 1 hit.
PROSITEiView protein in PROSITE
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS50234. VWFA. 1 hit.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01988111P → S1 Publication1
Natural variantiVAR_05480770R → H in EDM5. 1 PublicationCorresponds to variant dbSNP:rs104893640Ensembl.1
Natural variantiVAR_020844105F → S in EDM5. 1 Publication1
Natural variantiVAR_019882120T → M in EDM5; retained and accumulates within the cell. 4 PublicationsCorresponds to variant dbSNP:rs397515546Ensembl.1
Natural variantiVAR_013691121R → W in EDM5; retained and accumulates within the cell. 5 PublicationsCorresponds to variant dbSNP:rs104893637Ensembl.1
Natural variantiVAR_019883128A → P in EDM5; bilateral hereditary microepiphyseal dysplasia. 1 PublicationCorresponds to variant dbSNP:rs104893641Ensembl.1
Natural variantiVAR_019884134E → K in EDM5; retained and accumulates within the cell. 2 Publications1
Natural variantiVAR_066830171 – 176Missing in EDM5. 1 Publication6
Natural variantiVAR_066831173A → D in EDM5. 1 Publication1
Natural variantiVAR_019885192I → N in EDM5; retained and accumulates within the cell. 2 Publications1
Natural variantiVAR_013692194V → D in EDM5; retained and accumulates within the cell. 2 PublicationsCorresponds to variant dbSNP:rs104893645Ensembl.1
Natural variantiVAR_054808195T → K in EDM5. 2 Publications1
Natural variantiVAR_066832209R → P in EDM5. 1 PublicationCorresponds to variant dbSNP:rs749845872Ensembl.1
Natural variantiVAR_054809218Y → N in EDM5. 2 Publications1
Natural variantiVAR_019886219A → D in EDM5; retained and accumulates within the cell. 3 PublicationsCorresponds to variant dbSNP:rs28939677Ensembl.1
Natural variantiVAR_066833231K → N in EDM5. 1 PublicationCorresponds to variant dbSNP:rs773642745Ensembl.1
Natural variantiVAR_066834245V → M in EDM5. 1 PublicationCorresponds to variant dbSNP:rs182164052Ensembl.1
Natural variantiVAR_019887252E → K Secreted normally as the wild-type. 3 PublicationsCorresponds to variant dbSNP:rs52826764Ensembl.1
Natural variantiVAR_015852303T → M3 PublicationsCorresponds to variant dbSNP:rs28939676Ensembl.1
Natural variantiVAR_019888304C → S in SEMD-MATN3. 1 PublicationCorresponds to variant dbSNP:rs104893639Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054374266 – 307Missing in isoform 2. 1 PublicationAdd BLAST42

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.4. human. [O15232-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMATN3_HUMAN
AccessioniPrimary (citable) accession number: O15232
Secondary accession number(s): B2CPU0, Q4ZG02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 1999
Last modified: August 30, 2017
This is version 172 of the entry and version 2 of the sequence. See 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