MATN1_CHICK
ID MATN1_CHICK Reviewed; 493 AA.
AC P05099;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cartilage matrix protein;
DE AltName: Full=Matrilin-1;
DE Flags: Precursor;
GN Name=MATN1; Synonyms=CMP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-43.
RC STRAIN=White leghorn;
RX PubMed=2542265; DOI=10.1016/s0021-9258(18)83159-3;
RA Kiss I., Deak F., Holloway R.G. Jr., Delius H., Mebust K.A., Frimberger E.,
RA Argraves W.S., Tsonis P.A., Winterbottom N., Goetinck P.F.;
RT "Structure of the gene for cartilage matrix protein, a modular protein of
RT the extracellular matrix. Exon/intron organization, unusual splice sites,
RT and relation to alpha chains of beta 2 integrins, von Willebrand factor,
RT complement factors B and C2, and epidermal growth factor.";
RL J. Biol. Chem. 264:8126-8134(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-493.
RX PubMed=3025875; DOI=10.1073/pnas.84.2.464;
RA Argraves W.S., Deak F., Sparks K.J., Kiss I., Goetinck P.F.;
RT "Structural features of cartilage matrix protein deduced from cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:464-468(1987).
RN [3]
RP STRUCTURE BY NMR OF 447-493.
RX PubMed=9260286; DOI=10.1002/pro.5560060814;
RA Wiltscheck R., Kammerer R.A., Dames S.A., Schulthess T., Blommers M.J.,
RA Engel J., Alexandrescu A.T.;
RT "Heteronuclear NMR assignments and secondary structure of the coiled coil
RT trimerization domain from cartilage matrix protein in oxidized and reduced
RT forms.";
RL Protein Sci. 6:1734-1745(1997).
CC -!- FUNCTION: Cartilage matrix protein is a major component of the
CC extracellular matrix of non-articular cartilage. It binds to collagen.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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DR EMBL; X12353; CAA30915.1; -; Genomic_DNA.
DR EMBL; X12346; CAA30915.1; JOINED; Genomic_DNA.
DR EMBL; X12347; CAA30915.1; JOINED; Genomic_DNA.
DR EMBL; X12348; CAA30915.1; JOINED; Genomic_DNA.
DR EMBL; X12349; CAA30915.1; JOINED; Genomic_DNA.
DR EMBL; X12350; CAA30915.1; JOINED; Genomic_DNA.
DR EMBL; X12351; CAA30915.1; JOINED; Genomic_DNA.
DR EMBL; X12352; CAA30915.1; JOINED; Genomic_DNA.
DR EMBL; M14792; AAA48695.1; -; mRNA.
DR EMBL; M97497; AAC18872.1; -; Genomic_DNA.
DR PIR; A33809; A33809.
DR PDB; 1AQ5; NMR; -; A/B/C=451-493.
DR PDBsum; 1AQ5; -.
DR AlphaFoldDB; P05099; -.
DR BMRB; P05099; -.
DR SMR; P05099; -.
DR STRING; 9031.ENSGALP00000000760; -.
DR PaxDb; P05099; -.
DR VEuPathDB; HostDB:geneid_396505; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; P05099; -.
DR PhylomeDB; P05099; -.
DR EvolutionaryTrace; P05099; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR Gene3D; 1.20.5.30; -; 1.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR030751; Matrilin-1.
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; PTHR24020:SF16; PTHR24020:SF16; 1.
DR Pfam; PF10393; Matrilin_ccoil; 1.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM01279; Matrilin_ccoil; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF58002; SSF58002; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50234; VWFA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2542265"
FT CHAIN 24..493
FT /note="Cartilage matrix protein"
FT /id="PRO_0000007494"
FT DOMAIN 24..220
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 221..261
FT /note="EGF-like"
FT DOMAIN 262..450
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT COILED 462..492
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..219
FT /evidence="ECO:0000255"
FT DISULFID 225..236
FT /evidence="ECO:0000250"
FT DISULFID 232..245
FT /evidence="ECO:0000250"
FT DISULFID 247..260
FT /evidence="ECO:0000250"
FT DISULFID 263..449
FT /evidence="ECO:0000255"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:1AQ5"
FT HELIX 459..492
FT /evidence="ECO:0007829|PDB:1AQ5"
SQ SEQUENCE 493 AA; 54034 MW; E4D3DACFAB2B96A4 CRC64;
MDGIFCALPL SLLLLLQSCG VWGAPPQPRG TLCRTKPTDL VFIIDSSRSV RPQEFEKVKV
FLSRVIEGLD VGPNSTRVGV INYASAVKNE FSLKTHQTKA ELLQAVQRIE PLSTGTMTGL
AIQFAISRAF SDTEGARLRS PNINKVAIVV TDGRPQDGVQ DVSARARQAG IEIFAIGVGR
VDMHTLRQIA SEPLDDHVDY VESYSVIEKL THKFQEAFCV VSDLCATGDH DCEQICISTP
GSYKCACKEG FTLNNDGKTC SACSGGSGSA LDLVFLIDGS KSVRPENFEL VKKFINQIVE
SLEVSEKQAQ VGLVQYSSSV RQEFPLGQFK NKKDIKAAVK KMAYMEKGTM TGQALKYLVD
SSFSIANGAR PGVPKVGIVF TDGRSQDYIT DAAKKAKDLG FRMFAVGVGN AVEDELREIA
SEPVAEHYFY TADFRTISNI GKKLQMKICV EEDPCECKSI VKFQTKVEEL INTLQQKLEA
VAKRIEALEN KII
