ID A0A673XYP2_SALTR Unreviewed; 1379 AA.
AC A0A673XYP2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSSTUP00000027357.1};
GN Name=LOC115160620 {ECO:0000313|Ensembl:ENSSTUP00000027357.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000027357.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000027357.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSTUP00000027357.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSSTUT00000028640.1; ENSSTUP00000027357.1; ENSSTUG00000011874.1.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000472277; Chromosome 24.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF936; COLLAGEN TYPE VI ALPHA 2 CHAIN; 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 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:UP000472277};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1379
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025377207"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..322
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 373..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..423
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 504..513
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..544
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..599
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..855
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..964
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..984
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1130
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1379 AA; 142156 MW; EA4F063EE7A446FA CRC64;
MKMRCSSWLE TLVCSVLVLL TPAASQWPDE SGVSLLQLIG DPPPDEITKI YGPDNSPGYV
FGPDANTGQL ARAHLPSPFY RDFSLLFNLK PQSTNGGVIF SVTDPSQQIM YVGVKLSPVK
ANRQNVIFYY TEPDSQESYV AATFPVHNLA DQWNRFSISV LDDKVTFYIN CDDQPQVVRF
ERSPDEMELE SGAGVFVGQA GGADPNKFLG VIGELRVVGD PRAAERQCEE EGDDSDAASG
DGGSGDEGIP DGKKKGSGTS IWDAKVRKYV RVEDVKLTVT TTPTSSRPIQ QPPVTRKQPE
VSPKKERDQG GSRGEKGDKG AKGDIGPLGP KGDSGSESGT RGGARGEKGV LGEKGMKGKA
GFGYPGSKGD PGPAGPPGPP GLPGPAAEVV SRGDGSVVQT VAGPRGPAGP AGASGPEGPA
GADGEPGDPG EDGSQGPVGP PGFPGIPGDP GLKGEKGDRG EGQPGPRGPP GPPGQPAPAR
HDRPTFADME GSGFPDLETL RGPPGLPGPP GLPGAPGTSV VGTGVSGLFG PKGPPGQDGA
PGQPGLRGPP GADGRPGVAG ARGEKGDPGE LGLPGAVGAK GAQGLNGIPG QPGQGGLAGL
PGPMGPLGQP GPPGPPGPSY RVGFDDMEGS GVGVANGVPG ARGPEGHQGP PGIPGLPGKS
GFPGIPGEKG SEGPQGSDGR PGLDGFPGPN GQKGDRGDRG ERGESGRDGN GQPGPPGPPG
QIIYQTSSSY DGVVGGAGPQ GPIGPKGDMG DPGQPSYGVK GEKGEPGSII GPDGNTLYLG
RLSGEKGDRG PAGPVGPPGQ YGPPGIKGEF GMPGRPGRPG VNGYKGEKGE PSTGAGFSYP
GVPGPPGPPG PPGPAVPVDR FNGYDASRNY PVTKGEKGDS GAQGLPGPPG VASNFDIFTF
KNDLKGEHGD TGVKGEKGEP SGGYYDPRFG RQQGPPGPPG NPGLMGPKGD SITGPPGPQG
PPGSPGIGYD GRPGNPGPPG PPGPTGSHSL PGAYRPTHPI SIPGPPGPAG PPGIPGHTSG
VTVLRSYDTM IATARRQSEG TLIYIVDKTD LYIRVRNGFR QIMLSDYSPF YRDLDNEVAA
VQPPPVVNYP QSQDHSANNG AEQFSQGGAA THPIVPPPRQ PIEIPRPAQP NNRDPREPPQ
YDPRYPSQTD PRYPPQTDGR YSPVQPENRY PIQPERRYHI TPQRQPVPPP VPQPAGHVHT
SGPGLHLIAL NTPQVGNMRG IRGADFLCFQ QARAVGLKGT FRAFLSSKLQ DLYSIVRKSD
RDSLPILNLK DHVLFNSWES LFSKTEGRME ENAPIYSFDG RDILRDSAWP EKMVWHGSSS
EGHRQTDNYC ETWRTGDRTV TGLASSLQTG QLLQQLPSSC SNSYIVLCIE NSYLSHSKK
//
