ID A0A6P8GXN0_CLUHA Unreviewed; 1256 AA.
AC A0A6P8GXN0;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X1 {ECO:0000313|RefSeq:XP_031440237.1};
GN Name=col15a1a {ECO:0000313|RefSeq:XP_031440237.1};
OS Clupea harengus (Atlantic herring).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Clupei; Clupeiformes; Clupeoidei;
OC Clupeidae; Clupea.
OX NCBI_TaxID=7950 {ECO:0000313|Proteomes:UP000515152, ECO:0000313|RefSeq:XP_031440237.1};
RN [1] {ECO:0000313|RefSeq:XP_031440237.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR RefSeq; XP_031440237.1; XM_031584377.2.
DR AlphaFoldDB; A0A6P8GXN0; -.
DR GeneID; 105890075; -.
DR KEGG; char:105890075; -.
DR CTD; 792366; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000515152; Chromosome 17.
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 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_031440237.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000515152};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1256
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027700072"
FT DOMAIN 32..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 218..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..642
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..872
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..969
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1056
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 129099 MW; 5DDF0D98BC1BB873 CRC64;
MMSRGSLWSF ALFLWYCHPT TAFLEERGTK GQLDLTELIG VPLPPDVAFI TGFEGFPAYS
FGPGANVGRL ARSFVPDPFF RDFAIIVTAK PTTRQGGVLF AITDAMQKVV HLGVMLAAVE
DGTQRVVLYY TEPGAATTQE AASFKMGELT GRWARFTLAV QGHEVRLYMD CEEYHRVAFQ
RSAGQLTFQP SSGIFVGNAG NTGLERFVGS IQQLVLTPDP RAPDDQCEED DPYASGYGSG
DDLDDTERMD EVKKLVEERE YTMPEDFLTM PVQAPPTEEA SSDDEDLEEG TSGQAIDLPD
ERATEHTARV DTVHRETSLN PGLKGEKGDA GSAGPPGPPG PPGRSSPASG TSSGGGEPGP
RGPQGPSGTP GAPGKEGEPG VQGRDGSPGQ AGPQGFPGLP GDAGPTGEKG DPGVGLPGPP
GPPGPPGKST SPRYMDGLDG SGFEDFDSDT EVVRGPAGPP GPPGNPGPPG PSQALLPGQP
GLKGAPGTDG KDGEMGTPGL PGADGRPGNP GAQGEKGDLG FPGSPGLKGD LGQEGPPGLP
GPVGPEGPTG PAGQPGPPGP PGPPAQGFKF NLEDVEGSGE LSAMGAMLPK GPPGLPGQPG
VIGLKGERGA DGQPGLSVKG DAGERGHEGE PGLPGLPGAK GQLGDEGHPG LKGEPGRDAL
GLVGPPGPPG LPGPIINLQD LMLNDTEGLF NFSGILGPQG PMGPNGLKGE SGIPGVQGPS
GVKGEKGEPG ITMAADGSLM TGPEGPKGVK GDSGVPGPLG EKGPIGPVGP KGEFGLPGRP
GRPGMNGFKG DQGQAVFVHG PPGPPGPPGR PGMFNCPKGT VFPVPPRPHC KKGVNGESKG
EGATCLTNSS KGEKGDRGLQ GIPGIPAPAI AILPKGFSPN RGDQGYHGEK GEKGEAGLPG
LHGRSGLVGP KGESVMGPRG HPGIPGPPGV PGYGRDGPTG PPGPPGPRGP PGYGSALATP
GPPGPPGPRG SPGVSGGSTG VKTYPSLQSM TQRSYLDLDG TMYFVTDAGR LYLKVPGGWK
EIQLGKLLEV QSPIIPQDEA RPRPQSPGSS SSSMPQIHEG QALKLVALNT PLTGNIGSLT
AADQACRAQA QAMGIRDQYR AFLSNHLQDL VDVIHPQYRR TLPIVNLRGE VLFDNYEHIF
TKSSALPHGI PLFSFDGRDV MSDPFWPQKA IWHGSSPQGR RLQEKNCESW RAGDMAIVGQ
ASFLYTGLLN QQSRSCSNQF VVLCVEASPE PSSYQEVRRG TRYAYYYRNP RSSHRT
//
