BI52A_XENLA
ID BI52A_XENLA Reviewed; 157 AA.
AC Q50L39; Q5XGX1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Baculoviral IAP repeat-containing protein 5.2-A;
DE AltName: Full=Survivin2-A {ECO:0000303|PubMed:15853809};
DE Short=xSurvivin2A {ECO:0000312|EMBL:BAD98266.1};
DE Short=xSvv2/SIX {ECO:0000303|PubMed:15853809};
DE AltName: Full=xL_Survivin1 {ECO:0000303|PubMed:16759290};
DE Short=Su1 {ECO:0000303|PubMed:16759290};
GN Name=birc5.2-a;
GN Synonyms=su1 {ECO:0000303|PubMed:16759290},
GN svv2 {ECO:0000303|PubMed:15853809};
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:BAD98266.1}
RP NUCLEOTIDE SEQUENCE [MRNA], LACK OF ANTI-APOPTOTIC FUNCTION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:15853809};
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 [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF THR-47 AND CYS-97.
RC TISSUE=Oocyte {ECO:0000269|PubMed:16759290};
RX PubMed=16759290; DOI=10.1111/j.1432-0436.2006.00073.x;
RA Du Pasquier D., Phung A.C., Ymlahi-Ouazzani Q., Sinzelle L., Ballagny C.,
RA Bronchain O., Du Pasquier L., Mazabraud A.;
RT "Survivin increased vascular development during Xenopus ontogenesis.";
RL Differentiation 74:244-253(2006).
RN [3] {ECO:0000312|EMBL:AAH84306.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH84306.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) 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 (By similarity). Does
CC not appear to exhibit anti-apoptotic activity. Plays a role in
CC increasing blood vessel size during development.
CC {ECO:0000250|UniProtKB:Q804H7, ECO:0000269|PubMed:15853809,
CC ECO:0000269|PubMed:16759290}.
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 -!- TISSUE SPECIFICITY: Highly expressed in vascular endothelial cells of
CC tadpoles. {ECO:0000269|PubMed:16759290}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Although many papers suggest that Xenopus survivins are not expressed
CC in adults, PubMed:16759290 reports an increase in expression during
CC metamorphosis, and expression in multiple adult tissues.
CC {ECO:0000269|PubMed:15853809, ECO:0000269|PubMed:16759290}.
CC -!- DOMAIN: The BIR2 domain is required for vascular development.
CC {ECO:0000269|PubMed:16759290}.
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=AAH84306.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB197249; BAD98266.1; -; mRNA.
DR EMBL; BC084306; AAH84306.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q50L39; -.
DR SMR; Q50L39; -.
DR MEROPS; I32.005; -.
DR MaxQB; Q50L39; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0032133; C:chromosome passenger complex; ISS: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; 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:0001944; P:vasculature development; IMP: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-A"
FT /id="PRO_0000382464"
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 MUTAGEN 47
FT /note="T->A: Unable to increase blood vessel size."
FT /evidence="ECO:0000269|PubMed:16759290"
FT MUTAGEN 47
FT /note="T->E: Mimics phosphorylation. Only moderately able
FT to increase blood vessel size."
FT /evidence="ECO:0000269|PubMed:16759290"
FT MUTAGEN 97
FT /note="C->A: Unable to increase blood vessel size."
FT /evidence="ECO:0000269|PubMed:16759290"
FT CONFLICT 2
FT /note="M -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 18329 MW; 018D789D50106635 CRC64;
MMSISPIVSL RRCDNEPSMP DEWRLYKLAS RLRTFSNWPF TEDCACTPER MAEAGFVHCP
TDNSPDVVKC FFCLKELEGW QPEDDPMDEH KKHSPSCLFI ALKKKAEELT LSEFLKLDLE
HTKIKMQKQM NLHIERFQAK ANEVRGHLEK LDADETQ
