MID1_SCHPO
ID MID1_SCHPO Reviewed; 920 AA.
AC P78953;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Anillin-related medial ring protein mid1 {ECO:0000303|PubMed:8946912};
GN Name=mid1 {ECO:0000303|PubMed:8946912};
GN Synonyms=dmf1 {ECO:0000303|PubMed:8946912}; ORFNames=SPCC4B3.15;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8946912; DOI=10.1101/gad.10.21.2707;
RA Sohrmann M., Fankhauser C., Brodbeck C., Simanis V.;
RT "The dmf1/mid1 gene is essential for correct positioning of the division
RT septum in fission yeast.";
RL Genes Dev. 10:2707-2720(1996).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9852154; DOI=10.1083/jcb.143.6.1603;
RA Baehler J., Steever A.B., Wheatley S., Wang Y.L., Pringle J.R., Gould K.L.,
RA McCollum D.;
RT "Role of polo kinase and Mid1p in determining the site of cell division in
RT fission yeast.";
RL J. Cell Biol. 143:1603-1616(1998).
RN [4]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=10930468; DOI=10.1091/mbc.11.8.2757;
RA Paoletti A., Chang F.;
RT "Analysis of mid1p, a protein required for placement of the cell division
RT site, reveals a link between the nucleus and the cell surface in fission
RT yeast.";
RL Mol. Biol. Cell 11:2757-2773(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12186944; DOI=10.1242/jcs.00031;
RA Mulvihill D.P., Hyams J.S.;
RT "Cytokinetic actomyosin ring formation and septation in fission yeast are
RT dependent on the full recruitment of the polo-like kinase Plo1 to the
RT spindle pole body and a functional spindle assembly checkpoint.";
RL J. Cell Sci. 115:3575-3586(2002).
RN [6]
RP FUNCTION.
RX PubMed=15014440; DOI=10.1038/sj.emboj.7600156;
RA Gachet Y., Tournier S., Millar J.B., Hyams J.S.;
RT "Mechanism controlling perpendicular alignment of the spindle to the axis
RT of cell division in fission yeast.";
RL EMBO J. 23:1289-1300(2004).
RN [7]
RP FUNCTION.
RX PubMed=15184401; DOI=10.1083/jcb.200402097;
RA Motegi F., Mishra M., Balasubramanian M.K., Mabuchi I.;
RT "Myosin-II reorganization during mitosis is controlled temporally by its
RT dephosphorylation and spatially by Mid1 in fission yeast.";
RL J. Cell Biol. 165:685-695(2004).
RN [8]
RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=15572668; DOI=10.1128/mcb.24.24.10621-10635.2004;
RA Celton-Morizur S., Bordes N., Fraisier V., Tran P.T., Paoletti A.;
RT "C-terminal anchoring of mid1p to membranes stabilizes cytokinetic ring
RT position in early mitosis in fission yeast.";
RL Mol. Cell. Biol. 24:10621-10635(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17140794; DOI=10.1016/j.cub.2006.11.024;
RA Padte N.N., Martin S.G., Howard M., Chang F.;
RT "The cell-end factor pom1p inhibits mid1p in specification of the cell
RT division plane in fission yeast.";
RL Curr. Biol. 16:2480-2487(2006).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16864655; DOI=10.1083/jcb.200602032;
RA Wu J.Q., Sirotkin V., Kovar D.R., Lord M., Beltzner C.C., Kuhn J.R.,
RA Pollard T.D.;
RT "Assembly of the cytokinetic contractile ring from a broad band of nodes in
RT fission yeast.";
RL J. Cell Biol. 174:391-402(2006).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17077120; DOI=10.1242/jcs.03261;
RA Celton-Morizur S., Racine V., Sibarita J.B., Paoletti A.;
RT "Pom1 kinase links division plane position to cell polarity by regulating
RT Mid1p cortical distribution.";
RL J. Cell Sci. 119:4710-4718(2006).
RN [12]
RP FUNCTION, AND INTERACTION WITH CLP1.
