ID   A0A158PQE3_BRUPA        Unreviewed;       893 AA.
AC   A0A158PQE3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JAN-2026, entry version 43.
DE   SubName: Full=Endostatin domain-containing protein {ECO:0000313|WBParaSite:BPAG_0000166601-mRNA-1};
GN   ORFNames=BPAG_LOCUS1647 {ECO:0000313|EMBL:VDN82833.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|WBParaSite:BPAG_0000166601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0000166601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN82833.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UZAD01000145; VDN82833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158PQE3; -.
DR   STRING; 6280.A0A158PQE3; -.
DR   WBParaSite; BPAG_0000166601-mRNA-1; BPAG_0000166601-mRNA-1; BPAG_0000166601.
DR   Proteomes; UP000278627; 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   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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          360..405
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          706..870
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..65
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..176
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..344
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..591
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  98583 MW;  551AA53051339AAC CRC64;
     MKSLKEGSGV QDEELQEYEK TGKTTIAVPE QSSMHTSSDY PRDDQNSSSS SSSSCSSSSP
     SSHSSYITDS NDQLIVGKHT DSLILPSHQT TITERLISII PILEQIQSLE AISEIHEFWN
     NRGHRTDVKP EKGEKGDKGD RGEPGPPGEP GTCPIECQPG RDGRDGIPGM PGEMGPMGPM
     GPPGPAGPPG LSTQIVQEGP QGVQTVAGPT GPQGPPGPMG PRGPPGPRGV GEPGFPGAPG
     VPGRCERLHP EDIERIISDP RIKGEKGDCL PGIPIRHPGE SKELPPYDSY QRHYAMKGER
     GERGEIGRMG PMGPIGHPGP PGPPGPPGPP GPPGSPGHPG PAGPPLAAYP QPTHIAPGGV
     QVYPTTIELF TASHGMPIGS LTFCISSQQL YIRVNGGFKD IKLEGFHPIM ERRPTVEIEF
     EPPNENFMHY WVSYNCLPLD VVNEGVDESS KSEVQYQIPL MSNDDSLIPS QVSLSHHRIS
     PKLNIPQKNQ QLIPDTYDKQ SRTADIIHRP QIFDASQSIK SYQQHHKSLL SSEITPSTFS
     NQQSWQTFES KHHLSYPRTE YRPPAGQLYP RYRLPSGSSG SSGLSGLSRL SSNERLHKSH
     HLSQRLDHTP STLQSFPSSQ HISVQHQRIE HQNPSVKPDY HSEHIATTFS PEWSKQQATI
     SLADEQEAHR SRYPDHERLR YRERPGPDRT HSALLPHSLQ AKDLVLHLIA LNTPMSGNMR
     GVRGADLACY QQARQANFRT TFRAFLSSHV QDLNKVVHSG DRDTPVVNLR GERLFDSWSD
     IFQQRQMADL PIYSFNRRNV FADSIWPEKR IWHGSDLSGM RSESGYCSAW RSASTTQVGR
     ASFIGRGLPL LRDSRDSECS RELVVLCIEV LFFASFSQFF LKFFNNKFLN MQK
//