MPC70_YEAST
ID MPC70_YEAST Reviewed; 609 AA.
AC Q12411; D6W1X7;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Sporulation-specific protein 21;
DE AltName: Full=Meiotic plaque component protein 70;
GN Name=SPO21; Synonyms=MPC70; OrderedLocusNames=YOL091W;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP MPC54; NUD1 AND SPC42.
RX PubMed=10899120; DOI=10.1093/emboj/19.14.3657;
RA Knop M., Strasser K.;
RT "Role of the spindle pole body of yeast in mediating assembly of the
RT prospore membrane during meiosis.";
RL EMBO J. 19:3657-3667(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11408572; DOI=10.1091/mbc.12.6.1611;
RA Bajgier B.K., Malzone M., Nickas M., Neiman A.M.;
RT "SPO21 is required for meiosis-specific modification of the spindle pole
RT body in yeast.";
RL Mol. Biol. Cell 12:1611-1621(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11244080; DOI=10.1128/jb.183.7.2372-2375.2001;
RA Wesp A., Prinz S., Fink G.R.;
RT "Conservative duplication of spindle poles during meiosis in Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 183:2372-2375(2001).
RN [7]
RP INTERACTION WITH ADY3.
RX PubMed=11973299; DOI=10.1093/genetics/160.4.1439;
RA Nickas M.E., Neiman A.M.;
RT "Ady3p links spindle pole body function to spore wall synthesis in
RT Saccharomyces cerevisiae.";
RL Genetics 160:1439-1450(2002).
RN [8]
RP INTERACTION WITH ADY4.
RX PubMed=12796288; DOI=10.1128/ec.2.3.431-445.2003;
RA Nickas M.E., Schwartz C., Neiman A.M.;
RT "Ady4p and Spo74p are components of the meiotic spindle pole body that
RT promote growth of the prospore membrane in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 2:431-445(2003).
CC -!- FUNCTION: Involved in the pathway that organizes the shaping and sizing
CC of the prospore membrane (PSM) during sporulation. May provide a
CC meiosis-specific scaffold for the assembly of other proteins on spindle
CC pole bodies (SPBs), and may be a limiting component for SPB formation.
CC {ECO:0000269|PubMed:10899120, ECO:0000269|PubMed:11408572}.
CC -!- SUBUNIT: Interacts directly with MPC54, NUD1 and SPC42. Interacts with
CC ADY3. Interacts with ADY4. Probable component of a SPB complex composed
CC of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
CC {ECO:0000269|PubMed:10899120, ECO:0000269|PubMed:11973299,
CC ECO:0000269|PubMed:12796288}.
CC -!- INTERACTION:
CC Q12411; Q07732: ADY3; NbExp=5; IntAct=EBI-36275, EBI-33406;
CC Q12411; Q08550: MPC54; NbExp=3; IntAct=EBI-36275, EBI-34513;
CC Q12411; P32336: NUD1; NbExp=3; IntAct=EBI-36275, EBI-12361;
CC -!- SUBCELLULAR LOCATION: Prospore membrane. Cytoplasm, cytoskeleton,
CC spindle pole. Note=Localizes to the ends of spindle microtubules in
CC cells in meiosis.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific. Expressed during meiosis II,
CC from 3 to 9 hours after induction of sporulation. Not expressed during
CC mitosis. {ECO:0000269|PubMed:10899120}.
CC -!- SIMILARITY: Belongs to the MPC70 family. {ECO:0000305}.
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DR EMBL; X83121; CAA58188.1; -; Genomic_DNA.
DR EMBL; Z74833; CAA99103.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10693.1; -; Genomic_DNA.
DR PIR; S57378; S57378.
DR RefSeq; NP_014550.1; NM_001183345.1.
DR AlphaFoldDB; Q12411; -.
DR SMR; Q12411; -.
DR BioGRID; 34311; 95.
DR DIP; DIP-921N; -.
DR IntAct; Q12411; 13.
DR MINT; Q12411; -.
DR STRING; 4932.YOL091W; -.
DR iPTMnet; Q12411; -.
DR PaxDb; Q12411; -.
DR PRIDE; Q12411; -.
DR EnsemblFungi; YOL091W_mRNA; YOL091W; YOL091W.
DR GeneID; 854062; -.
DR KEGG; sce:YOL091W; -.
DR SGD; S000005451; SPO21.
DR VEuPathDB; FungiDB:YOL091W; -.
DR HOGENOM; CLU_532328_0_0_1; -.
DR InParanoid; Q12411; -.
DR OMA; SCISNHE; -.
DR BioCyc; YEAST:G3O-33491-MON; -.
DR PRO; PR:Q12411; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12411; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; HDA:SGD.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; TAS:SGD.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Meiosis;
KW Membrane; Reference proteome; Sporulation.
FT CHAIN 1..609
FT /note="Sporulation-specific protein 21"
FT /id="PRO_0000096556"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 283..342
FT /evidence="ECO:0000255"
FT COILED 357..393
FT /evidence="ECO:0000255"
FT COILED 424..483
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 69878 MW; E216B0C9B865B412 CRC64;
MDNILKASNM EGTSTMTVTS RSSEDSSCIS NHEQDTDTHK DGDTSGLENS KISKRKWMKE
FFKLSKSPAS KSSRSIGSMK SNQSLVSMKS SDDGNSYKND YSSICGNSLP SAGLSRSNSV
KELKLDSTGS QRSKNNVAML ARSSTTSQTT CSSSSSSSSY NSIKGNENDI LLQNNNHFRH
NKEIPQSKGS SNINTASIMS QYNVDTQATA IMSDMQKQYD SQQMTSPFVN EDLHFDPNGE
VSHVIKAIFK EIGYKYDDFS DIPVFQLMQE MYQLVKKNSS ARRTKITDYA SKLKEKEAQL
KSQNDKILKL ETTNKAYKTK YKEVSLENKK IKEAFKELDN ESYNHDEELL KKYKYTRETL
DRVNREQQLI IDQNEFLKKS VNELQNEVNA TNFKFSLFKE KYAKLADSIT ELNTSTKKRE
ALGENLTFEC NELKEICLKY KKNIENISNT NKNLQNSFKN ERKKVLDLRN ERNLLKKEIL
LIECHGSYSL LLVSNILTCY RFLLPSDTII ETESLIKELL NMNNSLSNHV SSSDEPPAEY
SKRLELKCVE FEEKLLYFYQ ELVTKKIIDV IYKCFINYYK KSRQTDQKSN QNSSTPYKQS
QRQVPHSIK
