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Database: UniProt
Entry: A0A0M3HVN6_ASCLU
LinkDB: A0A0M3HVN6_ASCLU
Original site: A0A0M3HVN6_ASCLU 
ID   A0A0M3HVN6_ASCLU        Unreviewed;       483 AA.
AC   A0A0M3HVN6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Fibrinogen C-terminal domain-containing protein {ECO:0000313|WBParaSite:ALUE_0000705301-mRNA-1};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000705301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0000705301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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DR   AlphaFoldDB; A0A0M3HVN6; -.
DR   WBParaSite; ALUE_0000705301-mRNA-1; ALUE_0000705301-mRNA-1; ALUE_0000705301.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR19143:SF327; FI21813P1-RELATED; 1.
DR   PANTHER; PTHR19143; FIBRINOGEN/TENASCIN/ANGIOPOEITIN; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          225..483
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   DOMAIN          431..476
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   REGION          88..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  54364 MW;  341BC0575B580CE5 CRC64;
     MREYNNRDVK SNEAELDPCI AAEVRMKKGL FSPRIRRSLL AAFVITILII LLSVLLFLLL
     SRSREESRPT IAAAPAIADY DQFEPVVQTS TSPRTTSAIT TQSSAQRSQH AAVVESQSES
     DDRPEMSWPK ESASEEDTQS SYTEKLFTIS AAPVVFPWLS DGTTTSTPIP TQSLTDGSAN
     KTDGRHTSSL QLEDRTVATE AATPAVTPST ELVTPQKVLE PVVSQNDSSS PRDCKTLLEE
     GKRTSGVYRL WLPKVGSFDA FCDMTTNGGG WTVVQRREDA SVYFSNRTWH EYEEGFGHLS
     TSFWLGLRKI HALVAKERGR SLILRIELNG DFCNDGDRCS QMPDGFWWGE WEFKASLLFN
     VYRRDARAYV SDASHNYMLT ISPAIAGNLT ERTNMDKFFY MNNGKPFTAI DKDNDRLSGN
     CAQFRDFGGW WHNDCGYVAL NGRYGDTSSK MRNAFFFYSR GSRPTVSYYI KPKFTKMMLR
     SRS
//
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