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Database: UniProt
Entry: A0A158P5Y2_ANGCA
LinkDB: A0A158P5Y2_ANGCA
Original site: A0A158P5Y2_ANGCA 
ID   A0A158P5Y2_ANGCA        Unreviewed;       429 AA.
AC   A0A158P5Y2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Endostatin domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000035001-mRNA-1};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Metastrongyloidea; Angiostrongylidae; Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000035001-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000035001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
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DR   AlphaFoldDB; A0A158P5Y2; -.
DR   STRING; 6313.A0A158P5Y2; -.
DR   WBParaSite; ACAC_0000035001-mRNA-1; ACAC_0000035001-mRNA-1; ACAC_0000035001.
DR   Proteomes; UP000035642; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR016187; CTDL_fold.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF391; COLLAGEN ALPHA-1(IX) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 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:UP000035642};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..429
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007630051"
FT   DOMAIN          376..422
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          139..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..239
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  46959 MW;  4BB64710C4F41CEB CRC64;
     MFISIVLFIL VLPSSYTEPI NQILNNERLI RSSNAADVDE TTSTQFYNAS NVSESNVVDY
     DDPLTKDSTN EQQFETPAED YSPVTNSLLQ DDNEFGGLIF QYTVPQEDNA MLDPQLTENI
     DFNSLPPPNF EPIDVVPFET DDEGSGFEKF KDQGDKEGKS GGVVFSPTPK PQLPDDLEQK
     QFNENVQSAL KGERGEPGPP GVCLQQCRDG MPGQSGPVGP QGPQGAQGPP GPPGPPGEPG
     YVHQSMYGGA EVQPIPGPPG LAGPPGPPGP QGIRGPRGET GYPGRDGRDF RGLTDRDIEL
     IVRHPMLKET ARPEAKPERR PSSSSRREAS PVLHSKDESL TVSAPGYVKD TPRPLPWFHP
     KPPPEYLAAF ERDRMIHMIA LNTPYDGNMH GMRGADLQCY REARMNGFTT TFRAMLSSNV
     QVRYILVAM
//
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