GenomeNet

Database: UniProt
Entry: A0A2P6QEX3_ROSCH
LinkDB: A0A2P6QEX3_ROSCH
Original site: A0A2P6QEX3_ROSCH 
ID   A0A2P6QEX3_ROSCH        Unreviewed;       183 AA.
AC   A0A2P6QEX3;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Putative bifunctional inhibitor/plant lipid transfer protein/seed storage helical {ECO:0000313|EMBL:PRQ32735.1};
GN   ORFNames=RchiOBHm_Chr5g0049721 {ECO:0000313|EMBL:PRQ32735.1};
OS   Rosa chinensis (China rose).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rosa.
OX   NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ32735.1, ECO:0000313|Proteomes:UP000238479};
RN   [1] {ECO:0000313|EMBL:PRQ32735.1, ECO:0000313|Proteomes:UP000238479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA   Bendahmane M.;
RT   "The Rosa genome provides new insights in the design of modern roses.";
RL   Nat. Genet. 0:0-0(2018).
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|ARBA:ARBA00003211}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the plant LTP family.
CC       {ECO:0000256|ARBA:ARBA00009748}.
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:PRQ32735.1}.
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; PDCK01000043; PRQ32735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6QEX3; -.
DR   STRING; 74649.A0A2P6QEX3; -.
DR   EnsemblPlants; PRQ32735; PRQ32735; RchiOBHm_Chr5g0049721.
DR   Gramene; PRQ32735; PRQ32735; RchiOBHm_Chr5g0049721.
DR   OMA; NITCKMA; -.
DR   OrthoDB; 472989at2759; -.
DR   Proteomes; UP000238479; Chromosome 5.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   CDD; cd00010; AAI_LTSS; 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; IPR043325; LTSS.
DR   PANTHER; PTHR33044; BIFUNCTIONAL INHIBITOR/LIPID-TRANSFER PROTEIN/SEED STORAGE 2S ALBUMIN SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33044:SF104; NON-SPECIFIC LIPID TRANSFER PROTEIN GPI-ANCHORED 2; 1.
DR   Pfam; PF14368; LTP_2; 1.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238479};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..183
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015164127"
FT   DOMAIN          41..121
FT                   /note="Bifunctional inhibitor/plant lipid transfer
FT                   protein/seed storage helical"
FT                   /evidence="ECO:0000259|SMART:SM00499"
FT   REGION          133..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   183 AA;  18795 MW;  9CCBEDE175102229 CRC64;
     MAFSTNLLAA VFTAMLFMLT FHSCGVSAQA PGPAPEASVD CSTQLLTLSD CLTYVEEGSN
     LTKPDKACCP ELAALVKSTP QCLCYLLQKN STSSYGIQID MNKALDLPSV CKVETPPTSA
     CALLGIPVAS EGPTANSPAG SELAPQGPSA SPGNQTDHGT STTAKSLMAL FIGLAIASLP
     TFF
//
DBGET integrated database retrieval system