BI52B_XENLA
ID BI52B_XENLA Reviewed; 157 AA.
AC Q804H7; B7ZQC9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Baculoviral IAP repeat-containing protein 5.2-B;
DE AltName: Full=Survivin in Xenopus {ECO:0000303|PubMed:12535669};
DE Short=SIX {ECO:0000312|EMBL:AAO20085.1};
DE AltName: Full=Survivin2-B {ECO:0000303|PubMed:15853809};
DE Short=XSurvivin2B {ECO:0000312|EMBL:BAE02679.1};
GN Name=birc5.2-b; Synonyms=six {ECO:0000303|PubMed:12535669};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO20085.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RXRA, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:12535669};
RX PubMed=12535669; DOI=10.1016/s0006-291x(02)03013-9;
RA Song K.-H., Kim T.-M., Kim H.-J., Kim J.W., Kim H.-H., Kwon H.-B.,
RA Kim W.S., Choi H.-S.;
RT "Molecular cloning and characterization of a novel inhibitor of apoptosis
RT protein from Xenopus laevis.";
RL Biochem. Biophys. Res. Commun. 301:236-242(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Oocyte;
RX PubMed=15853809; DOI=10.1111/j.1742-4658.2005.04648.x;
RA Tsuchiya Y., Murai S., Yamashita S.;
RT "Apoptosis-inhibiting activities of BIR family proteins in Xenopus egg
RT extracts.";
RL FEBS J. 272:2237-2250(2005).
RN [3] {ECO:0000312|EMBL:BAE02679.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAI69762.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH INCENP, AND IDENTIFICATION IN A COMPLEX WITH
RP AURKB; BIRC5.1; CDCA8; CDCA9 AND INCENP.
RX PubMed=17199039; DOI=10.1016/j.devcel.2006.11.001;
RA Kelly A.E., Sampath S.C., Maniar T.A., Woo E.M., Chait B.T., Funabiki H.;
RT "Chromosomal enrichment and activation of the aurora B pathway are coupled
RT to spatially regulate spindle assembly.";
RL Dev. Cell 12:31-43(2007).
RN [5] {ECO:0000305}
RP REVIEW.
RX PubMed=16344111; DOI=10.1016/s0074-7696(05)47002-3;
RA Wheatley S.P., McNeish I.A.;
RT "Survivin: a protein with dual roles in mitosis and apoptosis.";
RL Int. Rev. Cytol. 247:35-88(2005).
CC -!- FUNCTION: Does not appear to exhibit anti-apoptotic activity. Plays a
CC role in increasing blood vessel size during development (By
CC similarity). 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.
CC {ECO:0000250|UniProtKB:Q50L39, ECO:0000269|PubMed:15853809,
CC ECO:0000269|PubMed:16344111, ECO:0000269|PubMed:17199039}.
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.
CC {ECO:0000269|PubMed:12535669, ECO:0000269|PubMed:17199039}.
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 -!- TISSUE SPECIFICITY: Exhibits strong and homogeneous expression in
CC developing oocytes. In embryos, expressed in the animal hemisphere from
CC one-cell to yolk plug stages, and highly expressed in the future brain
CC and dorsal region of the neural tube at the neurula stage and early
CC tail-bud stage. At tadpole stages, expression is restricted at a low
CC level to the head region. {ECO:0000269|PubMed:12535669}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. In
CC oocytes, expression gradually decreases throughout successive oocyte
CC stages. Expression is maintained up to the larval stage (stage 35). Not
CC expressed in adults, with the exception of expression in the ovary and
CC weak expression in the testis. {ECO:0000269|PubMed:12535669}.
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}.
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DR EMBL; AY174765; AAO20085.1; -; mRNA.
DR EMBL; AB197250; BAE02679.1; -; mRNA.
DR EMBL; BC169762; AAI69762.1; -; mRNA.
DR EMBL; BC169764; AAI69764.1; -; mRNA.
DR RefSeq; NP_001082412.1; NM_001088943.1.
DR AlphaFoldDB; Q804H7; -.
DR SMR; Q804H7; -.
DR MEROPS; I32.005; -.
DR GeneID; 398454; -.
DR KEGG; xla:398454; -.
DR CTD; 398454; -.
DR Xenbase; XB-GENE-966748; birc5l.L.
DR OrthoDB; 1404665at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 398454; Expressed in blastula and 17 other tissues.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI: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: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 1: Evidence at protein 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..157
FT /note="Baculoviral IAP repeat-containing protein 5.2-B"
FT /id="PRO_0000382465"
FT REPEAT 31..101
FT /note="BIR"
FT /evidence="ECO:0000255"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 97
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 47
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
FT CONFLICT 122
FT /note="M -> T (in Ref. 3; AAI69764/AAI69762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 18341 MW; 1ED9C0B01E0AE627 CRC64;
MLSISPIVSL RRCDNEPSMP DEWRLYNLAT RLRTFSNWPF TEDCACTPER MAEAGFVHCP
TDNSPDVVKC FFCLKELEGW QPEDDPMDEH KKHSPSCLFI ALKKKAEELT LSEFLKLDLE
HMKIKMQKQM NLHIERFQAK ANEVRGHLEK LDADETQ
