ID A0A8C0KY09_CANLU Unreviewed; 1226 AA.
AC A0A8C0KY09;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Collagen type XV alpha 1 chain {ECO:0000313|Ensembl:ENSCAFP00020024003.1};
OS Canis lupus dingo (dingo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=286419 {ECO:0000313|Ensembl:ENSCAFP00020024003.1, ECO:0000313|Proteomes:UP000694391};
RN [1] {ECO:0000313|Ensembl:ENSCAFP00020024003.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCAFP00020024003.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR AlphaFoldDB; A0A8C0KY09; -.
DR Ensembl; ENSCAFT00020027722.1; ENSCAFP00020024003.1; ENSCAFG00020018790.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694391; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR FunFam; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 1.
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; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000694391};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 60..248
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 109..247
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..271
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..392
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..826
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..987
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 127747 MW; 15092539C00DBA50 CRC64;
VDPLPRAPGP RPRARLTSAP ATSCRRDARS WRLLWLLSVS ALLPAPTRTR SATELASQGP
LDLTELIGVP LPSSVSFVTG YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAISVTVKPS
SASGGVLFAI TDAFQKVIYL GLRLSGVEDG GQRVILYYTE PGSHVSHEAA AFLVPVMTHR
WNRFAVIVQG EEVTLLMDCE EHSHISFQRS SRALAFEPSA GIFVGNAGAT GLERFTGSIQ
QLTIHPDPRT PEEMCETEES SASGESSGLQ EPEGVAEILE AVTYTQAPSK EAKVEPINAP
PTPSPPSDDT ELSGEPVPEG TAETVNLSVS LHSIPEQGSG EVLNDTLEEV HTVDGAPITD
VGSGDGAFIH VTEEAVHTEE GLAATEATGE AEVPTSTAGE AEASSMPTRG PALSLSTEDM
GERVTLVSSS ENLLFLGDGG HQRWGQSLVF LIREVIPLAG FALQGPGDEG ELAAAVTAEP
LPTAEAEAPE VGGSLPERPP LPVPTVASER GVKPSGGNFF FLQVETEAEG SGLGWGSEIG
FGSGDLVRSE ELLRVSVRMG HPGIWDRLLR NPEDFPSTCV YIWHVCYSFH EQTQGRPVNL
SSSLQGDPGN RGLPGPPGKN GQVGSPGIMG PPGPPGPPGP PGPGCAMGLG FEDTEGSGSI
RLLHEPRISG PVAPSVSCFE GDRGMDGASI VGPPGPRGPP GRIEVLSSAL TNITHGFMNL
SDIPELIGPP VWSGGIPGLP GFPGPRGPKG DTGVPGFPGL KGEQGEKGEP GAILTGDIPL
ERLQGKKGEP GVHGAPGPMG PKGPPGHKGE FGLPGRPGRP GLNGLKGAKG DRGVMMPGPP
GLPGPPGPPG PPGAVINIKG VSRCGGGVKG EKGSWGLPGS KGEKGDQGAQ GPPGPPVDPT
YLRHFLNSLK GENGDRGIKG EKGDSHGDFL VSGPPGLPGS PGLVGQKGET VVGPQGPPGA
PGLPGPPGFG RPGSPGPPGP PGPPGPPAIL GAGQYWVTAF SSMDDMLQKA HLVIEGTFIY
LRDSTEFFIR VRDGWKKLQL GELIPIPADS PPPPAFSSNG WPSTLLTLTY FSQLHLVALN
TPFSGDIRAD FQCFQQARAA GLLSTYRAFL SSHLQDLSTV VRKAERYSLP IVNLKGQVLF
NNWDSIFSGH GGQFNAQVPI YSFDGRDVMT DPSWPQKVVW HGSSTHGVRL VDKYCEAKEI
AHNDYLSLGG PPPHPRPHPH PVPLTL
//
