ID A0A6P8ESE2_CLUHA Unreviewed; 1636 AA.
AC A0A6P8ESE2;
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 X3 {ECO:0000313|RefSeq:XP_031414974.1};
GN Name=LOC105894554 {ECO:0000313|RefSeq:XP_031414974.1};
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_031414974.1};
RN [1] {ECO:0000313|RefSeq:XP_031414974.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR RefSeq; XP_031414974.1; XM_031559114.2.
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; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
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; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1636
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028455815"
FT DOMAIN 161..288
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..670
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..701
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..804
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1018
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1041
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1072
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1636 AA; 168616 MW; 8D90A99403E8DA10 CRC64;
MADTRLWLCL SLMLALHTGP LHAWWWNAAT TPSPVNNPGT AAVAGTEMKE EKITDVGSEI
LDVASGIKQI MQTWDQDPRA GGAGRTGEQS TGNDRLRVEQ LVFGSEAGHG GSSGGEKGYD
GPLVTARALA DSGSGSTNPS GVGNDWRLRD VTVPAWMTAG DVSPVCLPRG SDWGFCSSGG
RASSTFTVPN FLNHTSAEEV GATLGDWAGL LSSRCHRDVE RFFCLLLAPA CPGSGALPSP
SPPPLLPCRS LCAILTDACW GALGGRELPV TCDSLPEGLP HQHPCQPVSS CRCAVDLTLQ
QIVEDPESSS VERSVDPDGN PAFIFSKKSG VSRLAYGLLD SPFHRNFALL FRLMAANDTG
MLFALTDKSQ MRIQLGVKLT RGKLTGRQVA VYYSDSKGKT YGKARFAPVA YFPLPTENHV
WTRFAISFSA NKISFFHNCN REPMVGTFSR SNAPQLVEAG AAIMVGQGGH QDGDKFEGQI
SQLTISGDPA AAERQCYTSD DEDEDDASGS GSGDGIDTDT DDGITTRPPK QKTQDVQLLP
EPPVSRTASK GSLDTGREET GPKGDSGFDT EGSGDTSEQE APREKGGKVV GSPGMKGDTG
PPGPPGPPGP QGPLTEVMDA GDGKVVHKVE GRQGPPGPRG PSGQPGPAGR DGQTGEKGDQ
GVEGAGGPHG FPGTPGNTGM KGQKGEHGVG QPGPPGLPGP PGNGETTFVD VEGSGGKMPV
RRGPPGLPGP PGPPGPAGSG EDSNGSGASG PNGKPGRPGP SGPMGKAGLP GPPGPRGEKG
DCGTLGLPGS GGDTGKLGNG GLPGSPGPMG PSGPPGLPGP PGPAGKVTIE QNGTEVTLVE
GPPGPPGSPG PKGPQGIPGL PGKAGFPGIA GQKGSEGPRG RDGFPGMDGF PGRPGDKGER
GLRGERGEAG KDGGPPGPPG LPGPPGEIVF PNVGDHEGVV GIAGPPGQPG LAGRAGFPGP
MGPKGDRGER GQSGVPTKGQ KGEPGVILAA DGSRLYPGLT SQPGEPGPTG PQGPPGIPGY
PGQKGEFGMP GRPGRPGLNG LKGERGDSVG GHGGYPFPGL PGPPGPPGPP GPAGAVLSLD
SFSKNGERSR HHPVLKGDKG DQGAPGIPGF SGGTGGFDFN AYKNELKGER GDTGMKGEKG
EAVGGGYYDQ RYGGIAGPPG PPGPQGPRGD SVRGPQGPAG PQGQPGYGRP GNPGPPGPPG
PQGSNLPGAH RSSHTVNVPG PPGPPGPPGV PGLASGVMVL RTYDSMASIS RQQPEGTLVY
ITDNTDLYIR VREGCRKVQL GEYTPFPREE NNVAAVNPPP VVQYPPDHTG PDSGASSSSE
RAPPQSEGQS ESLEIIPQSG YPHHPASPPR HPSNPSYPFN PAYPPQPGYP PQSGYPPQPG
YPPQPGYPPQ PGYPPQPGYP KYTVTSHGTY PQQPPPADPR YSPSQPEGRY PDHRYPNGRL
PSSTHRRPSD PQPPASTHEH RAGPALHLIA MNHPQEGNMR GIRGADHECF TQAQAIGMKG
TFRAFLSSRL QDLYSIVRRS DRERIPIVNL KDEELFSSWE SIFSESEGKI RANVTIFSFD
GRDVLTDDAW PEKMMWHGSS TRGQRVTDSY CETWREANHA LTGMASSLQD GRLLQQTQRS
CTNSYVLLCI ENSSIA
//
