BIRC5_CAVPO
ID BIRC5_CAVPO Reviewed; 142 AA.
AC E3SCZ8;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Baculoviral IAP repeat-containing protein 5 {ECO:0000305};
DE AltName: Full=Apoptosis inhibitor survivin {ECO:0000303|PubMed:20727954, ECO:0000303|PubMed:21364656};
GN Name=BIRC5 {ECO:0000303|PubMed:20627126, ECO:0000312|EMBL:ACZ18223.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1] {ECO:0000312|EMBL:ACZ18223.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTAGENESIS OF PHE-93; LEU-96 AND LEU-98, AND PHYLOGENETIC
RP ANALYSIS.
RC TISSUE=Spleen {ECO:0000303|PubMed:20727954};
RX PubMed=20727954; DOI=10.1016/j.gene.2010.08.007;
RA Habtemichael N., Wunsch D., Bier C., Tillmann S., Unruhe B.,
RA Frauenknecht K., Heinrich U.R., Mann W.J., Stauber R.H., Knauer S.K.;
RT "Cloning and functional characterization of the guinea pig apoptosis
RT inhibitor protein Survivin.";
RL Gene 469:9-17(2010).
RN [2] {ECO:0000312|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000312|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21364656; DOI=10.1038/cddis.2010.25;
RA Knauer S.K., Heinrich U.R., Bier C., Habtemichael N., Docter D.,
RA Helling K., Mann W.J., Stauber R.H.;
RT "An otoprotective role for the apoptosis inhibitor protein survivin.";
RL Cell Death Dis. 1:E51-E51(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20627126; DOI=10.1016/j.mcn.2010.07.003;
RA Habtemichael N., Heinrich U.R., Knauer S.K., Schmidtmann I., Bier C.,
RA Docter D., Brochhausen C., Helling K., Brieger J., Stauber R.H., Mann W.J.;
RT "Expression analysis suggests a potential cytoprotective role of Birc5 in
RT the inner ear.";
RL Mol. Cell. Neurosci. 45:297-305(2010).
CC -!- FUNCTION: Multitasking protein that has dual roles in promoting cell
CC proliferation and preventing apoptosis (PubMed:20727954,
CC PubMed:21364656, PubMed:20627126). Component of a chromosome passage
CC protein complex (CPC) which is essential for chromosome alignment and
CC segregation during mitosis and cytokinesis (PubMed:20727954). Acts as
CC an important regulator of the localization of this complex; directs CPC
CC movement to different locations from the inner centromere during
CC prometaphase to midbody during cytokinesis and participates in the
CC organization of the center spindle by associating with polymerized
CC microtubules (By similarity). Involved in the recruitment of CPC to
CC centromeres during early mitosis via association with histone H3
CC phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The
CC complex with RAN plays a role in mitotic spindle formation by serving
CC as a physical scaffold to help deliver the RAN effector molecule TPX2
CC to microtubules (By similarity). May counteract a default induction of
CC apoptosis in G2/M phase (By similarity). The acetylated form represses
CC STAT3 transactivation of target gene promoters (By similarity). May
CC play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity).
CC Essential for the maintenance of mitochondrial integrity and function
CC (By similarity). {ECO:0000250|UniProtKB:O15392,
CC ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
CC ECO:0000269|PubMed:21364656}.
CC -!- SUBUNIT: Monomer or homodimer. Exists as a homodimer in the apo state
CC and as a monomer in the CPC-bound state. The monomer protects cells
CC against apoptosis more efficiently than the dimer. Only the dimeric
CC form is capable of enhancing tubulin stability in cells. When
CC phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex
CC binds pro-CASP9, as well as active CASP9, but much less efficiently.
CC Component of the chromosomal passenger complex (CPC) composed of at
CC least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the
CC complex forms a triple-helix bundle-based subcomplex with INCENP and
CC CDCA8. Interacts with JTB. Interacts (via BIR domain) with histone H3
CC phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts with
CC GTP-bound RAN in both the S and M phases of the cell cycle. Interacts
CC with USP9X. Interacts with tubulin. Interacts with BIRC2/c-IAP1. The
CC monomeric form interacts with XIAP/BIRC4. Both the dimeric and
CC monomeric form can interact with DIABLO/SMAC. Interacts with
CC BIRC6/bruce. Interacts with FBXL7; this interaction facilitates the
CC polyubiquitination and subsequent proteasomal degradation of BIRC5 by
CC the SCF(FBXL7) E3 ubiquitin-protein ligase complex (By similarity).
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126,
CC ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Nucleus
CC {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
CC ECO:0000269|PubMed:21364656}. Chromosome
CC {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere
CC {ECO:0000269|PubMed:20727954}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:20727954}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000269|PubMed:20727954}.
CC Note=Localizes at the centromeres from prophase to metaphase, at the
CC spindle midzone during anaphase and a the midbody during telophase and
CC cytokinesis. Accumulates in the nucleus upon treatment with leptomycin
CC B (LMB), a XPO1/CRM1 nuclear export inhibitor (PubMed:20727954).
