ID A0A1S3PL21_SALSA Unreviewed; 1481 AA.
AC A0A1S3PL21;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X1 {ECO:0000313|RefSeq:XP_014028365.1};
GN Name=LOC106586062 {ECO:0000313|RefSeq:XP_014028365.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP001652741, ECO:0000313|RefSeq:XP_014028365.1};
RN [1] {ECO:0000313|RefSeq:XP_014028365.1}
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_014028365.1; XM_014172890.2.
DR GeneID; 106586062; -.
DR KEGG; sasa:106586062; -.
DR OMA; NQWKGER; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP001652741; Chromosome ssa25.
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 ECO:0000313|RefSeq:XP_014028365.1};
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:UP001652741};
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..1481
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010175416"
FT DOMAIN 125..314
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 32..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..127
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..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
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 507..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..654
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 749..759
FT /note="Low complexity"
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 806..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..957
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1066
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1086
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1232
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 153036 MW; 4CD51707CD92C540 CRC64;
MDCRIGFQLG VSFLLVLLVG RSEALWFSWG STDGTTEAPT LDNEGSGNPV ASGKSPKPDN
VGEDGAEIID VASGIRKFVQ TWDKNSKATE THKLTTVRSQ ARNERPMEKD TRWSTSRESK
PDESGVSLLQ LIGDPPPDEI TKIYGPDNSP GYVFGPDANT GQLARAHLPS PFYRDFSLLF
NLKPQSTNGG VIFSVTDPSQ QIMYVGVKLS PVKANRQNVI FYYTEPDSQE SYVAATFPVH
NLSDQWNRFS ISVLDDKVTF YINCDDQPQV VRFERSPDEM ELESGAGVFV GQAGGADPNK
FLGVIGELRV VGDPRAAERQ CEEEGDDSDA ASGDGGSGDE GIPDGKKKGS GTSIWDAKVR
KYVRVEDVKL TVTTTPTSSR PIQQPPLTRK QPEVSPKKER DQGGSRGEKG DKGAKGDIGP
LGSKGDSGSE SGARGGARGE KGVLGEKGMK GKAGFGYPGS KGDPGPAGPP GPPGLPGPAA
EVVSRGDGSV VQTVAGPRGP AGPPGAAGPE GPAGADGEPG DPGEDGSQGP VGPPGFPGIP
GDPGLKGEKG DRGEGQPGPR GPPGPPGQPA PARHDRPTFA DMEGSGFPDL ETLRGPPGLP
GPPGLPGAPG TSVVGTGVSG LFGPKGPPGQ DGAPGQPGLH GPPGADGRPG AAGARGEKGD
PGELGLPGAV GAKGAQGLNG IPGQPGQGGL AGLPGPMGPL GQPGPPGPPG PSYRVGFDDM
EGSGVGVANG VPGARGPEGH QGPPGIPGIP GKSGFPGIPG EKGSEGPQGS DGRPGLDGFP
GPNGQKGDRG DRGERGESGR DGNGQPGPPG PPGPPGQIIY QTSSSYDGVV GGTGPQGQAG
FPGPIGPKGD MGDPGQPSYG VKGEKGEPGS IIGPDGNTLY LGRLSGEKGD RGPAGPVGPP
GQYGPPGIKG EFGMPGRPGR PGVNGYKGEK GEPSTGAGFS YPGVPGPPGP PGPPGPAVPV
DRFNGYDASR NYPVTKGEKG DSGAQGLPGP PGVASNFDIF TFKNDLKGER GDTGVKGEKG
EPSGGYYDPR FGRQQGPPGP PGNPGLMGPK GDSITGPPGP QGPPGSPGIG YDGRPGNPGP
PGPPGPTGSH SLPGAYRPTH PISIPGPPGP AGPPGIPGHT SGVTVLRSYD TMIATARRQS
EGTLIYIVDK TDLYIRVRNG FRQIMLSDYS PFYRDLDNEV AAVQPPPVVN YPQSQDHSAN
NGAEQFSQGG AATNPIVPPP RQPIEIPRPA QPNNRDPREP PQYDPRYPSQ TDPRYPPQTD
GRYIPVQPEN RYPTQPERRY HITPQRQPVP PPVPQPAGHV HTSGPGLHLI ALNTPQVGNM
RGIRGADFLC FQQARAVGLK GTFRAFLSSK LQDLYSIVRK SDRDSLPILN LKDHVLFNSW
ESLFSKTEGR MEENASIYSF DGRDILRDSA WPEKMVWHGS SSEGHRQTDN YCETWRTGDR
AVTGLASSLQ TGQLLQQLPS SCSNSYIVLC IENSYLSHSK K
//
