ID A0A493TEN6_ANAPP Unreviewed; 1140 AA.
AC A0A493TEN6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE SubName: Full=Collagen type XV alpha 1 chain {ECO:0000313|Ensembl:ENSAPLP00000024371.1};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSAPLP00000024371.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000024371.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000024371.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000024371.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSAPLP00000024371.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A493TEN6; -.
DR Ensembl; ENSAPLT00000022872.1; ENSAPLP00000024371.1; ENSAPLG00000014374.2.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000016666; Chromosome 2.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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:UP000016666};
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..1140
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019858763"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..665
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..880
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 118889 MW; 505D1161567427D4 CRC64;
MLSWHAWWTW DLLLLLLGLS IHSGSAAEII EERGSKGSLD LTELIGVPLP PSVYFVTGYG
GFPAYSFGID ANIGRLTSAI IPLSFYRDFA IVVTVKPNSD RGGVLFAITD AFQKTIYLGM
RISPVDDSTQ RIIMYYTEPG SRISQEAASF KVPVMTNKWN RFTVTVQGNY IALFMDCEEY
QRVPFQRSAE ALVFDSDSGI FVGNAGATGL DKFTGSIQHL TIRSDPRATE DHCEDDDPYA
SGDMSGNGSI QEHENIPETQ EALSPSHLPI RLEDTLAEPV EAPPTILSFL EESNFSGHHR
TEETSETAKI REQDSAVMET GQGNSQSTTV TQKILGEEDA SGFSVLPTES GEKKGQNGED
GPTGPPGRPG IEDVQRKDPG SPGPSAKHGP PGLPGLDGVV GPPGQKGEKG DRGLPGSIGP
KGSTGDTGLI GPKGEAGPHG SPGKQGPPGP PGPPGPPGPP GSTGLSYSSG FEGERGNIGP
PGSKGLPGTK GKPGFPGIDG HPGNMGPKGE KGDPGPQGER GQDGNSIVGP PGPPGPPGPI
IAIPELLLND TDGIFNFSSV EELVGPPGPD GRPGLPGFPG PQGPKGDIGL PGPKGPKGQQ
GEKGEPGAII TADGSLTELL GRKGQKGEAG VVGPVGPRGP IGPAGPKGEL GFPGRPGRPG
LNGLRGVKGE RGEALNGMPG LPGPPGPPGR PGRIVYIKGT VFPVSRRPHC KMTVSATYPG
NEEALNVQGA KGNRDCWGLQ STGGSPDLKG EKGDRGDPGP PGPPLPPSYF SHFINSIKGE
KGDNGNTGVK GEKGEPNRGF YLTGPPGPPG RPGLIGPKGD SVVGPRGPPG LPGLPGLPGY
GKTGPPGPPG PPGPPGPPAI YGSASAMPGP PGPPGEPGPP VSRNLITTFQ NIAGMLEKVH
FVAEGTLIYL SETSEVFIRV RNGWRKLQLG ELIPIPDDSL PPPAISSHGF QSLPAPSPIS
NMNNGKPVLH LVALNLPFSG DMRADFQCFQ QAQLAGLTAT YRAFLSSHLQ DLATVVRKTD
RYNLPIVNLK GEMLFHNWES IFKGNGGEFN INVPIYSFDG RNVMTDPSWP QKVMWHGSTA
NGIRMVSNYC EAWHTSDLAA MGQASPLKKG KLLDQKAYSC SNQFIVLCIE NSFVSDPQGK
//