RX PubMed=18378776; DOI=10.1083/jcb.200709060;
RA Clifford D.M., Wolfe B.A., Roberts-Galbraith R.H., McDonald W.H.,
RA Yates J.R. III, Gould K.L.;
RT "The Clp1/Cdc14 phosphatase contributes to the robustness of cytokinesis by
RT association with anillin-related Mid1.";
RL J. Cell Biol. 181:79-88(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531, 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).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19427212; DOI=10.1016/j.cub.2009.04.024;
RA Almonacid M., Moseley J.B., Janvore J., Mayeux A., Fraisier V., Nurse P.,
RA Paoletti A.;
RT "Spatial control of cytokinesis by Cdr2 kinase and Mid1/anillin nuclear
RT export.";
RL Curr. Biol. 19:961-966(2009).
RN [15]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH BLT1 AND CDR2.
RX PubMed=19474789; DOI=10.1038/nature08074;
RA Moseley J.B., Mayeux A., Paoletti A., Nurse P.;
RT "A spatial gradient coordinates cell size and mitotic entry in fission
RT yeast.";
RL Nature 459:857-860(2009).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=20434336; DOI=10.1016/j.cub.2010.04.017;
RA Zhang D., Vjestica A., Oliferenko S.;
RT "The cortical ER network limits the permissive zone for actomyosin ring
RT assembly.";
RL Curr. Biol. 20:1029-1034(2010).
RN [17]
RP FUNCTON, AND INTERACTION WITH FKH2 AND SEP1.
RX PubMed=21098635; DOI=10.1242/jcs.073049;
RA Agarwal M., Papadopoulou K., Mayeux A., Vajrala V., Quintana D.M.,
RA Paoletti A., McInerny C.J.;
RT "Mid1p-dependent regulation of the M-G1 transcription wave in fission
RT yeast.";
RL J. Cell Sci. 123:4366-4373(2010).
RN [18]
RP FUNCTION.
RX PubMed=21376595; DOI=10.1016/j.cub.2011.01.059;
RA Padmanabhan A., Bakka K., Sevugan M., Naqvi N.I., D'souza V., Tang X.,
RA Mishra M., Balasubramanian M.K.;
RT "IQGAP-related Rng2p organizes cortical nodes and ensures position of cell
RT division in fission yeast.";
RL Curr. Biol. 21:467-472(2011).
RN [19]
RP FUNCTION, PHOSPHORYLATION AT SER-15; SER-24; THR-34; SER-46; SER-62 AND
RP SER-95, AND INTERACTION WITH PLO1 AND RNG2.
RX PubMed=21376600; DOI=10.1016/j.cub.2011.02.003;
RA Almonacid M., Celton-Morizur S., Jakubowski J.L., Dingli F., Loew D.,
RA Mayeux A., Chen J.S., Gould K.L., Clifford D.M., Paoletti A.;
RT "Temporal control of contractile ring assembly by Plo1 regulation of myosin
RT II recruitment by Mid1/anillin.";
RL Curr. Biol. 21:473-479(2011).
RN [20]
RP REVIEW ON FUNCTION.
RX PubMed=22888038; DOI=10.1002/cm.21056;
RA Rincon S.A., Paoletti A.;
RT "Mid1/anillin and the spatial regulation of cytokinesis in fission yeast.";
RL Cytoskeleton 69:764-777(2012).
RN [21]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=22427686; DOI=10.1242/jcs.102574;
RA Lee I.J., Wu J.Q.;
RT "Characterization of Mid1 domains for targeting and scaffolding in fission
RT yeast cytokinesis.";
RL J. Cell Sci. 125:2973-2985(2012).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GEF2.
RX PubMed=22298427; DOI=10.1091/mbc.e11-09-0800;
RA Ye Y., Lee I.J., Runge K.W., Wu J.Q.;
RT "Roles of putative Rho-GEF Gef2 in division-site positioning and
RT contractile-ring function in fission yeast cytokinesis.";
RL Mol. Biol. Cell 23:1181-1195(2012).
RN [23]
RP FUNCTION.
RX PubMed=22918943; DOI=10.1091/mbc.e12-07-0535;
RA Saha S., Pollard T.D.;
RT "Anillin-related protein Mid1p coordinates the assembly of the cytokinetic
RT contractile ring in fission yeast.";
RL Mol. Biol. Cell 23:3982-3992(2012).
