ID A0A1V4JVA0_PATFA Unreviewed; 1255 AA.
AC A0A1V4JVA0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-OCT-2025, entry version 29.
DE SubName: Full=Collagen alpha-1(XV) chain isoform A {ECO:0000313|EMBL:OPJ76122.1};
GN Name=COL15A1 {ECO:0000313|EMBL:OPJ76122.1};
GN ORFNames=AV530_015423 {ECO:0000313|EMBL:OPJ76122.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Columbimorphae; Columbiformes;
OC Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ76122.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ76122.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ76122.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ76122.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ76122.1}.
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DR EMBL; LSYS01006073; OPJ76122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JVA0; -.
DR STRING; 372326.A0A1V4JVA0; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 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:SF1077; COLLAGEN ALPHA-3(IV) CHAIN; 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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:OPJ76122.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1255
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013365145"
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 224..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..454
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..512
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..598
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..655
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..725
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..791
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..980
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1003
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 130007 MW; 7FD21B76CB305075 CRC64;
MLSRHAWWTW DLLLLLFGLL ICDGSPAEII EERGSKGHLD LMELIGVPLP PSVYFVTGYG
GFPAYSFGPD ANIGRLTRAI IPSPFYRDFT IVVTMKPNSD HGGVLFAITD ALQKTIYLGM
RLSPVDDNTQ RIIMYYTEPG SQLSREAASF KVPVMTNRWN RFTATVQGND VSLFMDCEEY
QRVQFQRSGE ALVFESGSGI FVGNAGATGL EKFTGSIQHL TIKSDPRATE DHCEDDDSYV
SGDNSGNGSI QDHEGTSETQ EVLAPSYLPI RPEDMLAEPV EAPPAVLSYL EENDSSGNHR
SEETSEGAKP KEQESAVMKT EQSNSEPTTV VQKISREEDG SGATVLPGVS REEGQKGQEG
EDGPTGSPRM PEVEDTQKKD QGPPGPPGKL GQHGQPGVPG KNGLPSDPGE GLPGPPGLPG
PPGLPGPEGP SAPSRGLNRP EPEESDSGDI DGETEILRGL PGPPGLPGLP GKPAPDSGVG
PPGSPGEDGA SGEQGSEGPQ GPPGLDGVVG PPGWKGEKGD RGLPGTVGPK GDPGVTGSRG
PKGEAGTVGS PGKPGPPGPP GSPGPPGPPG PPGPPGLSYS LGFEDMEGSG SIGLLSESRI
PGSRRPKSST ERQGQRWPLG PKGERGNTGP PGSKGEKGDQ GPQGEPGQDG NSIVGPPGPP
GPPGPIIAIP ELLLNNTDGI FNFTGIKGLL GPPGLDGKPG LPGFPGPRGP KGDTGLPGLQ
GPKGQQGEKG EPGAIISADG SLTELLGRKG EKGEAGVVGP MGPTGPIGPT GPKGELGFPG
RPGRPGLNGL RGVKGDRGEP FNGLPGLPGP RGPPGPPGRI VYIKGTVFPV SPRPHCKMPM
STSCPGNQGT LSVHGAKANR GSWGLHSSSD LKGEKGDRGA PGPPGPPLPP SYFSHFINSI
KGEKGDNGVS GVKGEKGEPN GGFFLTGPPG PPGRPGLVGP KGDSVVGPRG PPGLPGLPGL
PGYGKIGPPG PPGPPGPPGP TAIYGSAAAM PGPPGPPGEP GPPATRNLVT TFQNVEGMLE
KVHLVAEGTL MYLSETSEVF IRVRNGWRKL QLGELILVPA DSLPPPAISS HGFQSLPALS
PISNMNNGKP ALHLVALNLP FSGDVRADFQ CFQQAQLAGL TSTYRAFLSS HLQDLATIVR
KTDRYHLPIV NLKGETLFNN WESIFNGNGG QFNIHVPIYS FDGRNVMTDP AWPQKIIWHG
STANGIRLVS SYCEAWHTAD MRELGQASQL KTGKLLDQKE KTVKENIPQH KPHSS
//
