ID A0AAZ3P3P0_ONCTS Unreviewed; 1357 AA.
AC A0AAZ3P3P0;
DT 05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 1.
DT 28-JAN-2026, entry version 5.
DE RecName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0008006|Google:ProtNLM};
GN Name=LOC112260532 {ECO:0000313|Ensembl:ENSOTSP00005111160.1};
OS Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=74940 {ECO:0000313|Ensembl:ENSOTSP00005111160.1, ECO:0000313|Proteomes:UP000694402};
RN [1] {ECO:0000313|Proteomes:UP000694402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29621340;
RA Christensen K.A., Leong J.S., Sakhrani D., Biagi C.A., Minkley D.R.,
RA Withler R.E., Rondeau E.B., Koop B.F., Devlin R.H.;
RT "Chinook salmon (Oncorhynchus tshawytscha) genome and transcriptome.";
RL PLoS ONE 13:e0195461-e0195461(2018).
RN [2] {ECO:0000313|Ensembl:ENSOTSP00005111160.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOTSP00005111160.1}
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_024291481.1; XM_024435713.2.
DR Ensembl; ENSOTST00005132286.1; ENSOTSP00005111160.1; ENSOTSG00005042394.2.
DR GeneID; 112260532; -.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP000694402; Unassembled WGS sequence.
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; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1091; COLLAGEN ALPHA-3(IV) CHAIN-LIKE ISOFORM X1; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 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:UP000694402};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1357
FT /note="Collagen alpha-1(XVIII) chain-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044242745"
FT DOMAIN 110..300
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 159..299
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 301..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..553
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..601
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..652
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..688
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1072
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1357 AA; 140444 MW; B5A4C4899F021F5F CRC64;
MALPRLYSLL LLMAPVHGQW WSAFLGKAQE MTTQPLTTVP TTTQVLWTTE GTEVGQVGTQ
TEVFTTAPVQ STPLQSIQEP AGDGTTEIKP KAKKISLKMW KSRERGSTGH LDLTELIGVP
LPPSVSFITG YEGFPAYGFG PDANIGRLTK TFMPDPFFRD FAIIVTIRPS SKQGGVLFAI
TDAQQKVVQL GLALTPVEDE TQRIQLYYTE GGEESSHSQQ VASFKLPDMR NKWTRFTLSV
QDQEVRLYMD CDDFQAETFH RSSRQLSFEP SSGIFVGNAG GTGLEKFVGS IQQLVIKPDP
RAAEEQCEED DPYASGDGSG DDTLHDRETD DKLMKNMERK KETARPEDML SVPVRAPPTE
SPELELDEYT VHLTPTNQAH QEMLLEGSHQ TEEPGERSGD GRPLSYGQKG EQGEPGPMGP
AGPRGPPGPS TPSEDRSGHG QPGPRGPQGP SGAPGVPGKD GQPGSKGEDG DPGQRGPHGF
PGLAGEVGVK GDKGDTGVGL PGPPGPPGPL KSHSVPYGED ALGSGFGDLD DTEFIRGSPG
PPGPPGQPGP PGPTRFFEAS EGLFPGQPGS PGPPGRDGLV GKPGPPGPTG LDGDAGLTGP
TGLKGEQGLA GPNGPMGVSG DPGLTGATGP RGPEGKTGDP GPRGLPGPPG PPGGRFFVED
VEGSGKNDMV LGTELKGPQG PPGLPGPAGP KGEDGKDGAS GLSVKGEPGA SGPEGLQGLA
GLPGARGLKG DKGDPGPKGE CGPDGHNVPG PPGPPGPPGP IINLQDSLLN NTESMFNITE
IRGPPGPMGP EGEPGRAGFP GPRGPKGDSG LPGFQGPPGM KGAKGEAGVT IAADGTALTS
VRGPRGPKGI KGERGFPGAY GVMGPIGPTG QKGEYGFPGR PGRPGMAGKK GDQGDAIGQP
GLPGPPGPPG PPGPVTGLNG TVFPVRPRPF CKTPVNGSKG SSQGGRRRNG GAKGEKGEVG
LPGMPGEPDD ILPEGFVGEK GDMGYEGMKG DQGEPGLPGP PGLPGRSGLV GPKGESVIGT
VGHPGAPGEP GVLGIGRPGS RGPPGPAGPP GPPPVYGSAV SIPGPPGPPG PPGITGYENP
VSTYRNTNSL MRESHRAAEG SMAYVSDKGE LYVRTRDGWR KVQLGELILV PAESPSSAVS
QALSRPGDRT RPHRPHSQEL VGTSYVPNYN VLPHTVHSVP ALHLVALNTP FSGDMRGIRG
ADFQCYQQAR AMGLTATYRA FLSSHLQDLA TIVKKGDRYN MPVINLKGEV IYSSWMNIFS
GNGGVFDPSI PIYSFEGRNV MTDPTWPQKL VWHGSSTVGI RMTTNYCEAW RAGDMAVTGQ
ASLLQTGRLL GQHTRSCSNH FIVLCIENSY IDHRRSN
//
