ID   VDAC_DICDI              Reviewed;         275 AA.
AC   Q01501; Q55AH3; Q8T810;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Mitochondrial outer membrane protein porin;
DE   AltName: Full=Voltage-dependent anion-selective channel protein;
DE            Short=VDAC;
GN   Name=porA; Synonyms=porN; ORFNames=DDB_G0271848;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-12 AND 178-188.
RC   STRAIN=AX2;
RX   PubMed=1328220; DOI=10.1016/s0021-9258(19)36799-7;
RA   Troll H., Malchow D., Mueller-Taubenberger A., Humbel B., Lottspeich F.,
RA   Ecke M., Gerisch G., Schmid A., Benz R.;
RT   "Purification, functional characterization, and cDNA sequencing of
RT   mitochondrial porin from Dictyostelium discoideum.";
RL   J. Biol. Chem. 267:21072-21079(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Forms a channel of about 1,7 nM through the cell membrane
CC       that allows diffusion of small hydrophilic molecules. The channel
CC       adopts an open conformation at low or zero membrane potential and a
CC       closed conformation at potentials above 20 mv. The open state has a
CC       weak anion selectivity whereas the closed state is cation-selective.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane.
CC   -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets.
CC   -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
CC       Highly divergent. {ECO:0000305}.
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DR   EMBL; M96668; AAA33237.1; -; mRNA.
DR   EMBL; AAFI02000007; EAL71503.1; -; Genomic_DNA.
DR   PIR; A45076; S27805.
DR   RefSeq; XP_645436.1; XM_640344.1.
DR   AlphaFoldDB; Q01501; -.
DR   SMR; Q01501; -.
DR   TCDB; 1.B.8.1.13; the mitochondrial and plastid porin (mpp) family.
DR   PaxDb; Q01501; -.
DR   ABCD; Q01501; 1 sequenced antibody.
DR   EnsemblProtists; EAL71503; EAL71503; DDB_G0271848.
DR   GeneID; 8618176; -.
DR   KEGG; ddi:DDB_G0271848; -.
DR   dictyBase; DDB_G0271848; porA.
DR   HOGENOM; CLU_1013465_0_0_1; -.
DR   InParanoid; Q01501; -.
DR   OMA; YKIDSAS; -.
DR   PhylomeDB; Q01501; -.
DR   Reactome; R-DDI-70268; Pyruvate metabolism.
DR   PRO; PR:Q01501; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IDA:dictyBase.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; IBA:GO_Central.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IDA:dictyBase.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IDA:dictyBase.
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; Mitochondrion;
KW   Mitochondrion outer membrane; Porin; Reference proteome; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   CHAIN           1..275
FT                   /note="Mitochondrial outer membrane protein porin"
FT                   /id="PRO_0000050519"
FT   MOD_RES         1
FT                   /note="Blocked amino end (Met)"
SQ   SEQUENCE   275 AA;  30158 MW;  7D2F442551A23153 CRC64;
     MNPGLYADLT KPTADFIKKD FAETFKLDTT FKGKYGSIVA VTDIKDSGVV ASIQPKADFT
     KYLGKVSNGN FTVDTNGVKK GEFTIENIIP GLKAVANGDS KQNFSTEFQY KKDKIAFTLF
     GHNNKSFNTS LAFLINPTFS VGVQAEGNAK NTLKNVNATI TIRPRPDVFV SIVDRFMDKQ
     ILLSTLYTAT SKLSFAGDVT VDLKASEKAP SFNVGTQYKI DSASLLKAKV NNNRKVNISY
     IYNTSNNTKF VLGWNVNTKN FKQGNTFGAT VNLTL