ID   A0A8C4QLP5_EPTBU        Unreviewed;       707 AA.
AC   A0A8C4QLP5;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 20.
DE   SubName: Full=Collagen type XVIII alpha 1 chain b {ECO:0000313|Ensembl:ENSEBUP00000016800.1};
OS   Eptatretus burgeri (Inshore hagfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC   Myxiniformes; Myxinidae; Eptatretinae; Eptatretus.
OX   NCBI_TaxID=7764 {ECO:0000313|Ensembl:ENSEBUP00000016800.1, ECO:0000313|Proteomes:UP000694388};
RN   [1] {ECO:0000313|Ensembl:ENSEBUP00000016800.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSEBUP00000016800.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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DR   AlphaFoldDB; A0A8C4QLP5; -.
DR   Ensembl; ENSEBUT00000017377.1; ENSEBUP00000016800.1; ENSEBUG00000010540.1.
DR   GeneTree; ENSGT00940000158212; -.
DR   Proteomes; UP000694388; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   Gene3D; 3.40.1620.70; -; 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; IPR016187; CTDL_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694388}.
FT   DOMAIN          488..535
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          632..699
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          1..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..30
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..115
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..264
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..279
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..319
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..466
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  71957 MW;  6ECEEAAB5AD14649 CRC64;
     MNVDQEGSGV FTGEPGLPGL PGPTGISGTP GLPGPQGPKG LLGAKGERGL KGDVGFEGKP
     GPQGSPGNDG KPGLPGPQGP SGVKGEQGPS GKPGADGVGI SGLPGIPGPP GPPGSPGSLR
     EVIYGHTEVI SDLGFFVSIC GEDESIHRHM RRKQMFNKLL LFSFFFLHHQ DSDVVNLLNP
     GRPVAGVSGP PGAEGIPGRA GFPGPRGPKG DHGARGDIGR QGIKGDKGDP ATVITSAEAT
     ITGPPGQKGE RGEPGYAGTG GFLGPRGPRG MKGGIGLPGR PGRPGINGVK GEKGDSSDGS
     FGAQSSRPGP PGPPGPPGRP GASSQFGYIN GVEGHLGIQG LRGAMGHPGL PGNTGQKGDR
     GSPGPPGPAG YTSFVDGFDN QIKGEKGESG NKGEKGDPGS GYGTFNVGPP GPPGPPGKSG
     QKGLAGESIA GPRGPPGRPG SSTHGLPGPP GPAGPPGQSS YYSSGQDPIL QGRPGPPGPP
     GASHSGGVNI LSSFEDLQHM ARTITEGNLA FVKDREEIYV RVSGGWRQLH LGELVAVNKE
     QSNTHPSGTV NVIGWPEEDH QKFPPHERLT TSRGDPENRV PSNPITAPSH GILSWSAGPR
     DTRPHQPSGG RIVKLPLVPG HNIQTNNGRL GLHLIALNTP QVGNMGGIRG TDFQCFQQAQ
     EVGLHGTYRA FLSSKVQDLA SVVLRRDRKS VPVVNLRAQQ ARVARFR
//