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   27-MAR-2024, entry version 151.
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; 284812.Q10199; -.
DR   iPTMnet; Q10199; -.
DR   MaxQB; Q10199; -.
DR   PaxDb; 4896-SPBC11C11-02-1; -.
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:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; 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:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR   GO; GO:1990274; P:mitotic actomyosin contractile ring disassembly; IMP:PomBase.
DR   CDD; cd07651; F-BAR_PombeCdc15_like; 1.
DR   CDD; cd00174; SH3; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR23065:SF63; SEPTATION PROTEIN IMP2; 1.
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; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//