ANI1_CAEEL
ID ANI1_CAEEL Reviewed; 1159 AA.
AC Q9XTT4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Anillin-like protein 1;
GN Name=ani-1; ORFNames=Y49E10.19;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15930113; DOI=10.1242/dev.01828;
RA Maddox A.S., Habermann B., Desai A., Oegema K.;
RT "Distinct roles for two C. elegans anillins in the gonad and early
RT embryo.";
RL Development 132:2837-2848(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21055941; DOI=10.1016/j.cub.2010.10.030;
RA Dorn J.F., Zhang L., Paradis V., Edoh-Bedi D., Jusu S., Maddox P.S.,
RA Maddox A.S.;
RT "Actomyosin tube formation in polar body cytokinesis requires Anillin in C.
RT elegans.";
RL Curr. Biol. 20:2046-2051(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21737681; DOI=10.1091/mbc.e11-05-0399;
RA Tse Y.C., Piekny A., Glotzer M.;
RT "Anillin promotes astral microtubule-directed cortical myosin
RT polarization.";
RL Mol. Biol. Cell 22:3165-3175(2011).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24016757; DOI=10.1016/j.ydbio.2013.08.024;
RA Fotopoulos N., Wernike D., Chen Y., Makil N., Marte A., Piekny A.;
RT "Caenorhabditis elegans anillin (ani-1) regulates neuroblast cytokinesis
RT and epidermal morphogenesis during embryonic development.";
RL Dev. Biol. 383:61-74(2013).
CC -!- FUNCTION: Required for contractile events in embryos that occur prior
CC to mitosis, such as cortical ruffling and pseudocleavage. Promotes
CC membrane ruffling by organizing cortical patches of septins and myosin
CC II. Not generally required for cytokinesis in mitotic cells. Required
CC for the asymmetric cleavage events that extrude the two polar bodies
CC during oocyte meiosis. Not required for meiotic contractile ring
CC assembly, initiation or closure but is required for the transformation
CC of the contractile ring from a disk above the spindle to a tube around
CC the spindle midzone. Promotes astral microtubule-directed cortical
CC myosin polarization and cleavage furrow ingression. Regulates
CC neuroblast cytokinesis during mid- to late-embryogenesis and is
CC required for ventral enclosure. {ECO:0000269|PubMed:15930113,
CC ECO:0000269|PubMed:21055941, ECO:0000269|PubMed:21737681,
CC ECO:0000269|PubMed:24016757}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm, cytoskeleton.
CC Cytoplasm, cytoskeleton, spindle. Midbody. Cleavage furrow.
CC -!- TISSUE SPECIFICITY: Strongly expressed in dividing neuroblasts under
CC the ventral epidermal cells during ventral enclosure.
CC {ECO:0000269|PubMed:24016757}.
CC -!- DEVELOPMENTAL STAGE: Enriched in embryos, where it localizes
CC predominantly to cortical regions and the cytokinetic furrow in
CC telophase. {ECO:0000269|PubMed:15930113}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of the protein causes
CC 100% embryonic lethality. Abnormal polar body extrusion with large and
CC unstable polar bodies that often fuse with the oocyte. Failure of
CC contractile ring to transform from a disk to a tube during meiosis.
CC Ventral enclosure defects and failure of neuroblasts to complete
CC cytokinesis. Aberrant microtubule-directed cortical myosin
CC polarization. {ECO:0000269|PubMed:15930113,
CC ECO:0000269|PubMed:21055941, ECO:0000269|PubMed:21737681,
CC ECO:0000269|PubMed:24016757}.
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DR EMBL; Z98866; CAB11565.2; -; Genomic_DNA.
DR PIR; T27053; T27053.
DR RefSeq; NP_499624.2; NM_067223.6.
DR AlphaFoldDB; Q9XTT4; -.
DR SMR; Q9XTT4; -.
DR BioGRID; 41851; 30.
DR STRING; 6239.Y49E10.19; -.
DR iPTMnet; Q9XTT4; -.
DR EPD; Q9XTT4; -.
DR PaxDb; Q9XTT4; -.
DR PeptideAtlas; Q9XTT4; -.
DR EnsemblMetazoa; Y49E10.19.1; Y49E10.19.1; WBGene00013038.
DR EnsemblMetazoa; Y49E10.19.2; Y49E10.19.2; WBGene00013038.
