ID A0A8B6F802_MYTGA Unreviewed; 1712 AA.
AC A0A8B6F802;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=Collagen, type XVIII, alpha {ECO:0000313|EMBL:VDI44935.1};
GN ORFNames=MGAL_10B039461 {ECO:0000313|EMBL:VDI44935.1};
OS Mytilus galloprovincialis (Mediterranean mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=29158 {ECO:0000313|EMBL:VDI44935.1, ECO:0000313|Proteomes:UP000596742};
RN [1] {ECO:0000313|EMBL:VDI44935.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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:VDI44935.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYJE01006319; VDI44935.1; -; Genomic_DNA.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000596742; Unassembled WGS sequence.
DR GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR FunFam; 1.10.630.10:FF:000182; Cytochrome P450 3A4; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF918; COLLAGEN ALPHA-1(IX) CHAIN; 1.
DR Pfam; PF01391; Collagen; 7.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:VDI44935.1};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000596742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1712
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032312324"
FT DOMAIN 24..217
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 226..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..603
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..734
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..826
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1095
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1712 AA; 177552 MW; 60F727C4F747266F CRC64;
MWHFQVIFPL VCIFVQVYTQ SETEVDLLAA IGLPDPSKGV TYDVGLEGFP AFKLDKSSYI
RKAAETYFTD RIGKINDFAI GITVKVFSKD GILFAVKNIY ETVIAFGVRI TATGNGKHNV
ILYYKEDHQY GQMSVTIGNF TVDNIDRNSF TKLAIKVQGD TVTLFDNCEE VGRQQVLNRQ
PLQFSQGSPL YIGQGGPNFE DTSFEGVIQE LKYYTNPAKA EELDCLSLDS GSGSGDKDDD
EDRFKPVITL PPPTAKPGEK GEKGDVGEPG KDGKDGKDGE KGEKGDIGPV GPVGPPGPPP
SLTPPPPEML EDMMGAKGER GETGPRGEQG ETGIDGFPGQ KGEKGDPGNN GPEGPAGIQG
PKGDPGDRGL PGIGQVGPQG DPGLPASVNT QEIVDIILSQ VHMDQGQKGE KGETGDRGEN
GSDGSDGREG IPGRDGLPGL DGVKGEKGDT VVGPEGPRGL VGPQGENGLP GSNGVAGPVG
PMGPPGPPGL PGPGGLNIEG SGDGDGEPGL PGPPGPVGPM GPQGIQGVVG PMGPAGHKGD
AGIIGTPGIP GLPGTPGTPG VFAGNISEMI GKPGKDGAPG LQGEPGLPGE YGPRGFDGPV
GPAGDKGDKG DAGEPGPRGQ AGINGEPGAT GPIGPQGIQG LSGNDGSVGP QGLPGPPGPP
GSGYDGPRRG DTGLVDIEGS GDCGCEPGTP GIQGPQGPPG KQGLQGPAGI PGIPGEIGRQ
GPIGEPGIRG PAGPKGDSGK DGIHGTPGEE GIPGKPGLPG RQGDPGLNGQ NGPKGDTGEP
GKSIQGPTGA TGSPGVQGPA GPPGPPGKTI IETDGGSGDI DGGLGVRGPA QKGDKGDDGA
TGPAGPRGVD GVPGIPGEPG NPGLPGLQGL RGEDGLVGLR GSDGKDGKDG EAGPEGPSGP
PGVNGEKGER GLPGPIGVLP DGVTGGVGVK GEKGDTGEPG PMGPEGPQGP VGPRGFRGPK
GDIGMTGLPG YRGLRGRKGD RGRPGFNGLR GYKGDSGPVG PAGPPGPGFG GSGEILKGAK
GDLGERGLPG IPGTPGIGAQ GPRGDQGEPG RNGLPGFQGP PGPAGKAGTG EVIRGPPGPP
GPPGPSGVGT NGGGGGGGGA VTYRNYNELM SVARILPVGT MCYLVEEETV YLRVNKGFRV
IELGETVPLP PITTPAAGVR PLPTEEASNI IVLPEGEMQS DQPRLYIFAL NAPLSGRMGG
IRGADAKCYK QAKKAGKKGT YRAFLSTKTQ DLTSIVYYDI DKSVPIVNMK DQILFNSWKQ
LLNGHGGYFN TQRHIYSFDG EDIMTSPRWP QKIYTQIFVQ SFGVRIVSLC NHPANRLTSP
MIGQPNMTNR TRSIGYQGAN GLCADAVHLK YFITIGSPGP KGQQNQASSQ QFVDMFSTII
NIILHKDCFD LLNIPTGFHG LDIELVKKYG SVVGTYVGHF PSILISDPDM IKEIWVKDFK
HFSDRPELAY AGEMAYSAVT LAKGEHWKFL RHVLSPSFSP AKLKQMFSSI EDCSDQLIYQ
MKKQSQRNKH VNMEQICQGF SMDVICGTAF GLKVDSQENP NNEFIKMAKE MTSLKFSSPL
FLLQAFFPEL RHVFSKFEIR PFPSDAIDFF MDITKTAIQK RKDNKMTRPD FLQLMINNYK
GERDADIKNG TIEMYKQRGI TETEILANSL IFFLDGYDTT ASGLIFSIYR MAVHQEFQER
LFKEIDHEIG KVINTLSFCF CTDIVHCYNY VN
//
