ID PPF1_PEA Reviewed; 442 AA. AC Q9FY06; O04699; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2003, sequence version 2. DT 28-JAN-2026, entry version 79. DE RecName: Full=Inner membrane protein PPF-1, chloroplastic; DE AltName: Full=Post-floral-specific protein 1; DE Flags: Precursor; GN Name=PPF-1; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). 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; Hologalegina; IRL clade; Fabeae; Lathyrus. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. G2; TISSUE=Apical bud; RX PubMed=9479033; DOI=10.1016/s0378-1119(97)00613-6; RA Zhu Y., Zhang Y., Luo J., Davies P.J., Ho D.T.-H.; RT "PPF-1, a post-floral-specific gene expressed in short-day-grown G2 pea, RT may be important for its never-senescing phenotype."; RL Gene 208:1-6(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-107; GLY-127; PRO-150; PRO-250 RP AND 326-GLN-GLN-327 DELINS HIS-LYS. RC STRAIN=cv. Alaska; RA Xu Y., Wang M., Li Q., Ji X., Zhu Y.; RT "Cloning and sequencing of the homologous gene of PPF-1 from Alaska pea."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May be required for the insertion of some integral membrane CC proteins into the chloroplast thylakoid membrane. May play a role in CC inhibiting senescence. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Highly expressed in apical buds. Low levels of CC expression in leaves. Not expressed in roots, and stems. CC -!- DEVELOPMENTAL STAGE: Expressed after flower initiation. CC -!- INDUCTION: By the plant hormone gibberellin A3. Expression is induced CC to a greater extent by short day conditions than long day conditions. CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC (TC 2.A.9.2) family. CC {ECO:0000305}. 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; Y12618; CAA73179.1; -; mRNA. DR EMBL; AJ297606; CAC04249.1; -; mRNA. DR PIR; T06476; T06476. DR AlphaFoldDB; Q9FY06; -. DR SMR; Q9FY06; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032977; F:membrane insertase activity; IEA:InterPro. DR GO; GO:0051205; P:protein insertion into membrane; IEA:TreeGrafter. DR GO; GO:0072598; P:protein localization to chloroplast; IEA:TreeGrafter. DR GO; GO:0010027; P:thylakoid membrane organization; IEA:TreeGrafter. DR CDD; cd20070; 5TM_YidC_Alb3; 1. DR InterPro; IPR001708; YidC/ALB3/OXA1/COX18. DR InterPro; IPR028055; YidC/Oxa/ALB_C. DR InterPro; IPR047196; YidC_ALB_C. DR NCBIfam; TIGR03592; yidC_oxa1_cterm; 1. DR PANTHER; PTHR12428:SF47; INNER MEMBRANE PROTEIN ALBINO3, CHLOROPLASTIC; 1. DR PANTHER; PTHR12428; OXA1; 1. DR Pfam; PF02096; 60KD_IMP; 1. PE 2: Evidence at transcript level; KW Chloroplast; Membrane; Plastid; Thylakoid; Transit peptide; Transmembrane; KW Transmembrane helix. FT TRANSIT 1..? FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN ?..442 FT /note="Inner membrane protein PPF-1, chloroplastic" FT /id="PRO_0000020370" FT TOPO_DOM 1..108 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 109..129 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 130..183 FT /note="Stromal" FT /evidence="ECO:0000255" FT TRANSMEM 184..204 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 205..296 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 297..317 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 318..442 FT /note="Stromal" FT /evidence="ECO:0000255" FT REGION 350..371 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 390..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 358..371 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 414..427 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..442 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 107 FT /note="D -> G (in strain: cv. Alaska)" FT /evidence="ECO:0000269|Ref.2" FT VARIANT 127 FT /note="V -> G (in strain: cv. Alaska)" FT /evidence="ECO:0000269|Ref.2" FT VARIANT 150 FT /note="L -> P (in strain: cv. Alaska)" FT /evidence="ECO:0000269|Ref.2" FT VARIANT 250 FT /note="L -> P (in strain: cv. Alaska)" FT /evidence="ECO:0000269|Ref.2" FT VARIANT 326..327 FT /note="QQ -> HK (in strain: cv. Alaska)" FT /evidence="ECO:0000269|Ref.2" SQ SEQUENCE 442 AA; 48238 MW; 3D4D4C99C5BE9B04 CRC64; MAKTLISSPS FLGTPLPSLH RTFSPNRTRL FTKVQFSFHQ LPPIQSVSHS VDLSGIFARA EGLLYTLADA TVAADAAAST DVAAQKNGGW FGFISDGMEF VLKVLKDGLS SVHVPYSYGF AIILLTVIVK AATLPLTKQQ VESTLAMQNL QPKIKAIQER YAGNQERIQL ETSRLYTQAG VNPLAGCLPT LATIPVWIGL YQALSNVANE GLLTEGFLWI PSLGGPTSIA ARQSGSGISW LFPFVDGHPL LGWYDTAAYL VLPVLLIVSQ YVSMEIMKPP QTNDPNQKNT LLIFKFLPLM IGYFSLSVPS GLTIYWFTNN VLSTAQQVWL RKLGGAKPAV NENAGGIITA GQAKRSASKP EKGGERFRQL KEEEKKKKLI KALPVEEVQP LASASASNDG SDVENNKEQE VTEESNTSKV SQEVQSFSRE RRSKRSKRKP VA //