PER1_SCHPO
ID PER1_SCHPO Reviewed; 331 AA.
AC Q9P6N9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Protein PER1 homolog;
DE Flags: Precursor;
GN ORFNames=SPAC823.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Vacuole membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the PGAP3/PER1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB90152.1; -; Genomic_DNA.
DR RefSeq; NP_593834.1; NM_001019263.2.
DR AlphaFoldDB; Q9P6N9; -.
DR BioGRID; 280078; 3.
DR STRING; 4896.SPAC823.07.1; -.
DR PaxDb; Q9P6N9; -.
DR EnsemblFungi; SPAC823.07.1; SPAC823.07.1:pep; SPAC823.07.
DR GeneID; 2543664; -.
DR KEGG; spo:SPAC823.07; -.
DR PomBase; SPAC823.07; -.
DR VEuPathDB; FungiDB:SPAC823.07; -.
DR eggNOG; KOG2970; Eukaryota.
DR HOGENOM; CLU_032917_1_1_1; -.
DR InParanoid; Q9P6N9; -.
DR OMA; FMIEDCR; -.
DR PhylomeDB; Q9P6N9; -.
DR PRO; PR:Q9P6N9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
DR InterPro; IPR007217; Per1-like.
DR PANTHER; PTHR13148; PTHR13148; 1.
DR Pfam; PF04080; Per1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..331
FT /note="Protein PER1 homolog"
FT /id="PRO_0000318589"
FT TOPO_DOM 25..100
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..232
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..289
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 331 AA; 38356 MW; C5EC29F8C8B555C5 CRC64;
MRVLRNFTIF FLFTALSLFR QISASAGDLH PVYVSCVNRC IENKCHGNPS DTSKLPLDLK
LFRWDCGSNC GYECEITAEN YFAAHNLPSQ QYHGKWYFIR VFGIQELFSV FFSMLNFMIH
YNGYHIMRRC IPDEHPAKRL CLSWAIVGMN AWVWSSVFHI RDTPITEKLD YFSAGAFVLF
GSYCTLILML RLDQLPGGKL LCWIIGVIFI AAFIAHVSYL SFYSFDYGYN MKANVAVGLV
QNILWYYYSW SNRNSGLYWT RWPAYIVTSL MLATSLELFD FSPIANLIDA HALWHLSTVP
ITHYLYGFVV RKCSYDLTKG TFKIKAYDSS R
