ID A0A1V4JVM2_PATFA Unreviewed; 1173 AA.
AC A0A1V4JVM2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-OCT-2025, entry version 27.
DE SubName: Full=Collagen alpha-1(XV) chain isoform D {ECO:0000313|EMBL:OPJ76125.1};
GN Name=COL15A1 {ECO:0000313|EMBL:OPJ76125.1};
GN ORFNames=AV530_015423 {ECO:0000313|EMBL:OPJ76125.1};
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:OPJ76125.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ76125.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ76125.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ76125.1};
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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:OPJ76125.1}.
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DR EMBL; LSYS01006073; OPJ76125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JVM2; -.
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 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: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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:OPJ76125.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1173
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010703921"
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..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..925
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 289..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..372
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..430
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..643
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..709
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 121210 MW; 67A31A2967D484EA 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 RGQKGQEGED GPTGSPRMPE VEDTQKKDQG
PPGPPGKLGQ HGQPGVPGKN GLPSDPGEGL PGPPGLPGPP GLPGPEGPSA PSRGLNRPEP
EESDSGDIDG ETEILRGLPG PPGLPGLPGK PAPDSGVGPP GSPGEDGASG EQGSEGPQGP
PGLDGVVGPP GWKGEKGDRG LPGTVGPKGD PGVTGSRGPK GEAGTVGSPG KPGPPGPPGS
PGPPGPPGPP GPPGLSYSLG FEDMEGSGSI GLLSESRIPG SRRPKSSTER QGQRWPLGPK
GERGNTGPPG SKGEKGDQGP QGEPGQDGNS IVGPPGPPGP PGPIIAIPEL LLNNTDGIFN
FTGIKGLLGP PGLDGKPGLP GFPGPRGPKG DTGLPGLQGP KGQQGEKGEP GAIISADGSL
TELLGRKGEK GEAGVVGPMG PTGPIGPTGP KGELGFPGRP GRPGLNGLRG VKGDRGEPFN
GLPGLPGPRG PPGPPGRIVY IKGTVFPVSP RPHCKMPMST SCPGNQGTLS VHGAKANRGS
WGLHSSSDLK GEKGDRGAPG PPGPPLPPSY FSHFINSIKG EKGDNGVSGV KGEKGEPNGG
FFLTGPPGPP GRPGLVGPKG DSVVGPRGPP GLPGLPGLPG YGKIGPPGPP GPPGPPGPTA
IYGSAAAMPG PPGPPGEPGP PATRNLVTTF QNVEGMLEKV HLVAEGTLMY LSETSEVFIR
VRNGWRKLQL GELILVPADS LPPPAISSHG FQSLPALSPI SNMNNGKPAL HLVALNLPFS
GDVRADFQCF QQAQLAGLTS TYRAFLSSHL QDLATIVRKT DRYHLPIVNL KGETLFNNWE
SIFNGNGGQF NIHVPIYSFD GRNVMTDPAW PQKIIWHGST ANGIRLVSSY CEAWHTADMR
ELGQASQLKT GKLLDQKEKT VKENIPQHKP HSS
//
