ID BIRC6_HUMAN Reviewed; 4857 AA. AC Q9NR09; Q9ULD1; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 3. DT 27-MAR-2024, entry version 200. DE RecName: Full=Baculoviral IAP repeat-containing protein 6; DE EC=2.3.2.27 {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:18329369}; DE AltName: Full=BIR repeat-containing ubiquitin-conjugating enzyme; DE Short=BRUCE; DE AltName: Full=RING-type E3 ubiquitin transferase BIRC6 {ECO:0000305}; DE AltName: Full=Ubiquitin-conjugating BIR domain enzyme apollon; DE Short=APOLLON; GN Name=BIRC6; Synonyms=KIAA1289; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-4857. RC TISSUE=Brain; RX PubMed=10544019; DOI=10.1006/bbrc.1999.1585; RA Chen Z., Naito M., Hori S., Mashima T., Yamori T., Tsuruo T.; RT "A human IAP-family gene, apollon, expressed in human brain cancer cells."; RL Biochem. Biophys. Res. Commun. 264:847-854(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2063-4857. RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP INTERACTION WITH RNF41, UBIQUITINATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=14765125; DOI=10.1038/sj.emboj.7600075; RA Qiu X.B., Markant S.L., Yuan J., Goldberg A.L.; RT "Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway RT for triggering apoptosis."; RL EMBO J. 23:800-810(2004). RN [6] RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, DOMAIN BIR, AND INTERACTION WITH RP HTRA2; CASP3; CASP6; CASP7; CASP9 AND DIABLO/SMAC. RX PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018; RA Bartke T., Pohl C., Pyrowolakis G., Jentsch S.; RT "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin RT ligase."; RL Mol. Cell 14:801-811(2004). RN [7] RP REVIEW ON FUNCTION. RX PubMed=15340445; DOI=10.1038/ncb0904-804; RA Martin S.J.; RT "An Apollon vista of death and destruction."; RL Nat. Cell Biol. 6:804-806(2004). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, RP UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH KIF23/MKLP1; RP USP8/UBPY; BIRC5/SURVIVIN; MAP2K1/MEK1; RAB8A/RAB8; RAB11A/RAB11; PLK1; RP EXOC3/SEC6 AND EXOC4/SEC8. RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012; RA Pohl C., Jentsch S.; RT "Final stages of cytokinesis and midbody ring formation are controlled by RT BRUCE."; RL Cell 132:832-845(2008). RN [10] RP REVIEW ON FUNCTION. RX PubMed=18414036; DOI=10.4161/cc.7.8.5783; RA Dubrez-Daloz L., Dupoux A., Cartier J.; RT "IAPs: more than just inhibitors of apoptosis proteins."; RL Cell Cycle 7:1036-1046(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-581; SER-590; RP SER-2222; SER-2955; THR-3931 AND SER-4023, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND THR-1710, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 4498-4820. RG Structural genomics consortium (SGC); RT "Ubc domain of the ubiquitin-protein ligase baculoviral IAP repeat- RT containing protein 6."; RL Submitted (APR-2008) to the PDB data bank. RN [20] {ECO:0007744|PDB:3CEG} RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 4498-4820. RX PubMed=22496338; DOI=10.1074/mcp.o111.013706; RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V., RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H., RA Raught B., Dhe-Paganon S.; RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure- RT function screen."; RL Mol. Cell. Proteomics 11:329-341(2012). CC -!- FUNCTION: Anti-apoptotic protein which can regulate cell death by CC controlling caspases and by acting as an E3 ubiquitin-protein ligase. CC Has an unusual ubiquitin conjugation system in that it could combine in CC a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase CC (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its targets CC include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CC CASP9. Important regulator for the final stages of cytokinesis. Crucial CC for normal vesicle targeting to the site of abscission, but also for CC the integrity of the midbody and the midbody ring, and its striking CC ubiquitin modification. {ECO:0000269|PubMed:14765125, CC ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:18329369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:14765125, CC ECO:0000269|PubMed:18329369}; CC -!- ACTIVITY REGULATION: Inhibited by DIABLO/SMAC, HTRA2, CASP3, CASP6, CC CASP7 and CASP9. {ECO:0000269|PubMed:15200957}. CC -!- SUBUNIT: Homodimer. Binds the activated, processed forms of CASP3, CC CASP6, CASP7 and CASP9. Interacts with RNF41, DIABLO/SMAC, HTRA2, CC KIF23/MKLP1, USP8/UBPY, BIRC5/survivin, MAP2K1/MEK1, RAB8A/RAB8, CC RAB11A/RAB11, PLK1, EXOC3/SEC6 and EXOC4/SEC8. CC {ECO:0000269|PubMed:14765125, ECO:0000269|PubMed:15200957, CC ECO:0000269|PubMed:18329369}. CC -!