MATN3_HUMAN
ID MATN3_HUMAN Reviewed; 486 AA.
AC O15232; B2CPU0; Q4ZG02;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Matrilin-3;
DE Flags: Precursor;
GN Name=MATN3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Cartilage;
RX PubMed=9799608; DOI=10.1006/geno.1998.5519;
RA Belluoccio D., Schenker T., Baici A., Trueb B.;
RT "Characterization of human matrilin-3 (MATN3).";
RL Genomics 53:391-394(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Vincourt J.-B., Takigawa M.;
RT "Matrilin-3 increases not only upon osteoarthritis but also in cartilage-
RT forming tumors and down-regulates SOX9 via EGF domain 1-dependent
RT signaling.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 184-486 (ISOFORM 1).
RX PubMed=9350998; DOI=10.1016/s0014-5793(97)01126-5;
RA Belluoccio D., Trueb B.;
RT "Matrilin-3 from chicken cartilage.";
RL FEBS Lett. 415:212-216(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-486 (ISOFORM 1).
RX PubMed=9287130; DOI=10.1016/s0014-5793(97)00895-8;
RA Wagener R., Kobbe B., Paulsson M.;
RT "Primary structure of matrilin-3, a new member of a family of extracellular
RT matrix proteins related to cartilage matrix protein (matrilin-1) and von
RT Willebrand factor.";
RL FEBS Lett. 413:129-134(1997).
RN [8]
RP INTERACTION WITH COMP.
RX PubMed=15075323; DOI=10.1074/jbc.m403778200;
RA Mann H.H., Oezbek S., Engel J., Paulsson M., Wagener R.;
RT "Interactions between the cartilage oligomeric matrix protein and
RT matrilins. Implications for matrix assembly and the pathogenesis of
RT chondrodysplasias.";
RL J. Biol. Chem. 279:25294-25298(2004).
RN [9]
RP PHOSPHORYLATION AT SER-441 AND THR-442.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [10]
RP VARIANTS EDM5 TRP-121 AND ASP-194.
RX PubMed=11479597; DOI=10.1038/ng573;
RA Chapman K.L., Mortier G.R., Chapman K., Loughlin J., Grant M.E.,
RA Briggs M.D.;
RT "Mutations in the region encoding the von Willebrand factor A domain of
RT matrilin-3 are associated with multiple epiphyseal dysplasia.";
RL Nat. Genet. 28:393-396(2001).
RN [11]
RP VARIANT MET-303, AND INVOLVEMENT IN OS2.
RX PubMed=12736871; DOI=10.1086/375556;
RA Stefansson S.E., Jonsson H., Ingvarsson T., Manolescu I., Jonsson H.H.,
RA Olafsdottir G., Palsdottir E., Stefansdottir G., Sveinbjornsdottir G.,
RA Frigge M.L., Kong A., Gulcher J.R., Stefansson K.;
RT "Genomewide scan for hand osteoarthritis: a novel mutation in matrilin-3.";
RL Am. J. Hum. Genet. 72:1448-1459(2003).
RN [12]
RP VARIANT EDM5 PRO-128.
RX PubMed=12884427; DOI=10.1002/ajmg.a.20034;
RA Mostert A.K., Dijkstra P.F., Jansen B.R.H., van Horn J.R., de Graaf B.,
RA Heutink P., Lindhout D.;
RT "Familial multiple epiphyseal dysplasia due to a matrilin-3 mutation:
RT further delineation of the phenotype including 40 years follow-up.";
RL Am. J. Med. Genet. A 120:490-497(2003).
RN [13]
RP VARIANTS EDM5 SER-105; MET-120 AND TRP-121, AND VARIANTS SER-11; LYS-252
RP AND MET-303.
RX PubMed=15459972; DOI=10.1002/humu.9286;
RA Mabuchi A., Haga N., Maeda K., Nakashima E., Manabe N., Hiraoka H.,
RA Kitoh H., Kosaki R., Nishimura G., Ohashi H., Ikegawa S.;
RT "Novel and recurrent mutations clustered in the von Willebrand factor A
RT domain of MATN3 in multiple epiphyseal dysplasia.";
RL Hum. Mutat. 24:439-440(2004).
RN [14]
RP VARIANTS EDM5 MET-120; TRP-121; LYS-134; ASN-192 AND ASP-219, AND VARIANTS
RP LYS-252 AND MET-303.
