ID A0AAY5KFK1_ESOLU Unreviewed; 1295 AA.
AC A0AAY5KFK1;
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, type XV, alpha 1b {ECO:0008006|Google:ProtNLM};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000087868.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000087868.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Myers G., Karagic N., Meyer A., Pippel M., Reichard M., Winkler S.,
RA Tracey A., Sims Y., Howe K., Rhie A., Formenti G., Durbin R., Fedrigo O.,
RA Jarvis E.D.;
RT "Esox lucius (northern pike) genome, fEsoLuc1, primary haplotype.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSELUP00000087868.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSELUP00000087868.1}
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 Ensembl; ENSELUT00000104821.1; ENSELUP00000087868.1; ENSELUG00000015249.3.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP000265140; Chromosome 3.
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:SF1090; ALPHA2(IV)-LIKE COLLAGEN; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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:UP000265140};
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..1295
FT /note="Collagen, type XV, alpha 1b"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044338641"
FT DOMAIN 35..225
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 84..224
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 223..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..555
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..586
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..700
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..841
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 132850 MW; 648D57107F099492 CRC64;
MIIRLCGWSL VVNLVLLYHF SAAVQVIEER RSMGHLDLTE LIGVPLPPSV AFITGYEGFP
AYSFGPDANI GRLTKTFMPD PFFRDFAIIV TVRPSSRQGG VLFAITDAQQ KVVQLGLVLT
AVEDQTQRIQ LYYTDGSPGS SHSRQVASFK VPDMTNTWTR FTMSLQDQEV RLYMDCDEFH
SETFKRSRQQ LSFEPSSGIF VGSAGGTGLK RFVGSIQQLV ITPDPRAAEE QCEDDDPYAS
GEGSGDDLLE DRETEAELRK NTERRKETAQ PEDMLSRPVQ APPTESPEME LDESSGHLTA
TEQSHQEMLL KEPNQIEEPG ERSGDERPLS HGQKGEQGDP GPMGPVGPPG PSAPSEDSSS
GHGKPGSRGP QGLPGPTGAP GVPGKDGQPG SKGEDGSPGL RGPQGVPGLA GEVGVKGDKG
DPGTGLPGPP GPPGPPGPFR SHSVPYGEDA IGSGFGDVDD TEYIRGPPGP PGPPGQPGPA
GPTRSEDIFP GQPGPPGAPG RDGQVGKPGP PVIEDWYSGS GSGSGSEFGS GLLASGLGSG
EGPPGVVGHV GPMGPKGRKG EQGLAGSNGP TGESGDPGLP GTTGPRGPEG KKGDPGPRGP
PGPPGPPGRR YFVEDLEGSG KSDLFLGAGV QGPLGPPGLP GPAGPKGDKG KDGTPGLSVK
GEPGDPGHEG LAGLPGARGL KGDKGDPGPK GECGPDGLSL PGPPGPPGPP GPIVNLQDLL
LNDTEGLLNF TEIRGPPGPR GPEGDPGRAG FPGPRGPKGN MGSPGLQGPL GIKGAKGDPG
VTIAADGTVL TGIRGPQGPK GIKGERGFPG AAGIMGPVGP PGQKGEYGFP GRPGRPGMAG
AKGDKGDAVG LPGSPGLPGP PGPPGPVTGL NGVNGSKGLI QGVRRGSGGT KGEKGDAGLP
GTPGKSVDVL PQGFVGEKGD VGYKGMKGEK GDAGLPGPPG LPGRSGLVGP KGESIIGPAG
HSGAPGEPGI PGFGHPGPRG PPGPSGPPGP PPIYGSAVSI PGPPGPPGPP GITGYKNPVT
IYRNTHGLMR ESHLTAEGSM AYVLDKGELY LRSRDGWREV QLGELVPFPE ETQSSTVSQA
LSRPGDLSQP QRPRSQELVG TSYVPNHNVL PHTIHSTPGL HLVALNAPLT GDMRGIRGAD
FQCYQQARAM GLTATYRAFL SSHLQDLATI VKKGDRYSMP IVNLRGELLY SSWMNMFSGN
GGVFDPSIPI YSFDGRNVMT DPTWPQKLVW HGSGTTGIRM TTSYCEAWRA GDMAVTGQAS
LLQTGRLLGQ HTRSCSNHFI VLCIENSYID HRRSN
//
