ID A0A8U0UJS1_SALNM Unreviewed; 1452 AA.
AC A0A8U0UJS1;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0000313|RefSeq:XP_038854236.1};
GN Name=LOC120051446 {ECO:0000313|RefSeq:XP_038854236.1};
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_038854236.1};
RN [1] {ECO:0000313|RefSeq:XP_038854236.1}
RP IDENTIFICATION.
RC TISSUE=White muscle {ECO:0000313|RefSeq:XP_038854236.1};
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_038854236.1; XM_038998308.1.
DR GeneID; 120051446; -.
DR KEGG; snh:120051446; -.
DR Proteomes; UP000808372; Chromosome 7.
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:SF1038; COLLAGEN ALPHA-1(XVII) CHAIN ISOFORM X1; 1.
DR Pfam; PF01391; Collagen; 3.
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1452
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035752508"
FT DOMAIN 32..223
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 231..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..325
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..407
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..584
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..732
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..837
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..932
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..950
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1006
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1452 AA; 149362 MW; 8DC65530E830C9C0 CRC64;
MPCVDRWSLG LHTCVLLLVV TRTETQRTAE SGVTLLQLIG DLPPDESRAG PGGKPAYYFG
GLDGLTAAGQ PALAHLPNPF YRDFSLVFQI IPSSPGVLFS ITDASQKFMY VGVKLSAPDA
DGRNQKILFY YTEPDSEASY LAASFTVPSL DLVSWTKFSL SVFNDQVTFF MGCDASGKTV
KLERSPDDME LDRGAGIFVG QAGGADPDRF EGAIAELNVV GNPRAAELLC EDDDDSDAAS
GDFGSGDGDR RETGKTVKTT PPSLRPVPEP PLTSSVSDRL SETGPTGSNR EKGDRGEKGS
PGDRGPAGPK GDSGSFSSSA SSSGSSSGGG ERGEKGDTGL KGSSGFGYPG SKGDRGVPGP
PGPPGPGGPA AQVVRLGDGS VVQPVAGPMG PMGPPGVKGP AGPQGPEGEA GDPGEDGKLG
PAGDRGFPGT QGDSGVKGQK GDRGDGHPGP RGPPGPPGHP GPGTVDRATF VDMEGSGGFP
DLEKIQTLRG LPGPPGPPGP PGPSAGGVSS HESGSFGPPG PPGQDGARGL PGPAGPPGRP
GTPGPSSGEK GEAGDLGLPG PSGERGSQGD PGVPGQAGQG GLAGLPGPMG PIGPPGPPGP
PGPSYPVRYG DREGSGVTGV NGVAGVIGIP GPQGPPGIAG LPGRSGLPGL SGEKGSEGAR
GQNGTPGMDG FPGILGDKGE RGDRGERGEP GREGGPPGPP GAPGPPGQIY QTSGSFDGVL
GNQGQGGPGL PGRAGFPGPM GPKGDTGEPG QPGYAAKGEK GEPGIIMGPD GRPMYLGGLG
SQPGEKGLPG PEGPPGPYGP AGLKGDIGMP GRPGRPGLNG VKGERGDSAG GTGGYGGPPG
PPGPPGPPGP AVPLDRFNRY DDVSRLYPDS KGEKGDRGVP GIPGVPGLTS NFDIYTFKKE
MTGERGDSGM KGEKGEPAGG YYGGGYSGQG GQPGPPGLPG PKGESIIGPS GPQGPPGNPG
RGYEGRQGNP GPPGPPGPSG SSSSPGAYRP TQTISIPGPP GPPGPPGTDG HSSGVMVLRS
YDTMTATARR QAEGTLVYLV DQTDFYIRVR DGFRQIQLGP YIALPPDQGN EVAAVDPPPV
VYYQPDHPSN TATEQPPRQL DPHQPQPEGQ HPTYPDPHYP THPDPRYPAQ PDPRYPAQPD
PRYPAQPDPR YPAQPDPRYP AQRYPAQPDP RYPAQPDPRY PAQPDPRYPA QPDPRYPAQP
DPHYPSHSDP RYPSHTDPRY PSYTDRQHNP DPVQPVQPQP APVPQNPVYS DTRYPVTPQR
RPRPLETPSH QHTSGPSIHL VALNAPQGGN MRGIRGADFL CFNQARAIGL KGTFRAFLSS
KLQDLYSIVR KSDRDRMPIV NLKDEVLFDS WEAIFSDSEG RVKDNVPIYS FDGKDIFTDG
TWPDKMIWHG STSRGHGQVD NYCETWRIGE QALTGMASSL QGGQLLQQRT SSCHSSYAVL
CIENSYIEQF KR
//
