ID A0A0L7QUX6_9HYME Unreviewed; 884 AA.
AC A0A0L7QUX6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 05-FEB-2025, entry version 38.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:KOC62349.1};
GN ORFNames=WH47_05332 {ECO:0000313|EMBL:KOC62349.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC62349.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC62349.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC62349.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ414734; KOC62349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7QUX6; -.
DR STRING; 597456.A0A0L7QUX6; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000053825; 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 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; 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; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KOC62349.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825}.
FT DOMAIN 600..648
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 684..850
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..525
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 91594 MW; C7FD327006B20133 CRC64;
MGGQDSHSRS GLGHHPTPTT HPQGGGVLRE VRVTWVYGKN SGSQVVNGLF LIDCGLSISL
KLPVDCGLSA DHNLLANMVI RQIFEEDEDA GDTNIELIDG SGDIDINMTD IGRNDDEDRS
EESNPPPLIT PPPPNPDYKG PKGDKGDKGE KGESVRGPPG PPGPPGQDEG APGPPGERGL
EGPQGPKGDE GDMGILGPEG PQGQKGEPGR DGIPGEKGAQ GPPGPPGKGE FSGYDTEGIT
MRPGLPGQKG EAGLPGNPGP KGESGIAGEK GVKGETGHRG AKGDNGKEGP WGIQGSKGEP
GAPGSPGLPG APVLRKKGDK GDIGAPGDKG DKGTKGERGD KGDVGPAGIP GVNGFQGPQG
NKGVPGKNGT SGATGAKGEK GERGPPGATA IVSSGDYITI KGEKGTEGKR GRRGHPGPPG
PKGPPGKPGV MGEIGLPGWV GHPGTPGLPG PGGPKGEKGE PGRPSPYGVS VGVKGDKGDD
GFPGIPGQPG RDGQRGPPGP PGTPSQGNYI PVPGPPGPPG PPGPPGLSLI GQKGEPGIGR
GHMYGERDYY GVRQGARTSL DELKALRELK QLKELKEHLG AATAATRGPL ESTTKIVPGA
VTFQNTEAMT KMSAVSPVGT LAYIIDEQAL LVRVNNGWQY IALGSLLPIT TPAPPTTSPP
PANPPFEASN LVNQIPVKAD GTGLRMAALN EPFTGDMHGV RGADYACYRQ AKRAGLRGTF
RAFLSSRVQN VDSIVRLGDR DLPIVNIKGD VLFNSWKEMF NGNGAYFSQN PRIYSFNGKN
ILSDFAWPEK VAWHGSHKLG DRAMDTYCDA WHSSSSDRYG LGSPLTGGRL LEQVRYSCDN
KFALLCIEVS SETTRKRRSV ELVENEDEMS ENDYKEYLDS LMEN
//