- INTERACTION: CC Q9NR09; Q96A65: EXOC4; NbExp=3; IntAct=EBI-1765160, EBI-355383; CC Q9NR09; Q02241: KIF23; NbExp=4; IntAct=EBI-1765160, EBI-306852; CC Q9NR09; Q02750: MAP2K1; NbExp=2; IntAct=EBI-1765160, EBI-492564; CC Q9NR09; P53350: PLK1; NbExp=4; IntAct=EBI-1765160, EBI-476768; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18329369}. Endosome {ECO:0000269|PubMed:18329369}. CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18329369}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:18329369}. Midbody, Midbody ring CC {ECO:0000269|PubMed:18329369}. Note=Exhibits cell cycle-dependent CC localization. Concentrates in a pericentriolar compartment in CC interphase, moves partially to spindle poles in metaphase, and finally CC localizes to the spindle midzone and the midbody in telophase and CC during cytokinesis. On the midbody, localizes to the midbody ring, also CC called Flemming body (PubMed:18329369). In interphase cells, localizes CC to the trans-Golgi network membrane and endosomes. During cytokinesis, CC a fraction moves to the midzone where it specifically arrives at the CC midbody ring. After abscission completion, travels with the midbody CC remnant into one daughter cell, and remains bound to it until a new CC midbody ring is formed during the next cell division (PubMed:18329369). CC {ECO:0000269|PubMed:18329369}. CC -!- TISSUE SPECIFICITY: Expressed in brain cancer cells. CC -!- DOMAIN: The BIR domain is essential for its antiapoptotic function and CC is important for binding to DIABLO/SMAC and CASP9. CC {ECO:0000269|PubMed:15200957}. CC -!- PTM: Ubiquitinated. Ubiquitination is mediated by the RNF41 E3 ligase CC and leads to proteasomal degradation, impairing inhibition of CC apoptosis. Deubiquitinated by USP8/UBPY. {ECO:0000269|PubMed:14765125, CC ECO:0000269|PubMed:18329369}. CC -!- SIMILARITY: In the C-terminal section; belongs to the ubiquitin- CC conjugating enzyme family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86603.2; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/798/BIRC6"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC079837; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133243; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133245; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133246; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF265555; AAF75772.1; -; mRNA. DR EMBL; AB033115; BAA86603.2; ALT_FRAME; mRNA. DR CCDS; CCDS33175.2; -. DR RefSeq; NP_057336.3; NM_016252.3. DR PDB; 3CEG; X-ray; 2.01 A; A/B=4498-4820. DR PDB; 8ATM; EM; 3.30 A; A/B=1-4857. DR PDB; 8ATO; EM; 3.00 A; A/B=1-4857. DR PDB; 8ATU; EM; 3.30 A; A/B=1-4857. DR PDB; 8ATX; EM; 7.00 A; A/B=1-4857. DR PDB; 8AUK; EM; 6.20 A; A/B=1-4857. DR PDB; 8AUW; EM; 7.20 A; A/B=1-4857. DR PDB; 8E2D; EM; 2.07 A; A/B=1-4857. DR PDB; 8E2E; EM; 1.98 A; A/B=1-4857. DR PDB; 8E2F; EM; 2.47 A; A=1-4857. DR PDB; 8E2G; EM; 2.99 A; A=1-4857. DR PDB; 8E2H; EM; 2.30 A; A=1-4857. DR PDB; 8E2I; EM; 3.04 A; A/B=1-4857. DR PDB; 8E2K; EM; 3.21 A; A/B=1-4857. DR PDBsum; 3CEG; -. DR PDBsum; 8ATM; -. DR PDBsum; 8ATO; -. DR PDBsum; 8ATU; -. DR PDBsum; 8ATX; -. DR PDBsum; 8AUK; -. DR PDBsum; 8AUW; -. DR PDBsum; 8E2D; -. DR PDBsum; 8E2E; -. DR PDBsum; 8E2F; -. DR PDBsum; 8E2G; -. DR PDBsum; 8E2H; -. DR PDBsum; 8E2I; -. DR PDBsum; 8E2K; -. DR SMR; Q9NR09; -. DR BioGRID; 121521; 232. DR IntAct; Q9NR09; 55. DR MINT; Q9NR09; -. DR STRING; 9606.ENSP00000393596; -. DR MEROPS; I32.006; -. DR TCDB; 8.A.217.1.1; the apoptosis cell death regulator (acdr) family. DR GlyCosmos; Q9NR09; 1 site, 1 glycan. DR GlyGen; Q9NR09; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9NR09; -. DR PhosphoSitePlus; Q9NR09; -. DR SwissPalm; Q9NR09; -. DR BioMuta; BIRC6; -. DR DMDM; 313104079; -. DR EPD; Q9NR09; -. DR jPOST; Q9NR09; -. DR MassIVE; Q9NR09; -. DR MaxQB; Q9NR09; -. DR PaxDb; 9606-ENSP00000393596; -. DR PeptideAtlas; Q9NR09; -. DR ProteomicsDB; 82241; -. DR Pumba; Q9NR09; -. DR Antibodypedia; 29188; 252 antibodies from 31 providers. DR DNASU; 57448; -. DR Ensembl; ENST00000421745.7; ENSP00000393596.2; ENSG00000115760.16. DR GeneID; 57448; -. DR KEGG; hsa:57448; -. DR MANE-Select; ENST00000421745.7; ENSP00000393596.2; NM_016252.4; NP_057336.3. DR UCSC; uc010ezu.4; human. DR AGR; HGNC:13516; -. DR CTD; 57448; -. DR DisGeNET; 57448; -. DR GeneCards; BIRC6; -. DR HGNC; HGNC:13516; BIRC6. DR HPA; ENSG00000115760; Low tissue specificity. DR MIM; 605638; gene. DR neXtProt; NX_Q9NR09; -. DR OpenTargets; ENSG00000115760; -. DR PharmGKB; PA25363; -. DR VEuPathDB; HostDB:ENSG00000115760; -. DR eggNOG; KOG0895; Eukaryota. DR eggNOG; KOG1101; Eukaryota. DR GeneTree; ENSGT00940000156126; -. DR HOGENOM; CLU_000111_1_0_1; -. DR InParanoid; Q9NR09; -. DR OMA; LDAQCKL; -. DR OrthoDB; 117123at2759; -. DR PhylomeDB; Q9NR09; -. DR TreeFam; TF105357; -. DR PathwayCommons; Q9NR09; -. DR Reactome; R-HSA-9700645; ALK mutants bind TKIs. DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants. DR SignaLink; Q9NR09; -. DR SIGNOR; Q9NR09; -. DR BioGRID-ORCS; 57448; 223 hits in 1208 CRISPR screens. DR ChiTaRS; BIRC6; human. DR EvolutionaryTrace; Q9NR09; -. DR GeneWiki; BIRC6; -. DR GenomeRNAi; 57448; -. DR Pharos; Q9NR09; Tbio. DR PRO; PR:Q9NR09; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9NR09; Protein. DR Bgee; ENSG00000115760; Expressed in epithelial cell of pancreas and 196 other cell types or tissues. DR ExpressionAtlas; Q9NR09; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IMP:UniProtKB. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0060711; P:labyrinthine layer development; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; TAS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; TAS:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:UniProtKB. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB. DR GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl. DR CDD; cd00022; BIR; 1. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR IDEAL; IID00636; -. DR InterPro; IPR001370; BIR_rpt. DR InterPro; IPR022103; BIRC6. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR46116; (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME; 1. DR PANTHER; PTHR46116:SF39; BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 6; 1. DR Pfam; PF00653; BIR; 1. DR Pfam; PF12356; BIRC6; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00238; BIR; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF57924; Inhibitor of apoptosis (IAP) repeat; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS50143; BIR_REPEAT_2; 1. DR PROSITE; PS50127; UBC_2; 1. DR Genevisible; Q9NR09; HS. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Cell cycle; Cell division; Cytoplasm; KW Cytoskeleton; Endosome; Golgi apparatus; Membrane; Mitosis; Phosphoprotein; KW Protease inhibitor; Reference proteome; Thiol protease inhibitor; KW Transferase; Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..4857 FT /note="Baculoviral IAP repeat-containing protein 6" FT /id="PRO_0000122361" FT REPEAT 284..358 FT /note="BIR" FT DOMAIN 4573..4740 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT REGION 465..498 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 579..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 984..1004 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1053..1073 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2945..2973 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3923..3949 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4260..4283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4835..4857 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 988..1004 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1054..1073 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 4666 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT MOD_RES 473 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88738" FT MOD_RES 480 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 482 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88738" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 590 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1710 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 2222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2955 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 3931 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 4023 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CONFLICT 2319 FT /note="L -> F (in Ref. 3; BAA86603)" FT /evidence="ECO:0000305" FT CONFLICT 2674 FT /note="T -> S (in Ref. 2; AAF75772)" FT /evidence="ECO:0000305" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 77..80 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 121..124 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 147..150 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 159..166 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 167..178 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 189..203 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 218..224 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 225..242 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 248..262 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 286..292 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 306..311 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 326..328 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 329..331 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 344..351 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 356..360 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 368..372 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 400..404 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 407..413 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 414..417 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 419..425 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 431..436 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 504..513 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 566..574 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 626..634 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 716..721 FT /evidence="ECO:0007829|PDB:8E2G" FT HELIX 725..728 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 731..738 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 740..751 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 823..829 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 844..849 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 912..916 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 917..920 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 921..925 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 