SPO7_YEAST
ID SPO7_YEAST Reviewed; 259 AA.
AC P18410; D6VPK9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Sporulation-specific protein SPO7;
GN Name=SPO7; OrderedLocusNames=YAL009W;
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].
RX PubMed=2253888; DOI=10.1016/0378-1119(90)90414-m;
RA Whyte W., Koepp L.H., Lamb J., Crowley J.C., Kaback D.B.;
RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
RT isolation, characterization and regulation of the SPO7 sporulation gene.";
RL Gene 95:65-72(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [4]
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 [5]
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 [6]
RP FUNCTION, IDENTIFICATION IN THE NEM1-SPO7 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9822591; DOI=10.1093/emboj/17.22.6449;
RA Siniossoglou S., Santos-Rosa H., Rappsilber J., Mann M., Hurt E.;
RT "A novel complex of membrane proteins required for formation of a spherical
RT nucleus.";
RL EMBO J. 17:6449-6464(1998).
RN [7]
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 [8]
RP FUNCTION OF THE NEM1-SPO7 COMPLEX.
RX PubMed=15889145; DOI=10.1038/sj.emboj.7600672;
RA Santos-Rosa H., Leung J., Grimsey N., Peak-Chew S., Siniossoglou S.;
RT "The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane
RT growth.";
RL EMBO J. 24:1931-1941(2005).
RN [9]
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).
RN [10]
RP FUNCTION OF THE NEM1-SPO7 COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=29305265; DOI=10.1016/j.bbrc.2017.12.163;
RA Xu X., Okamoto K.;
RT "The Nem1-Spo7 protein phosphatase complex is required for efficient
RT mitophagy in yeast.";
RL Biochem. Biophys. Res. Commun. 496:51-57(2018).
CC -!- FUNCTION: Regulatory component of the NEM1-SPO7 complex which acts as a
CC phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase
CC PAH1 (PubMed:15889145). Essential for the formation of a spherical
CC nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein
CC phosphatase is required for efficient mitophagy under prolonged
CC respiration, as well as for reticulophagy and pexophagy
CC (PubMed:29305265). {ECO:0000269|PubMed:15889145,
CC ECO:0000269|PubMed:29305265, ECO:0000269|PubMed:9822591}.
CC -!- SUBUNIT: Component of the NEM1-SPO7 complex.
CC {ECO:0000269|PubMed:9822591}.
CC -!- INTERACTION:
CC P18410; P38757: NEM1; NbExp=3; IntAct=EBI-17857, EBI-24435;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9822591}. Nucleus membrane
CC {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9822591}.
CC -!- DISRUPTION PHENOTYPE: Leads to inefficient mitochondrial sequestration
CC and degradation, as well as to defective reticulophagy and pexophagy
CC (PubMed:29305265). {ECO:0000269|PubMed:29305265}.
CC -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M36073; AAA35073.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04949.1; -; Genomic_DNA.
DR EMBL; AY558585; AAS56911.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06979.1; -; Genomic_DNA.
DR PIR; JN0099; JN0099.
DR RefSeq; NP_009393.1; NM_001178154.1.
DR AlphaFoldDB; P18410; -.
DR BioGRID; 31757; 209.
DR ComplexPortal; CPX-1787; Nem1-Spo7 phosphatase complex.
DR DIP; DIP-2441N; -.
DR IntAct; P18410; 18.
DR MINT; P18410; -.
DR STRING; 4932.YAL009W; -.
DR iPTMnet; P18410; -.
DR MaxQB; P18410; -.
DR PaxDb; P18410; -.
DR PRIDE; P18410; -.
DR EnsemblFungi; YAL009W_mRNA; YAL009W; YAL009W.
DR GeneID; 851224; -.
DR KEGG; sce:YAL009W; -.
DR SGD; S000000007; SPO7.
DR VEuPathDB; FungiDB:YAL009W; -.
DR eggNOG; ENOG502QTI4; Eukaryota.
DR HOGENOM; CLU_065195_0_0_1; -.
DR InParanoid; P18410; -.
DR OMA; VIPRKFF; -.
DR BioCyc; YEAST:G3O-28822-MON; -.
DR PRO; PR:P18410; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P18410; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0071595; C:Nem1-Spo7 phosphatase complex; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IGI:SGD.
DR GO; GO:0006998; P:nuclear envelope organization; IDA:ComplexPortal.
DR GO; GO:1903740; P:positive regulation of phosphatidate phosphatase activity; IDA:SGD.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IMP:SGD.
DR GO; GO:0061709; P:reticulophagy; IDA:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR005605; Spo7.
DR PANTHER; PTHR28249; PTHR28249; 1.
DR Pfam; PF03907; Spo7; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Nucleus;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="Sporulation-specific protein SPO7"
FT /id="PRO_0000072145"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 259 AA; 30114 MW; 480A73B62EA85E18 CRC64;
MEPESIGDVG NHAQDDSASI VSGPRRRSTS KTSSAKNIRN SSNISPASMI FRNLLILEDD
LRRQAHEQKI LKWQFTLFLA SMAGVGAFTF YELYFTSDYV KGLHRVILQF TLSFISITVV
LFHISGQYRR TIVIPRRFFT STNKGIRQFN VKLVKVQSTW DEKYTDSVRF VSRTIAYCNI
YCLKKFLWLK DDNAIVKFWK SVTIQSQPRI GAVDVKLVLN PRAFSAEIRE GWEIYRDEFW
AREGARRRKQ AHELRPKSE
