ID A0A914DZ96_9BILA Unreviewed; 592 AA.
AC A0A914DZ96;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Endostatin domain-containing protein {ECO:0000313|WBParaSite:ACRNAN_scaffold493.g17086.t3};
OS Acrobeloides nanus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Cephalobomorpha; Cephaloboidea; Cephalobidae; Acrobeloides.
OX NCBI_TaxID=290746 {ECO:0000313|Proteomes:UP000887540, ECO:0000313|WBParaSite:ACRNAN_scaffold493.g17086.t3};
RN [1] {ECO:0000313|WBParaSite:ACRNAN_scaffold493.g17086.t3}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
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DR AlphaFoldDB; A0A914DZ96; -.
DR WBParaSite; ACRNAN_scaffold493.g17086.t3; ACRNAN_scaffold493.g17086.t3; ACRNAN_scaffold493.g17086.
DR Proteomes; UP000887540; Unplaced.
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; 3.40.1620.70; -; 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; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF861; ACETYLCHOLINESTERASE COLLAGENIC TAIL PEPTIDE; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000887540}.
FT DOMAIN 277..321
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 405..568
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..62
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 66187 MW; 623987BA9F7CEC12 CRC64;
WKGKRRNILR KGEEGSGLTD QPEIIPTRKI PSGLEDNRLP DDDDAEPEVT RMTTFSTTTL
TTPRSSHGYV KDGSGGPFSS QPDFTDSLIL PFAERRYIQN SVDAFPYVSP QSRDPFAPQL
TYAHGERGEK GDKGDPGPPG VCSADCSRFT TTSGLVGTPG PRGPPGPPGE PGYSRTTSDY
NRLSDEDIAR IASWPGIKGE KGDCVSYRST DETRMLETNR VEDVRTTAIP PYDPRLHKHT
TKGEKGDKGE MGMPGRPGPP GQAHTGPSPR YQAAGGVAVY QTTFELLSSA HNTPVGALAF
SISSQQLFIR VNNGWQEVKL DRFHQAMESR PSVPITQDTS SRDHLSYWTT SEEERRTYEQ
LPRPEPEIYT LAPPPPPKTI TRPEPPQADR RYEEERRVPN KDRVLHLVAL NSPVSGNMKG
IRGVDLACYQ QARQAGFKTT FRAFISSRVQ DLNKVVHSKD SETPVVNLQG ELLYDSWNHT
FNGTSARKVP LYSFNRRNVF ADPIWFDRNV WHGSTQDGAR QEGGFCEGWR SSDQSQFGMS
SVLRQGASLF GGTRETPCNR ELAVLCIEVM SKYNIDQRLS KRMQWKRYKM RK
//
