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   08-NOV-2023, entry version 150.
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; 361.
DR   DIP; DIP-5598N; -.
DR   IntAct; P25625; 1.
DR   MINT; P25625; -.
DR   STRING; 4932.YCR044C; -.
DR   PaxDb; 4932-YCR044C; -.
DR   PeptideAtlas; P25625; -.
DR   EnsemblFungi; YCR044C_mRNA; YCR044C; YCR044C.
DR   GeneID; 850411; -.
DR   KEGG; sce:YCR044C; -.
DR   AGR; SGD:S000000640; -.
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; DFMIEDC; -.
DR   OrthoDB; 445643at2759; -.
DR   BioCyc; YEAST:G3O-29355-MONOMER; -.
DR   BioGRID-ORCS; 850411; 0 hits in 10 CRISPR screens.
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:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR   GO; GO:0030026; P:intracellular manganese ion homeostasis; IMP:SGD.
DR   InterPro; IPR007217; Per1-like.
DR   PANTHER; PTHR13148; PER1-RELATED; 1.
DR   PANTHER; PTHR13148:SF0; POST-GPI ATTACHMENT TO PROTEINS FACTOR 3; 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
//