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PEX11_YEAST
ID   PEX11_YEAST             Reviewed;         236 AA.
AC   Q12462; D6W1S2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Peroxisomal membrane protein PMP27;
DE   AltName: Full=Peroxin-11;
GN   Name=PEX11; Synonyms=PMP24, PMP27; OrderedLocusNames=YOL147C;
GN   ORFNames=O0454;
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], AND PROTEIN SEQUENCE OF 2-28.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7860627; DOI=10.1083/jcb.128.4.509;
RA   Erdmann R., Blobel G.;
RT   "Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking
RT   the peroxisomal membrane protein Pmp27p.";
RL   J. Cell Biol. 128:509-523(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-30 AND
RP   192-207.
RC   STRAIN=S288c / GRF88;
RX   PubMed=7721939; DOI=10.1083/jcb.129.2.345;
RA   Marshall P.A., Krimkevich Y.I., Lark R.H., Dyer J.M., Veenhuis M.,
RA   Goodman J.M.;
RT   "Pmp27 promotes peroxisomal proliferation.";
RL   J. Cell Biol. 129:345-355(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8553699; DOI=10.1002/yea.320111308;
RA   Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J.,
RA   Gancedo C., Arino J.;
RT   "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
RT   chromosome XV containing seven new open reading frames.";
RL   Yeast 11:1281-1288(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH PEX34.
RX   PubMed=21441307; DOI=10.1091/mbc.e11-01-0084;
RA   Tower R.J., Fagarasanu A., Aitchison J.D., Rachubinski R.A.;
RT   "The peroxin Pex34p functions with the Pex11 family of peroxisomal
RT   divisional proteins to regulate the peroxisome population in yeast.";
RL   Mol. Biol. Cell 22:1727-1738(2011).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [8]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=14517321; DOI=10.1091/mbc.e03-03-0150;
RA   Tam Y.Y.C., Torres-Guzman J.C., Vizeacoumar F.J., Smith J.J., Marelli M.,
RA   Aitchison J.D., Rachubinski R.A.;
RT   "Pex11-related proteins in peroxisome dynamics: a role for the novel
RT   peroxin Pex27p in controlling peroxisome size and number in Saccharomyces
RT   cerevisiae.";
RL   Mol. Biol. Cell 14:4089-4102(2003).
RN   [9]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 201389 / BY4742;
RX   PubMed=14517338; DOI=10.1091/mbc.e03-03-0153;
RA   Rottensteiner H., Stein K., Sonnenhol E., Erdmann R.;
RT   "Conserved function of pex11p and the novel pex25p and pex27p in peroxisome
RT   biogenesis.";
RL   Mol. Biol. Cell 14:4316-4328(2003).
RN   [10]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [11]
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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Involved in peroxisomal proliferation. Promotes peroxisome
CC       division and biogenesis. {ECO:0000269|PubMed:14517321,
CC       ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:21441307}.
CC   -!- SUBUNIT: Homooligomer. Interacts with PEX34.
CC       {ECO:0000269|PubMed:14517321, ECO:0000269|PubMed:14517338,
CC       ECO:0000269|PubMed:21441307}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:14517338,
CC       ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR   EMBL; Z48239; CAA88280.1; -; Genomic_DNA.
DR   EMBL; Z74889; CAA99168.1; -; Genomic_DNA.
DR   EMBL; X81465; CAA57223.1; -; Genomic_DNA.
DR   EMBL; Z46846; CAA86903.1; -; Genomic_DNA.
DR   EMBL; AY558010; AAS56336.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10638.1; -; Genomic_DNA.
DR   PIR; A56509; A56509.
DR   RefSeq; NP_014494.1; NM_001183401.1.
DR   AlphaFoldDB; Q12462; -.
DR   BioGRID; 34270; 82.
DR   DIP; DIP-3839N; -.
DR   IntAct; Q12462; 31.
DR   MINT; Q12462; -.
DR   STRING; 4932.YOL147C; -.
DR   TCDB; 1.A.101.1.1; the peroxisomal pore-forming pex11 (pex11) family.
DR   TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR   iPTMnet; Q12462; -.
DR   MaxQB; Q12462; -.
DR   PaxDb; Q12462; -.
DR   PRIDE; Q12462; -.
DR   EnsemblFungi; YOL147C_mRNA; YOL147C; YOL147C.
DR   GeneID; 854018; -.
DR   KEGG; sce:YOL147C; -.
DR   SGD; S000005507; PEX11.
DR   VEuPathDB; FungiDB:YOL147C; -.
DR   eggNOG; KOG4186; Eukaryota.
DR   GeneTree; ENSGT00390000014273; -.
DR   HOGENOM; CLU_049216_0_1_1; -.
DR   InParanoid; Q12462; -.
DR   OMA; RFWAMGL; -.
DR   BioCyc; YEAST:G3O-33537-MON; -.
DR   Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import.
DR   PRO; PR:Q12462; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12462; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IDA:SGD.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0019395; P:fatty acid oxidation; IMP:SGD.
DR   GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
DR   GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR   GO; GO:0044375; P:regulation of peroxisome size; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   InterPro; IPR008733; PEX11.
DR   Pfam; PF05648; PEX11; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Peroxisome; Peroxisome biogenesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7721939,
FT                   ECO:0000269|PubMed:7860627"
FT   CHAIN           2..236
FT                   /note="Peroxisomal membrane protein PMP27"
FT                   /id="PRO_0000105974"
SQ   SEQUENCE   236 AA;  26875 MW;  26B95896D57018DD CRC64;
     MVCDTLVYHP SVTRFVKFLD GSAGREKVLR LLQYLARFLA VQNSSLLARQ LQAQFTTVRK
     FLRFLKPLNH LQAAAKFYDN KLASDNVVRV CNVLKNIFFA AYLSLDQVNL LRILKVIPVT
     VLTGKKIPRW SNWCWLFGLL SGLAMDLRKI QTSHAQIAAF VKAKSQSQGD EHEDHKKVLG
     KAYQDRYTAL RRLFWDAADS FIVLNNLGYL SSNEEYVALS GVVTSILGMQ DMWKAT
 
 
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