RX PubMed=14729835; DOI=10.1136/jmg.2003.011429;
RA Jackson G.C., Barker F.S., Jakkula E., Czarny-Ratajczak M., Maekitie O.,
RA Cole W.G., Wright M.J., Smithson S.F., Suri M., Rogala P., Mortier G.R.,
RA Baldock C., Wallace A., Elles R., Ala-Kokko L., Briggs M.D.;
RT "Missense mutations in the beta strands of the single A-domain of matrilin-
RT 3 result in multiple epiphyseal dysplasia.";
RL J. Med. Genet. 41:52-59(2004).
RN [15]
RP VARIANT SEMDBCD SER-304.
RX PubMed=15121775; DOI=10.1136/jmg.2003.013342;
RA Borochowitz Z.U., Scheffer D., Adir V., Dagoneau N., Munnich A.,
RA Cormier-Daire V.;
RT "Spondylo-epi-metaphyseal dysplasia (SEMD) matrilin 3 type: homozygote
RT matrilin 3 mutation in a novel form of SEMD.";
RL J. Med. Genet. 41:366-372(2004).
RN [16]
RP VARIANT EDM5 HIS-70.
RX PubMed=15948199; DOI=10.1002/ajmg.a.30832;
RA Maeda K., Nakashima E., Horikoshi T., Mabuchi A., Ikegawa S.;
RT "Mutation in the von Willebrand factor-A domain is not a prerequisite for
RT the MATN3 mutation in multiple epiphyseal dysplasia.";
RL Am. J. Med. Genet. A 136:285-286(2005).
RN [17]
RP VARIANTS EDM5 TRP-121; LYS-195 AND ASN-218, VARIANT LYS-252,
RP CHARACTERIZATION OF VARIANTS MET-120; TRP-121; LYS-134; ASN-192; ASP-194
RP AND ASP-219, AND CHARACTERIZATION OF VARIANT LYS-252.
RX PubMed=16287128; DOI=10.1002/humu.20263;
RA Cotterill S.L., Jackson G.C., Leighton M.P., Wagener R., Maekitie O.,
RA Cole W.G., Briggs M.D.;
RT "Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the
RT A-domain and prevent secretion of mutant matrilin-3.";
RL Hum. Mutat. 26:557-565(2005).
RN [18]
RP VARIANTS EDM5 MET-120; TRP-121; 171-ASP--VAL-176 DEL; ASP-173; LYS-195;
RP PRO-209; ASN-218; ASP-219; ASN-231 AND MET-245.
RX PubMed=21922596; DOI=10.1002/humu.21611;
RA Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J.,
RA Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A.,
RA Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R.,
RA Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.;
RT "Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year
RT comprehensive analysis of the known disease genes identify novel and
RT recurrent mutations and provides an accurate assessment of their relative
RT contribution.";
RL Hum. Mutat. 33:144-157(2012).
CC -!- FUNCTION: Major component of the extracellular matrix of cartilage and
CC may play a role in the formation of extracellular filamentous networks.
CC -!- SUBUNIT: Can form homooligomers (monomers, dimers, trimers and
CC tetramers) and heterooligomers with matrilin-1 (By similarity).
CC Interacts with COMP. Component of a complex containing at least CRELD2,
CC MANF, MATN3 and PDIA4 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O35701, ECO:0000269|PubMed:15075323}.
CC -!- INTERACTION:
CC O15232; Q0VD86: INCA1; NbExp=3; IntAct=EBI-6262458, EBI-6509505;
CC O15232; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-6262458, EBI-10171774;
CC O15232; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-6262458, EBI-945833;
CC O15232; P13667: PDIA4; NbExp=6; IntAct=EBI-6262458, EBI-1054653;
CC O15232; P15884: TCF4; NbExp=3; IntAct=EBI-6262458, EBI-533224;
CC O15232; P15884-3: TCF4; NbExp=3; IntAct=EBI-6262458, EBI-13636688;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O35701}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15232-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15232-2; Sequence=VSP_054374;
CC -!- TISSUE SPECIFICITY: Expressed only in cartilaginous tissues, such as
CC vertebrae, ribs and shoulders.
CC -!- DISEASE: Multiple epiphyseal dysplasia 5 (EDM5) [MIM:607078]: A
CC generalized skeletal dysplasia associated with significant morbidity.
