BIR52_XENTR
ID BIR52_XENTR Reviewed; 156 AA.
AC Q28ER3;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Baculoviral IAP repeat-containing protein 5.2;
DE AltName: Full=Survivin 2 {ECO:0000250|UniProtKB:Q50L39};
DE Short=Survivin {ECO:0000312|EMBL:CAJ83536.1};
GN Name=birc5.2; ORFNames=TGas042b13.1, TGas101d21.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ83536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:CAJ83536.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAJ83536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6 {ECO:0000312|EMBL:AAI23072.1};
RC TISSUE=Ovary {ECO:0000312|EMBL:AAI23072.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC complex that acts as a key regulator of mitosis. The CPC complex has
CC essential functions at the centromere in ensuring correct chromosome
CC alignment and segregation and is required for chromatin-induced
CC microtubule stabilization and spindle assembly. Does not appear to
CC exhibit anti-apoptotic activity. Plays a role in increasing blood
CC vessel size during development (By similarity).
CC {ECO:0000250|UniProtKB:Q50L39, ECO:0000250|UniProtKB:Q804H7}.
CC -!- SUBUNIT: Component of the CPC at least composed of survivin/birc5,
CC incenp, cdca8/borealin and/or cdca9/dasra-A, and aurkb/aurora-B.
CC Interacts directly with incenp (via N-terminus). Interacts with rxra;
CC the interaction is stronger in the absence of 9-cis retinoic acids (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus
CC {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Note=Localizes on chromosome arms and inner centromeres
CC from prophase through metaphase and then transferring to the spindle
CC midzone and midbody from anaphase through cytokinesis.
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- DOMAIN: The BIR2 domain is required for vascular development.
CC {ECO:0000250|UniProtKB:Q50L39}.
CC -!- PTM: Ubiquitination is required for centrosome-targeting.
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI23072.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAJ83536.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAJ83890.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR848111; CAJ83536.1; ALT_INIT; mRNA.
DR EMBL; CR761512; CAJ83890.1; ALT_INIT; mRNA.
DR EMBL; BC123071; AAI23072.1; ALT_INIT; mRNA.
DR RefSeq; NP_001037948.1; NM_001044483.2.
DR AlphaFoldDB; Q28ER3; -.
DR SMR; Q28ER3; -.
DR STRING; 8364.ENSXETP00000021977; -.
DR MEROPS; I32.005; -.
DR PaxDb; Q28ER3; -.
DR DNASU; 733575; -.
DR GeneID; 733575; -.
DR KEGG; xtr:733575; -.
DR CTD; 107768; -.
DR Xenbase; XB-GENE-966741; birc5l.
DR eggNOG; KOG1101; Eukaryota.
DR HOGENOM; CLU_016347_0_1_1; -.
DR InParanoid; Q28ER3; -.
DR OMA; FKDWPFP; -.
DR OrthoDB; 1404665at2759; -.
DR TreeFam; TF342652; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-8951664; Neddylation.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0001944; P:vasculature development; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Metal-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..156
FT /note="Baculoviral IAP repeat-containing protein 5.2"
FT /id="PRO_0000382466"
FT REPEAT 30..100
FT /note="BIR"
FT /evidence="ECO:0000255"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT MOD_RES 46
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 156 AA; 17882 MW; C9F7DBCC8CB20B82 CRC64;
MSASLISALP PCGNEPPMPD EWRLYRLATR LSTFANWPFT EDCACTPERM AEAGFVHCPS
DNSPDVVKCF FCLKELEGWQ PEDDPMDEHK KHSPSCLFIA LKKKAEELTL SEFLKLDLER
TKIKMQKQMN QHIENFQAKA NVVRGHLEKL DADETQ