CC Localizes on chromosome arms and inner centromeres from prophase
CC through metaphase. Localizes to kinetochores in metaphase, distributes
CC to the midzone microtubules in anaphase and at telophase, localizes
CC exclusively to the midbody. Colocalizes with AURKB at mitotic
CC chromosomes (By similarity). {ECO:0000250|UniProtKB:O15392,
CC ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
CC ECO:0000269|PubMed:21364656}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lung, brain, heart, kidney and
CC intestine (at protein level) (PubMed:20727954). Expressed in cochlea
CC including the organ of Corti, the lateral wall, the interdental cells
CC of the Limbus as well as in cells of the cochlear nerve and the spiral
CC ganglions (at protein level) (PubMed:20727954, PubMed:21364656,
CC PubMed:20627126). Also expressed in Schwann cells (at protein level)
CC (PubMed:21364656, PubMed:20627126). Not expressed in cells of the inner
CC and outer sulcus or the Reissner's membrane (at protein level)
CC (PubMed:20727954, PubMed:21364656, PubMed:20627126).
CC {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
CC ECO:0000269|PubMed:21364656}.
CC -!- INDUCTION: Expression is up-regulated in the spiral ligament and nerve
CC fibers of the cochlea upon moderate noise exposure causing only a
CC temporary hearing impairment. Expression is down-regulated in the organ
CC of Corti, the spiral ganglion, the stria vascularis and the spiral
CC ligament of the cochlea upon intratympanic injection of aminoglycoside
CC antibiotic gentamicin inducing cell damage and permanent hearing loss.
CC {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:21364656}.
CC -!- DOMAIN: The BIR repeat is necessary and sufficient for LAMTOR5 binding.
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex,
CC leading to its degradation. Ubiquitination is required for centrosomal
CC targeting. {ECO:0000250|UniProtKB:O15392}.
CC -!- PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction
CC with INCENP and localization to mitotic chromosomes. Phosphorylation at
CC Thr-48 by CK2 is critical for its mitotic and anti-apoptotic
CC activities. Phosphorylation at Thr-34 by CDK15 is critical for its
CC anti-apoptotic activity. Phosphorylation at Ser-20 by AURKC is critical
CC for regulation of proper chromosome alignment and segregation, and
CC possibly cytokinesis. {ECO:0000250|UniProtKB:O15392}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR EMBL; GQ496319; ACZ18223.1; -; mRNA.
DR EMBL; AAKN02047321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001186646.1; NM_001199717.1.
DR AlphaFoldDB; E3SCZ8; -.
DR SMR; E3SCZ8; -.
DR STRING; 10141.ENSCPOP00000016661; -.
DR MEROPS; I32.005; -.
DR Ensembl; ENSCPOT00000039725; ENSCPOP00000023297; ENSCPOG00000040469.
DR GeneID; 100527953; -.
DR KEGG; cpoc:100527953; -.
DR CTD; 332; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00510000047537; -.
DR HOGENOM; CLU_016347_0_1_1; -.
DR InParanoid; E3SCZ8; -.
DR OMA; FEGWPFD; -.
DR OrthoDB; 1404665at2759; -.
DR TreeFam; TF342652; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000040469; Expressed in testis and 13 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; 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:0007127; P:meiosis I; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEP: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 Acetylation; Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; Metal-binding;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Protease inhibitor;
KW Reference proteome; Repressor; Stress response; Thiol protease inhibitor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..142
FT /note="Baculoviral IAP repeat-containing protein 5"
FT /id="PRO_0000440217"
FT REPEAT 18..88
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 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT SITE 126
FT /note="Interaction with FBXL7"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 20
FT /note="Phosphoserine; by AURKC"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 34
FT /note="Phosphothreonine; by CDK1 and CDK15"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 48
FT /note="Phosphothreonine; by CK2; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 117
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MUTAGEN 93
FT /note="F->P: Disrupts nuclear export and loss of
FT cytoprotection; when associated with A-96 and A-98."
FT /evidence="ECO:0000269|PubMed:20727954"
FT MUTAGEN 96
FT /note="L->A: Disrupts nuclear export and loss of
FT cytoprotection; when associated with P-93 and A-98."
FT /evidence="ECO:0000269|PubMed:20727954"
FT MUTAGEN 98
FT /note="L->A: Disrupts nuclear export and loss of
FT cytoprotection; when associated with P-93 and A-96."
FT /evidence="ECO:0000269|PubMed:20727954"
SQ SEQUENCE 142 AA; 16356 MW; 791171160207C2C8 CRC64;
MGAPSLPRAW QLYLKEHRVS TFKNWPFVNG CSCTPERMAE AGFIHCPTEN EPDLAQCFFC
FKELEGWEPD DNPIEEHKKH SSGCAFLSVK KQFEELTLSE FLKLDKERAK NKIAKETNSK
QKEFEETAAK VRQAMEQLAA LE
