ID A0A8U1F761_SALNM Unreviewed; 1486 AA.
AC A0A8U1F761;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X3 {ECO:0000313|RefSeq:XP_038871040.1};
GN Name=LOC120064493 {ECO:0000313|RefSeq:XP_038871040.1};
OS Salvelinus namaycush (Lake trout) (Salmo namaycush).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salvelinus.
OX NCBI_TaxID=8040 {ECO:0000313|Proteomes:UP000808372, ECO:0000313|RefSeq:XP_038871040.1};
RN [1] {ECO:0000313|RefSeq:XP_038871040.1}
RP IDENTIFICATION.
RC TISSUE=White muscle {ECO:0000313|RefSeq:XP_038871040.1};
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_038871040.1; XM_039015112.1.
DR GeneID; 120064493; -.
DR Proteomes; UP000808372; Chromosome 19.
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:0032836; P:glomerular basement membrane development; 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: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:UP000808372};
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..1486
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036491826"
FT DOMAIN 125..314
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 33..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..382
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..523
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..696
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..715
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..964
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1094
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1486 AA; 152795 MW; C7C91A9A9D8C95AD CRC64;
MDCKIGFQLS ISLLVVVLVG RCEAFWFSWG STDGTTEDPS LDNEGSGNPV TSNESPMPEN
IEEVGADIID IASGIENFVQ TWNQNAKAKE APKLTTVRSK ARNERPMERG AGRHTSKGSK
PDEIGVSLLH LIGDPPPDEI TKIYGPDNSP GYVFGPDANT GQLARAHLPS PFYRDFSLLF
NLKPQSTKGG VIFSVTDASQ KIMYVGVKLS PVKASKQNVI FYYTEPDSQV SYVAATFPVH
SLADQWNRFS ISVLDDKVTF YINCDDQPQV VRFERSPDEM ELEAGAGVFV GQAGGADPDK
FLGVIGELRV VGNPRAAERQ CEEEGDDSDV ASGDGGSGDV EGKLDVKKKG PGTFKWDAEV
QKHVWVEDDR PTVTTTPPSS RPIQQPPVTR QQPEVSPKKE TGPGGSRGEK GDRGEKGDRG
PFGPKGDSGS ESGTRGGARG EKGVPGEKGL KGKAGFGYPG SKGDPGPAGP PGPPGSPGSP
GSAAEVVSRG DSSGIPTVAG PRGPAGTPGP AGPEGPAGAA GEPGDPGEDG SQGLVGPPGF
PGTPGDSGLK GEKGDRGEGQ PGPSGPPGPP GLPAPSSHDR PTFVDMEGSG FPDLETLRGL
PGLPGPPGLP GAPGPAVVGT GLSSSFGPRG PPGQDGAPGQ PGLPGPPGTD GRPAVAGARG
EKGDPGELGL PGAVGAKGAQ GLTGIPGQPG QGGLAGLPGP MGPVGQPGPP GPPGPSYHAG
FDDMEGSGVG VANGVPGARG PDGRQGTTGI PGLPGKPGFP GAAGEKGSEG LQGRDGRPGL
DGFPGPNGLK GDRGERGETG RDGNGQPGPP GPPGPPGQII YQTSSSYDGV VGGAGPQGGT
GLPGQAGFPG PIGSKGDMGD PGQPGYGVKG EKGEPGLIIG PDGSPLYLGE LSGEKGDRGP
AGPVGPPGQY GPSGIKGEFG MPGRPGRPGV NGYKGEKGEP TTGAGFGYPG VPGPPGPPGS
PGPAVPVDRF NGYDASRNYP ATKGEKGDHG AQGLPGTPGV ASNLDIFTFK NDLKGERGDS
GMKGEKGEPS GGYYDPRFRG QQGPPGPPGN PGLMGPKGDS IMGLPGPQGP PGSPGIGYDG
RPGIPGPSGP PGPPGSSSLP GAYRPNHSIN IPGPPGPAGP PGTPGHTSGV TVLRSYDTMI
ATARRQSEGT LIYIVDKTDL YIRVRDGFKQ VLLGDYSPFY RDLDNEVAAV QPPSVVNYPQ
SQDHSANNGA EHFSQGGTAT HPIKPPPRKP AEIPRPAKPD NRNPDPRYPP QYDPRYPPQP
DARYPPQTDG RYSHVQPENR YPTRPESRFP VTPQRRPVPQ PAGHLHTSGP GLHLIALNMP
QVGNMRGIRG SDFLCFQQAR AVGLKGTFRA FLSSKLQDLY SIVRKSDRDS LPIINLKDQV
LFNSWESMFS KTGGRMKENA PIYSFDGRDI LRDSAWPEKM VWHGSSNEGH RQTDNYCETW
RAGDRAVTGL ASSLQSGQLL QQLPSSCSSS YIVLCIENSS LSHSKK
//
