ID A0A9W2XIC9_BETSP Unreviewed; 1432 AA.
AC A0A9W2XIC9;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Collagen type XVIII alpha 1 chain a isoform X2 {ECO:0000313|RefSeq:XP_055361330.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_055361330.1};
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_055361330.1};
RN [1] {ECO:0000313|RefSeq:XP_055361330.1}
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_055361330.1; XM_055505355.1.
DR GeneID; 114847460; -.
DR CTD; 564123; -.
DR Proteomes; UP000515150; Chromosome 21.
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 CDD; cd00247; Endostatin-like; 1.
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 ECO:0000313|RefSeq:XP_055361330.1};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1432
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040853350"
FT DOMAIN 111..300
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 69..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..87
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..327
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..484
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..504
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..527
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..595
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..620
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..678
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..759
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..799
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1023
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1066
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1432 AA; 146322 MW; 0973D53089A3484A CRC64;
MKTQFGVLVF IAQGLLYSEA WFWSWSSTTT AAPAVDHEGS GSFPGSGEQL QEDGAAAEII
NEGHGIQEVA QTTERPPQTT LIPTTQLEND WAPEMSTEEG SSLASTPEDN GVSLLQLIGD
PPPSEISLVY GPDNSPRYVF GPDANVGQLA QTYLPNPFYR NFALIFNLKP TSDNGGVVFS
LTDEQQQIIY VGVKLSAVQG GHQHVILYYT EPDSQASYEA ARFRVPSMRD TWTRFAVAVR
DDKVMLYLNC DIDPQVMRIE RSPDEMELDA GAGVFVGQAG GADPDRFLGV IGELRVVGDP
SAAERHCEEE EDDSDAASGD GSGYAEARPT DPAVKRLTTA PPSSRPIQQP PLIRRDEVSI
TRETASDSQH ISVLVKPRPS APGSPGPAGP KGVKGDRGEK GDKGDRGPTG PKGETGSGSS
LRGGTRGEKG EPGEKGAKGS AGFGYQGKKG EPGPPGPAGP PGPPGPATEL SVGSDGSVVS
RVPGPRGPPG PPGVPGSEGP PGAEGEPGDP GEDGKTGPEG PRGFPGTPGD PGPKGEKGDR
GEGQPGPKGP PGPPGPPGQG LRSTFVDMEG SGFPDLESFR GLPGPPGPPG PPGPAGPSTT
GTITSSGAFG PPGKEGAPGK PGLPGLPGAD GSPGAPGPKG EKGDSGELGL PGAVGQKGAQ
GEAGLPGPTG EPGLAGLPGP MGPVGSPGPP GPPGPSYRVG FDDMEGSGGG FTNGLPGIRG
PQGRQGSPGV PGLPGQPGQP GTPGPKGSEG PAGGEGQPGL DGFPGAQGPK GDRGDKGERG
EPGRDGTGLP GPPGPPGPPG QIIYHTSGNV DSVIGNAGHQ GPVGPKGDRG DPGHPGYGVK
GEKGEPGLII GPDGNPLHLA GLTGPRGERG LPGPAGPTGP YGPPGLKGEI GMPGRPGRPG
VNGYKGEKGE SGGGAAYSYP GVPGPPGPPG PPGPPGPAIP LDRLNRHDET SRSYTAIKGE
KGERGLPGFP GTASNFDIYA FKSELKGEPG VKGEKGEPGG GYYDPRFGGV QGQPGPPGRP
GLPGPKGDSV IGPAGPQGPA GPPGIGYNGH PGPPGPPGPP GPPASPVPGT YGPNYSVSVP
GPPGPPGPPG SPGLSSGVTV LRSYDTMIGT ARRQAEGSLI YIIDKADLYL RVRDGVRQVM
LGDYSPFFRD LENEVAEVQP PPVILYPQSQ DQSQSNGAGH YSQGVPVIQP IGPPPQTPVE
PIYPPQYDSR FPNIKQTGHT DGSLATQQTD GRYSATPPRR PSPPVPQPGV HVDAFRSVLH
LVALNAPQTG NMRGIRGADF LCFQQARAVG LKGTFRAFLS SKLQDLYTIV RRTDRDNVHI
VNLKDQVLFS SWESLFSAED TMRDNVPIYS FDGRDILRDS AWPEKMVWHG SSTKGHRQTD
HYCETWRASD RAVTGLAASL QSGHLLQQTS SSCSGSYIVL CIENAITSHS SK
//
