ID   BIRC5_MOUSE             Reviewed;         140 AA.
AC   O70201; Q923F7; Q9WU53; Q9WU54;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Baculoviral IAP repeat-containing protein 5;
DE   AltName: Full=Apoptosis inhibitor 4;
DE   AltName: Full=Apoptosis inhibitor survivin;
DE   AltName: Full=TIAP;
GN   Name=Birc5; Synonyms=Api4, Iap4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Uren A.G., Vaux D.L.;
RT   "Mammalian inhibitor of apoptosis (IAP) homolog.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RA   Kobayashi K., Otaki M., Ogasawara T., Tokuhisa T.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
RX   PubMed=10666222;
RA   Conway E.M., Pollefeyt S., Cornelissen J., DeBaere I., Steiner-Mosonyi M.,
RA   Ong K., Baens M., Collen D., Schuh A.C.;
RT   "Three differentially expressed survivin cDNA variants encode proteins with
RT   distinct antiapoptotic functions.";
RL   Blood 95:1435-1442(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=25778398; DOI=10.1074/jbc.m114.629931;
RA   Liu Y., Lear T., Iannone O., Shiva S., Corey C., Rajbhandari S., Jerome J.,
RA   Chen B.B., Mallampalli R.K.;
RT   "The Proapoptotic F-box Protein Fbxl7 Regulates Mitochondrial Function by
RT   Mediating the Ubiquitylation and Proteasomal Degradation of Survivin.";
RL   J. Biol. Chem. 290:11843-11852(2015).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 7-118, AND PHOSPHORYLATION AT
RP   THR-34.
RX   PubMed=10949038; DOI=10.1016/s1097-2765(05)00019-5;
RA   Muchmore S.W., Chen J., Jakob C., Zakula D., Matayoshi E.D., Wu W.,
RA   Zhang H., Li F., Ng S.C., Altieri D.C.;
RT   "Crystal structure and mutagenic analysis of the inhibitor-of-apoptosis
RT   protein survivin.";
RL   Mol. Cell 6:173-182(2000).
CC   -!- FUNCTION: Multitasking protein that has dual roles in promoting cell
CC       proliferation and preventing apoptosis (PubMed:25778398). Component of
CC       a chromosome passage protein complex (CPC) which is essential for
CC       chromosome alignment and segregation during mitosis and cytokinesis (By
CC       similarity). Acts as an important regulator of the localization of this
CC       complex; directs CPC movement to different locations from the inner
CC       centromere during prometaphase to midbody during cytokinesis and
CC       participates in the organization of the center spindle by associating
CC       with polymerized microtubules (By similarity). Involved in the
CC       recruitment of CPC to centromeres during early mitosis via association
CC       with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By
CC       similarity). The complex with RAN plays a role in mitotic spindle
CC       formation by serving as a physical scaffold to help deliver the RAN
CC       effector molecule TPX2 to microtubules (By similarity). May counteract
CC       a default induction of apoptosis in G2/M phase (By similarity). The
CC       acetylated form represses STAT3 transactivation of target gene
CC       promoters (By similarity). May play a role in neoplasia. Inhibitor of
CC       CASP3 and CASP7 (By similarity). Essential for the maintenance of
CC       mitochondrial integrity and function (PubMed:25778398).
CC       {ECO:0000250|UniProtKB:O15392, ECO:0000269|PubMed:25778398}.
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       acetylated form at Lys-129 interacts with STAT3. The monomeric form
CC       deacetylated at Lys-129 interacts with XPO1/CRM1. The monomeric form
CC       interacts with XIAP/BIRC4. Both the dimeric and monomeric form can
CC       interact with DIABLO/SMAC. Interacts with BIRC6/bruce. Interacts with
CC       FBXL7; this interaction facilitates the polyubiquitination and
CC       subsequent proteasomal degradation of BIRC5 by the SCF(FBXL7) E3
CC       ubiquitin-protein ligase complex (By similarity).