940..945 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 947..949 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 951..956 FT /evidence="ECO:0007829|PDB:8E2G" FT STRAND 961..965 FT /evidence="ECO:0007829|PDB:8E2G" FT TURN 1012..1014 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1019..1027 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1031..1033 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1039..1041 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1046..1048 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1051..1054 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1056..1058 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1061..1066 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1070..1072 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1074..1079 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 1083..1086 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1089..1094 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1101..1110 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1120..1126 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1172..1176 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1178..1180 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1181..1187 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1188..1191 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1199..1203 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1206..1209 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1219..1226 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1292..1295 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1296..1306 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1314..1323 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1325..1335 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1340..1342 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1346..1363 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1377..1383 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1385..1394 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1398..1413 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1424..1435 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1436..1441 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1445..1458 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 1459..1462 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1463..1483 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1487..1495 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1562..1565 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1569..1574 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1578..1580 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1777..1781 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 1784..1786 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1788..1806 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1812..1822 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 1824..1827 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1829..1835 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 1837..1839 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1842..1844 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1852..1862 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1871..1874 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 1877..1883 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 1886..1888 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2012..2017 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2020..2040 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 2046..2048 FT /evidence="ECO:0007829|PDB:8E2F" FT STRAND 2049..2055 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2056..2066 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 2067..2069 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2072..2086 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2092..2104 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2114..2127 FT /evidence="ECO:0007829|PDB:8E2F" FT TURN 2128..2130 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2133..2146 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2147..2149 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2165..2181 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2326..2340 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2348..2364 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2569..2573 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 2577..2598 FT /evidence="ECO:0007829|PDB:8E2F" FT HELIX 3429..3440 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3446..3468 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3484..3487 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3491..3506 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3513..3516 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3519..3531 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3537..3552 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3554..3564 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3607..3616 