SPO7_SCHPO
ID SPO7_SCHPO Reviewed; 180 AA.
AC Q9USQ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Sporulation-specific protein spo7;
GN Name=spo7; ORFNames=SPBC902.03;
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: Probable regulatory component of the nem1-spo7 complex which
CC acts as a phosphatase and may be required for proper nuclear membrane
CC morphology. {ECO:0000250}.
CC -!- SUBUNIT: Component of the nem1-spo7 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
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DR EMBL; CU329671; CAB62097.1; -; Genomic_DNA.
DR PIR; T50384; T50384.
DR RefSeq; NP_595201.1; NM_001021107.2.
DR AlphaFoldDB; Q9USQ0; -.
DR BioGRID; 277795; 7.
DR STRING; 4896.SPBC902.03.1; -.
DR iPTMnet; Q9USQ0; -.
DR PaxDb; Q9USQ0; -.
DR PRIDE; Q9USQ0; -.
DR EnsemblFungi; SPBC902.03.1; SPBC902.03.1:pep; SPBC902.03.
DR GeneID; 2541282; -.
DR KEGG; spo:SPBC902.03; -.
DR PomBase; SPBC902.03; -.
DR VEuPathDB; FungiDB:SPBC902.03; -.
DR eggNOG; ENOG502QTI4; Eukaryota.
DR HOGENOM; CLU_101485_0_0_1; -.
DR InParanoid; Q9USQ0; -.
DR OMA; FVPHCNR; -.
DR PhylomeDB; Q9USQ0; -.
DR Reactome; R-SPO-4419969; Depolymerisation of the Nuclear Lamina.
DR PRO; PR:Q9USQ0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071595; C:Nem1-Spo7 phosphatase complex; ISO:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019888; F:protein phosphatase regulator activity; NAS:PomBase.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; ISO:PomBase.
DR GO; GO:0006998; P:nuclear envelope organization; ISO:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR InterPro; IPR005605; Spo7.
DR PANTHER; PTHR28249; PTHR28249; 1.
DR Pfam; PF03907; Spo7; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..180
FT /note="Sporulation-specific protein spo7"
FT /id="PRO_0000315976"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 180 AA; 21373 MW; A662DEC3CB28FDE5 CRC64;
MSSYVPNTLS VYHNLLILEA SFRKTYLQLQ VRRQKYMAFY VSLLVWNFYF GYRVFYRISK
YSLIDLTYKL CLLCGIVTLL LFYFSGLYRT TIVYPSRYVQ QVNKAMRFFN IRLVITPVPW
FQVRKPLDCG VHLILSSKRF DILVIEGWEA FRSSYFASIH RKNNSIQSNE SSESPSSKQN
