ID A0A673XZ16_SALTR Unreviewed; 1478 AA.
AC A0A673XZ16;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSSTUP00000027474.1};
GN Name=LOC115160620 {ECO:0000313|Ensembl:ENSSTUP00000027474.1};
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:ENSSTUP00000027474.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000027474.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSTUP00000027474.1}
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 RefSeq; XP_029566685.1; XM_029710825.1.
DR Ensembl; ENSSTUT00000028761.1; ENSSTUP00000027474.1; ENSSTUG00000011874.1.
DR GeneID; 115160620; -.
DR KEGG; stru:115160620; -.
DR GeneTree; ENSGT00940000158212; -.
DR InParanoid; A0A673XZ16; -.
DR OMA; NQWKGER; -.
DR OrthoDB; 5983381at2759; -.
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1478
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025360316"
FT DOMAIN 125..314
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..449
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 495..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..637
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..692
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1063
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1083
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1229
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1478 AA; 152771 MW; FDF4F81B71C1DF87 CRC64;
MDCRIGFQLG VSFLLVLLVG RSEALWFSWG STDGTTEAPT LDNEGSGNPV ASGKSPKLDN
VGEDGAEIID VASGIRKFVQ TWDKNSKATA THKLTTVRSQ ARNEHPMEKD TRWSTSRESK
PDESGVSLLQ LIGDPPPDEI TKIYGPDNSP GYVFGPDANT GQLARAHLPS PFYRDFSLLF
NLKPQSTNGG VIFSVTDPSQ QIMYVGVKLS PVKANRQNVI FYYTEPDSQE SYVAATFPVH
NLADQWNRFS ISVLDDKVTF YINCDDQPQV VRFERSPDEM ELESGAGVFV GQAGGADPNK
FLGVIGELRV VGDPRAAERQ CEEEGDDSDA ASGDGGSGDE GIPDGKKKGS GTSIWDAKVR
KYVRVEDVKL TVTTTPTSSR PIQQPPVTRK QPEVSPKKER DQGGSRGEKG DKGAKGDIGP
LGPKGDSGSE SGTRGGARGE KGVLGEKGMK GKAGFGYPGS KGDPGPAGPP GPPGLPGPAA
EVVSRGDGSV VQTVAGPRGP AGPAGASGPE GPAGADGEPG DPGEDGSQGP VGPPGFPGIP
GDPGLKGEKG DRGEGQPGPR GPPGPPGQPA PARHDRPTFA DMEGSGFPDL ETLRGPPGLP
GPPGLPGAPG TSVVGTGVSG LFGPKGPPGQ DGAPGQPGLR GPPGADGRPG VAGARGEKGD
PGELGLPGAV GAKGAQGLNG IPGQPGQGGL AGLPGPMGPL GQPGPPGPPG PSYRVGFDDM
EGSGVGVANG VPGARGPEGH QGPPGIPGLP GKSGFPGIPG EKGSEGPQGS DGRPGLDGFP
GPNGQKGDRG DRGERGESGR DGNGQPGPPG PPGQIIYQTS SSYDGVVGGA GPQGQAGFPG
PIGPKGDMGD PGQPSYGVKG EKGEPGSIIG PDGNTLYLGR LSGEKGDRGP AGPVGPPGQY
GPPGIKGEFG MPGRPGRPGV NGYKGEKGEP STGAGFSYPG VPGPPGPPGP PGPAVPVDRF
NGYDASRNYP VTKGEKGDSG AQGLPGPPGV ASNFDIFTFK NDLKGEHGDT GVKGEKGEPS
GGYYDPRFGR QQGPPGPPGN PGLMGPKGDS ITGPPGPQGP PGSPGIGYDG RPGNPGPPGP
PGPTGSHSLP GAYRPTHPIS IPGPPGPAGP PGIPGHTSGV TVLRSYDTMI ATARRQSEGT
LIYIVDKTDL YIRVRNGFRQ IMLSDYSPFY RDLDNEVAAV QPPPVVNYPQ SQDHSANNGA
EQFSQGGAAT HPIVPPPRQP IEIPRPAQPN NRDPREPPQY DPRYPSQTDP RYPPQTDGRY
SPVQPENRYP IQPERRYHIT PQRQPVPPPV PQPAGHVHTS GPGLHLIALN TPQVGNMRGI
RGADFLCFQQ ARAVGLKGTF RAFLSSKLQD LYSIVRKSDR DSLPILNLKD HVLFNSWESL
FSKTEGRMEE NAPIYSFDGR DILRDSAWPE KMVWHGSSSE GHRQTDNYCE TWRTGDRTVT
GLASSLQTGQ LLQQLPSSCS NSYIVLCIEN SYLSHSKK
//