ID A0A8M1HD52_BETSP Unreviewed; 1077 AA.
AC A0A8M1HD52;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X4 {ECO:0000313|RefSeq:XP_040926375.1, ECO:0000313|RefSeq:XP_055364185.1};
GN Name=LOC114853843 {ECO:0000313|RefSeq:XP_040926375.1,
GN ECO:0000313|RefSeq:XP_055364185.1};
OS Betta splendens (Siamese fighting fish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Osphronemidae; Betta.
OX NCBI_TaxID=158456 {ECO:0000313|Proteomes:UP000515150, ECO:0000313|RefSeq:XP_040926375.1};
RN [1] {ECO:0000313|RefSeq:XP_040926375.1, ECO:0000313|RefSeq:XP_055364185.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
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DR RefSeq; XP_040926375.1; XM_041070441.2.
DR RefSeq; XP_055364185.1; XM_055508210.1.
DR AlphaFoldDB; A0A8M1HD52; -.
DR GeneID; 114853843; -.
DR Proteomes; UP000515150; Chromosome 4.
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; 2.60.120.200; -; 1.
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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1109; COLLAGEN ALPHA-4(IV) CHAIN-LIKE; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000515150}.
FT DOMAIN 827..875
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 907..1073
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 74..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..216
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..440
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..568
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..817
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 109439 MW; 6434639B53B8636C CRC64;
MSDLTGRWAR FTLTVQGAEV RLYMDCEEYH RVAFTRSPQP LTFEASSGIF VGNAGGTGLT
RFVGSIQQLL LKSDPTAPDD QCEEDDPYAS GYGSGDDTYR SLEEGDEVKK VVEERDYPMP
FPDLEPSYST MISAPPTEMS VPVDDDDDDD NDEDIEISGQ EDEVTTVKVR TPHEATPASV
PDTVSSGRKG EPGEPGPAGP PGPTGPPGQA TGQEPGPRGP QGPEGPPGPP GEPGKDGQPG
SKGQTGLNGA AGIPGFPGLQ GDPGPKGEKG DPGVGQPGAQ GPPGPPGPPG LKSSMFPEGS
GFEDFDSDAE IFRGPPGPPG PPGPPGTPAE GIFSGQAGKD GKDGETGEPG LPGVDGKDGD
PGPAGEKGEK GDPGLIGLPG QKGDQGPPGF PGLPGSEGPD GQPGPRGPPG PPGPPGKPLP
FDFEDLEGSG LLSGFGSGGP QGPPGLPGLR GPKGKDGFDG SPGKPGLKGE PGVAGPPGFP
GIDGQKGAEG AKGDKGDLGQ KGEAGQDGLS LRGPPGPPGP PGPIINLQDL LLNDTDGAFN
FSGIFEAQGP PGPKGDIGLP GLQGPPGLKG EKGAAGFVIT ADGSIVSGPT GPRGVKGDNG
VPGPPGAPGP VGPAGPKGEL GFPGRNGRPG LTGPKGERGD SVGLPGPPGP PGPPGRPGMF
NCPKGTVFPI PPRPHCKVVL NGGGTVSVGN CQTGGKGEKG ERGLPGMPAP SNSFVSRGDL
GVKGDQGIKG EKGDKGEAGL PGQPGRPGLV GPKGESVLGP PGPPGVPGSP GIQGYGRTGP
VGPPGPPGPP GPPGPPSRYG SALTIAGPPG PPGPAGPPGS LSNAASVKTF ATRESMMQQT
MRNPEGTLLY VTSTGSLFLK VSQGWKEIQL GNMIYLSNNI IPQDEPRVAY HVRGEVKERI
ASANERLNLV ALNQPHTGDM MGLDMADRMC YEQAKAMGLP PHYRAFISSH RQDLVHVVYP
GSRDTLPVTN LRGDVIFRNW RSIFNGDGGR INPRIPIYSF DGRDVLVDPF WPQKSIWHGS
TSRGLRVVDK HCETWHADHM SVIGQSSSLT SGLLLGQQTR SCSNEYIVLC IETHKNL
//
