O15232 (MATN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Matrilin-3

Gene names

Name:

MATN3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.
Subunit structure	Can form homooligomers (monomers, dimers, trimers and tetramers) and heterooligomers with matrilin-1 By similarity. Interacts with COMP. Ref.8
Subcellular location	Secreted.
Tissue specificity	Expressed only in cartilaginous tissues, such as vertebrae, ribs and shoulders.
Involvement in disease	Multiple epiphyseal dysplasia 5 (EDM5) [MIM:607078]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Spondyloepimetaphyseal dysplasia MATN3-related (SEMD-MATN3) [MIM:608728]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Osteoarthritis 2 (OS2) [MIM:140600]: A 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.10
Sequence similarities	Contains 4 EGF-like domains. Contains 1 VWFA domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dwarfism
Domain	Coiled coil EGF-like domain Repeat Signal
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	extracellular matrix organization Traceable author statement. Source: Reactome skeletal system development Traceable author statement Ref.6. Source: ProtInc
Cellular_component	extracellular region Traceable author statement. Source: Reactome proteinaceous extracellular matrix Traceable author statement Ref.6. Source: ProtInc
Molecular_function	extracellular matrix structural constituent Traceable author statement Ref.6. Source: ProtInc protein binding Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15232-1)

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 2 (identifier: O15232-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 486	458	Matrilin-3		PRO_0000007657
Regions
	Domain	83 – 258	176	VWFA
	Domain	264 – 305	42	EGF-like 1
	Domain	306 – 347	42	EGF-like 2
	Domain	348 – 389	42	EGF-like 3
	Domain	390 – 431	42	EGF-like 4
	Coiled coil	456 – 480	25	By similarity
Amino acid modifications
	Disulfide bond	268 ↔ 279		By similarity
	Disulfide bond	275 ↔ 289		By similarity
	Disulfide bond	291 ↔ 304		By similarity
	Disulfide bond	310 ↔ 321		By similarity
	Disulfide bond	317 ↔ 331		By similarity
	Disulfide bond	333 ↔ 346		By similarity
	Disulfide bond	352 ↔ 363		By similarity
	Disulfide bond	359 ↔ 373		By similarity
	Disulfide bond	375 ↔ 388		By similarity
	Disulfide bond	394 ↔ 405		By similarity
	Disulfide bond	401 ↔ 415		By similarity
	Disulfide bond	417 ↔ 430		By similarity
Natural variations
	Alternative sequence	266 – 307	42	Missing in isoform 2.		VSP_054374
	Natural variant	11	1	P → S. Ref.12		VAR_019881
	Natural variant	70	1	R → H in EDM5. Ref.15		VAR_054807
	Natural variant	105	1	F → S in EDM5. Ref.12		VAR_020844
	Natural variant	120	1	T → M in EDM5; retained and accumulates within the cell. Ref.12 Ref.13 Ref.16 Ref.17		VAR_019882
	Natural variant	121	1	R → W in EDM5; retained and accumulates within the cell. Ref.9 Ref.12 Ref.13 Ref.16 Ref.17		VAR_013691
	Natural variant	128	1	A → P in EDM5; bilateral hereditary microepiphyseal dysplasia. Ref.11		VAR_019883
	Natural variant	134	1	E → K in EDM5; retained and accumulates within the cell. Ref.13 Ref.16		VAR_019884
	Natural variant	171 – 176	6	Missing in EDM5.		VAR_066830
	Natural variant	173	1	A → D in EDM5. Ref.17		VAR_066831
	Natural variant	192	1	I → N in EDM5; retained and accumulates within the cell. Ref.13 Ref.16		VAR_019885
	Natural variant	194	1	V → D in EDM5; retained and accumulates within the cell. Ref.9 Ref.16		VAR_013692
	Natural variant	195	1	T → K in EDM5. Ref.16 Ref.17		VAR_054808
	Natural variant	209	1	R → P in EDM5. Ref.17		VAR_066832
	Natural variant	218	1	Y → N in EDM5. Ref.16 Ref.17		VAR_054809
	Natural variant	219	1	A → D in EDM5; retained and accumulates within the cell. Ref.13 Ref.16 Ref.17 Corresponds to variant rs28939677 [ dbSNP | Ensembl ].		VAR_019886
	Natural variant	231	1	K → N in EDM5. Ref.17		VAR_066833
	Natural variant	245	1	V → M in EDM5. Ref.17 Corresponds to variant rs182164052 [ dbSNP | Ensembl ].		VAR_066834
	Natural variant	252	1	E → K Secreted normally as the wild-type. Ref.12 Ref.13 Ref.16 Corresponds to variant rs52826764 [ dbSNP | Ensembl ].		VAR_019887
	Natural variant	303	1	T → M. Ref.10 Ref.12 Ref.13 Corresponds to variant rs28939676 [ dbSNP | Ensembl ].		VAR_015852
	Natural variant	304	1	C → S in SEMD-MATN3. Ref.14		VAR_019888

