ID A0A7M7MJ18_VARDE Unreviewed; 1353 AA.
AC A0A7M7MJ18;
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_022669369};
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_022669369, ECO:0000313|Proteomes:UP000594260};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_022669369}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
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DR RefSeq; XP_022669369.1; XM_022813634.1.
DR EnsemblMetazoa; XM_022813634; XP_022669369; 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 1029..1063
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 1093..1258
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..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1303
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 436..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..614
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..663
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..944
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..957
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..998
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1353 AA; 143385 MW; 84918421EA874FAB CRC64;
MLLRSVSYGV LGLGWILLRA YLLVFASQGT LESLKIFSFS SHAPAEVLCD DTFLVLGNGE
FHEDERGDHL IDDTQLTVDG SGDDLRNYVP PTPSEGRYFV KQDTVKHKDA LHRDEKEEHV
AHRERHHRQR HRQPHQQQHS HNRHQVHGGA YEDGGLGAAH ADREDIEHFG NQVAETSAVI
ASFNKGPHEG GDKIEPFVTA KDDNVRESRT KDNPLKQLEV DSRRGTNERQ QPLDTDNAIG
YHTALLSTTL FLSTSERPTT FVVEYNNYDA KNNGAILSPA EADIGYMDNH STKHETTQTR
RLEDLSAPPF RGRGVGSSQF MATARDDRST AATVPMTANG KMKAMDELTH VRDSELLSTH
DVRKHIVYSQ ANANHDEEEE GRADFSGEGE YIDAENRLDS NKQADVVLPN DVQAREDLGS
GQGDNNAEES PLYDSNPKSG QGFQESSTER PDNRLDTVGR TDEKIAQTDE EGCKEPDADM
SNAVEEHVAK DERCSFDLLA AWIDENKHGL REKLRGPAGN CSCSSDFVNL ETLRGQAGRD
GRDGLDGTPG RPGLPGSEGP RGEMGLPGPE GPQGPPGQQG PAGPRGEKGD SGSEGTPGMQ
GPQGPPGPPG PPGPSHGRYF DFDTGLADGT YGTYMGAPGP VGPQGSQGPP GPKGARGPGG
EKGAPGEPGT KGFRGLRGPP GVTGRQGSKG EPGIPGAYGR PGAPGRVGER GPPGERGEKG
DPGIGLPGPP GPPGRSVLTH DDYENGLILE SIKGDKGDPG VNGSEGAPGL QGEPGERGPP
GPVGPKGEAG PVTLLGDNVA IRVMKGDKGD TGRRGKRGFP GPPGPSQGPE GPPGPPGPPG
IPGRNLGIKG DKGDPGPPGV VTGANGDVIR GEPGDPGPVG PRGDVGERGE RGERGLPGPP
GPPGPVTFSD GSSFDVATIK GEKGEPGLGV QGPPGPQGAQ GVGAPGPPGP PGPPGPAGPS
WDTSSNGNAP VSAMLRAPGP MMSHFMGPRG PPGPPGPPGE CTCHSNQKPS QVVPGGLIVK
DQKALHEITD FTSPGVLAYI GDDEALMLRV PQGWQYVGLG PTILPAITAT TSTTEPPRPP
LTADDLRNVP TIRMAALNSA SSGDMHGVRS ADYECYRESR NAGLNGTFKA FLASRIQNVD
SLVRARDAIA PVVNLKGELL FNSWREIFSG GLGHFPISPR IYSFDGKNVM NDPSWPQKVV
WHGADRNGAR SMENYCDAWN SASPRKTGFG SSLLHGRLLD QQKYPCNMRF VVLCVEVSSS
LSNTGSFTQS GSHNGGHRDE ASKWRRRRRS ANNGELDALS SSTPQHKLMP FEEYFDLANR
VIEPRDGADK VNKDKKSRES WFGDWTIEND PHL
//
