SPO15_SCHPO
ID SPO15_SCHPO Reviewed; 1957 AA.
AC Q10411; Q9USE9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sporulation-specific protein 15;
GN Name=spo15; ORFNames=SPAC1F3.06c;
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, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10639340; DOI=10.1242/jcs.113.3.545;
RA Ikemoto S., Nakamura T., Kubo M., Shimoda C.;
RT "S. pombe sporulation-specific coiled-coil protein Spo15p is localized to
RT the spindle pole body and essential for its modification.";
RL J. Cell Sci. 113:545-554(2000).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 705-871.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15654021; DOI=10.1242/jcs.01629;
RA Saito T.T., Tougan T., Okuzaki D., Kasama T., Nojima H.;
RT "Mcp6, a meiosis-specific coiled-coil protein of Schizosaccharomyces pombe,
RT localizes to the spindle pole body and is required for horsetail movement
RT and recombination.";
RL J. Cell Sci. 118:447-459(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in the initiation of spore membrane formation.
CC {ECO:0000269|PubMed:10639340}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10639340}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:10639340,
CC ECO:0000269|PubMed:15654021}.
CC -!- SIMILARITY: Belongs to the MPC70 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA94624.1; -; Genomic_DNA.
DR EMBL; AB027811; BAA87115.1; -; Genomic_DNA.
DR PIR; T38077; T38077.
DR RefSeq; NP_593009.1; NM_001018408.2.
DR AlphaFoldDB; Q10411; -.
DR SMR; Q10411; -.
DR BioGRID; 278145; 20.
DR STRING; 4896.SPAC1F3.06c.1; -.
DR iPTMnet; Q10411; -.
DR MaxQB; Q10411; -.
DR PaxDb; Q10411; -.
DR PRIDE; Q10411; -.
DR EnsemblFungi; SPAC1F3.06c.1; SPAC1F3.06c.1:pep; SPAC1F3.06c.
DR GeneID; 2541649; -.
DR KEGG; spo:SPAC1F3.06c; -.
DR PomBase; SPAC1F3.06c; spo15.
DR VEuPathDB; FungiDB:SPAC1F3.06c; -.
DR eggNOG; KOG4674; Eukaryota.
DR HOGENOM; CLU_234945_0_0_1; -.
DR InParanoid; Q10411; -.
DR OMA; DEFRNQG; -.
DR PhylomeDB; Q10411; -.
DR PRO; PR:Q10411; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0031322; P:ascospore-type prospore-specific spindle pole body remodeling; IMP:PomBase.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Sporulation.
FT CHAIN 1..1957
FT /note="Sporulation-specific protein 15"
FT /id="PRO_0000072135"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 199..785
FT /evidence="ECO:0000255"
FT COILED 804..1235
FT /evidence="ECO:0000255"
FT COILED 1320..1471
FT /evidence="ECO:0000255"
FT COILED 1481..1723
FT /evidence="ECO:0000255"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1957 AA; 222787 MW; 3F480CA06171D9DA CRC64;
MSNQSSSGSN TSDLDEESAS SLVSSAASPF IDSDLETPRP NISRASTGQL AEDGDTSSQH
EDSSEELKRQ EVRGMRRHSD LSIDAKLGSS EGSTASSALP LTPRSPSNAS WLLVRGGLLD
SPILDINSVT QKSNLLNELK QVRSKLAALE HENGILSLQL SSSNKKDKNT SSVTTLTSEE
DVSYFQKKLT NMESNFSAKQ SEAYDLSRQL LTVTEKLDKK EKDYEKIKED VSSIKASLAE
EQASNKSLRG EQERLEKLLV SSNKTVSTLR QTENSLRAEC KTLQEKLEKC AINEEDSKLL
EELKHNVANY SDAIVHKDKL IEDLSTRISE FDNLKSERDT LSIKNEKLEK LLRNTIGSLK
DSRTSNSQLE EEMVELKESN RTIHSQLTDA ESKLSSFEQE NKSLKGSIDE YQNNLSSKDK
MVKQVSSQLE EARSSLAHAT GKLAEINSER DFQNKKIKDF EKIEQDLRAC LNSSSNELKE
KSALIDKKDQ ELNNLREQIK EQKKVSESTQ SSLQSLQRDI LNEKKKHEVY ESQLNELKGE
LQTEISNSEH LSSQLSTLAA EKEAAVATNN ELSESKNSLQ TLCNAFQEKL AKSVMQLKEN
EQNFSSLDTS FKKLNESHQE LENNHQTITK QLKDTSSKLQ QLQLERANFE QKESTLSDEN
NDLRTKLLKL EESNKSLIKK QEDVDSLEKN IQTLKEDLRK SEEALRFSKL EAKNLREVID
NLKGKHETLE AQRNDLHSSL SDAKNTNAIL SSELTKSSED VKRLTANVET LTQDSKAMKQ
SFTSLVNSYQ SISNLYHELR DDHVNMQSQN NTLLESESKL KTDCENLTQQ NMTLIDNVQK
LMHKHVNQES KVSELKEVNG KLSLDLKNLR SSLNVAISDN DQILTQLAEL SKNYDSLEQE
SAQLNSGLKS LEAEKQLLHT ENEELHIRLD KLTGKLKIEE SKSSDLGKKL TARQEEISNL
KEENMSQSQA ITSVKSKLDE TLSKSSKLEA DIEHLKNKVS EVEVERNALL ASNERLMDDL
KNNGENIASL QTEIEKKRAE NDDLQSKLSV VSSEYENLLL ISSQTNKSLE DKTNQLKYIE
KNVQKLLDEK DQRNVELEEL TSKYGKLGEE NAQIKDELLA LRKKSKKQHD LCANFVDDLK
EKSDALEQLT NEKNELIVSL EQSNSNNEAL VEERSDLANR LSDMKKSLSD SDNVISVIRS
DLVRVNDELD TLKKDKDSLS TQYSEVCQDR DDLLDSLKGC EESFNKYAVS LRELCTKSEI
DVPVSEILDD NFVFNAGNFS ELSRLTVLSL ENYLDAFNQV NFKKMELDNR LTTTDAEFTK
VVADLEKLQH EHDDWLIQRG DLEKALKDSE KNFLRKEAEM TENIHSLEEG KEETKKEIAE
LSSRLEDNQL ATNKLKNQLD HLNQEIRLKE DVLKEKESLI ISLEESLSNQ RQKESSLLDA
KNELEHMLDD TSRKNSSLME KIESINSSLD DKSFELASAV EKLGALQKLH SESLSLMENI
KSQLQEAKEK IQVDESTIQE LDHEITASKN NYEGKLNDKD SIIRDLSENI EQLNNLLAEE
KSAVKRLSTE KESEILQFNS RLADLEYHKS QVESELGRSK LKLASTTEEL QLAENERLSL
TTRMLDLQNQ VKDLSNIKDS LSEDLRTLRS LEDSVASLQK ECKIKSNTVE SLQDVLTSVQ
ARNAELEDEV SRSVDKIRRR DDRCEHLSGK LKKLHSQLEE QHETFFRAEQ QRMTQLGFLK
ETVKKQEKLL KKLNLRQEQL IPRSSILVYE SYIRDIEKEI IVLQERLNGI ELSQQLPKGY
FGYFFKTNRV EMEVLDSFKQ QVAKLQFLAG AEFIVKFKED LEKCAAEEKE KQATFDNYSE
KVENLGKSIE ALYFALNREI SFRKSLALSK SAYHNLLVRD SPKFNPDSQI TYSIPVTNTK
QSLLRSAILC VISLQRLRLL GQRHSFCEEV IENLSCV
