PER1_YEAST
ID PER1_YEAST Reviewed; 357 AA.
AC P25625; D6VR53;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein PER1;
DE AltName: Full=Protein processing in the ER protein 1;
DE Flags: Precursor;
GN Name=PER1; Synonyms=COS16; OrderedLocusNames=YCR044C; ORFNames=YCR44C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
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 [3]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=17021251; DOI=10.1091/mbc.e06-08-0715;
RA Fujita M., Umemura M., Yoko-o T., Jigami Y.;
RT "PER1 is required for GPI-phospholipase A2 activity and involved in lipid
RT remodeling of GPI-anchored proteins.";
RL Mol. Biol. Cell 17:5253-5264(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC maturation. Lipid remodeling steps consist in the generation of 2
CC saturated fatty chains at the sn-2 position of GPI-anchors proteins.
CC Required for phospholipase A2 activity that removes an acyl-chain at
CC the sn-2 position of GPI-anchors during the remodeling of GPI. Required
CC for efficient transport of GPI-anchor proteins.
CC {ECO:0000269|PubMed:17021251}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17021251}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:17021251}.
CC -!- MISCELLANEOUS: Present with 3050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PGAP3/PER1 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42292.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07522.1; -; Genomic_DNA.
DR PIR; S19457; S19457.
DR RefSeq; NP_009973.1; NM_001178758.1.
DR AlphaFoldDB; P25625; -.
DR BioGRID; 31026; 357.
DR DIP; DIP-5598N; -.
DR IntAct; P25625; 1.
DR MINT; P25625; -.
DR STRING; 4932.YCR044C; -.
DR PaxDb; P25625; -.
DR PRIDE; P25625; -.
DR EnsemblFungi; YCR044C_mRNA; YCR044C; YCR044C.
DR GeneID; 850411; -.
DR KEGG; sce:YCR044C; -.
DR SGD; S000000640; PER1.
DR VEuPathDB; FungiDB:YCR044C; -.
DR eggNOG; KOG2970; Eukaryota.
DR GeneTree; ENSGT00390000001304; -.
DR HOGENOM; CLU_032917_1_1_1; -.
DR InParanoid; P25625; -.
DR OMA; FMIEDCR; -.
DR BioCyc; YEAST:G3O-29355-MON; -.
DR PRO; PR:P25625; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25625; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IBA:GO_Central.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR InterPro; IPR007217; Per1-like.
DR PANTHER; PTHR13148; PTHR13148; 1.
DR Pfam; PF04080; Per1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..357
FT /note="Protein PER1"
FT /id="PRO_0000202569"
FT TOPO_DOM 23..113
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..189
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..248
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 357 AA; 42541 MW; 6841B84BBFAF9187 CRC64;
MRLAVVVTLL VHCFLVTCSP GDNLDEFIDC TYACEYNRRC PNSQINYIDP ETNMFHDIEF
FDTPPLYSKL LFWDCISDCD YQCQHIITRW RIDEEEEIYQ FHGKWPFLRV LGTQEFFSTI
FSIGNFIPHY KGFVKFSRII REEGDRRRKN SRSILIWNYL YVTVAGMLAW TASSVFHCRD
LIITEKLDYF FAGLTVLTGF HAIFARMTSM FLYPKIAQAF TASVAAIFAL HILRLYVDWS
YTYNMRFNIF FGVLQYILLI MLSCQNYHAL QKQKLMGEFK KTAYSSFKRQ IFKLCVIPIL
LVIVTTMAMS LELFDFFSYE WQIDAHALWH LCTIWPSWVL YDFFLEDYAY WGNRQLY
