MATN3_CHICK
ID MATN3_CHICK Reviewed; 452 AA.
AC O42401;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Matrilin-3;
DE Flags: Precursor;
GN Name=MATN3;
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 [MRNA].
RC TISSUE=Cartilage;
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).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expression is restricted to cartilaginous tissues.
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DR EMBL; AJ000055; CAA03885.1; -; mRNA.
DR RefSeq; NP_990403.1; NM_205072.1.
DR AlphaFoldDB; O42401; -.
DR SMR; O42401; -.
DR STRING; 9031.ENSGALP00000036079; -.
DR PaxDb; O42401; -.
DR Ensembl; ENSGALT00000036867; ENSGALP00000036079; ENSGALG00000016478.
DR GeneID; 395954; -.
DR KEGG; gga:395954; -.
DR CTD; 4148; -.
DR VEuPathDB; HostDB:geneid_395954; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000157581; -.
DR HOGENOM; CLU_008905_6_1_1; -.
DR InParanoid; O42401; -.
DR OMA; PCMLGTH; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; O42401; -.
DR Reactome; R-GGA-3000178; ECM proteoglycans.
DR Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-GGA-8957275; Post-translational protein phosphorylation.
DR PRO; PR:O42401; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000016478; Expressed in testis and 7 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; PF07645; EGF_CA; 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; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Disulfide bond; EGF-like domain; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..452
FT /note="Matrilin-3"
FT /id="PRO_0000007659"
FT DOMAIN 54..229
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 235..275
FT /note="EGF-like 1"
FT DOMAIN 276..316
FT /note="EGF-like 2"
FT DOMAIN 317..357
FT /note="EGF-like 3"
FT DOMAIN 358..398
FT /note="EGF-like 4"
FT COILED 419..451
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 239..250
FT /evidence="ECO:0000250"
FT DISULFID 246..259
FT /evidence="ECO:0000250"
FT DISULFID 261..274
FT /evidence="ECO:0000250"
FT DISULFID 280..291
FT /evidence="ECO:0000250"
FT DISULFID 287..300
FT /evidence="ECO:0000250"
FT DISULFID 302..315
FT /evidence="ECO:0000250"
FT DISULFID 321..332
FT /evidence="ECO:0000250"
FT DISULFID 328..341
FT /evidence="ECO:0000250"
FT DISULFID 343..356
FT /evidence="ECO:0000250"
FT DISULFID 362..373
FT /evidence="ECO:0000250"
FT DISULFID 369..382
FT /evidence="ECO:0000250"
FT DISULFID 384..397
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 49622 MW; 2D65324CEAED4CFB CRC64;
MRRALGTLGC CLALLLPLLP AARGVPHRHR RQPLGSGLGR HGAADTACKN RPLDLVFIID
SSRSVRPEEF EKVKIFLSKM IDTLDVGERT TRVAVMNYAS TVKVEFPLRT YFDKASMKEA
VSRIQPLSAG TMTGLAIQAA MDEVFTEEMG TRPANFNIPK VVIIVTDGRP QDQVENVAAN
ARTAGIEIYA VGVGRADMQS LRIMASEPLD EHVFYVETYG VIEKLTSKFR ETFCAANTCA
LGTHDCEQVC VSNDGSYLCD CYEGYTLNPD KRTCSAVDVC APGRHECDQI CVSNNGSYVC
ECFEGYTLNP DKKTCSAMDV CAPGRHDCAQ VCRRNGGSYS CDCFEGFTLN PDKKTCSAVD
VCAPGRHDCE QVCVRDDLFY TCDCYQGYVL NPDKKTCSRA TTSSLVTDEE ACKCEAIAAL
QDSVTSRLEA LSTKLDEVSQ KLQAYQDRQQ VV
