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Database: UniProt
Entry: A0A6P8ESF0_CLUHA
LinkDB: A0A6P8ESF0_CLUHA
Original site: A0A6P8ESF0_CLUHA 
ID   A0A6P8ESF0_CLUHA        Unreviewed;      1457 AA.
AC   A0A6P8ESF0;
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-like isoform X4 {ECO:0000313|RefSeq:XP_031414975.1};
GN   Name=LOC105894554 {ECO:0000313|RefSeq:XP_031414975.1};
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_031414975.1};
RN   [1] {ECO:0000313|RefSeq:XP_031414975.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_031414975.1; XM_031559115.2.
DR   GeneID; 105894554; -.
DR   Proteomes; UP000515152; Chromosome 21.
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: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   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:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 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   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515152};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1457
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5027792286"
FT   DOMAIN          93..286
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          290..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1111..1281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..408
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..467
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..498
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..533
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..644
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..673
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..746
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..839
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..862
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..893
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..962
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1022
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1051
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1135..1153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1219
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1457 AA;  150367 MW;  8A620B850F2DD155 CRC64;
     MADTRLWLCL SLMLALHTGP LHAWWWNAAT TPSPVNNPGT AAVAGTEMKE EKITDVGSEI
     LDVASGIKQI MQTWDQDPRA GGAGRTGEQS TVDLTLQQIV EDPESSSVER SVDPDGNPAF
     IFSKKSGVSR LAYGLLDSPF HRNFALLFRL MAANDTGMLF ALTDKSQMRI QLGVKLTRGK
     LTGRQVAVYY SDSKGKTYGK ARFAPVAYFP LPTENHVWTR FAISFSANKI SFFHNCNREP
     MVGTFSRSNA PQLVEAGAAI MVGQGGHQDG DKFEGQISQL TISGDPAAAE RQCYTSDDED
     EDDASGSGSG DGIDTDTDDG ITTRPPKQKT QDVQLLPEPP VSRTASKGSL DTGREETGPK
     GDSGFDTEGS GDTSEQEAPR EKGGKVVGSP GMKGDTGPPG PPGPPGPQGP LTEVMDAGDG
     KVVHKVEGRQ GPPGPRGPSG QPGPAGRDGQ TGEKGDQGVE GAGGPHGFPG TPGNTGMKGQ
     KGEHGVGQPG PPGLPGPPGN GETTFVDVEG SGGKMPVRRG PPGLPGPPGP PGPAGSGEDS
     NGSGASGPNG KPGRPGPSGP MGKAGLPGPP GPRGEKGDCG TLGLPGSGGD TQDGFSVTSF
     FDNWLPYFSS TAAPQGKLGN GGLPGSPGPM GPSGPPGLPG PPGPAGKVTI EQNGTEVTLV
     EGPPGPPGSP GPKGPQGIPG LPGKAGFPGI AGQKGSEGPR GRDGFPGMDG FPGRPGDKGE
     RGLRGERGEA GKDGGPPGPP GLPGPPGEIV FPNVGDHEGV VGIAGPPGQP GLAGRAGFPG
     PMGPKGDRGE RGQSGVPTKG QKGEPGVILA ADGSRLYPGL TSQPGEPGPT GPQGPPGIPG
     YPGQKGEFGM PGRPGRPGLN GLKGERGDSV GGHGGYPFPG LPGPPGPPGP PGPAGAVLSL
     DSFSKNGERS RHHPVLKGDK GDQGAPGIPG FSGGTGGFDF NAYKNELKGE RGDTGMKGEK
     GEAVGGGYYD QRYGGIAGPP GPPGPQGPRG DSVRGPQGPA GPQGQPGYGR PGNPGPPGPP
     GPQGSNLPGA HRSSHTVNVP GPPGPPGPPG VPGLASGVMV LRTYDSMASI SRQQPEGTLV
     YITDNTDLYI RVREGCRKVQ LGEYTPFPRE ENNVAAVNPP PVVQYPPDHT GPDSGASSSS
     ERAPPQSEGQ SESLEIIPQS GYPHHPASPP RHPSNPSYPF NPAYPPQPGY PPQSGYPPQP
     GYPPQPGYPP QPGYPPQPGY PKYTVTSHGT YPQQPPPADP RYSPSQPEGR YPDHRYPNGR
     LPSSTHRRPS DPQPPASTHE HRAGPALHLI AMNHPQEGNM RGIRGADHEC FTQAQAIGMK
     GTFRAFLSSR LQDLYSIVRR SDRERIPIVN LKDEELFSSW ESIFSESEGK IRANVTIFSF
     DGRDVLTDDA WPEKMMWHGS STRGQRVTDS YCETWREANH ALTGMASSLQ DGRLLQQTQR
     SCTNSYVLLC IENSSIA
//
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