CC Joint pain, joint deformity, waddling gait, and short stature are the
CC main clinical signs and symptoms. Radiological examination of the
CC skeleton shows delayed, irregular mineralization of the epiphyseal
CC ossification centers and of the centers of the carpal and tarsal bones.
CC Multiple epiphyseal dysplasia is broadly categorized into the more
CC severe Fairbank and the milder Ribbing types. The Fairbank type is
CC characterized by shortness of stature, short and stubby fingers, small
CC epiphyses in several joints, including the knee, ankle, hand, and hip.
CC The Ribbing type is confined predominantly to the hip joints and is
CC characterized by hands that are normal and stature that is normal or
CC near-normal. Multiple epiphyseal dysplasia type 5 is relatively mild
CC and clinically variable. It is primarily characterized by delayed and
CC irregular ossification of the epiphyses and early-onset osteoarthritis.
CC {ECO:0000269|PubMed:11479597, ECO:0000269|PubMed:12884427,
CC ECO:0000269|PubMed:14729835, ECO:0000269|PubMed:15459972,
CC ECO:0000269|PubMed:15948199, ECO:0000269|PubMed:16287128,
CC ECO:0000269|PubMed:21922596}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, Borochowitz-Cormier-Daire
CC type (SEMDBCD) [MIM:608728]: An autosomal recessive bone disease
CC characterized by disproportionate early-onset dwarfism, bowing of the
CC lower limbs, lumbar lordosis and normal hands. Skeletal abnormalities
CC include short, wide and stocky long bones with severe epiphyseal and
CC metaphyseal changes, hypoplastic iliac bones and flat, ovoid vertebral
CC bodies. {ECO:0000269|PubMed:15121775}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Osteoarthritis 2 (OS2) [MIM:140600]: A degenerative disease of
CC the joints characterized by degradation of the hyaline articular
CC cartilage and remodeling of the subchondral bone with sclerosis.
CC Clinical symptoms include pain and joint stiffness often leading to
CC significant disability and joint replacement. In the hand,
CC osteoarthritis can develop in the distal interphalangeal and the first
CC carpometacarpal (base of thumb) and proximal interphalangeal joints.
CC Patients with osteoarthritis may have one, a few, or all of these sites
CC affected. {ECO:0000269|PubMed:12736871}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
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DR EMBL; AJ224741; CAA12110.1; -; mRNA.
DR EMBL; EU541440; ACB29772.1; -; mRNA.
DR EMBL; AC079145; AAX88937.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00837.1; -; Genomic_DNA.
DR EMBL; BC139907; AAI39908.1; -; mRNA.
DR EMBL; AJ001047; CAA04501.1; -; mRNA.
DR EMBL; Y13341; CAA73785.1; -; mRNA.
DR CCDS; CCDS46226.1; -. [O15232-1]
DR RefSeq; NP_002372.1; NM_002381.4. [O15232-1]
DR AlphaFoldDB; O15232; -.
DR SMR; O15232; -.
DR BioGRID; 110318; 12.
DR ComplexPortal; CPX-4469; Matrilin-3 complex.
DR ComplexPortal; CPX-4503; Matrilin-1 - Matrilin-3 complex.
DR IntAct; O15232; 23.
DR STRING; 9606.ENSP00000383894; -.
DR iPTMnet; O15232; -.
DR PhosphoSitePlus; O15232; -.
DR BioMuta; MATN3; -.
DR jPOST; O15232; -.
DR MassIVE; O15232; -.
DR MaxQB; O15232; -.
DR PaxDb; O15232; -.
DR PeptideAtlas; O15232; -.
DR PRIDE; O15232; -.
DR ProteomicsDB; 3408; -.
DR ProteomicsDB; 48527; -. [O15232-1]
DR Antibodypedia; 27187; 220 antibodies from 27 providers.
DR DNASU; 4148; -.
DR Ensembl; ENST00000407540.8; ENSP00000383894.3; ENSG00000132031.13. [O15232-1]
DR Ensembl; ENST00000421259.2; ENSP00000398753.2; ENSG00000132031.13. [O15232-2]
DR GeneID; 4148; -.
DR KEGG; hsa:4148; -.
