ID A0A9W2XHZ3_BETSP Unreviewed; 1351 AA.
AC A0A9W2XHZ3;
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 X5 {ECO:0000313|RefSeq:XP_055361332.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_055361332.1};
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_055361332.1};
RN [1] {ECO:0000313|RefSeq:XP_055361332.1}
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_055361332.1; XM_055505357.1.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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_055361332.1};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1351
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040931543"
FT DOMAIN 30..219
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 220..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..246
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..423
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..446
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..539
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..597
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..614
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..678
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..857
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..985
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1351 AA; 137789 MW; 37491FBCB6E1C086 CRC64;
MRCSSELKRF VCCLLVLVSP AAAQWPEDNG VSLLQLIGDP PPSEISLVYG PDNSPRYVFG
PDANVGQLAQ TYLPNPFYRN FALIFNLKPT SDNGGVVFSL TDEQQQIIYV GVKLSAVQGG
HQHVILYYTE PDSQASYEAA RFRVPSMRDT WTRFAVAVRD DKVMLYLNCD IDPQVMRIER
SPDEMELDAG AGVFVGQAGG ADPDRFLGVI GELRVVGDPS AAERHCEEEE DDSDAASGDG
SGYAEARPTD PAVKRLTTAP PSSRPIQQPP LIRRDEVSIT RETASDSQHI SVLVKPRPSA
PGSPGPAGPK GVKGDRGEKG DKGDRGPTGP KGETGSGSSL RGGTRGEKGE PGEKGAKGSA
GFGYQGKKGE PGPPGPAGPP GPPGPATELS VGSDGSVVSR VPGPRGPPGP PGVPGSEGPP
GAEGEPGDPG EDGKTGPEGP RGFPGTPGDP GPKGEKGDRG EGQPGPKGPP GPPGPPGQGL
RSTFVDMEGS GFPDLESFRG LPGPPGPPGP PGPAGPSTTG TITSSGAFGP PGKEGAPGKP
GLPGLPGADG SPGAPGPKGE KGDSGELGLP GAVGQKGAQG EAGLPGPTGE PGLAGLPGPM
GPVGSPGPPG PPGPSYRVGF DDMEGSGGGF TNGLPGIRGP QGRQGSPGVP GLPGQPGQPG
TPGPKGSEGP AGGEGQPGLD GFPGAQGPKG DRGDKGERGE PGRDGTGLPG PPGPPGPPGQ
IIYHTSGNVD SVIGNAGHQG PVGPKGDRGD PGHPGYGVKG EKGEPGLIIG PDGNPLHLAG
LTGPRGERGL PGPAGPTGPY GPPGLKGEIG MPGRPGRPGV NGYKGEKGES GGGAAYSYPG
VPGPPGPPGP PGPPGPAIPL DRLNRHDETS RSYTAIKGEK GERGLPGFPG TASNFDIYAF
KSELKGEPGV KGEKGEPGGG YYDPRFGGVQ GQPGPPGRPG LPGPKGDSVI GPAGPQGPAG
PPGIGYNGHP GPPGPPGPPG PPASPVPGTY GPNYSVSVPG PPGPPGPPGS PGLSSGVTVL
RSYDTMIGTA RRQAEGSLIY IIDKADLYLR VRDGVRQVML GDYSPFFRDL ENEVAEVQPP
PVILYPQSQD QSQSNGAGHY SQGVPVIQPI GPPPQTPVEP IYPPQYDSRF PNIKQTGHTD
GSLATQQTDG RYSATPPRRP SPPVPQPGVH VDAFRSVLHL VALNAPQTGN MRGIRGADFL
CFQQARAVGL KGTFRAFLSS KLQDLYTIVR RTDRDNVHIV NLKDQVLFSS WESLFSAEDT
MRDNVPIYSF DGRDILRDSA WPEKMVWHGS STKGHRQTDH YCETWRASDR AVTGLAASLQ
SGHLLQQTSS SCSGSYIVLC IENAITSHSS K
//
