ID A0A212FK74_DANPL Unreviewed; 939 AA.
AC A0A212FK74;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 02-APR-2025, entry version 30.
DE SubName: Full=Collagen alpha-1 {ECO:0000313|EMBL:OWR54132.1};
GN ORFNames=KGM_207308 {ECO:0000313|EMBL:OWR54132.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR54132.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR54132.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR54132.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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:OWR54132.1}.
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DR EMBL; AGBW02008127; OWR54132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212FK74; -.
DR KEGG; dpl:KGM_207308; -.
DR eggNOG; KOG3546; Eukaryota.
DR InParanoid; A0A212FK74; -.
DR Proteomes; UP000007151; 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 Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; 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 SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:OWR54132.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..939
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012329505"
FT DOMAIN 698..744
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 783..937
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 267..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..552
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..654
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..771
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 100763 MW; 5AD5B7CC202B2998 CRC64;
MVLFFRWFGA FSPMVIAEPD NYDILSLVRA NVLTDFIDIV KGTDVYGAIK LVKNELITIK
LDQFPDPINH LATPFEIYAL VKLNVDVTSC LFQIISNKEN KLSLCFTPEG EDLIRITLNG
SDLPENGISF HYLIEDYNAF VNIILAVNDK NVEFYSNCEK IETQYFDSDY TIENINLEKD
SILHFGKLTE ESNLFEAAIQ TLVIYPKPDI NGRRYICSDD KLPASIKANP STESNDFTKA
ENLEVNTFID FDSSEKISTN SLFDSTEETV VKGEKGDKGD KGEKGDRGDK GERGESVMGE
RGPIGPDGAP GTPGVMGKEG SCKCSEAIVS DLLLKMPEMR GPPGDYGLKG DRGEKGVKGD
SGLPGKDGRD GNEGDPGIQG PPGTPGLVRK EIVETKVPVV GEKGERGPVG PPGTPGRDGL
RGEKGDKGEP GLMGLPAKLS SILDEDIDPN EEKAIVEKFR GYKGASGPEG PKGEKGDTGA
IGPQGETGRD GIQGPPGKHG HKGETGKDGS KGDKGEPGIP GPPGTVPSSQ ISLMKGPKGD
RGPPGQTGPR GPTGHHGKVG PIGPPGKSHK GEPGKPGPMG PKGEKGATGP RGEKGEGLSP
SDIERLKGHK GDRGEIGLPG EAGKPGLPGT CGECVRVSIP GPSGPPGPPG PSGPPGVSII
GPKGEPGGLV TKKSFFAFND IHHESTDEDD DFYTAATVIF KTTTGLLKRT TDTPLGTLAY
ILQEKILLMR VENGWQYVVM GSFLQTRESH TSTTFRPTYY SSTPSSPPSS DETTENNEDN
YIRLVALNQA YAGNILMANN RTGRNAADQE CYRQAYIHNF KSTFAAFLAT RVEDLRFIVK
RKRDRYVPVV NLYGQVLFDS WASMFNGSGA LFAKSSIYSF NGKNVQIDTT WPLKAVWHGS
NSFGTVLSRA NCNEWTSDSP LNVGAASLLY THRLLEEEQ
//
