SPO71_SCHPO
ID SPO71_SCHPO Reviewed; 965 AA.
AC O13992;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Forespore membrane adapter protein MUG56 {ECO:0000305};
DE AltName: Full=Meiotically up-regulated gene 56 protein;
GN Name=mug56 {ECO:0000312|PomBase:SPAC26H5.11};
GN ORFNames=SPAC26H5.11 {ECO:0000312|PomBase:SPAC26H5.11};
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
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: May recruit a lipid transfer protein to the forespore
CC membrane during sporulation, thereby aiding forespore membrane
CC formation (By similarity). Required for meiosis (PubMed:16303567).
CC {ECO:0000250|UniProtKB:Q03868, ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}. Prospore membrane
CC {ECO:0000250|UniProtKB:Q03868}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SPO71 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16196.1; -; Genomic_DNA.
DR PIR; T38430; T38430.
DR RefSeq; NP_594458.1; NM_001019887.2.
DR AlphaFoldDB; O13992; -.
DR STRING; 4896.SPAC26H5.11.1; -.
DR iPTMnet; O13992; -.
DR PaxDb; O13992; -.
DR PRIDE; O13992; -.
DR EnsemblFungi; SPAC26H5.11.1; SPAC26H5.11.1:pep; SPAC26H5.11.
DR GeneID; 2542692; -.
DR KEGG; spo:SPAC26H5.11; -.
DR PomBase; SPAC26H5.11; mug56.
DR VEuPathDB; FungiDB:SPAC26H5.11; -.
DR eggNOG; ENOG502QRAT; Eukaryota.
DR HOGENOM; CLU_003938_0_0_1; -.
DR InParanoid; O13992; -.
DR OMA; MFLARTR; -.
DR PhylomeDB; O13992; -.
DR PRO; PR:O13992; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005619; C:ascospore wall; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISO:PomBase.
DR GO; GO:0030476; P:ascospore wall assembly; ISO:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; ISO:PomBase.
DR GO; GO:1902657; P:protein localization to prospore membrane; IBA:GO_Central.
DR InterPro; IPR040345; Mug56/Spo71.
DR InterPro; IPR039486; Mug56/Spo71_PH.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR28076; PTHR28076; 3.
DR Pfam; PF15404; PH_4; 1.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Meiosis; Membrane; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..965
FT /note="Forespore membrane adapter protein MUG56"
FT /id="PRO_0000278501"
FT DOMAIN 562..737
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 800..961
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 70..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 110905 MW; 921BA5E3D16639F7 CRC64;
MNEEDTDFAW LHNNSAEHLR FLSHRIFIGP IPSNFIHSTS GFFNKRFQNY TKRQICYNVA
SPNEPPIDFS FLMHKSTDEN PDTPSNLDSP STQNVGSTNN TRASQSLLRR SSSFFRRRHR
KNGTHASTDN NPFSESSTLQ PQTAERTSQQ AVRSAITETT NPSVSVQNSN STSTSSAAMI
IPHRDSQNSL EIAPLISPES QLSSLHPSSS RRHLISTPHV NRGTQFKRSS SCRNSRQPLL
SGVDKHLTSN FTDANLIIKQ SVVLARIEST FTVLPSDYND SAAQRVPRKT ISPWSQCLLV
ARQTDVENSI RLDFISKKLR KRLNGDVVHN LDVPHDKSYK SNYLFSVVLS PHQASWNIYN
SFDNSMVLWC PYGKNKTLIC LLNFQSSLLS FEWISIISRA LLFSPRPSLL ISVPAFHIHL
RLNFPCFKDT TRPHTNETFV TTDDITQLSR TSTLSLSTAS PRLVHDLVMK SWDISEDQFV
ESCLGVLEVN PEWSGIVKTW SKSHTLGLCW RMYDRLEWIN SFSSLKYVGL LAAKDLYQLE
LRPKLHYPNH VTFRDGSKMD EPTPVEGYLI RLTSSTGRKT RYGRMFHKEL YFAIFNNFLF
AIQPDSVLPL SMLSKSLNLD DKLPFLSNNE NDKYVYEFDP FKIANCRASG LNETIDSSVR
ESFLLLLQAE RKRELDMLTI ADSFLDLSRV ESVCPVEDVE ERNIFEITMT NGMKLVFQSY
CERTRNLWIN KITEVASYWK QRLFLDLQEY HDVRETNINI LHIEQSIEPD VACYLNHWEV
AGCVASTLIY HYCSMLGCRV IRMQGTLFKK KDALFEKCFA ILIPGQLVFF QDATRTKFGK
LCTKTHYRKR YSISLKNAFI YTGLSTMDEF ARGPNDPQPH ISRLPRCYED GWQSFDRDDM
LSFVIWSSGG VDYDLRPHHS VPDTAYGMAK DKLSKPKRFM FLARTRQERD VWAKRISKEI
NRGHS
