ID   PEX12_CRILO             Reviewed;         359 AA.
AC   Q9ET67;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Peroxisome assembly protein 12;
DE   AltName: Full=Peroxin-12;
GN   Name=PEX12;
OS   Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10837480; DOI=10.1074/jbc.m003303200;
RA   Okumoto K., Abe I., Fujiki Y.;
RT   "Molecular anatomy of the peroxin Pex12p. Ring finger domain is essential
RT   for Pex12p function and interacts with the peroxisome-targeting signal type
RT   1-receptor Pex5p and a ring peroxin, Pex10p.";
RL   J. Biol. Chem. 275:25700-25710(2000).
CC   -!- FUNCTION: Required for protein import into peroxisomes.
CC   -!- SUBUNIT: Interacts with PEX19 via its cytoplasmic domain (By
CC       similarity). Interacts with PEX5 and PEX10. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
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DR   EMBL; AB041733; BAB11978.1; -; mRNA.
DR   AlphaFoldDB; Q9ET67; -.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; ISS:UniProtKB.
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; Transmembrane; Transmembrane helix;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..359
FT                   /note="Peroxisome assembly protein 12"
FT                   /id="PRO_0000218609"
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..341
FT                   /note="RING-type; degenerate"
SQ   SEQUENCE   359 AA;  40736 MW;  A852FA2801811E37 CRC64;
     MAEHGAHITT ASVVDDQPSI FEVVAQDSLM TAVRPALQHV VKVLAESNPA HYGFFWRWFD
     EIFTLLDFLL QQHYLSRTSA SFSEHFYGLK RIVAGSSQQP QRPASAGLPK EHLWKSTMFL
     VLLPYLKVKL EKLASSLREE DEYSIHPPSS HWKRFYRAFL AAYPFVNMAW EGWFLTQQLR
     YILGKAEHHS PLLKLAGVRL GRLTAQDIQA IEHRLSEASV MQDPVRSVGE KIKLALKKAV
     GGIALSLSTG LSVGVFFLQF LDWWYSSENQ ETIKSLTALP TPPPPVHLDY NSDSPLLPKM
     KTVCPLCRKT RVNDTVLATS GYVFCYRCVF NYVRSHQACP ITGYPTEVQH LIKLYSPEN