ID   PAP1_BRACM              Reviewed;         327 AA.
AC   Q94FZ9; Q94KU9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Plastid lipid-associated protein 1, chloroplastic;
DE   Flags: Precursor;
GN   Name=PAP1;
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 85-97, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11351096; DOI=10.1104/pp.126.1.330;
RA   Kim H.U., Wu S.S.H., Ratnayake C., Huang A.H.C.;
RT   "Brassica rapa has three genes that encode proteins associated with
RT   different neutral lipids in plastids of specific tissues.";
RL   Plant Physiol. 126:330-341(2001).
CC   -!- FUNCTION: May modulate the action of carotenoids.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- TISSUE SPECIFICITY: Expressed in anthers, sepals seeds, fruit coats,
CC       and leaves. Very low in petals and pistils and not detected in roots.
CC       {ECO:0000269|PubMed:11351096}.
CC   -!- DEVELOPMENTAL STAGE: Most abundant in anthers when the tapetum cells
CC       start to accumulate steryl-ester globules. High expression in mature
CC       leaves, medium in young leaves, and low in senescing leaves.
CC       {ECO:0000269|PubMed:11351096}.
CC   -!- INDUCTION: Down-regulated by drought and oxidative stresses. Up-
CC       regulated by wounding.
CC   -!- SIMILARITY: Belongs to the PAP/fibrillin family. {ECO:0000305}.
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DR   EMBL; AF290566; AAK57564.1; -; Genomic_DNA.
DR   EMBL; AF290563; AAK57561.1; -; mRNA.
DR   RefSeq; XP_009134286.1; XM_009136038.1.
DR   AlphaFoldDB; Q94FZ9; -.
DR   STRING; 3711.Bra000785.1-P; -.
DR   EnsemblPlants; Bra000785.1; Bra000785.1-P; Bra000785.
DR   GeneID; 103858647; -.
DR   Gramene; Bra000785.1; Bra000785.1-P; Bra000785.
DR   KEGG; brp:103858647; -.
DR   OMA; HDFKIRA; -.
DR   OrthoDB; 1037321at2759; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   InterPro; IPR039633; PAP.
DR   InterPro; IPR006843; PAP/fibrillin_dom.
DR   PANTHER; PTHR31906; PTHR31906; 1.
DR   Pfam; PF04755; PAP_fibrillin; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Coiled coil; Direct protein sequencing; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..84
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:11351096"
FT   CHAIN           85..327
FT                   /note="Plastid lipid-associated protein 1, chloroplastic"
FT                   /id="PRO_0000023205"
FT   REGION          56..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          85..107
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        56..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        249
FT                   /note="L -> F (in Ref. 1; AAK57561)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  35644 MW;  6116E7F1B6C02C88 CRC64;
     MATTVPLFSQ FTCKTPITSS STSSFQSKSP ILLPINPINR RIAVHRHDFK VRASDVNDEW
     GPDSKGRGGD VDDEWGPEIG LNSSVAEKVA EEAIESAEET ERLKRVLAGS LYGTDRGLSA
     SSETRAEISE LITQLESKNP NPAPNEALFL LNGKWILVYT SFVGLFPLLS RRISPLVKVD
     EISQTIDSDS FTVHNSVRFA SPLATTSLST NAKFEVRSPK RVQVKFEQGV IGTPQLTDSI
     EIPEFVEVLG QKIDLNPIKG LLTSVQDTAS SVARTISSQP PLKFSLPGDS AQSWLLTTYL
     DKDLRISRGD GGSVFVLIRE GSSLLNP