DR MANE-Select; ENST00000407540.8; ENSP00000383894.3; NM_002381.5; NP_002372.1.
DR UCSC; uc002rdl.4; human. [O15232-1]
DR CTD; 4148; -.
DR DisGeNET; 4148; -.
DR GeneCards; MATN3; -.
DR GeneReviews; MATN3; -.
DR HGNC; HGNC:6909; MATN3.
DR HPA; ENSG00000132031; Tissue enhanced (lung, placenta).
DR MalaCards; MATN3; -.
DR MIM; 140600; phenotype.
DR MIM; 602109; gene.
DR MIM; 607078; phenotype.
DR MIM; 608728; phenotype.
DR neXtProt; NX_O15232; -.
DR OpenTargets; ENSG00000132031; -.
DR Orphanet; 93311; Multiple epiphyseal dysplasia type 5.
DR Orphanet; 156728; Spondyloepimetaphyseal dysplasia, matrilin-3 type.
DR PharmGKB; PA30652; -.
DR VEuPathDB; HostDB:ENSG00000132031; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000157581; -.
DR HOGENOM; CLU_008905_6_1_1; -.
DR InParanoid; O15232; -.
DR OMA; PCMLGTH; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; O15232; -.
DR TreeFam; TF330078; -.
DR PathwayCommons; O15232; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; O15232; -.
DR BioGRID-ORCS; 4148; 17 hits in 1063 CRISPR screens.
DR ChiTaRS; MATN3; human.
DR GeneWiki; MATN3; -.
DR GenomeRNAi; 4148; -.
DR Pharos; O15232; Tbio.
DR PRO; PR:O15232; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O15232; protein.
DR Bgee; ENSG00000132031; Expressed in tibia and 100 other tissues.
DR Genevisible; O15232; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0120216; C:matrilin complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IC:ComplexPortal.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR Gene3D; 1.20.5.30; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR030765; Matrilin_3.
DR InterPro; IPR036337; Matrilin_cc_sf.
DR InterPro; IPR019466; Matrilin_coiled-coil_trimer.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24034:SF105; PTHR24034:SF105; 2.
DR Pfam; PF10393; Matrilin_ccoil; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM01279; Matrilin_ccoil; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF58002; SSF58002; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disease variant; Disulfide bond;
KW Dwarfism; EGF-like domain; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..486
FT /note="Matrilin-3"
FT /id="PRO_0000007657"
FT DOMAIN 83..258
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 264..305
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 306..347
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 348..389
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 390..431
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 32..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 456..480
FT /evidence="ECO:0000250"
FT MOD_RES 198
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35701"
FT MOD_RES 441
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 442
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT DISULFID 268..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 275..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 291..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 310..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 317..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 333..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 352..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 359..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 375..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 394..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 401..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 417..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 266..307
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_054374"
FT VARIANT 11
FT /note="P -> S (in dbSNP:rs963330242)"
FT /evidence="ECO:0000269|PubMed:15459972"
FT /id="VAR_019881"