RN [24]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=22918954; DOI=10.1091/mbc.e12-07-0536;
RA Saha S., Pollard T.D.;
RT "Characterization of structural and functional domains of the anillin-
RT related protein Mid1p that contribute to cytokinesis in fission yeast.";
RL Mol. Biol. Cell 23:3993-4007(2012).
RN [25]
RP FUNCTION, AND INTERACTION WITH BLT1.
RX PubMed=23149940; DOI=10.1128/mcb.01286-12;
RA Guzman-Vendrell M., Baldissard S., Almonacid M., Mayeux A., Paoletti A.,
RA Moseley J.B.;
RT "Blt1 and Mid1 provide overlapping membrane anchors to position the
RT division plane in fission yeast.";
RL Mol. Cell. Biol. 33:418-428(2013).
RN [26]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDR2.
RX PubMed=24982431; DOI=10.1083/jcb.201311097;
RA Rincon S.A., Bhatia P., Bicho C., Guzman-Vendrell M., Fraisier V.,
RA Borek W.E., Alves F.L., Dingli F., Loew D., Rappsilber J., Sawin K.E.,
RA Martin S.G., Paoletti A.;
RT "Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial
RT control of cytokinesis.";
RL J. Cell Biol. 206:61-77(2014).
RN [27]
RP SUBCELLULAR LOCATION.
RX PubMed=25501814; DOI=10.1242/jcs.160077;
RA Pu K.M., Akamatsu M., Pollard T.D.;
RT "The septation initiation network controls the assembly of nodes containing
RT Cdr2p for cytokinesis in fission yeast.";
RL J. Cell Sci. 128:441-446(2015).
RN [28]
RP FUNCTION, AND PHOSPHORYLATION BY SID2.
RX PubMed=28605916; DOI=10.1021/acs.orglett.7b01534;
RA Liu N., Hung Y.S., Gao S.S., Hang L., Zou Y., Chooi Y.H., Tang Y.;
RT "Identification and heterologous production of a benzoyl-primed
RT tricarboxylic acid polyketide intermediate from the zaragozic acid A
RT biosynthetic pathway.";
RL Org. Lett. 19:3560-3563(2017).
RN [29]
RP FUNCTION, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=31243991; DOI=10.1021/acs.biochem.9b00217;
RA Chatterjee M., Pollard T.D.;
RT "The functionally important N-terminal half of fission yeast Mid1p anillin
RT is intrinsically disordered and undergoes phase separation.";
RL Biochemistry 58:3031-3041(2019).
RN [30] {ECO:0007744|PDB:4XOH}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 579-680 AND 710-920, SUBUNIT,
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF GLY-718.
RX PubMed=25959226; DOI=10.1016/j.devcel.2015.03.003;
RA Sun L., Guan R., Lee I.J., Liu Y., Chen M., Wang J., Wu J.Q., Chen Z.;
RT "Mechanistic insights into the anchorage of the contractile ring by anillin
RT and Mid1.";
RL Dev. Cell 33:413-426(2015).
CC -!- FUNCTION: Scaffold protein that anchors the contractile ring (CR) at
CC the cell equator during cytokinesis (PubMed:8946912, PubMed:9852154,
CC PubMed:10930468, PubMed:12186944, PubMed:17140794, PubMed:16864655,
CC PubMed:17077120, PubMed:19427212, PubMed:19474789, PubMed:22888038,
CC PubMed:22427686, PubMed:22298427, PubMed:22918954, PubMed:23149940,
CC PubMed:28605916, PubMed:25959226). At the onset of mitosis, membrane-
CC bound oligomers of mid1 assemble recruitment platforms for cytokinetic
CC ring components at the medial cortex and stabilize the ring position
CC during its compaction (PubMed:8946912, PubMed:9852154, PubMed:10930468,
CC PubMed:12186944, PubMed:17140794, PubMed:16864655, PubMed:17077120,
CC PubMed:19474789, PubMed:28605916, PubMed:25959226, PubMed:15572668).
