ID A0A7L4H357_PODST Unreviewed; 1314 AA.
AC A0A7L4H357;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:NXX19070.1};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NXX19070.1};
GN ORFNames=PODSTR_R01051 {ECO:0000313|EMBL:NXX19070.1};
OS Podargus strigoides (Tawny frogmouth) (Caprimulgus strigoides).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Strisores; Caprimulgiformes;
OC Podargidae; Podargus.
OX NCBI_TaxID=8905 {ECO:0000313|EMBL:NXX19070.1, ECO:0000313|Proteomes:UP000584326};
RN [1] {ECO:0000313|EMBL:NXX19070.1, ECO:0000313|Proteomes:UP000584326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-40 {ECO:0000313|EMBL:NXX19070.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXX19070.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:NXX19070.1}.
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DR EMBL; VZTK01020517; NXX19070.1; -; Genomic_DNA.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000584326; 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: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:SF912; COLLAGEN ALPHA-1(XV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000584326};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..196
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 57..195
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 552..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..598
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..776
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..842
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1054
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXX19070.1"
FT NON_TER 1314
FT /evidence="ECO:0000313|EMBL:NXX19070.1"
SQ SEQUENCE 1314 AA; 137961 MW; 00C95247C82CAED8 CRC64;
TERGSKGHLD LMELIGVPLP PSVYFVTGYG GFPAYSFGPD ANIGRLTSAI IPLPFYRDFT
IAVTVKPNSD RGGVLFAITD AFQKTIYLGM RLSLVDDSTQ RIIIYYTEPG SHVSREAASF
KVPVMTNRWN RFTVTVQGND VTLFMDCEEY QRVQFQRSDQ ALVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDLYA SGDISGNGSI QEREGISETQ EVLAPSHLPP
EDMLAEPVEA PPTVLSYLEE KDLSGDHRSE ETFKAAKFKE QGTASFLFVY SAVMETGEGN
SDPTTVTQKI LRDDDGSGAS VLPGVSREEH AKTEITFSVL ECPLISDSKS GTLCKRLTGP
RGPPRPAGPS APSRGLVSVW GSLSVSLACL RGIQNETGGF IWESSLTGTE IIMVFIFQMF
STQAMLKNVR LEHEESGSGD IDRESEILRV SIYWCLFLIS IIKSLVLLIH IVEGPFHDGN
FICSCPPRLA LQSRGHFYSS KHSQVLNKST ASQCNSNSMK KQFEMNGEKT NYFPLFSNPL
ISFWLSPPEL PALPGNPAPG SDIGPPGSPG EDGASGEPGR EGPQGPPGLD GVVGPPGQKG
EKGDRGLPGS VGPKGDTGAT GSIGRKGEAG AVGSSGKPGP PGPPGPPGPP GPPGPPGLNY
ILGSEVFCYY GVCCSYGSTS SRGGTGPKGE KGDPGLQGEP GQDGNSIVGP PGPPGPIIKI
PELLLNNTDG IFNFTGIKGL LGPPGPDGKP GLPGFPGPRG PKGDTGLPGS QGPKGQQGEK
GEPGAIIGAD GSLTELLGRK GDKGETGVVG PVGPMGPIGP TGPKGELGFP GRPGRPGLNG
PRGVKGDPGE SFHGLPGLPG PPGPPGPPGR ILYIKGTVFP VSPRPHCKMP VIIPYPGNQE
ALNVHGAKAN RDSWGLHSSA DLKGEKGDRG APGPPGPPLP PSYFSHFLNS IKGEKGDNGV
TGVKGEKGEP NGGFFLTGPP GPPGRPGLVG PKGDSVVGPR GPPGLPGLPG LPGYGKIGPP
GPPGPPGPPG PPAIYGSAAA MPGPPGPPGE PGPPATRNLV TTFQNIQGML EKVHFVAEGT
LIYLSETSEL FIRVRNGWRK FQLGELIPIP ADSLPPPAIS SHGFQPLPAL SPISNTNNGK
PALHLVALNL PFSGDMRADF QCFQQAQLAG LTSTYRAFLS SHLQDLATVV RKTDRYHLPI
VNLKGEILFN NWESIFNGNG GQFNIHVPIY SFDGRNVMTD PSWPQKVIWH GSTATGIRLV
SKYCEAWHTA DMGAMGQASP LKMGKLLDQK VYSCNNQFIV LCIENSFVSD PQGK
//
