ID A0A3Q3G408_9LABR Unreviewed; 963 AA.
AC A0A3Q3G408;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0000313|Ensembl:ENSLBEP00000025743.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000025743.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000025743.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLBEP00000025743.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR AlphaFoldDB; A0A3Q3G408; -.
DR STRING; 56723.ENSLBEP00000025743; -.
DR Ensembl; ENSLBET00000027032.1; ENSLBEP00000025743.1; ENSLBEG00000019644.1.
DR GeneTree; ENSGT00940000164061; -.
DR InParanoid; A0A3Q3G408; -.
DR Proteomes; UP000261660; 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 GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; 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:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT DOMAIN 735..781
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 815..927
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..115
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..132
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..533
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..631
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..673
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 97202 MW; D1A7EBFF0DA86656 CRC64;
MEGREEVKKI VEEREYTMPH PELDPTYSTP VQAPPTEMSQ FDDEDIEETS GEEAERTTVR
VKPLQTDHPA SIPDTSLQVS PRQKGEQGEP GPAGPPGPPG PPGQGSGDGQ GGEPGPRGPQ
GPPGTEGTPG LPGKDGQPGS KGETGNAGAT GIPGFPGLQG EPGPKGEKGD TGFGLPGPPG
PPGPPSKSSR FLEGSGFEDF DSDAEIMRGP PGPPGPPGLP GNPSEDLFRG PPGAPGKDGK
NGERGEPGLP GVDGRDGDPG PAGKTGDKGE PGVGGQPGPK GDQGPPGFPG LSGADGPEGP
SGPRGQPGPP GPPGPPGKGY TFDFEDLEGS GILSGAGAVP SRGPPGPPGI PGLEGPKGKD
GLTGVPGGPG QKGEDGIIGR PGFPGLEGLK GAEGPKGNRG DPGLKGEAGR DGKGLPGPPG
PPGPPGPIIN LQDLLLNDTD GAFNFSRIYE AQGASGQGGD MGLPGVRGPP GLKGEKGEPG
FFMAADGAMM SDLAGPKGNK GDIGVAGPAG ITGPVGPSGP KGEFGFPGRP GRPGQNGLKG
AKGESAGQPG LPGPPGPPGR PGLFTCPKGI VFPIPPRPHC KMGLNPDGTV TAGNCQTGIK
GDKGERGQPG PPAPPNTFFP RGGWGAGGDQ GVKGEKGDKG EAGLSGQPGV PGRPGPVGPK
GESVLGPQGL PGVPGSPGVP GYGRPGPVGP PGPPGPPGLP VSSSRYGSAL TFAGPPGPQG
PAGPPGASGS AAPLKTFLSR ESMMQHTLRD TEGTLAYVTG TGSLYLKVSQ GWKEIQLGSL
IHLSNNIIPQ DEPRAAYQIR GDTLERVRSV TERINLVALN QPHSGDMMGL DTADRMCYEQ
AKAMGLPPNY RAFISSHRQD LVHVVYPGFR ETLPVTNLRG DIMFRNWRSI FSGDGGPINS
KIPIYSFDGR DVLVDPFWPH KNIWHMSVMG QSSSLTSGLL LGQQIRSCSN QYIVLCIETH
KNL
//