DR GeneID; 176672; -.
DR KEGG; cel:CELE_Y49E10.19; -.
DR UCSC; Y49E10.19; c. elegans.
DR CTD; 176672; -.
DR WormBase; Y49E10.19; CE33878; WBGene00013038; ani-1.
DR eggNOG; KOG3640; Eukaryota.
DR HOGENOM; CLU_277216_0_0_1; -.
DR InParanoid; Q9XTT4; -.
DR OMA; HITHENT; -.
DR OrthoDB; 200480at2759; -.
DR PRO; PR:Q9XTT4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013038; Expressed in embryo and 4 other tissues.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0031252; C:cell leading edge; IDA:WormBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030426; C:growth cone; IDA:WormBase.
DR GO; GO:0005874; C:microtubule; IDA:WormBase.
DR GO; GO:0030496; C:midbody; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0008017; F:microtubule binding; IDA:WormBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:WormBase.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0030590; P:first cell cycle pseudocleavage; IMP:WormBase.
DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0031106; P:septin ring organization; IMP:WormBase.
DR CDD; cd01263; PH_anillin; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012966; AHD.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037840; PH_Anillin.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF08174; Anillin; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Developmental protein;
KW Meiosis; Mitosis; Reference proteome.
FT CHAIN 1..1159
FT /note="Anillin-like protein 1"
FT /id="PRO_0000227969"
FT DOMAIN 1029..1147
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 43..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..685
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 126803 MW; A1667EFC6B1BD147 CRC64;
MGDQFDSLME RIRVRQAEMS GEGEVAKENG PVTSKITSVK QEVASPTKVF GSSSKCNDGP
STPVHFHPQE PKETTPNMKE NAENSLNSFK DATVNESSSK KTSRFSMLAQ EIDEYEYDYQ
SQYNKPKEAY MKGRSPRMSI GETRPAVLCT PAGAQAMKSP NVAVSSKSAP EIALGMSDFE
ARRIKFAQPI VNVNYLPNES SIFSGGSGSS VNDQSTVLGG SAEMMNVTTS SLSCGELSMN
QHITHENTII NAQSCDNREA ILRERQQVSN EEYGPHTFMR KKVPKEASSA TSSSSSTTTL
TTISGASGST TSGISNAPQD SASTKTTTNT FTSSYLLTKT SNNNINALVS SSPKPFSKDI
GRSMFSPVHF TPKSTSSPKT LSESIFSPSK SAAVEGSIAT TRRLQFEEKL KKSSSANVTA
PPAPTSAPVP TPRHVAPLAP TVAQQSHLTP NHRHAAQQKK HLFPVVGIVA TAPIPVQTQW
RGQSNTPVVQ GARADEKTAG NEPPVGAGVG KLKNLKSRWE FSSATGTPIH PDATEDSLIA
TAIKMKESAI PKQLGHRSER KGPSASSLYS QGARSNTASP ASKSTRYEQE EEDDVFEAPE
FNDGGDVISE DGILQEEEED TSKFIDNAFG FMEGSGAGTP SPYREPPLQR LEKNRPPAEV
IEEETENEDE SEPYEPEEEE DDDATTQFPV PERSRKSSSQ LAYSVSFYRK IQRDRNEESS
TVLAGPVISQ ISPSAPPMSS SLTSQQKLRQ LTTGPANGAR IVESAKDAHD RIKRAIQVEE
QLVAQSKRAM ILARDKPSFR GSREEFEAQW AMLRHVEKHR ALLTEYDRLK RDGPRIIDGP
RGTITVSQLS VNMARDYVSA NIASSKKSDE VFYFAAILRY GEQVDVSKMV TSDGGLNRRG
VLEFPVPLML TGIPPDFRAT VEIYGQRSMR ESTSHEDKYK LKNSTFKAKT RNTFLGGGST
SSANQSLFVD PAASSSSTSS TTSNFNLLGT FSFDINCPGK HLYNMSHTVY PLEGITQMKV
RKQAIDGADI TYHGFLSMYQ RTGEGLGSWT RYWCALENGE MKFWKQPEDE GTKGYTALMD
LSTCCRSEGA SVVEDICPFP NSFHIDVWAP KMDTSDPRGI ERLRVMLAAD TAQDLQTWLS
LINSTSKQLC TWRNPIVNQ
