PEX3_YEAST
ID PEX3_YEAST Reviewed; 441 AA.
AC P28795; D6VSW1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Peroxisomal biogenesis factor 3;
DE AltName: Full=Peroxin-3 {ECO:0000303|PubMed:1894692};
GN Name=PEX3; Synonyms=PAS3 {ECO:0000303|PubMed:1894692};
GN OrderedLocusNames=YDR329C; ORFNames=D9798.15;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=1894692; DOI=10.1083/jcb.114.6.1167;
RA Hoehfeld J., Veenhuis M., Kunau W.-H.;
RT "PAS3, a Saccharomyces cerevisiae gene encoding a peroxisomal integral
RT membrane protein essential for peroxisome biogenesis.";
RL J. Cell Biol. 114:1167-1178(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH MSP1.
RX PubMed=32541053; DOI=10.1073/pnas.1920109117;
RA Castanzo D.T., LaFrance B., Martin A.;
RT "The AAA+ ATPase Msp1 is a processive protein translocase with robust
RT unfoldase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:14970-14977(2020).
CC -!- FUNCTION: Involved in peroxisome biosynthesis (PubMed:1894692). Acts as
CC a regulator of MSP1 by inhibiting the ability of MSP1 to unfold target
CC proteins (PubMed:32541053). {ECO:0000269|PubMed:1894692,
CC ECO:0000269|PubMed:32541053}.
CC -!- SUBUNIT: Interacts with MSP1; leading to inhibit the translocase
CC activity of MSP1. {ECO:0000269|PubMed:32541053}.
CC -!- INTERACTION:
CC P28795; Q03694: INP1; NbExp=6; IntAct=EBI-13164, EBI-27445;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:1894692};
CC Single-pass membrane protein.
CC -!- INDUCTION: By oleic acid. {ECO:0000269|PubMed:1894692}.
CC -!- DISRUPTION PHENOTYPE: Lack of this protein causes the peroxisomal-
CC deficient phenotype and mislocalization in the cytosol of peroxisomal
CC matrix proteins. {ECO:0000269|PubMed:1894692}.
CC -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxin-3 family. {ECO:0000305}.
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DR EMBL; X58407; CAA41309.1; -; Genomic_DNA.
DR EMBL; U32517; AAB64764.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12171.1; -; Genomic_DNA.
DR PIR; A40550; A40550.
DR RefSeq; NP_010616.3; NM_001180637.3.
DR AlphaFoldDB; P28795; -.
DR SMR; P28795; -.
DR BioGRID; 32386; 123.
DR DIP; DIP-2477N; -.
DR IntAct; P28795; 8.
DR MINT; P28795; -.
DR STRING; 4932.YDR329C; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR TCDB; 9.A.17.1.1; the integral membrane peroxisomal protein importer-2 (ppi2) family.
DR iPTMnet; P28795; -.
DR MaxQB; P28795; -.
DR PaxDb; P28795; -.
DR PRIDE; P28795; -.
DR EnsemblFungi; YDR329C_mRNA; YDR329C; YDR329C.
DR GeneID; 851929; -.
DR KEGG; sce:YDR329C; -.
DR SGD; S000002737; PEX3.
DR VEuPathDB; FungiDB:YDR329C; -.
DR eggNOG; KOG4444; Eukaryota.
DR HOGENOM; CLU_017002_0_0_1; -.
DR InParanoid; P28795; -.
DR OMA; KQRFIQT; -.
DR BioCyc; YEAST:G3O-29885-MON; -.
DR Reactome; R-SCE-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:P28795; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P28795; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0032581; P:ER-dependent peroxisome organization; IDA:SGD.
DR GO; GO:0045033; P:peroxisome inheritance; IMP:SGD.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IMP:SGD.
DR InterPro; IPR006966; Peroxin-3.
DR PANTHER; PTHR28080; PTHR28080; 1.
DR Pfam; PF04882; Peroxin-3; 2.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..441
FT /note="Peroxisomal biogenesis factor 3"
FT /id="PRO_0000208747"
FT TOPO_DOM 1..17
FT /note="Peroxisomal"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 441 AA; 50676 MW; 3CDC1D036DF0D0F9 CRC64;
MAPNQRSRSL LQRHRGKVLI SLTGIAALFT TGSVVVFFVK RWLYKQQLRI TEQHFIKEQI
KRRFEQTQED SLYTIYELLP VWRMVLNEND LNLDSIVTQL KDQKNQLTRA KSSESRESSP
LKSKAELWNE LELKSLIKLV TVTYTVSSLI LLTRLQLNIL TRNEYLDSAI KLTMQQENCN
KLQNRFYNWV TSWWSDPEDK ADDAMVMAAK KSKKEGQEVY INEQAFLSLS WWILNKGWLS
YNEIITNQIE IEFDGIHPRD TLTLEEFSSR LTNIFRNTNS QIFQQNNNNL TSILLPKDSS
GQEFLLSQTL DADALTSFHS NTLVFNQLVN ELTQCIESTA TSIVLESLIN ESFHFIMNKV
GIKTIAKKKP GQEDQQQYQM AVFAMSMKDC CQEMLQTTAG SSHSGSVNEY LATLDSVQPL
DDLSASVYSN FGVSSSFSFK P
