ID A0A6P7LT47_BETSP Unreviewed; 1242 AA.
AC A0A6P7LT47;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X6 {ECO:0000313|RefSeq:XP_028997991.1};
GN Name=LOC114850138 {ECO:0000313|RefSeq:XP_028997991.1};
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_028997991.1};
RN [1] {ECO:0000313|RefSeq:XP_028997991.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR RefSeq; XP_028997991.1; XM_029142158.3.
DR AlphaFoldDB; A0A6P7LT47; -.
DR GeneID; 114850138; -.
DR Proteomes; UP000515150; Chromosome 2.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000515150};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1242
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027669777"
FT DOMAIN 34..223
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 284..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..323
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..410
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..542
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..641
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..882
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 128090 MW; C64242DB886E6295 CRC64;
MFLCESWSML TLQTCIFILT VVTQTTSQQR EGSGISLHQL IRDPPPNDIT RTNGPSGETI
YVFTSAAVSS QPALAHVPNP FYRHFSLLFN IKPSTPAASV LFSITDGSQK LMYIAVKLSE
VQSGHQNVQF FYTEPDSEAS YKAASFEVPS LVGTWSRFSL AVFEEQVTFY LGCDSEPQVV
KIERSPDPME LDRGAGIFVG HAGGADPDKF QGEIAELRVV GNPHIAESLC DNDVDAASGD
FGSGDGDGTQ TGHTLKAHSV KTTAAPLHPV PEPPLVFSEG RELLESSKGQ SGPEGKAGDK
GEKGLKGDKG PTGPKGDSGS GSSFNTGVSS EAGEDGQKGE KGAKGSSGFG YPGNKGERGA
QGPPGPPGPP GPAAEVVRLG DGSVVQQVAG PPGPPGQPGL DGPAGPPGAD GEPGDPGEDG
KTGAAGPRGF PGNTGTSGAK GQKGERGESQ PGPRGPPGLP GPPGPGTVSA FMDMEGSGFP
DLDKFKHVRG PPGPPGPPGP PGIPGTSMAI GASGPIAFGP PGPPGQDGAP GLPALPGPRG
APGRPGPRGE KGDSGELGLP GPAGEKGSQG EPGRTGTPGQ IGLAGLPGPM GPVGPPGPPG
PPGPPYSIDS SDQDKHKMIS GLPGLTGQPG PQGPPGIAGL PGKPGLPGNH GDKGAEGPRG
PPGIPGKDGF PGLPGEKGET GRKGEMGLPG RDGGPPGPPG LPGPPGQVIY RSRDDYNELN
ENDRWQGEMG PPGPMGPSGP PGLKGEIGFP GRPGRPGLNG AKGEKGDSGS GSGYGYPGPP
GPPGPPGPPG PLAPVDKLAE YEDFYRYFSG VRPNFDIHSF KNDMKGEPGS PGLKGEKGDP
AGGYYGVPGA PGVPGTPGPK GDSIVGPPGP QGPPGPPGPP LPGIYRGTQT ISIPGPPGPP
GLPGHSGVTV LKNYKTMTAT ARRQPEGSLV YILDQTDLYL RVQHGFRQVQ LGTFVPLPSD
NRNEVASVEP RKDVSYNTVH QSNSATSINS AQISPDSSDP QPDLRYLSPT DPRFPSYSDR
LENPDGRYSV YTGQDRLVHP DSRDAVPPQR RPLPLVPHIP VHHHTLGPAL HLIALNSPHT
GSMRGIRGAD FLCFSQAKAI GMKGTFRAFL SAKLQDLYSI VRKADRDRLP IVNLNDEVLF
DSWEAMLNGG RMKDNVRIYS FDGKDILSDS TWPDKVVWHG STSTGHRHMD NFCETWRVDD
RALSGMASLL QSGSLLQQSS SSCSSSYIVL CIENSYMGQS KR
//
