ID INN1_YEAST Reviewed; 409 AA. AC P53901; D6W131; Q6Q5J6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 163. DE RecName: Full=Ingression protein 1; GN Name=INN1; OrderedLocusNames=YNL152W; ORFNames=N1765; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8686380; RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b; RA Nasr F., Becam A.-M., Herbert C.J.; RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24 RT complete open reading frames: 18 correspond to new genes, one of which RT encodes a protein similar to the human myotonic dystrophy kinase."; RL Yeast 12:169-175(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH CYK2 AND IQG1, AND RP MUTAGENESIS OF LYS-28 AND LYS-31. RX PubMed=18344988; DOI=10.1038/ncb1701; RA Sanchez-Diaz A., Marchesi V., Murray S., Jones R., Pereira G., RA Edmondson R., Allen T., Labib K.; RT "Inn1 couples contraction of the actomyosin ring to membrane ingression RT during cytokinesis in budding yeast."; RL Nat. Cell Biol. 10:395-406(2008). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYK2 AND CYK3. RX PubMed=19528296; DOI=10.1083/jcb.200903125; RA Nishihama R., Schreiter J.H., Onishi M., Vallen E.A., Hanna J., RA Moravcevic K., Lippincott M.F., Han H., Lemmon M.A., Pringle J.R., Bi E.; RT "Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage RT furrow and septum formation in S. cerevisiae."; RL J. Cell Biol. 185:995-1012(2009). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYK3. RX PubMed=19707790; DOI=10.1007/s00438-009-0476-0; RA Jendretzki A., Ciklic I., Rodicio R., Schmitz H.P., Heinisch J.J.; RT "Cyk3 acts in actomyosin ring independent cytokinesis by recruiting Inn1 to RT the yeast bud neck."; RL Mol. Genet. Genomics 282:437-451(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=20442249; DOI=10.1242/jcs.063891; RA Meitinger F., Petrova B., Lombardi I.M., Bertazzi D.T., Hub B., RA Zentgraf H., Pereira G.; RT "Targeted localization of Inn1, Cyk3 and Chs2 by the mitotic-exit network RT regulates cytokinesis in budding yeast."; RL J. Cell Sci. 123:1851-1861(2010). CC -!- FUNCTION: Required for the ingression of the plasma membrane into the CC bud neck at the end of cytokinesis, leading to the separation of the CC mother and daughter cells. Stimulates the synthesis of the primary CC septum (PS) by CHS2. {ECO:0000269|PubMed:18344988, CC ECO:0000269|PubMed:19528296, ECO:0000269|PubMed:19707790}. CC -!- SUBUNIT: Interacts with CYK2, CYK3 and IQG1. CC {ECO:0000269|PubMed:18344988, ECO:0000269|PubMed:19528296, CC ECO:0000269|PubMed:19707790}. CC -!- INTERACTION: CC P53901; Q05080: HOF1; NbExp=6; IntAct=EBI-28955, EBI-5412; CC P53901; P80667: PEX13; NbExp=2; IntAct=EBI-28955, EBI-13206; CC P53901; P40073: SHO1; NbExp=4; IntAct=EBI-28955, EBI-18140; CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:18344988, CC ECO:0000269|PubMed:19528296, ECO:0000269|PubMed:19707790, CC ECO:0000269|PubMed:20442249}. Note=Localizes at the contractile CC actinomyosin ring at the end of cytokinesis. Recruitment to the bud CC neck requires either CYK2 or CYK3. CC -!- DOMAIN: The C2 domain is essential for membrane ingression during CC cytokinesis, but not for recruitment to the actomyosin ring. CC {ECO:0000269|PubMed:18344988}. CC -!- SIMILARITY: Belongs to the INN1/fic1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X92517; CAA63287.1; -; Genomic_DNA. DR EMBL; Z71428; CAA96039.1; -; Genomic_DNA. DR EMBL; AY558026; AAS56352.