ID G8BRQ0_TETPH Unreviewed; 395 AA.
AC G8BRQ0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Peroxisome assembly protein 12 {ECO:0000256|ARBA:ARBA00018980};
DE AltName: Full=Peroxin-12 {ECO:0000256|ARBA:ARBA00029692};
GN Name=TPHA0C02730 {ECO:0000313|EMBL:CCE62426.1};
GN OrderedLocusNames=TPHA_0C02730 {ECO:0000313|EMBL:CCE62426.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62426.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE62426.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel,
CC composed of PEX2, PEX10 and PEX12. {ECO:0000256|ARBA:ARBA00034505}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Peroxisome
CC membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004585}.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family.
CC {ECO:0000256|ARBA:ARBA00008704}.
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DR EMBL; HE612858; CCE62426.1; -; Genomic_DNA.
DR RefSeq; XP_003684860.1; XM_003684812.1.
DR AlphaFoldDB; G8BRQ0; -.
DR STRING; 1071381.G8BRQ0; -.
DR GeneID; 11533503; -.
DR KEGG; tpf:TPHA_0C02730; -.
DR eggNOG; KOG0826; Eukaryota.
DR HOGENOM; CLU_031067_0_0_1; -.
DR OMA; RCPITGY; -.
DR OrthoDB; 65730at2759; -.
DR Proteomes; UP000005666; Chromosome 3.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR017375; PEX12.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12888:SF0; PEROXISOME ASSEMBLY PROTEIN 12; 1.
DR PANTHER; PTHR12888; PEROXISOME ASSEMBLY PROTEIN 12 PEROXIN-12; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 30..292
FT /note="Pex N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04757"
SQ SEQUENCE 395 AA; 46810 MW; AD0449E8D7C46EC6 CRC64;
MSFYSNLPSI QNNDSSNSVY PTIYEPISSS EIDELVPYSV RYILTNYWIT RYPNWYTLQV
NNYFDEWFNL GLKGLIEWHH IDKYNSTFID KFYGLQRFNA ENKVLLKSHV KDNSIDKKWP
LGLQLTKLQK RALFIEQIVF PYFRTKLDHY HDTLTHLVIQ NEEGTEMVPG LSKYMKVLFR
KFYPIIKRCF QIFNLLIKLK FLAGKTGSLS LIDYLFNIAY SRALFPLESK NRSLTQNIGR
HNRERLQRQN YYKFRSNFNE NFTDTLSVLS YLGTKVFPTF LFTLRIYQWW TAENISSKIE
RKLNNIDRAI PRPPLTESNL QQNRKSADKC PVCKDKIQNP CVIETGYVMC YPCALDYITQ
HEGRCPVTNK KLLGCKYNSL TKNWNIVNGI RRLII
//
