ID A0A8U1C4T3_SALNM Unreviewed; 1422 AA.
AC A0A8U1C4T3;
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 X2 {ECO:0000313|RefSeq:XP_038862598.1};
GN Name=LOC120058186 {ECO:0000313|RefSeq:XP_038862598.1};
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_038862598.1};
RN [1] {ECO:0000313|RefSeq:XP_038862598.1}
RP IDENTIFICATION.
RC TISSUE=White muscle {ECO:0000313|RefSeq:XP_038862598.1};
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_038862598.1; XM_039006670.1.
DR GeneID; 120058186; -.
DR Proteomes; UP000808372; Chromosome 13.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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: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..1422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036457701"
FT DOMAIN 79..268
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 33..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1224
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 292..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..469
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..645
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..664
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..706
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..768
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..910
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1039
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1069
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1187
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 146338 MW; 5F91F770FA2FF550 CRC64;
MDCRIGFQLG VSFLLVLLVG RSEALWFSWG STDGTTEAPT LDNEGSGNPV ASGKSPKPDN
VGEDGAEIID VASGIHESGV SLLQLIGDPP PDEITKIYGP DNSPGYVFGP DANTGQLARA
HLPSPFYRDF SLLFNLKPQS TNGGVIFSVT DPSQQIMYVG VKLSPVKANR QNVIFYYTEP
DSQESYVAAT FPVHNLADQW NRFSISVLDD KVTFYINCDD QPQVVRFERS PDEMELESGA
GVFVGQAGGA DPNKFLGVIG ELRVVGDPRA AERQCEEEGD DSDAASGDGG SGDERIQDGK
KKGSGTSIWD AKVRKYERVE DVRLTVTTTP TSSRPIQQPP VTRKQPEVSP KKERDQGGSR
GDKGDRGEKG DRGPIGSKGD SGSESGTRGA RGEKGVFGEK GMKGKAGFGY PGSKGDPGPV
GPPGPPGLPG PAAEVVSRGD GSVVQTVAGP RGPAGPPGTS GPEGPAGADG EPGDPGEDGS
QGPVGPPGFP GIPGDPGLTG EKGDRGEGQP GPRGPPGPPG QPAPTRHDRP TFADMEGSGF
PDLETLRGLP GLPGPPGLPG APGTSVVETG VSGLFGPKGP PGLDGAPGQP GLHGPPGADG
RPGAAGAGGE KGDPGELGLP GAVGAKGAQG LNGIPGQPGQ GGLAGLPGPM GPLGQPGPPG
PPGPSYRVGF DDMEGSGVGV ANGVPGARGP EGQQGPPGIP GLPGKSGFPG IPGEKGSEGP
RGSDGRPGLD GFPGPNGQKG DSGDRGERGE SGRDGNGQPG PPGPPGPPGQ IIYQTSSSYD
GAVGGAGPQG QAGFPGPIGP KGDMGDPGQP SYGVKGEKGE SGSIIGPDGN TLYLGRLSGE
KGDRGPAGPV GPPGQYGSPG IKGEFGMPGR PGRPGVNGYK GEKGEPTTGA GFSYPGVPGP
PGPPGPPGPA VPVDRFNGYD ASRNYPVTKG EKGDFGAQGL PGPPGVASNF DIFTFKNDLK
GEHGDTGVKG EKGEPSGGYY DPRFGRQQGP PGPPGNPGLM GPKGDSITGP PGPQGPPGSS
GIGYDGRPGN PGPPGPPGPT GSHSLPGAYR PTHPISIPGP PGPAGPPGIP GHTSGVTVLR
SYDTMIATAR RQSEGTLIYI VDKADLYIRV RNGFRQIMLS DYSPFYRDLD NEVAAVQPPP
VVNYPQSQDH SANNGAEQFS HGGAATHPIV PPPRQPIEIP RPAQPNNRDP RDPPQYDPRY
PPQTDGRYSP VQPENRYPSQ PERRYHITPQ RQPVPQPAGH VHTSGPGLHL IALNTPQVGN
MRGIRGADFL CFQQARAVGL KGTFRAFLSS KLQDLYSIVR KSDRDSLPIL NLKDHVLFNS
WESLFSKTEG RMEENAPIYS FDGRDILRDS AWPEKLVWHG SSSEGHRQTD NYCETWRAGD
RAVTGLASSL QTGQLLQQLP SSCSSSYIVL CIENSYLSHS KK
//
