ID A0A6P7MBA0_BETSP Unreviewed; 1223 AA.
AC A0A6P7MBA0;
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 X1 {ECO:0000313|RefSeq:XP_029003498.1};
GN Name=LOC114853843 {ECO:0000313|RefSeq:XP_029003498.1};
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_029003498.1};
RN [1] {ECO:0000313|RefSeq:XP_029003498.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_029003498.1; XM_029147665.3.
DR AlphaFoldDB; A0A6P7MBA0; -.
DR GeneID; 114853843; -.
DR KEGG; bspl:114853843; -.
DR InParanoid; A0A6P7MBA0; -.
DR OrthoDB; 10060752at2759; -.
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 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; 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 SMART; SM00210; TSPN; 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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1223
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028294473"
FT DOMAIN 33..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 220..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..362
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..586
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..714
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 125238 MW; 624C2CE4C9310AC9 CRC64;
MTSRFPPWVF GLFLLVCCSS GDQLLGDRGS KGDLDLTELI GVPLPPSVSF VTGFEGYPAY
SFGADANVGR LAKSFVPDPF YHDFGITVTA KPTTRRGGVL FAITDAYQKI VHLGVALSEV
EDGSQRVVLY YTDPGTRRTQ EAASFKMSDL TGRWARFTLT VQGAEVRLYM DCEEYHRVAF
TRSPQPLTFE ASSGIFVGNA GGTGLTRFVG SIQQLLLKSD PTAPDDQCEE DDPYASGYGS
GDDTYRSLEE GDEVKKVVEE RDYPMPFPDL EPSYSTMISA PPTEMSVPVD DDDDDDNDED
IEISGQEDEV TTVKVRTPHE ATPASVPDTV SSGRKGEPGE PGPAGPPGPT GPPGQATGQE
PGPRGPQGPE GPPGPPGEPG KDGQPGSKGQ TGLNGAAGIP GFPGLQGDPG PKGEKGDPGV
GQPGAQGPPG PPGPPGLKSS MFPEGSGFED FDSDAEIFRG PPGPPGPPGP PGTPAEGIFS
GQAGKDGKDG ETGEPGLPGV DGKDGDPGPA GEKGEKGDPG LIGLPGQKGD QGPPGFPGLP
GSEGPDGQPG PRGPPGPPGP PGKPLPFDFE DLEGSGLLSG FGSGGPQGPP GLPGLRGPKG
KDGFDGSPGK PGLKGEPGVA GPPGFPGIDG QKGAEGAKGD KGDLGQKGEA GQDGLSLRGP
PGPPGPPGPI INLQDLLLND TDGAFNFSGI FEAQGPPGPK GDIGLPGLQG PPGLKGEKGA
AGFVITADGS IVSGPTGPRG VKGDNGVPGP PGAPGPVGPA GPKGELGFPG RNGRPGLTGP
KGERGDSVGL PGPPGPPGPP GRPGMFNCPK GTVFPIPPRP HCKVVLNGGG TVSVGNCQTG
GKGEKGERGL PGMPAPSNSF VSRGDLGVKG DQGIKGEKGD KGEAGLPGQP GRPGLVGPKG
ESVLGPPGPP GVPGSPGIQG YGRTGPVGPP GPPGPPGPPG PPSRYGSALT IAGPPGPPGP
AGPPGSLSNA ASVKTFATRE SMMQQTMRNP EGTLLYVTST GSLFLKVSQG WKEIQLGNMI
YLSNNIIPQD EPRVAYHVRG EVKERIASAN ERLNLVALNQ PHTGDMMGLD MADRMCYEQA
KAMGLPPHYR AFISSHRQDL VHVVYPGSRD TLPVTNLRGD VIFRNWRSIF NGDGGRINPR
IPIYSFDGRD VLVDPFWPQK SIWHGSTSRG LRVVDKHCET WHADHMSVIG QSSSLTSGLL
LGQQTRSCSN EYIVLCIETH KNL
//
