ID A0A493TZH9_ANAPP Unreviewed; 1163 AA.
AC A0A493TZH9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE SubName: Full=Collagen type XV alpha 1 chain {ECO:0000313|Ensembl:ENSAPLP00000031282.1};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSAPLP00000031282.1};
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:ENSAPLP00000031282.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000031282.1, 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:ENSAPLP00000031282.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSAPLP00000031282.1}
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; A0A493TZH9; -.
DR STRING; 8840.ENSAPLP00000031282; -.
DR Ensembl; ENSAPLT00000046444.1; ENSAPLP00000031282.1; ENSAPLG00000014374.2.
DR GeneTree; ENSGT00940000158302; -.
DR OMA; RATEDQC; -.
DR Proteomes; UP000016666; Chromosome 2.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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; 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; 4.
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..1163
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019785847"
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..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..906
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 553..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..688
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..713
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..790
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 121273 MW; 55D432BC8EEF61BA 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 FEDMEGSGII
GLLSESRITG SRVPKGERGN IGPPGSKGLP GTKGKPGFPG IDGHPGNMGP KGEKGDPGPQ
GERGQDGNSI VGPPGPPGPP GPIIAIPELL LNDTDGIFNF SSVEELVGPP GPDGRPGLPG
FPGPQGPKGD IGLPGPKGPK GQQGEKGEPG AIITADGSLT ELLGRKGQKG EAGVVGPVGP
RGPIGPAGPK GELGFPGRPG RPGLNGLRGV KGERGEALNG MPGLPGPPGP PGRPGRIVYI
KGTVFPVSRR PHCKMTVSAT YPGNEEALNV QGAKGNRDCW GLQSTGGSPD LKGEKGDRGD
PGPPGPPLPP SYFSHFINSI KGEKGDNGNT GVKGEKGEPN RGFYLTGPPG PPGRPGLIGP
KGDSVVGPRG PPGLPGLPGL PGYGKTGPPG PPGPPGPPGP PAIYGSASAM PGPPGPPGEP
GPPVSRNLIT TFQNIAGMLE KVHFVAEGTL IYLSETSEVF IRVRNGWRKL QLGELIPIPD
DSLPPPAISS HGFQSLPAPS PISNMNNGKP VLHLVALNLP FSGDMRADFQ CFQQAQLAGL
TATYRAFLSS HLQDLATVVR KTDRYNLPIV NLKGEMLFHN WESIFKGNGG EFNINVPIYS
FDGRNVMTDP SWPQKVMWHG STANGIRMVS NYCEAWHTSD LAAMGQASPL KKGKLLDQKA
YSCSNQFIVL CIENSFVSDP QGK
//
