ID A0A9W2XM51_BETSP Unreviewed; 1704 AA.
AC A0A9W2XM51;
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 alpha-1(XVIII) chain-like isoform X2 {ECO:0000313|RefSeq:XP_055362732.1};
GN Name=LOC114850138 {ECO:0000313|RefSeq:XP_055362732.1};
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_055362732.1};
RN [1] {ECO:0000313|RefSeq:XP_055362732.1}
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_055362732.1; XM_055506757.1.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1109; COLLAGEN ALPHA-4(IV) CHAIN-LIKE; 1.
DR Pfam; PF01391; Collagen; 3.
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1704
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040787506"
FT DOMAIN 498..687
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 357..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..785
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..872
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..965
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1004
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1067
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1103
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1704 AA; 177706 MW; B71AFA20B8B0F4AA CRC64;
MLRIQMLLFL LVWWVSNARQ TTETPTEATP TETSTRATDM APTMTTAMET TSIAMTSIPA
ETLPATFIPP ETTMSEKTTA IGTNLALTPT QVIPHGTMAN ESRPSDSPEV TTLNKTKPTE
TTLVKITPEG KMVNKTIPTE TSTRDTRTTK MAPTMTTAKE TTLIAMTSMP AETLPATFIP
PETTMSEKTT AIGTNLALTP TQVLPHGTMA NESRPSDSPE VTTLNKTKPT ETTLVKITPE
GTMVNKTMPT ETSTRDTRTM KMAPTMTTDK ETTSIAMTPV PAETLPTTFI PSESTLNQTM
SEGITATTTK PAFALTQIIL HGKMANETRP SDSPTKITEV TPEETTLNMI RPTETTPKRT
VVNSTRPSKT SLANTSKRSP TSITPTHMEL MPEGTKANGI KLQTAKTENM PKEMPTEKAK
TASVTAGTMT GATRNNEVEE VDSVFGFRKE NINIATEEAE LCTIWSVSTS TMTTNPGLIE
KVEIASTTGT DGFREGSGIS LHQLIRDPPP NDITRTNGPS GETIYVFTSA AVSSQPALAH
VPNPFYRHFS LLFNIKPSTP AASVLFSITD GSQKLMYIAV KLSEVQSGHQ NVQFFYTEPD
SEASYKAASF EVPSLVGTWS RFSLAVFEEQ VTFYLGCDSE PQVVKIERSP DPMELDRGAG
IFVGHAGGAD PDKFQGEIAE LRVVGNPHIA ESLCDNDVDA ASGDFGSGDG DGTQTGHTLK
AHSTTAAPLH PVPEPPLVFS EGRELLESSK GQSGPEGKAG DKGEKGLKGD KGPTGPKGDS
GSGSSFNTGV SSEAGEDGQK GEKGAKGSSG FGYPGNKGER GAQGPPGPPG PPGPAAEVVR
LGDGSVVQQV AGPPGPPGQP GLDGPAGPPG ADGEPGDPGE DGKTGAAGPR GFPGNTGTSG
AKGQKGERGE SQPGPRGPPG LPGPPGPGTV SAFMDMEGSG FPDLDKFKHV RGPPGPPGPP
GPPGIPGTSM AIGASGPIAF GPPGPPGQDG APGLPALPGP RGAPGRPGPR GEKGDSGELG
LPGPAGEKGS QGEPGRTGTP GQIGLAGLPG PMGPVGPPGP PGPPGPPYSI DSSDQDKHKM
ISGLPGLTGQ PGPQGPPGIA GLPGKPGLPG NHGDKGAEGP RGPPGIPGKD GFPGLPGEKG
ETGRKGEMGL PGRDGGPPGP PGLPGPPGQV IYRSRDDYNE LNENDRWQGE MGPPGPMGPS
GPPGLKGEIG FPGRPGRPGL NGAKGEKGDS GSGSGYGYPG PPGPPGPPGP PGPLAPVDKL
AEYEDFYRYF SGVRPNFDIH SFKNDMKGEP GSPGLKGEKG DPAGGYYGVP GAPGVPGTPG
PKGDSIVGPP GPQGPPGPPG PPLPGIYRGT QTISIPGPPG PPGLPGHSGV TVLKNYKTMT
ATARRQPEGS LVYILDQTDL YLRVQHGFRQ VQLGTFVPLP SDNRNEVASV EPRKDVSYNT
VHQSNSATSI NSAQISPDSS DPQPDLRYLS PTDPRFPSYS DRLENPDGRY SVYTGQDRLV
HPDSRDAVPP QRRPLPLVPH IPVHHHTLGP ALHLIALNSP HTGSMRGIRG ADFLCFSQAK
AIGMKGTFRA FLSAKLQDLY SIVRKADRDR LPIVNLNDEV LFDSWEAMLN GGRMKDNVRI
YSFDGKDILS DSTWPDKVVW HGSTSTGHRH MDNFCETWRV DDRALSGMAS LLQSGSLLQQ
SSSSCSSSYI VLCIENSYMG QSKR
//
