ID   PEX3_RAT                Reviewed;         372 AA.
AC   Q9JJK4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Peroxisomal biogenesis factor 3;
DE   AltName: Full=Peroxin-3;
DE   AltName: Full=Peroxisomal assembly protein PEX3;
GN   Name=Pex3;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH PEX19.
RC   TISSUE=Liver;
RX   PubMed=10848631; DOI=10.1091/mbc.11.6.2085;
RA   Ghaedi K., Tamura S., Okumoto K., Matsuzono Y., Fujiki Y.;
RT   "The peroxin pex3p initiates membrane assembly in peroxisome biogenesis.";
RL   Mol. Biol. Cell 11:2085-2102(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-12.
RC   TISSUE=Liver;
RX   PubMed=10527525; DOI=10.1006/abio.1999.4281;
RA   Gouveia A.M.M., Reguenga C., Oliveira M.E.M., Eckerskorn C., Sa-Miranda C.,
RA   Azevedo J.E.;
RT   "Alkaline density gradient floatation of membranes: polypeptide composition
RT   of the mammalian peroxisomal membrane.";
RL   Anal. Biochem. 274:270-277(1999).
CC   -!- FUNCTION: Involved in peroxisome biosynthesis and integrity. Assembles
CC       membrane vesicles before the matrix proteins are translocated. As a
CC       docking factor for PEX19, is necessary for the import of peroxisomal
CC       membrane proteins in the peroxisomes. {ECO:0000269|PubMed:10848631}.
CC   -!- SUBUNIT: Interacts with PEX19. {ECO:0000269|PubMed:10848631}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000269|PubMed:10848631}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the peroxin-3 family. {ECO:0000305}.
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DR   EMBL; AB035306; BAA97992.1; -; mRNA.
DR   EMBL; BC062046; AAH62046.1; -; mRNA.
DR   RefSeq; NP_112640.1; NM_031350.1.
DR   AlphaFoldDB; Q9JJK4; -.
DR   SMR; Q9JJK4; -.
DR   BioGRID; 249738; 1.
DR   STRING; 10116.ENSRNOP00000021524; -.
DR   jPOST; Q9JJK4; -.
DR   PaxDb; Q9JJK4; -.
DR   PRIDE; Q9JJK4; -.
DR   GeneID; 83519; -.
DR   KEGG; rno:83519; -.
DR   UCSC; RGD:621636; rat.
DR   CTD; 8504; -.
DR   RGD; 621636; Pex3.
DR   VEuPathDB; HostDB:ENSRNOG00000015660; -.
DR   eggNOG; KOG4444; Eukaryota.
DR   HOGENOM; CLU_041367_2_0_1; -.
DR   InParanoid; Q9JJK4; -.
DR   OMA; WSLQMAI; -.
DR   OrthoDB; 891261at2759; -.
DR   PhylomeDB; Q9JJK4; -.
DR   TreeFam; TF352826; -.
DR   Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR   Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR   PRO; PR:Q9JJK4; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015660; Expressed in testis and 20 other tissues.
DR   Genevisible; Q9JJK4; RN.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; ISO:RGD.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0032994; C:protein-lipid complex; ISO:RGD.
DR   GO; GO:0008289; F:lipid binding; ISO:RGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0016557; P:peroxisome membrane biogenesis; IDA:RGD.
DR   GO; GO:0007031; P:peroxisome organization; IMP:RGD.
DR   GO; GO:0045046; P:protein import into peroxisome membrane; ISO:RGD.
DR   InterPro; IPR006966; Peroxin-3.
DR   PANTHER; PTHR28080; PTHR28080; 1.
DR   Pfam; PF04882; Peroxin-3; 3.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Peroxisome; Peroxisome biogenesis;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..372
FT                   /note="Peroxisomal biogenesis factor 3"
FT                   /id="PRO_0000208740"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..116
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Targeting to peroxisomes"
FT                   /evidence="ECO:0000250|UniProtKB:P56589"
FT   REGION          120..136
FT                   /note="Interaction with PEX19"
FT                   /evidence="ECO:0000250|UniProtKB:P56589"
SQ   SEQUENCE   372 AA;  42210 MW;  922528FD2A107AB2 CRC64;
     MLRSMWNFLK RHKKKCIFLG TVLGGVYILG KYGQKKLREI QEREAAEYIA QARRQYHFES
     NQRTCNMTVL SMLPTLREAL MQQLNSESLT ALLKNRPSNK LEIWEDLKII SFTRSIVAVY
     STCMLVVLLR VQLNIIGGYI YLDNATVGKN GTSILAPPDV QQQYLSSIQH LLGDGLTELV
     TVIKQAVQRI LGSISLKHSL SLLDLEQKLK EIRTLVEQHR SCWNDKDASK SSLCHYMMPD
     EETPLAAQAY GLSPRDITTI KLLNETRDML ESPDFSTVLN TCLNRGFSRL LDNMAEFFRP
     TEQDLQHGNS INSLSSVSLP LAKIIPIVNG QIHSVCSETP SHFVQDLLMM EQVKDFAANV
     YEAFSTPQQL EK