ID A0A7M7KQZ3_VARDE Unreviewed; 1206 AA.
AC A0A7M7KQZ3;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:XP_022669373};
OS Varroa destructor (Honeybee mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Varroidae; Varroa.
OX NCBI_TaxID=109461 {ECO:0000313|EnsemblMetazoa:XP_022669373, ECO:0000313|Proteomes:UP000594260};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_022669373}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
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DR RefSeq; XP_022669373.1; XM_022813638.1.
DR AlphaFoldDB; A0A7M7KQZ3; -.
DR EnsemblMetazoa; XM_022813638; XP_022669373; LOC111253745.
DR GeneID; 111253745; -.
DR Proteomes; UP000594260; Unplaced.
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 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; 3.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000594260}.
FT DOMAIN 878..912
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 946..1111
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 109..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..512
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..793
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..847
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1206 AA; 127263 MW; 8D92EC4437A76108 CRC64;
MLLRSVSYGV LGLGWILLRA YLLVFASQGT LESLKIFSFS SHAPAEVLCD DTFLVLGNGE
FHEDERGDHL IDDTQLTVDG SGDDLRNYVP PTPSEGRYFV KQDTVKHKDA LHRDEKEEHV
AHRERHHRQR HRQPHQQQHS HNRHQVHGGA YEDGGLGAAH ADREDIEHFG NQVAETSAVI
ASFNKGPHEG GDKIEPFVTA KDDNVRESRT KDNPLKQLEV DSRRGTNERQ QPLDTGEGEY
IDAENRLDSN KQADVVLPND VQAREDLGSG QGDNNAEESP LYDSNPKSGQ GFQESSTERP
DNRLDTVGRT DEKIAQTDEE GCKEPDADMS NAVEEHVAKD ERCSFDLLAA WIDENKHGLR
EKLRGPAGNC SCSSDFVNLE TLRGQAGRDG RDGLDGTPGR PGLPGSEGPR GEMGLPGPEG
PQGPPGQQGP AGPRGEKGDS GSEGTPGMQG PQGPPGPPGP PGPSHGRYFD FDTGLADGTY
GTYMGAPGPV GPQGSQGPPG PKGARGPGGE KGAPGEPGTK GFRGLRGPPG VTGRQGSKGE
PGIPGAYGRP GAPGRVGERG PPGERGEKGD PGIGLPGPPG PPGRSVLTHD DYENGLILES
IKGDKGDPGV NGSEGAPGLQ GEPGERGPPG PVGPKGEAGP VTLLGDNVAI RVMKGDKGDT
GRRGKRGFPG PPGPSQGPEG PPGPPGPPGI PGRNLGIKGD KGDPGPPGVV TGANGDVIRG
EPGDPGPVGP RGDVGERGER GERGLPGPPG PPGPVTFSDG SSFDVATIKG EKGEPGLGVQ
GPPGPQGAQG VGAPGPPGPP GPPGPAGPSW DTSSNGNAPV SAMLRAPGPM MSHFMGPRGP
PGPPGPPGEC TCHSNQKPSQ VVPGGLIVKD QKALHEITDF TSPGVLAYIG DDEALMLRVP
QGWQYVGLGP TILPAITATT STTEPPRPPL TADDLRNVPT KRRKIRMAAL NSASSGDMHG
VRSADYECYR ESRNAGLNGT FKAFLASRIQ NVDSLVRARD AIAPVVNLKG ELLFNSWREI
FSGGLGHFPI SPRIYSFDGK NVMNDPSWPQ KVVWHGADRN GARSMENYCD AWNSASPRKT
GFGSSLLHGR LLDQQKYPCN MRFVVLCVEV SSSLSNTGSF TQSGSHNGGH RDEASKWRRR
RRSANNGELD ALSSSTPQHK LMPFEEYFDL ANRVIEPRDG ADKVNKDKKS RESWFGDWTI
ENDPHL
//
