ID A0A7K7U158_9CHAR Unreviewed; 390 AA.
AC A0A7K7U158;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=Matrilin-3 {ECO:0000256|ARBA:ARBA00074606};
DE Flags: Fragment;
GN Name=Matn3 {ECO:0000313|EMBL:NXA22709.1};
GN ORFNames=IBISTR_R14410 {ECO:0000313|EMBL:NXA22709.1};
OS Ibidorhyncha struthersii.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Charadriidae;
OC Ibidorhyncha.
OX NCBI_TaxID=425643 {ECO:0000313|EMBL:NXA22709.1, ECO:0000313|Proteomes:UP000587655};
RN [1] {ECO:0000313|EMBL:NXA22709.1, ECO:0000313|Proteomes:UP000587655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-030-25 {ECO:0000313|EMBL:NXA22709.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Major component of the extracellular matrix of cartilage and
CC may play a role in the formation of extracellular filamentous networks.
CC {ECO:0000256|ARBA:ARBA00056017}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXA22709.1}.
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DR EMBL; VZSZ01005122; NXA22709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K7U158; -.
DR Proteomes; UP000587655; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:UniProtKB-ARBA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR FunFam; 3.40.50.410:FF:000018; Matrilin 1; 1.
DR FunFam; 2.10.25.10:FF:000126; Matrilin 3; 1.
DR FunFam; 2.10.25.10:FF:000871; Matrilin 3; 3.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR050525; ECM_Assembly_Org.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR019466; Matrilin_CC_trimer.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24020:SF12; MATRILIN-3; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF10393; Matrilin_ccoil; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Reference proteome {ECO:0000313|Proteomes:UP000587655};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 10..185
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXA22709.1"
FT NON_TER 390
FT /evidence="ECO:0000313|EMBL:NXA22709.1"
SQ SEQUENCE 390 AA; 42747 MW; 14D9C9707F88B5C3 CRC64;
DVACKNRPLD LVFIIDSSRS VRPEEFEKVK IFLSEMIDTL DVGERTTRVA VMNYASTVKV
EFPLRTYFDK ASMKEAISHI EPLSAGTMTG LAIQTAMDEV FTEEMGTRPA TFNIPKVVIV
VTDGRPQDQV QDVAASARTA GIEIYAVGVD RADMQSLRIM ASEPLDEHVF YVETYGVIEK
LTSKFRETFC AATACALGTH DCEQVCVSNG GSYLCDCYEG YTLNPDKRTC SAVDACAPGR
HECDQICVSN NGSYVCECYE GYTLNPDKKT CSATDMCAPG RHDCAQVCLS NDGSYSCGCF
EGYTLNPDKK TCSAVDMCAP GRHDCEQVCV RDDLFYTCDC YQGYTLNPDK KTCSRATTSS
LVTTEESCKC EAIAALQDSV TSRLEALSTK
//