CC Recruits dephosphorylated myo2, but also rng2, clp1 and cdc15 to nodes
CC and to place cytokinetic nodes around the cell equator the medial
CC cortex to promote the ring assembly in cooperation with F-actin
CC (PubMed:15184401, PubMed:18378776, PubMed:21376595, PubMed:21376600,
CC PubMed:22918943). Necessary to stabilize the mitotic spindle
CC perpendicular to the axis of cell division (PubMed:15014440). Recruits
CC also the cdr2 kinase to the CR (PubMed:19474789, PubMed:24982431,
CC PubMed:28605916). {ECO:0000269|PubMed:10930468,
CC ECO:0000269|PubMed:12186944, ECO:0000269|PubMed:15014440,
CC ECO:0000269|PubMed:15184401, ECO:0000269|PubMed:15572668,
CC ECO:0000269|PubMed:16864655, ECO:0000269|PubMed:17077120,
CC ECO:0000269|PubMed:17140794, ECO:0000269|PubMed:18378776,
CC ECO:0000269|PubMed:19427212, ECO:0000269|PubMed:19474789,
CC ECO:0000269|PubMed:21376595, ECO:0000269|PubMed:21376600,
CC ECO:0000269|PubMed:22298427, ECO:0000269|PubMed:22427686,
CC ECO:0000269|PubMed:22888038, ECO:0000269|PubMed:22918943,
CC ECO:0000269|PubMed:22918954, ECO:0000269|PubMed:23149940,
CC ECO:0000269|PubMed:24982431, ECO:0000269|PubMed:25959226,
CC ECO:0000269|PubMed:28605916, ECO:0000269|PubMed:8946912,
CC ECO:0000269|PubMed:9852154}.
CC -!- FUNCTION: In the nucleus, binds to the promoter regions of M-G1
CC transcribed genes to negatively regulate their expression.
CC {ECO:0000269|PubMed:21098635}.
CC -!- SUBUNIT: Homodimer (PubMed:15572668, PubMed:25959226). Interacts with
CC blt1 and cdr2 (PubMed:19474789, PubMed:23149940, PubMed:24982431).
CC Interacts with gef2 (PubMed:22298427). Interacts with plo1 and rng2
CC (PubMed:21376600). Interacts with fhk2 and sep1 (PubMed:21098635).
CC Interacts with clp1 (PubMed:18378776). {ECO:0000269|PubMed:15572668,
CC ECO:0000269|PubMed:18378776, ECO:0000269|PubMed:19474789,
CC ECO:0000269|PubMed:21098635, ECO:0000269|PubMed:21376600,
CC ECO:0000269|PubMed:22298427, ECO:0000269|PubMed:23149940,
CC ECO:0000269|PubMed:24982431, ECO:0000269|PubMed:25959226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10930468,
CC ECO:0000269|PubMed:12186944, ECO:0000269|PubMed:19427212,
CC ECO:0000269|PubMed:19474789, ECO:0000269|PubMed:9852154}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:10930468, ECO:0000269|PubMed:12186944,
CC ECO:0000269|PubMed:16864655, ECO:0000269|PubMed:17077120,
CC ECO:0000269|PubMed:17140794, ECO:0000269|PubMed:19427212,
CC ECO:0000269|PubMed:19474789, ECO:0000269|PubMed:20434336,
CC ECO:0000269|PubMed:22298427, ECO:0000269|PubMed:22427686,
CC ECO:0000269|PubMed:22918954, ECO:0000269|PubMed:25501814,
CC ECO:0000269|PubMed:9852154}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19474789}. Note=During interphase, is exported from
CC the nucleus and relocates to medial ring at the cell cortex
CC (PubMed:12186944, PubMed:16864655, PubMed:19427212, PubMed:19474789).
CC The localization to the cell division plane is regulated by the cell-
CC end factor pom1 (PubMed:17140794, PubMed:17077120). First forms a
CC diffuse cortical band during spindle formation and then coalesces into
CC a ring before anaphase (PubMed:9852154). Binding to the medial cortex
CC is facilitated by gef2 (PubMed:22298427). Phosphorylation by sid2 leads
CC to removal from the cortex (PubMed:28605916). The cortical ER network
CC restricts the lateral motion of mid1 and hence generates a permissive
CC zone for actomyosin ring assembly precisely at the cell equator
CC (PubMed:20434336). {ECO:0000269|PubMed:12186944,
CC ECO:0000269|PubMed:16864655, ECO:0000269|PubMed:17077120,
CC ECO:0000269|PubMed:17140794, ECO:0000269|PubMed:19427212,
CC ECO:0000269|PubMed:19474789, ECO:0000269|PubMed:20434336,
CC ECO:0000269|PubMed:22298427, ECO:0000269|PubMed:28605916,
CC ECO:0000269|PubMed:9852154}.
