ID A0A8B9DSC9_ANSCY Unreviewed; 1139 AA.
AC A0A8B9DSC9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0008006|Google:ProtNLM};
OS Anser cygnoides (Swan goose).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anserinae; Anser.
OX NCBI_TaxID=8845 {ECO:0000313|Ensembl:ENSACDP00005010899.1, ECO:0000313|Proteomes:UP000694521};
RN [1] {ECO:0000313|Ensembl:ENSACDP00005010899.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSACDP00005010899.1}
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 AlphaFoldDB; A0A8B9DSC9; -.
DR Ensembl; ENSACDT00005013065.1; ENSACDP00005010899.1; ENSACDG00005007927.1.
DR Proteomes; UP000694521; Unplaced.
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; 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 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 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:UP000694521};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1139
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034494340"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 87..225
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 225..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..379
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..659
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..857
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 118538 MW; 73C1F4CCB5410BA4 CRC64;
MLSWHAWWTW DLLLLLLGLS IHAGSAAEII EERGSKGSLD LTELIGVPLP PSVYFVTGYG
GFPAYSFGID ANIGRLTSAI IPLSFYRDFA IVVTVKPNSD RGGVLFAITD AFQKTIYLGM
RLSPVDDSTQ RIIMYYTEPG SRISQEAASF KVPVMTNRWN RFTVTVQGNY IALFMDCEEY
QRVPFQRSAG ALVFDSDSGI FVGNAGATGL EKFTGSIQHL IIRSDPRATE DHCEDDDPYL
EDTPAEPVEA PPTILSFLEE SNFSGHHRPE ETSETAKIKE QDSSVMETGQ GNSQSTIVTQ
KILREEDASG SSVLPTASRE KGQKGQNGED GPTGPPGRPG IGDVQKKDPG SPGPSAKNGQ
HDPPGLPGLP GLDGVVGPPG QKGEKGDRGL PGSVGPKGNT GDTGLIGPKG EAGPHGSPGK
QGPPGPPGPP GPPGPPGSTG LSYGSGFEDM EGSGITGLLS ESRITGSRVP KGERGNIGPP
GSKGLPGTKG KPGFPGIAGH PGNMGPKGEK GDPGPQGERG QDGNSIVGPP GPRGPPGPII
AIPELLLNDT NGIFNFTSIE ELLGPPGPDG KPGLPGFPGP QGPKGDIGLP GPKGPKGQQG
EKGEPGVIIT ADGSSTELLG RKGQKGEAGV VGPVGPRGPI GPAGPKGELG FPGRPGRPGL
NGLRGVKGER GEALNGMPGL PGPPGPPGRP GRIVYIKGTV FPVSRRPHCK MTVSAPYPGN
EEALNVQGAK GNRDCWGLQS TGSSADLKGE KGDRGDPGPP GPPLPPSYFS HFINSIKGEK
GDNGNTGVKG EKGEPNRGFY LTGPPGPPGR PGLIGPKGDS VVGPRGPPGL PGLPGLPGYG
KTGPPGPPGP PGPPGPPAIY GSAAAMPGPP GPPGEPGSPV SRNLITTFQN IAGMLEKVHF
VAEGTLIYLS ETSEVFIRVR NGWRKLQLGE LIPIPADSLP PPAISSHGFQ SLPAPSPISN
MNNGKPVLHL VALNLPFSGD MRADFQCFQQ AQLAGLTATY RAFLSSHLQD LATVVRKTDR
YNLPIVNLKG EMLFHNWESI FKGNGGEFNI NVPIYSFDGR NVMTDPSWPQ KVIWHGSTAN
GIRMVSNYCE AWHTSDLAAM GQASPLKKGK LLDQKAYSCS NQFIVLCIEN SFVSDPQGK
//
