BIR1_CAEEL
ID BIR1_CAEEL Reviewed; 155 AA.
AC G5EFA2;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Chromosomal passenger complex protein bir-1 {ECO:0000305};
DE AltName: Full=Baculoviral IAP repeat-containing protein bir-1 {ECO:0000305};
GN Name=bir-1 {ECO:0000312|WormBase:T27F2.3};
GN ORFNames=T27F2.3 {ECO:0000312|WormBase:T27F2.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAB94330.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=10983970; DOI=10.1016/s1097-2765(00)00023-x;
RA Speliotes E.K., Uren A., Vaux D., Horvitz H.R.;
RT "The survivin-like C. elegans BIR-1 protein acts with the Aurora-like
RT kinase AIR-2 to affect chromosomes and the spindle midzone.";
RL Mol. Cell 6:211-223(2000).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=10209096; DOI=10.1016/s0960-9822(99)80137-7;
RA Fraser A.G., James C., Evan G.I., Hengartner M.O.;
RT "Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-
RT 1 plays a conserved role in cytokinesis.";
RL Curr. Biol. 9:292-301(1999).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE CHROMOSOMAL PASSENGER COMPLEX, INTERACTION
RP WITH CSC-1; ICP-1 AND AIR-2, AND MUTAGENESIS OF CYS-83.
RX PubMed=12707312; DOI=10.1083/jcb.200207117;
RA Romano A., Guse A., Krascenicova I., Schnabel H., Schnabel R., Glotzer M.;
RT "CSC-1: a subunit of the Aurora B kinase complex that binds to the
RT survivin-like protein BIR-1 and the incenp-like protein ICP-1.";
RL J. Cell Biol. 161:229-236(2003).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12682297; DOI=10.1073/pnas.0730770100;
RA Kostrouchova M., Kostrouch Z., Saudek V., Piatigorsky J., Rall J.E.;
RT "BIR-1, a Caenorhabditis elegans homologue of Survivin, regulates
RT transcription and development.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5240-5245(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17116281;
RA Liby P., Pohludka M., Vohanka J., Kostrouchova M., Kostrouch D.,
RA Kostrouchova M., Rall J.E., Kostrouch Z.;
RT "BIR-1, the homologue of human Survivin, regulates expression of
RT developmentally active collagen genes in C. elegans.";
RL Folia Biol. (Praha) 52:101-108(2006).
CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC complex that acts as a key regulator of chromosome segregation and
CC cytokinesis (PubMed:12707312, PubMed:10209096, PubMed:10983970). The
CC CPC complex has essential functions at the centromere in ensuring
CC correct chromosome condensation, alignment and segregation
CC (PubMed:12707312, PubMed:10983970). In the complex, required to direct
CC the Aurora B/air-2 kinase to chromosomes (PubMed:12707312,
CC PubMed:10983970). Also functions in spindle midzone formation and in
CC the formation of polar bodies during oogenesis (PubMed:10209096,
CC PubMed:10983970). Required for the localization of the kinetochore
CC component hcp-1 to chromosomes (PubMed:10983970). Involved in the
CC positive regulation of transcription (PubMed:12682297). Involved in the
CC transcriptional regulation of collagen genes (PubMed:17116281).
CC {ECO:0000269|PubMed:10209096, ECO:0000269|PubMed:10983970,
CC ECO:0000269|PubMed:12682297, ECO:0000269|PubMed:12707312,
CC ECO:0000269|PubMed:17116281}.
CC -!- SUBUNIT: Component of the CPC complex which consists of icp-1; csc-1;
CC bir-1 and air-2. Within the complex, interacts with csc-1, icp-1 and
CC air-2. Interacts with csc-1 in a zinc-dependent-manner; the interaction
CC is direct. {ECO:0000269|PubMed:12707312}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:10983970}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10983970}. Midbody
CC {ECO:0000269|PubMed:10983970}. Note=In mitosis and meiosis, localizes
CC to chromosomes during prometaphase and metaphase, localizes to both
CC chromosomes and the spindle midzone during anaphase and disappears from
CC chromosomes during telophase but remains at the spindle midzone.
CC Persists at the cytokinetic remnant during cytokinesis. Also localizes
CC to the chromosome of polar bodies during oogenesis.
CC {ECO:0000269|PubMed:10983970}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes and sperm.
