PEX2_CRIGR
ID PEX2_CRIGR Reviewed; 304 AA.
AC Q06438;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Peroxisome biogenesis factor 2;
DE AltName: Full=Peroxin-2;
DE AltName: Full=Peroxisomal membrane protein 3;
DE AltName: Full=Peroxisome assembly factor 1;
DE Short=PAF-1;
GN Name=PEX2; Synonyms=PAF1, PMP35, PXMP3;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7685346; DOI=10.1016/s0021-9258(18)31435-2;
RA Thieringer R., Raetz C.R.H.;
RT "Peroxisome-deficient Chinese hamster ovary cells with point mutations in
RT peroxisome assembly factor-1.";
RL J. Biol. Chem. 268:12631-12636(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8035823; DOI=10.1128/mcb.14.8.5458-5465.1994;
RA Tsukamoto T., Shimozawa N., Fujiki Y.;
RT "Peroxisome assembly factor 1: nonsense mutation in a peroxisome-deficient
RT Chinese hamster ovary cell mutant and deletion analysis.";
RL Mol. Cell. Biol. 14:5458-5465(1994).
CC -!- FUNCTION: Somewhat implicated in the biogenesis of peroxisomes.
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; Z17220; CAA78929.1; -; mRNA.
DR EMBL; D30618; BAA06308.1; -; mRNA.
DR PIR; A45989; A45989.
DR RefSeq; NP_001230964.1; NM_001244035.1.
DR RefSeq; XP_007644647.1; XM_007646457.2.
DR AlphaFoldDB; Q06438; -.
DR STRING; 10029.NP_001230964.1; -.
DR PRIDE; Q06438; -.
DR Ensembl; ENSCGRT00001018576; ENSCGRP00001014339; ENSCGRG00001015243.
DR GeneID; 100689047; -.
DR KEGG; cge:100689047; -.
DR CTD; 5828; -.
DR eggNOG; KOG2879; Eukaryota.
DR GeneTree; ENSGT00390000001846; -.
DR OMA; SCFHGFK; -.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IEA:Ensembl.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:Ensembl.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006845; Pex_N.
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 Pfam; PF04757; Pex2_Pex12; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Peroxisome; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT CHAIN 1..304
FT /note="Peroxisome biogenesis factor 2"
FT /id="PRO_0000056368"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000250"
FT ZN_FING 243..283
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 246
FT /note="C->Y: Loss of function."
SQ SEQUENCE 304 AA; 34795 MW; 84EC5FA613C148BF CRC64;
MAGREKTKSA NRVLRISQLD ALELNKALEQ LVWSQFTQCF HGFKPGLLAR FEPEVKACLW
LFLWRFTIYS KNATVGQSVL NIQYKNDFSS NSRYQPPSKN QKLWYAVCTI GGRWLEERCY
DLFRNRHLAS FGKVKQCMNV MVGLLKLGEL INFLIFLQKG KFATLTERLL GIHSVFCKPQ
NIREVGFDYM NRELLWHGFA EFLIFLLPLI NIQKFKAKLS SWCIPLTGAA SSDSALASSG
KECALCGEWP TMPHTIGCEH VFCYYCVKSS FLFDMYFTCP KCGIEVHSVQ PLKSGIEMSE
VNAL