CC       {ECO:0000250|UniProtKB:O15392}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus
CC       {ECO:0000250|UniProtKB:O15392}. Chromosome
CC       {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000250|UniProtKB:O15392}.
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 (By similarity).
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. Acetylation at Lys-129 directs its localization to the
CC       nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-
CC       mediated nuclear export (By similarity). {ECO:0000250|UniProtKB:E3SCZ8,
CC       ECO:0000250|UniProtKB:O15392}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Survivin 140;
CC         IsoId=O70201-1; Sequence=Displayed;
CC       Name=2; Synonyms=Survivin 121;
CC         IsoId=O70201-2; Sequence=VSP_002457;
CC       Name=3; Synonyms=Survivin 40;
CC         IsoId=O70201-3; Sequence=VSP_002455, VSP_002456;
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. Deubiquitinated by USP35 or USP38; leading to stabilization.
CC       {ECO:0000250|UniProtKB:O15392}.
CC   -!- PTM: Acetylation at Lys-129 results in its homodimerization, while
CC       deacetylation promotes the formation of monomers which heterodimerize
CC       with XPO1/CRM1 which facilitates its nuclear export. The acetylated
CC       form represses STAT3 transactivation. The dynamic equilibrium between
CC       its acetylation and deacetylation at Lys-129 determines its interaction
CC       with XPO1/CRM1, its subsequent subcellular localization, and its
CC       ability to inhibit STAT3 transactivation.
CC       {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. {ECO:0000250|UniProtKB:O15392}.
CC   -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR   EMBL; AF077349; AAD34225.1; -; mRNA.
DR   EMBL; AB013819; BAA28266.1; -; mRNA.
DR   EMBL; AF115517; AAD26199.1; -; Genomic_DNA.
DR   EMBL; AF115517; AAD26200.1; -; Genomic_DNA.
DR   EMBL; AF115517; AAD26201.1; -; Genomic_DNA.
DR   EMBL; BC004702; AAH04702.1; -; mRNA.
DR   CCDS; CCDS25694.1; -. [O70201-1]
DR   CCDS; CCDS25695.1; -. [O70201-2]
DR   RefSeq; NP_001012273.1; NM_001012273.1. [O70201-2]
DR   RefSeq; NP_033819.1; NM_009689.2. [O70201-1]
DR   PDB; 1M4M; X-ray; 2.80 A; A=1-140.
DR   PDBsum; 1M4M; -.
DR   AlphaFoldDB; O70201; -.
DR   SMR; O70201; -.
DR   BioGRID; 198150; 2.
DR   ComplexPortal; CPX-113; Survivin homodimer complex.
DR   ComplexPortal; CPX-119; Chromosomal passenger complex.
DR   STRING; 10090.ENSMUSP00000079124; -.
DR   MEROPS; I32.005; -.
DR   iPTMnet; O70201; -.
DR   PhosphoSitePlus; O70201; -.
DR   EPD; O70201; -.
DR   MaxQB; O70201; -.
DR   PaxDb; 10090-ENSMUSP00000079124; -.
DR   PeptideAtlas; O70201; -.
DR   ProteomicsDB; 273492; -. [O70201-1]
DR   ProteomicsDB; 273493; -. [O70201-2]
DR   ProteomicsDB; 273494; -. [O70201-3]
DR   Pumba; O70201; -.
DR   Antibodypedia; 1073; 1986 antibodies from 53 providers.
DR   DNASU; 11799; -.
DR   Ensembl; ENSMUST00000081387.11; ENSMUSP00000079124.5; ENSMUSG00000017716.16. [O70201-1]
DR   Ensembl; ENSMUST00000093906.5; ENSMUSP00000091433.5; ENSMUSG00000017716.16. [O70201-2]
DR   GeneID; 11799; -.
DR   KEGG; mmu:11799; -.
DR   UCSC; uc007mod.1; mouse. [O70201-1]
DR   UCSC; uc007moe.1; mouse. [O70201-2]
DR   AGR; MGI:1203517; -.
DR   CTD; 332; -.
DR   MGI; MGI:1203517; Birc5.