CC {ECO:0000269|PubMed:10983970}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adult
CC animals, with high expression in embryos and in dividing cells (at
CC protein level). {ECO:0000269|PubMed:10209096,
CC ECO:0000269|PubMed:10983970}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in high embryonic
CC lethality (PubMed:10209096). Causes a failure in cytokinesis resulting
CC in a lack of cellularization and in polyploidy (PubMed:10209096,
CC PubMed:10983970). Defective extrusion of the polar body during
CC oogenesis (PubMed:10209096, PubMed:10983970). Defects in chromosome
CC condensation, compromised alignment and segregation of paired homologs
CC and defects in spindle midzone formation during meiosis and mitosis
CC (PubMed:10983970). Disruption of air-2 and hcp-1 localization to
CC chromosomes (PubMed:10983970). Decreased phosphorylation of histone H3
CC 'Ser-10' and decreased acetylation of histone H3 'Lys-14' and 'Lys-9'
CC (PubMed:10983970, PubMed:12682297). Surviving animals exhibit a shorter
CC and stouter body morphology, slow uncoordinated movements, are egg-
CC laying defective, have abnormal germ line growth and exhibit protruding
CC vulvas (PubMed:12682297). Decrease in the transcription of several
CC genes including collagen genes (PubMed:12682297, PubMed:17116281).
CC {ECO:0000269|PubMed:10209096, ECO:0000269|PubMed:10983970,
CC ECO:0000269|PubMed:12682297, ECO:0000269|PubMed:17116281}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR EMBL; U85911; AAB94330.1; -; mRNA.
DR EMBL; BX284605; CAA98553.1; -; Genomic_DNA.
DR PIR; T37471; T37471.
DR RefSeq; NP_505949.1; NM_073548.6.
DR AlphaFoldDB; G5EFA2; -.
DR SMR; G5EFA2; -.
DR ComplexPortal; CPX-3461; Chromosomal passenger complex.
DR IntAct; G5EFA2; 12.
DR STRING; 6239.T27F2.3.2; -.
DR EPD; G5EFA2; -.
DR PaxDb; G5EFA2; -.
DR PeptideAtlas; G5EFA2; -.
DR EnsemblMetazoa; T27F2.3.1; T27F2.3.1; WBGene00000249.
DR EnsemblMetazoa; T27F2.3.2; T27F2.3.2; WBGene00000249.
DR GeneID; 179597; -.
DR KEGG; cel:CELE_T27F2.3; -.
DR CTD; 179597; -.
DR WormBase; T27F2.3; CE06521; WBGene00000249; bir-1.
DR eggNOG; KOG1101; Eukaryota.
DR HOGENOM; CLU_016347_0_3_1; -.
DR InParanoid; G5EFA2; -.
DR OMA; IDIAACF; -.
DR OrthoDB; 1404665at2759; -.
DR PhylomeDB; G5EFA2; -.
DR SignaLink; G5EFA2; -.
DR PRO; PR:G5EFA2; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000249; Expressed in embryo and 4 other tissues.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:ComplexPortal.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:ComplexPortal.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0051233; C:spindle midzone; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IMP:WormBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:WormBase.
DR GO; GO:0016573; P:histone acetylation; IDA:WormBase.
DR GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IC:ComplexPortal.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:WormBase.
DR CDD; cd00022; BIR; 1.
DR InterPro; IPR001370; BIR_rpt.
DR Pfam; PF00653; BIR; 1.
DR SMART; SM00238; BIR; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Chromosome partition; Cytoplasm;
KW Cytoskeleton; Meiosis; Metal-binding; Mitosis; Reference proteome; Zinc.
FT CHAIN 1..155
FT /note="Chromosomal passenger complex protein bir-1"
FT /id="PRO_0000441160"
FT REPEAT 20..87
FT /note="BIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT MUTAGEN 83
FT /note="C->A: Abolishes the interaction with csc-1."
FT /evidence="ECO:0000269|PubMed:12707312"
SQ SEQUENCE 155 AA; 17720 MW; B4E6F40A62B5D97D CRC64;
MAPGTKKKSD MAKFTFYKDR LMTFKNFEYD RDPDAKCTSQ AVAQAGFYCT GPQSGKCAFC
NKELDFDPED DPWYEHTKRD EPCEFVRIGK LDDSELTIND TVRLSQTAMI MTKLFEHEMM
INNLSNHSSS DALFDQLKKV PNTASTTKSN SRRGK
