SPO3_SCHPO
ID SPO3_SCHPO Reviewed; 1028 AA.
AC Q9US08;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Sporulation-specific protein 3;
GN Name=spo3; ORFNames=SPAC607.10;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11739793; DOI=10.1091/mbc.12.12.3955;
RA Nakamura T., Nakamura-Kubo M., Hirata A., Shimoda C.;
RT "The Schizosaccharomyces pombe spo3+ gene is required for assembly of the
RT forespore membrane and genetically interacts with psy1(+)-encoding
RT syntaxin-like protein.";
RL Mol. Biol. Cell 12:3955-3972(2001).
RN [2]
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).
CC -!- FUNCTION: Has a role in spore morphogenesis. Involved in the assembly
CC of the forespore membrane. {ECO:0000269|PubMed:11739793}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11739793};
CC Peripheral membrane protein {ECO:0000269|PubMed:11739793}. Prospore
CC membrane {ECO:0000269|PubMed:11739793}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11739793}. Note=Associated with the plasma and
CC forespore membranes.
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DR EMBL; CU329670; CAB63797.1; -; Genomic_DNA.
DR PIR; T50230; T50230.
DR RefSeq; NP_593599.1; NM_001019030.2.
DR AlphaFoldDB; Q9US08; -.
DR BioGRID; 279938; 6.
DR STRING; 4896.SPAC607.10.1; -.
DR iPTMnet; Q9US08; -.
DR PaxDb; Q9US08; -.
DR PRIDE; Q9US08; -.
DR EnsemblFungi; SPAC607.10.1; SPAC607.10.1:pep; SPAC607.10.
DR GeneID; 2543520; -.
DR KEGG; spo:SPAC607.10; -.
DR PomBase; SPAC607.10; spo3.
DR VEuPathDB; FungiDB:SPAC607.10; -.
DR HOGENOM; CLU_298787_0_0_1; -.
DR OMA; YNILANK; -.
DR PRO; PR:Q9US08; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0070056; C:prospore membrane leading edge; IDA:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
PE 4: Predicted;
KW Cell membrane; Membrane; Reference proteome; Sporulation.
FT CHAIN 1..1028
FT /note="Sporulation-specific protein 3"
FT /id="PRO_0000072138"
SQ SEQUENCE 1028 AA; 119407 MW; 2FE1860008CFB59F CRC64;
MGILSVIRIF IYCLIRLFSF NSRKRNSSID ELERGEINAF ACDKQNTPSP NSECRPLTPL
NSPFRRTVEG DTANLQAPSP TACPSFDSAS SIKSSKEDIA CRKLSTERFF YSPNGIDEMK
KQQQFKKIPT VSITEVEPAF IPSNMEQALF SEEPFVIQDD LSHQINLDDN RKFSRIQKNK
LDPLITVNLV PIVNGENCFN FYETQMETNF LSPEFIKKPS MVDHKRDSEI NAVTAVSADG
SFSPLTETLS STISTLSNDS LDGLSSQKNE FTGFNSNSEW IPNDTVDYIC NSDASSVVSN
LSDFEDCFDQ FGVYDKEYEK KIEKTKRNFP KFQSSATYPP FSAHHQARRN NPQGFRNVKK
RFQLFKDDCT ALTDSDFLDA LPFFNARVII ALYVEWRLRV YETMIIKGEE SLKNLQRARD
GPHNKLWLGV FGNKDTIKKL SNYDRRAISN PYVSNHLNFN VRRVKSDTVY IPTILQLLRS
STQLMTEQAF VASSNLKSTK GLRETRLIQK YKVKGDFEYV YAALYYAAFT QESTLKAVTI
DDILSEDELE DWWYLNLRYT SFITPQLCFE FLDKEADSCR DRLTEVKSEP PKAVIYEEPL
NKLSRFSSDR LFTSHELVAI AELISLNEPP LESGKKFYYE EFQKACQKKR DDYRYSPEIE
FKAAFREKFL QSNEKVPFPR PGEIYEKRCD YFSKYACQNI FISKPLKRSG SIYEVFSDGI
GRVIYGSVLD YEATRNNILL HFGFEIHCAP SEEELIEREE AFKDFHNMLS FKYSANEIYE
FCGTHSRAEV HKNEVLKRMA YYLIDENKEI SILRRILSLR IVEPTTSFTR YEYDLWRTFY
PDVLYLNYSK SGRIPTGSPY IMNGQWRKDL CVSTPPMVDI NSALFPHWFK LSASNLFAGA
EHAGLNRQKP DKIDLDLYEP LPENSYLVAA ELRVLRALRH KNPENIPLLE KWEVRALHQL
MAKIRKYYTV PTDYLSLRMD GLQAMLRKRE YMSCYTFNYF DYACLMDHAY RLYEGFNNQV
VNLPPRIM