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Septin ring organizing protein mid2

 MID2_SCHPO              Reviewed;         706 AA.
Q9P7Y8; Q8X1T2;
23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
13-JUN-2012, sequence version 2.
28-MAR-2018, entry version 101.
RecName: Full=Septin ring organizing protein mid2;
Name=mid2; Synonyms=bud4; ORFNames=SPAPYUG7.03c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
REVISION OF GENE MODEL.
PubMed=21511999; DOI=10.1126/science.1203357;
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
"Comparative functional genomics of the fission yeasts.";
Science 332:930-936(2011).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
STRAIN=972 / ATCC 24843;
PubMed=11041002;
Shpakovski G.V., Baranova G.M.;
"Chromosomal localization of the rpb9+ and tfa1+ genes encoding
components of the mRNA synthesis machinery of Schizosaccharomyces
pombe.";
Bioorg. Khim. 26:623-630(2000).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12654901; DOI=10.1083/jcb.200212016;
Berlin A., Paoletti A., Chang F.;
"Mid2p stabilizes septin rings during cytokinesis in fission yeast.";
J. Cell Biol. 160:1083-1092(2003).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=12668659; DOI=10.1083/jcb.200211126;
Tasto J.J., Morrell J.L., Gould K.L.;
"An anillin homologue, Mid2p, acts during fission yeast cytokinesis to
organize the septin ring and promote cell separation.";
J. Cell Biol. 160:1093-1103(2003).
[6]
INDUCTION BY ACE2.
PubMed=16317047; DOI=10.1242/jcs.02687;
Petit C.S., Mehta S., Roberts R.H., Gould K.L.;
"Ace2p contributes to fission yeast septin ring assembly by regulating
mid2+ expression.";
J. Cell Sci. 118:5731-5742(2005).
[7]
INDUCTION BY ACE2.
PubMed=15689498; DOI=10.1091/mbc.E04-06-0442;
Alonso-Nunez M.L., An H., Martin-Cuadrado A.B., Mehta S., Petit C.S.,
Sipiczki M., del Rey F., Gould K.L., Vazquez de Aldana C.R.;
"Ace2p controls the expression of genes required for cell separation
in Schizosaccharomyces pombe.";
Mol. Biol. Cell 16:2003-2017(2005).
[8]
FUNCTION.
PubMed=16079182; DOI=10.1091/mbc.E04-12-1114;
Martin-Cuadrado A.B., Morrell J.L., Konomi M., An H., Petit C.S.,
Osumi M., Balasubramanian M., Gould K.L., Del Rey F.,
Vazquez de Aldana C.R.;
"Role of septins and the exocyst complex in the function of hydrolytic
enzymes responsible for fission yeast cell separation.";
Mol. Biol. Cell 16:4867-4881(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Responsible for the proper stability and function of
septins during cytokinesis. Required for the correct formation of
the medial septin ring structure in mitosis and for the proper
localization of endo-glucanases agn1 and eng1, which are needed
for efficient cell separation. May act as a landmark for the
localization of hydrolytic proteins to the medial region.
{ECO:0000269|PubMed:12654901, ECO:0000269|PubMed:12668659,
ECO:0000269|PubMed:16079182}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
{ECO:0000269|PubMed:12654901}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:12668659}. Note=Localizes to the medial ring
at the cell cortex of dividing cells (PubMed:12654901). Initially
forms a single ring, which subsequently splits into two distinct
rings as the septum forms, and disappears as cells separate
(PubMed:12654901). Requires septins for proper localization
(PubMed:12654901).
-!- INDUCTION: Cell cycle-regulated with a peak during septation (at
protein level). Induced by transcription factor ace2 during
mitosis. Degraded via SCF-dependent proteolysis.
{ECO:0000269|PubMed:15689498, ECO:0000269|PubMed:16317047}.
-!- SIMILARITY: Belongs to the BUD4 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CU329670; CAB66312.2; -; Genomic_DNA.
EMBL; AF237418; AAL55661.1; -; Genomic_DNA.
PIR; T50303; T50303.
RefSeq; NP_594704.2; NM_001020131.2.
BioGrid; 279136; 15.
STRING; 4896.SPAPYUG7.03c.1; -.
iPTMnet; Q9P7Y8; -.
MaxQB; Q9P7Y8; -.
PaxDb; Q9P7Y8; -.
PRIDE; Q9P7Y8; -.
EnsemblFungi; SPAPYUG7.03c.1; SPAPYUG7.03c.1:pep; SPAPYUG7.03c.
GeneID; 2542683; -.
KEGG; spo:SPAPYUG7.03c; -.
EuPathDB; FungiDB:SPAPYUG7.03c; -.
PomBase; SPAPYUG7.03c; mid2.
InParanoid; Q9P7Y8; -.
OrthoDB; EOG092C30T0; -.
PRO; PR:Q9P7Y8; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0032153; C:cell division site; HDA:PomBase.
GO; GO:0005737; C:cytoplasm; HDA:PomBase.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0032168; C:hyphal septin ring; IBA:GO_Central.
GO; GO:0031097; C:medial cortex; IDA:PomBase.
GO; GO:0005940; C:septin ring; IDA:PomBase.
GO; GO:0005525; F:GTP binding; ISS:PomBase.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; TAS:PomBase.
GO; GO:0019954; P:asexual reproduction; IBA:GO_Central.
GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
GO; GO:0031107; P:septin ring disassembly; IMP:PomBase.
GO; GO:0031106; P:septin ring organization; IMP:PomBase.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF00169; PH; 1.
SMART; SM00233; PH; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Mitosis; Phosphoprotein; Reference proteome.
CHAIN 1 706 Septin ring organizing protein mid2.
/FTId=PRO_0000096484.
DOMAIN 583 688 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
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


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