PEX12_RAT
ID PEX12_RAT Reviewed; 359 AA.
AC O88177;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Peroxisome assembly protein 12;
DE AltName: Full=Peroxin-12;
DE AltName: Full=Peroxisome assembly factor 3;
DE Short=PAF-3;
GN Name=Pex12; Synonyms=Paf3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9632816; DOI=10.1128/mcb.18.7.4324;
RA Okumoto K., Shimozawa N., Kawai A., Tamura S., Tsukamoto T., Osumi T.,
RA Moser H., Wanders R.J.A., Suzuki Y., Kondo N., Fujiki Y.;
RT "PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning
RT by functional complementation on a CHO cell mutant, patient analysis, and
RT characterization of PEX12p.";
RL Mol. Cell. Biol. 18:4324-4336(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Required for protein import into peroxisomes.
CC -!- SUBUNIT: Interacts with PEX5 and PEX10. Interacts with PEX19 via its
CC cytoplasmic domain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {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; AB002111; BAA31558.1; -; mRNA.
DR EMBL; BC072481; AAH72481.1; -; mRNA.
DR RefSeq; NP_446373.1; NM_053921.1.
DR RefSeq; XP_003750938.1; XM_003750890.4.
DR RefSeq; XP_008766156.1; XM_008767934.2.
DR RefSeq; XP_008772090.1; XM_008773868.2.
DR RefSeq; XP_017452452.1; XM_017596963.1.
DR RefSeq; XP_017458013.1; XM_017602524.1.
DR AlphaFoldDB; O88177; -.
DR STRING; 10116.ENSRNOP00000013233; -.
DR PaxDb; O88177; -.
DR Ensembl; ENSRNOT00000013233; ENSRNOP00000013233; ENSRNOG00000009718.
DR GeneID; 116718; -.
DR KEGG; rno:116718; -.
DR CTD; 5193; -.
DR RGD; 620757; Pex12.
DR eggNOG; KOG0826; Eukaryota.
DR GeneTree; ENSGT00390000016209; -.
DR HOGENOM; CLU_031067_1_0_1; -.
DR InParanoid; O88177; -.
DR OMA; NPAIIET; -.
DR OrthoDB; 1204472at2759; -.
DR PhylomeDB; O88177; -.
DR TreeFam; TF314511; -.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:O88177; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000009718; Expressed in testis and 19 other tissues.
DR Genevisible; O88177; RN.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISO:RGD.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR GO; GO:0005777; C:peroxisome; IDA:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0007031; P:peroxisome organization; IMP:RGD.
DR GO; GO:0016558; P:protein import into peroxisome matrix; ISO:RGD.
DR GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017375; PEX12.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12888; PTHR12888; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR PIRSF; PIRSF038074; Peroxisome_assembly_p12; 1.
PE 2: Evidence at transcript level;
KW Membrane; Metal-binding; Peroxisome; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc-finger.
FT CHAIN 1..359
FT /note="Peroxisome assembly protein 12"
FT /id="PRO_0000218612"
FT TOPO_DOM 1..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..239
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 304..343
FT /note="RING-type; degenerate"
SQ SEQUENCE 359 AA; 40681 MW; E63C39801406733D CRC64;
MAEHGAHITT ASVADDQPSI FEVVAQDSLM TAVRPALQHV VKVLAESNPA HYGFFWRWFD
EIFTLLDFLL QQHYLSRTSA SFSEHFYGLK RIVAGSSPQL QRPASAGLPK EHLWKSAMFL
VLLPYLKVKL EKLASTLREE DEYSIHPPSS HWKRFYRVFL AAYPFVTMTW EGWFLTQQLR
YILGKAEHHS PLLKLAGVRL GRLTAQDIQA MEHRLVEASA MQEPVRSIGK KIKSALKKAV
GGVALSLSTG LSVGVFFLQF LDWWYSSENQ ETIKSLTALP TPPPPVHLDY NSDSPLLPKM
KTVCPLCRKA RVNDTVLATS GYVFCYRCVF NYVRSHQACP ITGYPTEVQH LIKLYSPEN