ID A0A9Y4NHP4_9TELE Unreviewed; 1410 AA.
AC A0A9Y4NHP4;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0000313|RefSeq:XP_008297477.1};
GN Name=LOC103370267 {ECO:0000313|RefSeq:XP_008297477.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Proteomes:UP000694891, ECO:0000313|RefSeq:XP_008297477.1};
RN [1] {ECO:0000313|RefSeq:XP_008297477.1}
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_008297477.1; XM_008299255.1.
DR GeneID; 103370267; -.
DR Proteomes; UP000694891; Unplaced.
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:UP000694891};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 9..198
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 203..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..303
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..376
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..580
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..793
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..814
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..925
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..969
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_008297477.1"
SQ SEQUENCE 1410 AA; 144453 MW; E7D43D201C0A62B0 CRC64;
ISCFAEESGV SLLQLIGDPP PNAITRDYGP SGETAYVFTS AAASGQPALA HVPNPFYRHF
SLIFHIKPSR SAASVLFSIT DGPQRLMYIG VKLSAVQSGR QKVQFFYTEP DSEASYEAAS
FTVPSLVDTW SRFSLAVFEE QVTFYHGCDS EPQVVKFERS PDPMELDSAA GIFVGQAGGA
DDDKFQGSIA ELKVVGNPRA AERLCDDEDD ADAASGDYGS GESDRRQSGH SAKTTPASFR
PVPEPPLTSS QGSRVKESGP GGAKGEKGDR GEKGLRGDRG PTGPKGEPGS GSGSGSSSGG
GGQKGEKGAK GSSGFGYPGN KGDRGAQGPP GPPGPPGPAA EVVRLGDGSV VQQVAGPAGP
PGPAGADGAA GPPGTDGEPG DPGEDGKAGP AGPRGFPGTP GSAGAKGQKG ERGEAQPGPR
GPPGPPGPPG PGNGDRPTFF DMEGSGFPDL DRMRGPRGPP GLPGPPGPPG TSVALGTNGA
VAFGPPGPPG QDGVPGLPGP PGPPGPPGRP GTVKGEKGDS GELGLPGAAG EKQNAQDSGF
FTGLFSYFTP SSTVCSGSQG AQGDPGQTGT PGQTGLAGLP GPMGPIGPPG PPGPPGPPYR
VGYNDQNGYE VFNGGTGVGG PPGPQGPPGI AGLPGKPGLP GSHGNKGAEG PRGPPGISGL
DGFPGQQGEK GERGVKGDMG LPGRDGGPPG PPGPPGPPGQ TVYQPTGDYN DVYWNEGGQG
GGIPGRAGFP GPIGPKGDKG ESGPPGYAPK GEKGEPGLIM GPDGRPLYVG GLQGKPGDPG
LPGPEGPPGP YGPSGPKGEI GLPGRPGRPG LNGARGEKGD SGGGSGYGYP GPPGPPGPPG
PPGPSVPVDG ARGYDDYSRY FPVKGDKGDP GPPGTLEIPG FGSNVDIYTL KYQLKGDVGS
KGEKGEPGGG YYDPRYGGSG VGAPGAPGPP GPPGDPIVGP PGPPGPQGPP GRGYDGQPGP
PGPPGPPGPT LSGTHRGTQT ISIPGPPGPP GAPGLPGHSS GVTVLRSYET MAATARRQPE
GSLVYVIEQT DLYLRVRDGV RQVQLGSYIP LPIGDGNEVA AVEPPPVVPY YPDHHHNNPG
TATHESQRPP ENPVETQPQP QPEQPYPDPR YQPDPRYQPE QPYPDPRYQP EQPYPDPRYQ
PEQPYPDPRY QPEQPYPDPR YQPEQPYPDP RYQPDPRYQP DPRYPAPTDP RFPSYSDRLN
QPDGRYSVPE SRHPVTPARR PPPPVPQTPL HRHTSGPGLH LVALNSPQTG AMRGIRGADF
MCFTQAQAIG MKGTFRAFLS ARLQDLHSIV RKADRDSMPI VNLKDEVLFD SWDAIFNDGR
MKDRVPIYSF DGRDVLSDSA WPEKTMWHGS TSGGQRHVDS FCETWRVGER ALTGMASPLQ
GGGGLLQQSS SSCSSSYIVL CIENSYIAKR
//
