ID A0A914E182_9BILA Unreviewed; 524 AA.
AC A0A914E182;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Endostatin domain-containing protein {ECO:0000313|WBParaSite:ACRNAN_scaffold493.g17086.t2};
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.t2};
RN [1] {ECO:0000313|WBParaSite:ACRNAN_scaffold493.g17086.t2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
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DR AlphaFoldDB; A0A914E182; -.
DR WBParaSite; ACRNAN_scaffold493.g17086.t2; ACRNAN_scaffold493.g17086.t2; 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 224..268
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 337..500
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..328
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 70..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 58525 MW; 0EE328457BD3D42A CRC64;
WKGKRRNILR KGEEGSGLTD QPEIIPTRKI PSGLEDNRLP DDDDAEPEVT RMTTFSTTTL
TTPRSSHGYV KGERGEKGDK GDPGPPGVCS ADCSRFTTTS GLVGTPGPRG PPGPPGEPGY
SRTTSDYNRL SDEDIARIAS WPGIKGEKGD CVSYRSTDET RMLETNRVED VRTTAIPPYD
PRLHKHTTKG EKGDKGEMGM PGRPGPPGQA HTGPSPRYQA AGGVAVYQTT FELLSSAHNT
PVGALAFSIS SQQLFIRVNN GWQEVKLDRF HQAMESRPSV TTSEEERRTY EQLPRPEPEI
YTLAPPPPPK TITRPEPPQA DRRYEEERRV PNKDRVLHLV ALNSPVSGNM KGIRGVDLAC
YQQARQAGFK TTFRAFISSR VQDLNKVVHS KDSETPVVNL QGELLYDSWN HTFNGTSARK
VPLYSFNRRN VFADPIWFDR NVWHGSTQDG ARQEGGFCEG WRSSDQSQFG MSSVLRQGAS
LFGGTRETPC NRELAVLCIE VMSKYNIDQR LSKRMQWKRY KMRK
//
