ID   VDAC_PEA                Reviewed;         276 AA.
AC   P42054;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Outer plastidial membrane protein porin;
DE   AltName: Full=Voltage-dependent anion-selective channel protein;
DE            Short=VDAC;
GN   Name=POR1;
OS   Pisum sativum (Garden pea).
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; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-23; 158-166 AND
RP   196-209.
RC   STRAIN=cv. Kleine Rheinlaenderin; TISSUE=Root;
RX   PubMed=7523392; DOI=10.1016/s0021-9258(18)47312-7;
RA   Fischer K., Weber A., Brink S., Arbinger B., Schuenemann D., Borchert S.,
RA   Heldt H.W., Popp B., Benz R., Link T., Eckerskorn C., Fluegge U.I.;
RT   "Porins from plants. Molecular cloning and functional characterization of
RT   two new members of the porin family.";
RL   J. Biol. Chem. 269:25754-25760(1994).
CC   -!- FUNCTION: Forms a channel through the cell membrane that allows
CC       diffusion of small hydrophilic molecules. The channel adopts an open
CC       conformation at low or zero membrane potential and a closed
CC       conformation at potentials above 30-40 mV. The open state has a weak
CC       anion selectivity whereas the closed state is cation-selective (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid outer membrane. Note=Found in non-
CC       photosynthetic root plastids only.
CC   -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets.
CC   -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin (TC 1.B.8.1)
CC       family. {ECO:0000305}.
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DR   EMBL; Z25540; CAA80988.1; -; mRNA.
DR   PIR; S36454; S36454.
DR   AlphaFoldDB; P42054; -.
DR   SMR; P42054; -.
DR   TCDB; 1.B.8.1.5; the mitochondrial and plastid porin (mpp) family.
DR   PRIDE; P42054; -.
DR   EnsemblPlants; Psat3g195320.1; Psat3g195320.1.cds; Psat3g195320.
DR   Gramene; Psat3g195320.1; Psat3g195320.1.cds; Psat3g195320.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:AgBase.
DR   GO; GO:0009527; C:plastid outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; IEA:InterPro.
DR   CDD; cd07306; Porin3_VDAC; 1.
DR   Gene3D; 2.40.160.10; -; 1.
DR   InterPro; IPR023614; Porin_dom_sf.
DR   InterPro; IPR001925; Porin_Euk.
DR   InterPro; IPR027246; Porin_Euk/Tom40.
DR   PANTHER; PTHR11743; PTHR11743; 1.
DR   Pfam; PF01459; Porin_3; 1.
DR   PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Ion transport; Membrane; Plastid;
KW   Plastid outer membrane; Porin; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7523392"
FT   CHAIN           2..276
FT                   /note="Outer plastidial membrane protein porin"
FT                   /id="PRO_0000050530"
SQ   SEQUENCE   276 AA;  29597 MW;  C817BF4359B9AFBA CRC64;
     MVKGPGLYTD IGKKARDLLY KDYHSDKKFT ISTYSPTGVA ITSSGTKKGE LFLGDVNTQL
     KNKNITTDIK VDTNSNLFTT ITVNEPAPGV KAILSFKVPE QTSGKVELQY LHEYAGISSS
     VGLKANPIVN FSSVIGTNAL AFGADISFDT KLGELTKSNA AVNFVKDDLI GSLTLNEKGD
     LLSASYYHAI NPLSNTAVGV DISHRFSTKE NTFTLGTQHA LDPLTTVKGR VTNSGKASAL
     IQHEWRPKSL ITISSEVDTK AIEKSAKIGL SLALKP