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10397.1; -; Genomic_DNA. DR PIR; S60975; S60975. DR RefSeq; NP_014247.1; NM_001182990.1. DR AlphaFoldDB; P53901; -. DR SMR; P53901; -. DR BioGRID; 35677; 204. DR ComplexPortal; CPX-1140; HICS complex. DR DIP; DIP-4339N; -. DR IntAct; P53901; 12. DR MINT; P53901; -. DR STRING; 4932.YNL152W; -. DR GlyGen; P53901; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P53901; -. DR MaxQB; P53901; -. DR PaxDb; 4932-YNL152W; -. DR PeptideAtlas; P53901; -. DR TopDownProteomics; P53901; -. DR EnsemblFungi; YNL152W_mRNA; YNL152W; YNL152W. DR GeneID; 855570; -. DR KEGG; sce:YNL152W; -. DR AGR; SGD:S000005096; -. DR SGD; S000005096; INN1. DR VEuPathDB; FungiDB:YNL152W; -. DR eggNOG; ENOG502QSUF; Eukaryota. DR HOGENOM; CLU_673016_0_0_1; -. DR InParanoid; P53901; -. DR OMA; TRFHFAN; -. DR OrthoDB; 5471322at2759; -. DR BioCyc; YEAST:G3O-33169-MONOMER; -. DR BioGRID-ORCS; 855570; 8 hits in 10 CRISPR screens. DR PRO; PR:P53901; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P53901; Protein. DR GO; GO:0005935; C:cellular bud neck; NAS:ComplexPortal. DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD. DR GO; GO:0032154; C:cleavage furrow; IMP:CACAO. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0044697; C:HICS complex; IPI:SGD. DR GO; GO:0016020; C:membrane; NAS:ComplexPortal. DR GO; GO:0030234; F:enzyme regulator activity; IGI:SGD. DR GO; GO:0051276; P:chromosome organization; IMP:SGD. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD. DR GO; GO:1902410; P:mitotic cytokinetic process; NAS:ComplexPortal. DR GO; GO:1990344; P:secondary cell septum biogenesis; IMP:SGD. DR CDD; cd08681; C2_fungal_Inn1p-like; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR037791; C2_fungal_Inn1. DR PANTHER; PTHR47052; CONSERVED SERINE PROLINE-RICH PROTEIN (AFU_ORTHOLOGUE AFUA_2G01790); 1. DR PANTHER; PTHR47052:SF3; INGRESSION PROTEIN 1; 1. DR Pfam; PF00168; C2; 1. DR SMART; SM00239; C2; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR PROSITE; PS50004; C2; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Mitosis; Phosphoprotein; Reference proteome. FT CHAIN 1..409 FT /note="Ingression protein 1" FT /id="PRO_0000203419" FT DOMAIN 1..114 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 300..409 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 362..399 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 392 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MUTAGEN 28 FT /note="K->A: Impairs plasma membrane ingression; when FT associated with A-31." FT /evidence="ECO:0000269|PubMed:18344988" FT MUTAGEN 31 FT /note="K->A: Impairs plasma membrane ingression; when FT associated with A-28." FT /evidence="ECO:0000269|PubMed:18344988" FT CONFLICT 221 FT /note="D -> G (in Ref. 2; AAS56352)" FT /evidence="ECO:0000305" SQ SEQUENCE 409 AA; 46226 MW; 66C2B81D21CE5520 CRC64; MSEEVWNGNQ GILSVYVSKA RDLPNLNKLD KQNVMLRLRI AHMTRASNTL HRAGQNPVFH YLEKFDITPE IKPLMYVEVY CDRRKKSPLP IGRCEIDLLN AIRADPKEGY CTWYELKRSG DEFAGTIFIE LTFTPKVPRL NRDDLNKEMD RLDSSMAMRP IPPLPTESEY DYVHGSTMRQ ITPQCVSTSH EDKDEGQPYR NGNVFSMSSK SDTAVLANSN DPIILPPTFS ASMGTTSTLE TNDTAISNTS NTKFHFANLR KLKEKINIFK NPDSSTNNCQ NESNKVDIEA LQKAIGVTSL SYDEDDDDDD ENDAFYSSSH RVSHNYNQPP LPPIPTRDDM SNYSSSRNTP LVRRDRPSRL DSSSPNSHPH PSGLNSPKLP PLPTTSNSNF NSRKNSMSPT RKRPPPRLS //