CC -!- DOMAIN: The N-terminal part (residues 1 to 452) is intrinsically
CC disordered but moderately compact and is able to demixe into liquid
CC droplets at concentrations far below its concentration in cytokinesis
CC organizing centers (also called nodes); these physical properties are
CC appropriate for scaffolding other proteins in nodes (PubMed:31243991).
CC The N-terminus has the ability to associate faintly with the medial
CC cortex and is sufficient to form tight rings (PubMed:15572668,
CC PubMed:22427686). This domain is responsible for oligomerization that
CC may contribute to the activity of mid1 as a scaffold for other proteins
CC in cytokinetic nodes and contractile rings (PubMed:22918954).
CC {ECO:0000269|PubMed:15572668, ECO:0000269|PubMed:22427686,
CC ECO:0000269|PubMed:22918954, ECO:0000269|PubMed:31243991}.
CC -!- DOMAIN: The C-terminus contains a cryptic lipid-binding C2 domain and a
CC PH domain, and is involved in the anchorage to membranes, which
CC stabilizes cytokinetic ring position. {ECO:0000269|PubMed:15572668,
CC ECO:0000269|PubMed:22427686, ECO:0000269|PubMed:22918954,
CC ECO:0000269|PubMed:25959226}.
CC -!- DOMAIN: The nuclear localization sequence (NLS) is required for nuclear
CC import, whereas both leucine-rich nuclear export sequences NES1 and
CC NES2 are required for nuclear export. {ECO:0000269|PubMed:10930468}.
CC -!- PTM: Phosphorylated (PubMed:18257517, PubMed:8946912). At the onset of
CC mitosis, becomes hyperphosphorylated, leaves the nucleus, and forms a
CC medial ring (PubMed:8946912). Phosphorylation by plo1 and other kinases
CC may contribute to solubilizing mid1 for export from the nucleus
CC (PubMed:21376600) (Probable). Phosphorylation by sid2 drives removal
CC from the cortex at the actomyosin contractile ring constriction onset
CC (PubMed:28605916). {ECO:0000269|PubMed:18257517,
CC ECO:0000269|PubMed:21376600, ECO:0000269|PubMed:28605916,
CC ECO:0000269|PubMed:8946912, ECO:0000305|PubMed:31243991}.
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DR EMBL; Y07599; CAA68873.1; -; mRNA.
DR EMBL; CU329672; CAB60689.1; -; Genomic_DNA.
DR PIR; T43263; T43263.
DR RefSeq; NP_588075.1; NM_001023067.2.
DR PDB; 4XOH; X-ray; 2.80 A; A/B/C=579-680, A/B/C=710-920.
DR PDBsum; 4XOH; -.
DR AlphaFoldDB; P78953; -.
DR SMR; P78953; -.
DR BioGRID; 275775; 209.
DR DIP; DIP-36604N; -.
DR IntAct; P78953; 3.
DR STRING; 4896.SPCC4B3.15.1; -.
DR iPTMnet; P78953; -.
DR MaxQB; P78953; -.
DR PaxDb; P78953; -.
DR PRIDE; P78953; -.
DR EnsemblFungi; SPCC4B3.15.1; SPCC4B3.15.1:pep; SPCC4B3.15.
DR GeneID; 2539205; -.
DR KEGG; spo:SPCC4B3.15; -.
DR PomBase; SPCC4B3.15; mid1.
DR VEuPathDB; FungiDB:SPCC4B3.15; -.
DR HOGENOM; CLU_326017_0_0_1; -.
DR OMA; YGHNDAL; -.
DR Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR Reactome; R-SPO-9013026; RHOB GTPase cycle.
DR Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR PRO; PR:P78953; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IPI:PomBase.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0090488; F:polo box domain specific binding; IPI:PomBase.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:1903486; P:establishment of mitotic actomyosin contractile ring localization; IMP:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:1902408; P:mitotic cytokinesis, site selection; IMP:PomBase.
DR GO; GO:0031106; P:septin ring organization; IMP:PomBase.
