ID   FVE_FLAVE               Reviewed;         114 AA.
AC   P80412;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Immunomodulatory protein FIP-Fve;
OS   Flammulina velutipes (Agaricus velutipes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Flammulina.
OX   NCBI_TaxID=38945;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX   PubMed=7705335; DOI=10.1111/j.1432-1033.1995.tb20256.x;
RA   Ko J.-L., Hsu C.-I., Lin R.-H., Kao C.-L., Lin J.-Y.;
RT   "A new fungal immunomodulatory protein, FIP-fve isolated from the edible
RT   mushroom, Flammulina velutipes and its complete amino acid sequence.";
RL   Eur. J. Biochem. 228:244-249(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=12948495; DOI=10.1016/s0022-2836(03)00923-9;
RA   Paaventhan P., Joseph J.S., Seow S.V., Vaday S., Robinson H., Chua K.Y.,
RA   Kolatkar P.R.;
RT   "A 1.7A structure of Fve, a member of the new fungal immunomodulatory
RT   protein family.";
RL   J. Mol. Biol. 332:461-470(2003).
CC   -!- FUNCTION: Lectin with specificity for complex cell-surface
CC       carbohydrates. Possesses immunomodulatory activity, stimulates
CC       lymphocyte mitogenesis, suppresses systemic anaphylaxis reactions and
CC       edema, enhances transcription of IL-2, IFN-gamma and TNF-alpha and
CC       hemagglutinates red blood cells.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the fungal immunomodulatory protein (FIP)
CC       family. {ECO:0000305}.
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DR   PIR; S69147; S69147.
DR   PDB; 1OSY; X-ray; 1.70 A; A/B=1-114.
DR   PDBsum; 1OSY; -.
DR   AlphaFoldDB; P80412; -.
DR   SMR; P80412; -.
DR   UniLectin; P80412; -.
DR   iPTMnet; P80412; -.
DR   EvolutionaryTrace; P80412; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0002682; P:regulation of immune system process; IEA:InterPro.
DR   InterPro; IPR036344; FIP_sf.
DR   InterPro; IPR015339; Immunomodulatory_FIP-Fve_fun.
DR   Pfam; PF09259; Fve; 1.
DR   SUPFAM; SSF101542; SSF101542; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Lectin.
FT   CHAIN           1..114
FT                   /note="Immunomodulatory protein FIP-Fve"
FT                   /id="PRO_0000087390"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:7705335"
FT   HELIX           2..13
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          32..40
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   TURN            79..82
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:1OSY"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:1OSY"
SQ   SEQUENCE   114 AA;  12704 MW;  D38C641DCC112A94 CRC64;
     SATSLTFQLA YLVKKIDFDY TPNWGRGTPS SYIDNLTFPK VLTDKKYSYR VVVNGSDLGV
     ESNFAVTPSG GQTINFLQYN KGYGVADTKT IQVFVVIPDT GNSEEYIIAE WKKT