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Database: UniProt
Entry: A0A673XZ16_SALTR
LinkDB: A0A673XZ16_SALTR
Original site: A0A673XZ16_SALTR 
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
//
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