ID PEX2_DICDI Reviewed; 423 AA.
AC Q75JQ3; Q559N0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Peroxisome biogenesis factor 2 {ECO:0000305};
DE EC=2.3.2.36 {ECO:0000250|UniProtKB:P32800};
DE AltName: Full=Peroxin-2 {ECO:0000305};
GN Name=pex2; ORFNames=DDB_G0272234;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation
CC channel required for peroxisome organization by mediating export of the
CC PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5
CC recycling. The retrotranslocation channel is composed of PEX2, PEX10
CC and PEX12; each subunit contributing transmembrane segments that
CC coassemble into an open channel that specifically allows the passage of
CC PEX5 through the peroxisomal membrane. PEX2 also regulates peroxisome
CC organization by acting as a E3 ubiquitin-protein ligase. PEX2
CC ubiquitinates PEX5 during its passage through the retrotranslocation
CC channel: catalyzes monoubiquitination of PEX5 at 'Cys-11', a
CC modification that acts as a signal for PEX5 extraction into the
CC cytosol. {ECO:0000250|UniProtKB:P32800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine.; EC=2.3.2.36;
CC Evidence={ECO:0000250|UniProtKB:P32800};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P32800}.
CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel.
CC {ECO:0000250|UniProtKB:P32800}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P32800}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The three subunits of the retrotranslocation channel (PEX2,
CC PEX10 and PEX12) coassemble in the membrane into a channel with an open
CC 10 Angstrom pore. The RING-type zinc-fingers that catalyze PEX5
CC receptor ubiquitination are positioned above the pore on the cytosolic
CC side of the complex. {ECO:0000250|UniProtKB:G2Q1C9}.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
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DR EMBL; AAFI02000008; EAL71269.1; -; Genomic_DNA.
DR RefSeq; XP_645304.1; XM_640212.1.
DR AlphaFoldDB; Q75JQ3; -.
DR SMR; Q75JQ3; -.
DR STRING; 44689.Q75JQ3; -.
DR PaxDb; 44689-DDB0238045; -.
DR EnsemblProtists; EAL71269; EAL71269; DDB_G0272234.
DR GeneID; 8618470; -.
DR KEGG; ddi:DDB_G0272234; -.
DR dictyBase; DDB_G0272234; pex2.
DR eggNOG; KOG2879; Eukaryota.
DR HOGENOM; CLU_024591_3_1_1; -.
DR InParanoid; Q75JQ3; -.
DR OMA; YLICTVG; -.
DR PhylomeDB; Q75JQ3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q75JQ3; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007031; P:peroxisome organization; ISS:dictyBase.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16526; RING-HC_PEX2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR025654; PEX2/10.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR045859; RING-HC_PEX2.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR48178; PEROXISOME BIOGENESIS FACTOR 2; 1.
DR PANTHER; PTHR48178:SF1; PEROXISOME BIOGENESIS FACTOR 2; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane; Metal-binding; Peroxisome; Peroxisome biogenesis;
KW Protein transport; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..423
FT /note="Peroxisome biogenesis factor 2"
FT /id="PRO_0000371403"
FT TOPO_DOM 1..109
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TRANSMEM 110..136
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TOPO_DOM 137..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TRANSMEM 143..168
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TOPO_DOM 169..197
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TRANSMEM 198..224
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TOPO_DOM 225..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TRANSMEM 235..265
FT /note="Helical; Name=TM4"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TOPO_DOM 266..292
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TRANSMEM 293..316
FT /note="Helical; Name=TM5"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT TOPO_DOM 317..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT ZN_FING 369..410
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q1C9"
SQ SEQUENCE 423 AA; 48982 MW; 9DDCF47269BA4315 CRC64;
MVDNYNNNNI LPTNTSTTTT TNTTITPTPP LPPPPPISNI LDNNNNNNLI KNDIKNDKVA
VSNSNVRPSS SSVSYENSDW NKVYNSEREK LHEVNKQILN IKRPSTSIVR VSQLDSARLD
EEILDLLRSQ FMKIFTFFKP NFIHNFQPEI NLVLKSVIYK LSIFNLGTTY GNQLQNLTYR
NEKAFDPIRG SDQLNKLTMR QKWLSGLINI GGEWLWTRIN RYLINNNWSE HPPNDIRKKF
WNFLNFAESA YKALALLNFL TFLFNGKYVT LVNRILHMRL VYAHPTLSRN ISFEYMNRLL
VWHGFTEFIL FIMPLINIDR IKSFLYRLLV KTSFGNSSGN NNNTASNPLQ QLQKQQLLIQ
QQQMALAKCP ICMNDPISMP YSADCGHLFC YYCIKTSCMI DSSFTCPRCN SLISNIKRFS
IQD
//
