ID A0A371II62_MUCPR Unreviewed; 241 AA.
AC A0A371II62;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Non-specific lipid-transfer protein {ECO:0000256|RuleBase:RU000628};
DE Flags: Fragment;
GN ORFNames=CR513_00125 {ECO:0000313|EMBL:RDY14752.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDY14752.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDY14752.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDY14752.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC phospholipids as well as galactolipids across membranes. May play a
CC role in wax or cutin deposition in the cell walls of expanding
CC epidermal cells and certain secretory tissues.
CC {ECO:0000256|RuleBase:RU000628}.
CC -!- SIMILARITY: Belongs to the plant LTP family.
CC {ECO:0000256|ARBA:ARBA00009748, ECO:0000256|RuleBase:RU000628}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDY14752.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QJKJ01000020; RDY14752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371II62; -.
DR STRING; 157652.A0A371II62; -.
DR Proteomes; UP000257109; Unassembled WGS sequence.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR CDD; cd01960; nsLTP1; 1.
DR Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33076:SF73; AAI DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33076; NON-SPECIFIC LIPID-TRANSFER PROTEIN 2-RELATED; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lipid-binding {ECO:0000256|RuleBase:RU000628};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|RuleBase:RU000628}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..241
FT /note="Non-specific lipid-transfer protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016686964"
FT DOMAIN 32..117
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|SMART:SM00499"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDY14752.1"
SQ SEQUENCE 241 AA; 26774 MW; 299809BDA0B3F728 CRC64;
MSRAASIHHL AEVVSIVILL ITRCETVTSV SCSTVFEEVA PCTGFLQESS KKPSEACCSG
VKKISDEAGT REDRTAICEC LKKGLAQIGN YDPQQQLHDM NVHLWAAATG NLTGKYYKGS
IKLNDAISFK VTLQEMHLGV LFFSYSSFSM NPKWTILVLK NQHNLPVQDW YIFKETVRSA
LAANLDAYTV APRLRVDPSS SAKASCSLSC ASYNDLSIFF FQYRRHAACM KQAAHVFHCE
E
//
