IMP2_SCHPO
ID IMP2_SCHPO Reviewed; 670 AA.
AC Q10199;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Septation protein imp2;
GN Name=imp2; ORFNames=SPBC11C11.02;
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, AND SUBCELLULAR LOCATION.
RX PubMed=9786952; DOI=10.1083/jcb.143.2.415;
RA Demeter J., Sazer S.;
RT "imp2, a new component of the actin ring in the fission yeast
RT Schizosaccharomyces pombe.";
RL J. Cell Biol. 143:415-427(1998).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-503 AND THR-531, AND
RP IDENTIFICATION BY 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: Required for normal septation. Involved in the disassembly of
CC the medial ring during septation. {ECO:0000269|PubMed:9786952}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9786952}. Note=Associates with the medial ring
CC during septation.
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DR EMBL; CU329671; CAA20684.1; -; Genomic_DNA.
DR PIR; T39317; S67383.
DR RefSeq; NP_596391.1; NM_001022312.2.
DR PDB; 5C1F; X-ray; 2.36 A; A/B=15-320.
DR PDBsum; 5C1F; -.
DR AlphaFoldDB; Q10199; -.
DR SMR; Q10199; -.
DR BioGRID; 276649; 32.
DR STRING; 4896.SPBC11C11.02.1; -.
DR iPTMnet; Q10199; -.
DR MaxQB; Q10199; -.
DR PaxDb; Q10199; -.
DR PRIDE; Q10199; -.
DR EnsemblFungi; SPBC11C11.02.1; SPBC11C11.02.1:pep; SPBC11C11.02.
DR GeneID; 2540112; -.
DR KEGG; spo:SPBC11C11.02; -.
DR PomBase; SPBC11C11.02; imp2.
DR VEuPathDB; FungiDB:SPBC11C11.02; -.
DR eggNOG; KOG2398; Eukaryota.
DR HOGENOM; CLU_003525_1_1_1; -.
DR InParanoid; Q10199; -.
DR OMA; RFAKSWN; -.
DR PhylomeDB; Q10199; -.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q10199; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005826; C:actomyosin contractile ring; EXP:PomBase.
DR GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA: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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IPI:PomBase.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:PomBase.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:PomBase.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:PomBase.
DR GO; GO:0005543; F:phospholipid binding; EXP:PomBase.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:1990274; P:mitotic actomyosin contractile ring disassembly; IMP:PomBase.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..670
FT /note="Septation protein imp2"
FT /id="PRO_0000084186"
FT DOMAIN 16..269
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 607..670
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 353..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 531
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:5C1F"
FT HELIX 28..69
FT /evidence="ECO:0007829|PDB:5C1F"
FT HELIX 79..108
FT /evidence="ECO:0007829|PDB:5C1F"
FT HELIX 111..165
FT /evidence="ECO:0007829|PDB:5C1F"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5C1F"
FT HELIX 172..262
FT /evidence="ECO:0007829|PDB:5C1F"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:5C1F"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:5C1F"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5C1F"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5C1F"
SQ SEQUENCE 670 AA; 75167 MW; 03551FBB56FC91AE CRC64;
MSQQLSFNAS SAKPDKSFSN YFWGANDEGY HALLSRFSDV KHINEELRSF YHERANIEED
YAKRMAKLSR TTFSSLETGC LKESVQVMKA EVDNMAKSHL QISQLLQDDV ENAFTRYAAS
LKDKKKMIVS GIEKVHKDKL SKHQALVKAQ DKYHYLCKKV NYYVSQQNML FGKELEKNNA
KLNKTQNAIT ASSSDYQSAV AAVRDSYARW TNEWRSTCDK LQDIEEERRH FLKSVMWTFT
LLISRSCFND DQACERIRKN LEQCSVSQDV LEFIDAKSTG TGIPQPPKFY DYYKGEVPDD
SVELVQANFQ RAQTKIENDN MPLNRPYVLS ATARNESSFE NTLPNTPSAI QSLTTVSSNS
SQNGRSSPKK SFLSKFKLTS RPSTPNVGNT APDALSSPRN DSPLTSAADE QMKHLSLQEE
PKQNPTPAAP GAFPNSNTLP PRYNELGSLP SPNSVSFTED SRPNVNTPSR RQQIQEEFGS
VLQMENRAVS PVYDSRKNGS RSSFTLRKSR SPKRPSSSLS QNASRLPRSL TPGNLEPNYD
FGVRVDPASG TAPTDDEPYT DRDSSFVDDT INTKATGNTS NRLSLPAYPT DGGDTSIDNP
TSTDGQRILG YVSALYDYDA AIPEEISFRK GDTIAVLKLY EDGWWEGFVV GEDDHNRGQF
PSNFVREIEV