DR DisProt; DP02903; -.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..920
FT /note="Anillin-related medial ring protein mid1"
FT /id="PRO_0000079937"
FT DOMAIN 802..901
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..452
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:31243991"
FT REGION 538..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..920
FT /note="Cryptic lipid-binding C2 domain"
FT /evidence="ECO:0000269|PubMed:25959226"
FT MOTIF 69..81
FT /note="Nuclear export sequence (NES) 1"
FT /evidence="ECO:0000269|PubMed:10930468"
FT MOTIF 681..710
FT /note="Nuclear localization sequence (NLS)"
FT /evidence="ECO:0000269|PubMed:10930468"
FT MOTIF 763..773
FT /note="Nuclear export sequence (NES) 2"
FT /evidence="ECO:0000269|PubMed:10930468"
FT COMPBIAS 20..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21376600"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21376600"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21376600"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21376600"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21376600"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21376600"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 718
FT /note="G->D: Disrupts the structural integrity of the C2
FT membrane-binding domain and impairs the function."
FT /evidence="ECO:0000269|PubMed:25959226"
FT STRAND 583..595
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 605..611
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 628..638
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 642..652
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 714..723
FT /evidence="ECO:0007829|PDB:4XOH"
FT HELIX 724..726
FT /evidence="ECO:0007829|PDB:4XOH"
FT HELIX 728..731
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 736..744
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 762..774
FT /evidence="ECO:0007829|PDB:4XOH"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:4XOH"
FT HELIX 787..794
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 803..810
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 818..824
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 827..832
FT /evidence="ECO:0007829|PDB:4XOH"
FT TURN 833..836
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 837..844
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:4XOH"
FT HELIX 860..863
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 867..873
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 878..884
FT /evidence="ECO:0007829|PDB:4XOH"
FT HELIX 886..896
FT /evidence="ECO:0007829|PDB:4XOH"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:4XOH"
FT HELIX 910..918
FT /evidence="ECO:0007829|PDB:4XOH"
SQ SEQUENCE 920 AA; 102367 MW; CA95FB48A20549B5 CRC64;
MKEQEFSYRE AKDVSLDSKG LENSFLSSPN REKTPLFFEG NSNETSGYDQ TKNFTHGDGD
MSLGNLSELN VATDLLESLD LRSMYMHGYG HLDSSFSSQH SPDNRKRMSS TSVFKRINSE
EEGRIPSLTY SAGTMNSTSS STASLKGADI VADYETFNPD QNLAELSFDR SKSSRKRAVE
VAEFSRAKTM SPLEYTVQHP YQSHNELSTN PARARAGSVP NLARIPSDVK PVPPAHLSAS
STVGPRILPS LPKDTTEDNP ALERVETTAS LDMDYKPLEP LAPIQEAPVE DTSEPFSSVP
EATLDDSDIS TESLRKKVLA KMEAKRISSG SSYASTLRKV YDFSELSLPT NGKDYDELYL
QSSRNSEPEI STIINDSLQQ ENMDEDISAT SIPKSQAAYG HGSVTYHEVP RYNLTSASVG
YSISSQRGRI KSSSTIDNLS AILSSEDLRH PSMQPVPGTK RTYSNYCENE PNKSSQSLVS
SESHNVEGWN YSETGTVGFY DPSAEISASI DELRQSTPVA RDSELLSRAH SFDLNRLDLP
SQDKSTSYEV PNGTENQSPR PVTSLGFVNE TFFEEKPKAP LPLGRFYIHL NSILNISISE
VHSPIKIIVN TPTQNMQLPW QAVNGNNRLD HDFAFHVDDN FKVSFMFLDI PIEDKSNGSK
GVSATKDVSN GKPAETKSKA RKFFDKLFNR RKKRKLNKAA AVENSKAKKS VVIKKVSGTA
TLNLGNVKDS CFGKAFNVEI PIISRGFLEA IPVKINSIGK RTLGNLTLTC LYIPELSVPE
QELPFTLEQA TMDLRHVRSN YLYNEGYLYR LEDSSIRRRF VVLRSKQLNF YAEKGGQYLD
TFQLSKTVVS IPMVNFSEAV SNLGLVAGIL ATSVDRRHVQ LFADSKKVCQ KWLQVMNSRS
FALDRGTEKL WLQEYVNFMA
