ID A0A6P8GN59_CLUHA Unreviewed; 1252 AA.
AC A0A6P8GN59;
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 X2 {ECO:0000313|RefSeq:XP_031440238.1};
GN Name=col15a1a {ECO:0000313|RefSeq:XP_031440238.1};
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_031440238.1};
RN [1] {ECO:0000313|RefSeq:XP_031440238.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_031440238.1; XM_031584378.1.
DR AlphaFoldDB; A0A6P8GN59; -.
DR GeneID; 105890075; -.
DR CTD; 792366; -.
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 GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; 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:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 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_031440238.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000515152};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 28..216
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 214..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..285
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..638
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..868
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..965
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1052
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 128448 MW; 9BB1D8DBFA29D380 CRC64;
MQQRLAFHAS CCRPGVLISI NKRGTKGQLD LTELIGVPLP PDVAFITGFE GFPAYSFGPG
ANVGRLARSF VPDPFFRDFA IIVTAKPTTR QGGVLFAITD AMQKVVHLGV MLAAVEDGTQ
RVVLYYTEPG AATTQEAASF KMGELTGRWA RFTLAVQGHE VRLYMDCEEY HRVAFQRSAG
QLTFQPSSGI FVGNAGNTGL ERFVGSIQQL VLTPDPRAPD DQCEEDDPYA SGYGSGDDLD
DTERMDEVKK LVEEREYTMP EDFLTMPVQA PPTEEASSDD EDLEEGTSGQ AIDLPDERAT
EHTARVDTVH RETSLNPGLK GEKGDAGSAG PPGPPGPPGR SSPASGTSSG GGEPGPRGPQ
GPSGTPGAPG KEGEPGVQGR DGSPGQAGPQ GFPGLPGDAG PTGEKGDPGV GLPGPPGPPG
PPGKSTSPRY MDGLDGSGFE DFDSDTEVVR GPAGPPGPPG NPGPPGPSQA LLPGQPGLKG
APGTDGKDGE MGTPGLPGAD GRPGNPGAQG EKGDLGFPGS PGLKGDLGQE GPPGLPGPVG
PEGPTGPAGQ PGPPGPPGPP AQGFKFNLED VEGSGELSAM GAMLPKGPPG LPGQPGVIGL
KGERGADGQP GLSVKGDAGE RGHEGEPGLP GLPGAKGQLG DEGHPGLKGE PGRDALGLVG
PPGPPGLPGP IINLQDLMLN DTEGLFNFSG ILGPQGPMGP NGLKGESGIP GVQGPSGVKG
EKGEPGITMA ADGSLMTGPE GPKGVKGDSG VPGPLGEKGP IGPVGPKGEF GLPGRPGRPG
MNGFKGDQGQ AVFVHGPPGP PGPPGRPGMF NCPKGTVFPV PPRPHCKKGV NGESKGEGAT
CLTNSSKGEK GDRGLQGIPG IPAPAIAILP KGFSPNRGDQ GYHGEKGEKG EAGLPGLHGR
SGLVGPKGES VMGPRGHPGI PGPPGVPGYG RDGPTGPPGP PGPRGPPGYG SALATPGPPG
PPGPRGSPGV SGGSTGVKTY PSLQSMTQRS YLDLDGTMYF VTDAGRLYLK VPGGWKEIQL
GKLLEVQSPI IPQDEARPRP QSPGSSSSSM PQIHEGQALK LVALNTPLTG NIGSLTAADQ
ACRAQAQAMG IRDQYRAFLS NHLQDLVDVI HPQYRRTLPI VNLRGEVLFD NYEHIFTKSS
ALPHGIPLFS FDGRDVMSDP FWPQKAIWHG SSPQGRRLQE KNCESWRAGD MAIVGQASFL
YTGLLNQQSR SCSNQFVVLC VEASPEPSSY QEVRRGTRYA YYYRNPRSSH RT
//