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: 688847BCC791B331	FASTA	486	52,817
	10 20 30 40 50 60 MPRPAPARRL PGLLLLLWPL LLLPSAAPDP VARPGFRRLE TRGPGGSPGR RPSPAAPDGA 70 80 90 100 110 120 PASGTSEPGR ARGAGVCKSR PLDLVFIIDS SRSVRPLEFT KVKTFVSRII DTLDIGPADT 130 140 150 160 170 180 RVAVVNYAST VKIEFQLQAY TDKQSLKQAV GRITPLSTGT MSGLAIQTAM DEAFTVEAGA 190 200 210 220 230 240 REPSSNIPKV AIIVTDGRPQ DQVNEVAARA QASGIELYAV GVDRADMASL KMMASEPLEE 250 260 270 280 290 300 HVFYVETYGV IEKLSSRFQE TFCALDPCVL GTHQCQHVCI SDGEGKHHCE CSQGYTLNAD 310 320 330 340 350 360 KKTCSALDRC ALNTHGCEHI CVNDRSGSYH CECYEGYTLN EDRKTCSAQD KCALGTHGCQ 370 380 390 400 410 420 HICVNDRTGS HHCECYEGYT LNADKKTCSV RDKCALGSHG CQHICVSDGA ASYHCDCYPG 430 440 450 460 470 480 YTLNEDKKTC SATEEARRLV STEDACGCEA TLAFQDKVSS YLQRLNTKLD DILEKLKINE YGQIHR
	Isoform 2 [UniParc]. Checksum: 86E2198CA1627B15	FASTA	444	48,317
	10 20 30 40 50 60 MPRPAPARRL PGLLLLLWPL LLLPSAAPDP VARPGFRRLE TRGPGGSPGR RPSPAAPDGA 70 80 90 100 110 120 PASGTSEPGR ARGAGVCKSR PLDLVFIIDS SRSVRPLEFT KVKTFVSRII DTLDIGPADT 130 140 150 160 170 180 RVAVVNYAST VKIEFQLQAY TDKQSLKQAV GRITPLSTGT MSGLAIQTAM DEAFTVEAGA 190 200 210 220 230 240 REPSSNIPKV AIIVTDGRPQ DQVNEVAARA QASGIELYAV GVDRADMASL KMMASEPLEE 250 260 270 280 290 300 HVFYVETYGV IEKLSSRFQE TFCALDRCAL NTHGCEHICV NDRSGSYHCE CYEGYTLNED 310 320 330 340 350 360 RKTCSAQDKC ALGTHGCQHI CVNDRTGSHH CECYEGYTLN ADKKTCSVRD KCALGSHGCQ 370 380 390 400 410 420 HICVSDGAAS YHCDCYPGYT LNEDKKTCSA TEEARRLVST EDACGCEATL AFQDKVSSYL 430 440 QRLNTKLDDI LEKLKINEYG QIHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Matrilin-3 from chicken cartilage." Belluoccio D., Trueb B. FEBS Lett. 415:212-216(1997) [PubMed] [Europe PMC] [Abstract] 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]	"Genomewide scan for hand osteoarthritis: a novel mutation in matrilin-3." Stefansson S.E., Jonsson H., Ingvarsson T., Manolescu I., Jonsson H.H., Olafsdottir G., Palsdottir E., Stefansdottir G., Sveinbjornsdottir G., Frigge M.L., Kong A., Gulcher J.R., Stefansson K. Am. J. Hum. Genet. 72:1448-1459(2003) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
CCDS	CCDS46226.1.
RefSeq	NP_002372.1. NM_002381.4. [O15232-1]
UniGene	Hs.656199.
3D structure databases
ProteinModelPortal	O15232.
SMR	O15232. Positions 82-245, 255-432.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	110318. 3 interactions.
IntAct	O15232. 1 interaction.
STRING	9606.ENSP00000383894.
PTM databases
PhosphoSite	O15232.
Proteomic databases
MaxQB	O15232.
PaxDb	O15232.
PRIDE	O15232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000407540; ENSP00000383894; ENSG00000132031. ENST00000421259; ENSP00000398753; ENSG00000132031.
GeneID	4148.
KEGG	hsa:4148.
UCSC	uc002rdl.3. human. [O15232-1]
Organism-specific databases
CTD	4148.
GeneCards	GC02M020191.
GeneReviews	MATN3.
HGNC	HGNC:6909. MATN3.
MIM	140600. phenotype. 602109. gene. 607078. phenotype. 608728. phenotype.
neXtProt	NX_O15232.
Orphanet	93311. Multiple epiphyseal dysplasia type 5. 156728. Spondyloepimetaphyseal dysplasia, matrilin-3 type.
PharmGKB	PA30652.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG300624.
HOGENOM	HOG000263415.
HOVERGEN	HBG056906.
InParanoid	O15232.
OMA	RFQETFC.
OrthoDB	EOG7X9G6P.
PhylomeDB	O15232.
TreeFam	TF330078.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	O15232.
Bgee	O15232.
CleanEx	HS_MATN3.
Genevestigator	O15232.
Family and domain databases
Gene3D	1.20.5.30. 1 hit. 3.40.50.410. 1 hit.
InterPro	IPR000742. EG-like_dom. IPR013032. EGF-like_CS. IPR009030. Growth_fac_rcpt_N_dom. IPR019466. Matrilin_coiled-coil_trimer. IPR002035. VWF_A. [Graphical view]
Pfam	PF10393. Matrilin_ccoil. 1 hit. PF00092. VWA. 1 hit. [Graphical view]
SMART	SM00181. EGF. 4 hits. SM00327. VWA. 1 hit. [Graphical view]
SUPFAM	SSF53300. SSF53300. 1 hit. SSF57184. SSF57184. 1 hit.
PROSITE	PS01186. EGF_2. 4 hits. PS50026. EGF_3. 4 hits. PS50234. VWFA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GeneWiki	MATN3.
GenomeRNAi	4148.
NextBio	16298.
PMAP-CutDB	O15232.
PRO	O15232.
SOURCE	Search...

Entry information

Entry name

MATN3_HUMAN

Accession

Primary (citable) accession number: O15232
Secondary accession number(s): B2CPU0, Q4ZG02

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	May 1, 1999
Last modified:	July 9, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.