FT VARIANT 70
FT /note="R -> H (in EDM5; dbSNP:rs104893640)"
FT /evidence="ECO:0000269|PubMed:15948199"
FT /id="VAR_054807"
FT VARIANT 105
FT /note="F -> S (in EDM5)"
FT /evidence="ECO:0000269|PubMed:15459972"
FT /id="VAR_020844"
FT VARIANT 120
FT /note="T -> M (in EDM5; retained and accumulates within the
FT cell; dbSNP:rs397515546)"
FT /evidence="ECO:0000269|PubMed:14729835,
FT ECO:0000269|PubMed:15459972, ECO:0000269|PubMed:16287128,
FT ECO:0000269|PubMed:21922596"
FT /id="VAR_019882"
FT VARIANT 121
FT /note="R -> W (in EDM5; retained and accumulates within the
FT cell; dbSNP:rs104893637)"
FT /evidence="ECO:0000269|PubMed:11479597,
FT ECO:0000269|PubMed:14729835, ECO:0000269|PubMed:15459972,
FT ECO:0000269|PubMed:16287128, ECO:0000269|PubMed:21922596"
FT /id="VAR_013691"
FT VARIANT 128
FT /note="A -> P (in EDM5; bilateral hereditary
FT microepiphyseal dysplasia; dbSNP:rs104893641)"
FT /evidence="ECO:0000269|PubMed:12884427"
FT /id="VAR_019883"
FT VARIANT 134
FT /note="E -> K (in EDM5; retained and accumulates within the
FT cell)"
FT /evidence="ECO:0000269|PubMed:14729835,
FT ECO:0000269|PubMed:16287128"
FT /id="VAR_019884"
FT VARIANT 171..176
FT /note="Missing (in EDM5)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066830"
FT VARIANT 173
FT /note="A -> D (in EDM5; dbSNP:rs779413744)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066831"
FT VARIANT 192
FT /note="I -> N (in EDM5; retained and accumulates within the
FT cell)"
FT /evidence="ECO:0000269|PubMed:14729835,
FT ECO:0000269|PubMed:16287128"
FT /id="VAR_019885"
FT VARIANT 194
FT /note="V -> D (in EDM5; retained and accumulates within the
FT cell; dbSNP:rs104893645)"
FT /evidence="ECO:0000269|PubMed:11479597,
FT ECO:0000269|PubMed:16287128"
FT /id="VAR_013692"
FT VARIANT 195
FT /note="T -> K (in EDM5)"
FT /evidence="ECO:0000269|PubMed:16287128,
FT ECO:0000269|PubMed:21922596"
FT /id="VAR_054808"
FT VARIANT 209
FT /note="R -> P (in EDM5; dbSNP:rs749845872)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066832"
FT VARIANT 218
FT /note="Y -> N (in EDM5)"
FT /evidence="ECO:0000269|PubMed:16287128,
FT ECO:0000269|PubMed:21922596"
FT /id="VAR_054809"
FT VARIANT 219
FT /note="A -> D (in EDM5; retained and accumulates within the
FT cell; dbSNP:rs28939677)"
FT /evidence="ECO:0000269|PubMed:14729835,
FT ECO:0000269|PubMed:16287128, ECO:0000269|PubMed:21922596"
FT /id="VAR_019886"
FT VARIANT 231
FT /note="K -> N (in EDM5; dbSNP:rs773642745)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066833"
FT VARIANT 245
FT /note="V -> M (in EDM5; dbSNP:rs182164052)"
FT /evidence="ECO:0000269|PubMed:21922596"
FT /id="VAR_066834"
FT VARIANT 252
FT /note="E -> K (secreted normally as the wild-type;
FT dbSNP:rs52826764)"
FT /evidence="ECO:0000269|PubMed:14729835,
FT ECO:0000269|PubMed:15459972, ECO:0000269|PubMed:16287128"
FT /id="VAR_019887"
FT VARIANT 303
FT /note="T -> M (in dbSNP:rs77245812)"
FT /evidence="ECO:0000269|PubMed:12736871,
FT ECO:0000269|PubMed:14729835, ECO:0000269|PubMed:15459972"
FT /id="VAR_015852"
FT VARIANT 304
FT /note="C -> S (in SEMDBCD; dbSNP:rs104893639)"
FT /evidence="ECO:0000269|PubMed:15121775"
FT /id="VAR_019888"
SQ SEQUENCE 486 AA; 52817 MW; 688847BCC791B331 CRC64;
MPRPAPARRL PGLLLLLWPL LLLPSAAPDP VARPGFRRLE TRGPGGSPGR RPSPAAPDGA
PASGTSEPGR ARGAGVCKSR PLDLVFIIDS SRSVRPLEFT KVKTFVSRII DTLDIGPADT
RVAVVNYAST VKIEFQLQAY TDKQSLKQAV GRITPLSTGT MSGLAIQTAM DEAFTVEAGA
REPSSNIPKV AIIVTDGRPQ DQVNEVAARA QASGIELYAV GVDRADMASL KMMASEPLEE
HVFYVETYGV IEKLSSRFQE TFCALDPCVL GTHQCQHVCI SDGEGKHHCE CSQGYTLNAD
KKTCSALDRC ALNTHGCEHI CVNDRSGSYH CECYEGYTLN EDRKTCSAQD KCALGTHGCQ
HICVNDRTGS HHCECYEGYT LNADKKTCSV RDKCALGSHG CQHICVSDGA ASYHCDCYPG
YTLNEDKKTC SATEEARRLV STEDACGCEA TLAFQDKVSS YLQRLNTKLD DILEKLKINE
YGQIHR