DR   VEuPathDB; HostDB:ENSMUSG00000017716; -.
DR   eggNOG; KOG1101; Eukaryota.
DR   GeneTree; ENSGT00510000047537; -.
DR   HOGENOM; CLU_016347_0_1_1; -.
DR   InParanoid; O70201; -.
DR   OMA; IKMYFYE; -.
DR   OrthoDB; 2882335at2759; -.
DR   PhylomeDB; O70201; -.
DR   TreeFam; TF342652; -.
DR   BioGRID-ORCS; 11799; 23 hits in 75 CRISPR screens.
DR   ChiTaRS; Birc5; mouse.
DR   EvolutionaryTrace; O70201; -.
DR   PRO; PR:O70201; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O70201; Protein.
DR   Bgee; ENSMUSG00000017716; Expressed in fetal liver hematopoietic progenitor cell and 224 other cell types or tissues.
DR   ExpressionAtlas; O70201; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0031021; C:interphase microtubule organizing center; ISS:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR   GO; GO:1990713; C:survivin complex; ISO:MGI.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:0051303; P:establishment of chromosome localization; ISS:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0007127; P:meiosis I; IDA:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0000278; P:mitotic cell cycle; NAS:ComplexPortal.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0051256; P:mitotic spindle midzone assembly; NAS:ComplexPortal.
DR   GO; GO:0007052; P:mitotic spindle organization; NAS:ComplexPortal.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; NAS:ComplexPortal.
DR   GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
DR   GO; GO:0031536; P:positive regulation of exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; NAS:ComplexPortal.
DR   GO; GO:1903490; P:positive regulation of mitotic cytokinesis; NAS:ComplexPortal.
DR   GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; NAS:ComplexPortal.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; NAS:ComplexPortal.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031503; P:protein-containing complex localization; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IMP:MGI.
DR   CDD; cd00022; BIR; 1.
DR   DisProt; DP02534; -.
DR   InterPro; IPR001370; BIR_rpt.
DR   PANTHER; PTHR46771:SF3; BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR46771; DETERIN; 1.
DR   Pfam; PF00653; BIR; 1.
DR   SMART; SM00238; BIR; 1.
DR   SUPFAM; SSF57924; Inhibitor of apoptosis (IAP) repeat; 1.
DR   PROSITE; PS50143; BIR_REPEAT_2; 1.
DR   Genevisible; O70201; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell cycle;
KW   Cell division; Centromere; Chromosome; Chromosome partition; Cytoplasm;
KW   Cytoskeleton; Kinetochore; Metal-binding; Microtubule; Mitosis; Nucleus;
KW   Phosphoprotein; Protease inhibitor; Reference proteome; Repressor;
KW   Thiol protease inhibitor; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc.
FT   CHAIN           1..140
FT                   /note="Baculoviral IAP repeat-containing protein 5"
FT                   /id="PRO_0000122357"
FT   REPEAT          18..88
FT                   /note="BIR"
FT   REGION          113..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   SITE            126
FT                   /note="Interaction with FBXL7"
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:0000269|PubMed:10949038"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
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   MOD_RES         129
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O15392"
FT   VAR_SEQ         38..40
FT                   /note="MAE -> RGA (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002455"
FT   VAR_SEQ         41..140
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002456"
FT   VAR_SEQ         114..140
FT                   /note="AKETNNKQKEFEETAKTTRQSIEQLAA -> VCMIENKD (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002457"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   HELIX           15..20
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   HELIX           35..40
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:1M4M"
FT   HELIX           98..116
FT                   /evidence="ECO:0007829|PDB:1M4M"
SQ   SEQUENCE   140 AA;  16298 MW;  26F5ABF501A6D83C CRC64;
     MGAPALPQIW QLYLKNYRIA TFKNWPFLED CACTPERMAE AGFIHCPTEN EPDLAQCFFC
     FKELEGWEPD DNPIEEHRKH SPGCAFLTVK KQMEELTVSE FLKLDRQRAK NKIAKETNNK
     QKEFEETAKT TRQSIEQLAA
//