MID2_SCHPO
ID MID2_SCHPO Reviewed; 706 AA.
AC Q9P7Y8; Q8X1T2;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Septin ring organizing protein mid2;
GN Name=mid2; Synonyms=bud4; ORFNames=SPAPYUG7.03c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11041002;
RA Shpakovski G.V., Baranova G.M.;
RT "Chromosomal localization of the rpb9+ and tfa1+ genes encoding components
RT of the mRNA synthesis machinery of Schizosaccharomyces pombe.";
RL Bioorg. Khim. 26:623-630(2000).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12654901; DOI=10.1083/jcb.200212016;
RA Berlin A., Paoletti A., Chang F.;
RT "Mid2p stabilizes septin rings during cytokinesis in fission yeast.";
RL J. Cell Biol. 160:1083-1092(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12668659; DOI=10.1083/jcb.200211126;
RA Tasto J.J., Morrell J.L., Gould K.L.;
RT "An anillin homologue, Mid2p, acts during fission yeast cytokinesis to
RT organize the septin ring and promote cell separation.";
RL J. Cell Biol. 160:1093-1103(2003).
RN [6]
RP INDUCTION BY ACE2.
RX PubMed=16317047; DOI=10.1242/jcs.02687;
RA Petit C.S., Mehta S., Roberts R.H., Gould K.L.;
RT "Ace2p contributes to fission yeast septin ring assembly by regulating
RT mid2+ expression.";
RL J. Cell Sci. 118:5731-5742(2005).
RN [7]
RP INDUCTION BY ACE2.
RX PubMed=15689498; DOI=10.1091/mbc.e04-06-0442;
RA Alonso-Nunez M.L., An H., Martin-Cuadrado A.B., Mehta S., Petit C.S.,
RA Sipiczki M., del Rey F., Gould K.L., Vazquez de Aldana C.R.;
RT "Ace2p controls the expression of genes required for cell separation in
RT Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 16:2003-2017(2005).
RN [8]
RP FUNCTION.
RX PubMed=16079182; DOI=10.1091/mbc.e04-12-1114;
RA Martin-Cuadrado A.B., Morrell J.L., Konomi M., An H., Petit C.S., Osumi M.,
RA Balasubramanian M., Gould K.L., Del Rey F., Vazquez de Aldana C.R.;
RT "Role of septins and the exocyst complex in the function of hydrolytic
RT enzymes responsible for fission yeast cell separation.";
RL Mol. Biol. Cell 16:4867-4881(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, 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: Responsible for the proper stability and function of septins
CC during cytokinesis. Required for the correct formation of the medial
CC septin ring structure in mitosis and for the proper localization of
CC endo-glucanases agn1 and eng1, which are needed for efficient cell
CC separation. May act as a landmark for the localization of hydrolytic
CC proteins to the medial region. {ECO:0000269|PubMed:12654901,
CC ECO:0000269|PubMed:12668659, ECO:0000269|PubMed:16079182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:12654901}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12668659}. Note=Localizes to the medial ring at the
CC cell cortex of dividing cells (PubMed:12654901). Initially forms a
CC single ring, which subsequently splits into two distinct rings as the
CC septum forms, and disappears as cells separate (PubMed:12654901).
CC Requires septins for proper localization (PubMed:12654901).
CC -!- INDUCTION: Cell cycle-regulated with a peak during septation (at
CC protein level). Induced by transcription factor ace2 during mitosis.
CC Degraded via SCF-dependent proteolysis. {ECO:0000269|PubMed:15689498,
CC ECO:0000269|PubMed:16317047}.
CC -!- SIMILARITY: Belongs to the BUD4 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB66312.2; -; Genomic_DNA.
DR EMBL; AF237418; AAL55661.1; -; Genomic_DNA.
DR PIR; T50303; T50303.
DR RefSeq; NP_594704.2; NM_001020131.2.
DR AlphaFoldDB; Q9P7Y8; -.
DR SMR; Q9P7Y8; -.
DR BioGRID; 279136; 15.
DR STRING; 4896.SPAPYUG7.03c.1; -.
DR iPTMnet; Q9P7Y8; -.
DR MaxQB; Q9P7Y8; -.
DR PaxDb; Q9P7Y8; -.
DR PRIDE; Q9P7Y8; -.
DR EnsemblFungi; SPAPYUG7.03c.1; SPAPYUG7.03c.1:pep; SPAPYUG7.03c.
DR GeneID; 2542683; -.
DR KEGG; spo:SPAPYUG7.03c; -.
DR PomBase; SPAPYUG7.03c; mid2.
DR VEuPathDB; FungiDB:SPAPYUG7.03c; -.
DR eggNOG; ENOG502REBM; Eukaryota.
DR HOGENOM; CLU_393377_0_0_1; -.
DR InParanoid; Q9P7Y8; -.
DR OMA; DNHYSDE; -.
DR PRO; PR:Q9P7Y8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0036391; C:medial cortex septin ring; IDA:PomBase.
DR GO; GO:0032176; C:split septin rings; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; ISS:PomBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; TAS:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031106; P:septin ring organization; IDA:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..706
FT /note="Septin ring organizing protein mid2"
FT /id="PRO_0000096484"
FT DOMAIN 583..688
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 62..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 706 AA; 78961 MW; 94A8EFC25FB342D1 CRC64;
MLMTASQQDQ HAKMYLADIH RALRIPSPIP STDYECSDYA STIASISRES TMRNFNRSNI
SSTAPSFAES EDAEDGDSFP YDQTLSNSSS FDDHQSLLPF STEVRRTPTY SVMNETDSSS
TSVEDVNKEN ILSLNDSCLI KLSDDEASNK SSRSSTPRNS IKSNSSNQGH GDIPIPKKNP
ARSVCNSKLF NEDTLPAEFE EVSISPPVKL ELPTHSHNSS DTSFTNSIVS SVSDMVGLGE
GINSIASFGF SEDSSSFQDI KTPPRLSFAD ENRENCRTDI YRSDSIHEYE EPLTSSITSL
DSPHVLDENA PIPLLPKVVS LPDPRFTNVL SAFDALTRTY LLRQNSKVVH ATSQKQEMQT
SRRVVNSCYM PESLSRNLSS SLQQTGGSGR LFVRLMEIRN LTIPLASGMT TRFTYTISGK
HIQVPWNALH STTKIENEYT FDESISSSIV CTLRAAYDPP KVRTRSTLGK VFSTNKRKSM
TTDPVSEALH GFVSEDGTFG EVTINTDSVS RTALGRCQSM VLPIMNKWTV DPAAKDVKPL
PRKVGELEIH VFFLPALPVS LKELPASIES AMYDLKLAEW DRTLLCDGYL CQQGGDCPYW
RRRYFQLIGS KLVAFQQFSK VRRATIDLSE ATHIVDDNHY SDEEELEGYL YFESGFRIIF
SNGDYIDFYA ETVGEKDEWM STLRQHLGQC SMVHKNWTKS FLSLSF
