INN1_SCHPO
ID INN1_SCHPO Reviewed; 272 AA.
AC O94701;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Ingression protein fic1;
DE AltName: Full=Cdc15-interacting C2 domain-containing protein 1;
GN Name=fic1; ORFNames=SPBC83.18c;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP INTERACTION WITH CDC15 AND IMP2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19139265; DOI=10.1083/jcb.200806044;
RA Roberts-Galbraith R.H., Chen J.-S., Wang J., Gould K.L.;
RT "The SH3 domains of two PCH family members cooperate in assembly of the
RT Schizosaccharomyces pombe contractile ring.";
RL J. Cell Biol. 184:113-127(2009).
CC -!- FUNCTION: Involved in the ingression of the plasma membrane during
CC cytokinesis, leading to the separation of the daughter cells. Unlike
CC its S.cerevisiae ortholog INN1, it does not play an essential role,
CC probably because the actinomyosin ring is connected to the cell cortex
CC by many more proteins. {ECO:0000269|PubMed:19139265}.
CC -!- SUBUNIT: Interacts with cdc15 and imp2. {ECO:0000269|PubMed:19139265}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum and
CC the cell tip. {ECO:0000269|PubMed:19139265}.
CC -!- SIMILARITY: Belongs to the INN1/fic1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB36880.1; -; Genomic_DNA.
DR PIR; T40707; T40707.
DR RefSeq; NP_595651.1; NM_001021545.2.
DR AlphaFoldDB; O94701; -.
DR SMR; O94701; -.
DR BioGRID; 277717; 31.
DR STRING; 4896.SPBC83.18c.1; -.
DR MaxQB; O94701; -.
DR PaxDb; O94701; -.
DR EnsemblFungi; SPBC83.18c.1; SPBC83.18c.1:pep; SPBC83.18c.
DR GeneID; 2541203; -.
DR KEGG; spo:SPBC83.18c; -.
DR PomBase; SPBC83.18c; fic1.
DR VEuPathDB; FungiDB:SPBC83.18c; -.
DR eggNOG; ENOG502RDJ2; Eukaryota.
DR HOGENOM; CLU_977141_0_0_1; -.
DR InParanoid; O94701; -.
DR OMA; PPQASTY; -.
DR PRO; PR:O94701; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IPI:PomBase.
DR GO; GO:0005543; F:phospholipid binding; ISO:PomBase.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:PomBase.
DR GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IDA:PomBase.
DR GO; GO:1990274; P:mitotic actomyosin contractile ring disassembly; EXP:PomBase.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
DR CDD; cd08681; C2_fungal_Inn1p-like; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037791; C2_fungal_Inn1.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..272
FT /note="Ingression protein fic1"
FT /id="PRO_0000303953"
FT DOMAIN 1..107
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 155..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 30855 MW; EBC017D63A67CF09 CRC64;
MSKNPLGTLV VRIWKAKNLP NKALVGKQSP YCVCRVGEVV KRTQTDKRSG QEPSWNAVLE
FNIPSESYHI MKITVFHEGF RKHPHLIGDT VLSFEKAMKE ELQSEWYELK NEFQFAGELS
VQFKFIPTDP LYFDRASSKP VLQFPYSSVA ALTPVPKKPS KPSKPRKKVP VSHPLPPTPP
SREEHVSVPR ESSLFTYEDD PLPSFPSPYM VDDYYTQDVF VSDNVNDYSY GVQNPTNPRL
SVEDYDANHS SLPPVPPPHL ILPTASSSQI FH