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3620..3628 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3631..3643 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3680..3694 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3697..3703 FT /evidence="ECO:0007829|PDB:8E2H" FT TURN 3706..3708 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3709..3719 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3753..3771 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3775..3789 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3807..3815 FT /evidence="ECO:0007829|PDB:8E2H" FT STRAND 3821..3827 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3847..3849 FT /evidence="ECO:0007829|PDB:8E2H" FT STRAND 3855..3861 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3866..3873 FT /evidence="ECO:0007829|PDB:8E2H" FT STRAND 3966..3968 FT /evidence="ECO:0007829|PDB:8E2H" FT TURN 3971..3974 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 3983..3992 FT /evidence="ECO:0007829|PDB:8E2H" FT STRAND 4000..4007 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4070..4076 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4079..4084 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4155..4164 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4170..4174 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4178..4188 FT /evidence="ECO:0007829|PDB:8E2H" FT STRAND 4195..4197 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4209..4211 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4212..4222 FT /evidence="ECO:0007829|PDB:8E2H" FT STRAND 4226..4228 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4229..4241 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4243..4255 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4306..4331 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4360..4366 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4369..4377 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4382..4385 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4389..4403 FT /evidence="ECO:0007829|PDB:8E2H" FT TURN 4406..4408 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4409..4411 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4433..4454 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4474..4498 FT /evidence="ECO:0007829|PDB:8E2H" FT HELIX 4524..4533 FT /evidence="ECO:0007829|PDB:3CEG" FT STRAND 4536..4540 FT /evidence="ECO:0007829|PDB:3CEG" FT STRAND 4543..4545 FT /evidence="ECO:0007829|PDB:3CEG" FT STRAND 4551..4555 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4560..4564 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4572..4588 FT /evidence="ECO:0007829|PDB:3CEG" FT STRAND 4597..4604 FT /evidence="ECO:0007829|PDB:3CEG" FT STRAND 4608..4615 FT /evidence="ECO:0007829|PDB:3CEG" FT STRAND 4625..4631 FT /evidence="ECO:0007829|PDB:3CEG" FT TURN 4634..4638 FT /evidence="ECO:0007829|PDB:3CEG" FT STRAND 4642..4645 FT /evidence="ECO:0007829|PDB:3CEG" FT TURN 4649..4652 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4668..4670 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4677..4679 FT /evidence="ECO:0007829|PDB:3CEG" FT TURN 4683..4685 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4688..4698 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4704..4707 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4711..4714 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4718..4738 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4741..4745 FT /evidence="ECO:0007829|PDB:3CEG" FT TURN 4749..4751 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4752..4777 FT /evidence="ECO:0007829|PDB:3CEG" FT HELIX 4788..4810 FT /evidence="ECO:0007829|PDB:3CEG" SQ SEQUENCE 4857 AA; 530269 MW; ACA0EB5B3EFBA0C0 CRC64; MVTGGGAAPP GTVTEPLPSV IVLSAGRKMA AAAAAASGPG CSSAAGAGAA GVSEWLVLRD GCMHCDADGL HSLSYHPALN AILAVTSRGT IKVIDGTSGA TLQASALSAK PGGQVKCQYI SAVDKVIFVD DYAVGCRKDL NGILLLDTAL QTPVSKQDDV VQLELPVTEA QQLLSACLEK VDISSTEGYD LFITQLKDGL KNTSHETAAN HKVAKWATVT FHLPHHVLKS IASAIVNELK KINQNVAALP VASSVMDRLS YLLPSARPEL GVGPGRSVDR SLMYSEANRR ETFTSWPHVG YRWAQPDPMA QAGFYHQPAS SGDDRAMCFT CSVCLVCWEP TDEPWSEHER HSPNCPFVKG EHTQNVPLSV TLATSPAQFP CTDGTDRISC FGSGSCPHFL AAATKRGKIC IWDVSKLMKV HLKFEINAYD PAIVQQLILS GDPSSGVDSR RPTLAWLEDS SSCSDIPKLE GDSDDLLEDS DSEEHSRSDS VTGHTSQKEA MEVSLDITAL SILQQPEKLQ WEIVANVLED TVKDLEELGA NPCLTNSKSE KTKEKHQEQH NIPFPCLLAG GLLTYKSPAT SPISSNSHRS LDGLSRTQGE SISEQGSTDN ESCTNSELNS PLVRRTLPVL LLYSIKESDE KAGKIFSQMN NIMSKSLHDD GFTVPQIIEM ELDSQEQLLL QDPPVTYIQQ FADAAANLTS PDSEKWNSVF PKPGTLVQCL RLPKFAEEEN LCIDSITPCA DGIHLLVGLR TCPVESLSAI NQVEALNNLN KLNSALCNRR KGELESNLAV VNGANISVIQ HESPADVQTP LIIQPEQRNV SGGYLVLYKM NYATRIVTLE EEPIKIQHIK DPQDTITSLI LLPPDILDNR EDDCEEPIED MQLTSKNGFE REKTSDISTL GHLVITTQGG YVKILDLSNF EILAKVEPPK KEGTEEQDTF VSVIYCSGTD RLCACTKGGE LHFLQIGGTC DDIDEADILV DGSLSKGIEP SSEGSKPLSN PSSPGISGVD LLVDQPFTLE ILTSLVELTR FETLTPRFSA TVPPCWVEVQ QEQQQRRHPQ HLHQQHHGDA AQHTRTWKLQ TDSNSWDEHV FELVLPKACM VGHVDFKFVL NSNITNIPQI QVTLLKNKAP GLGKVNALNI EVEQNGKPSL VDLNEEMQHM DVEESQCLRL CPFLEDHKED ILCGPVWLAS GLDLSGHAGM LTLTSPKLVK GMAGGKYRSF LIHVKAVNER GTEEICNGGM RPVVRLPSLK HQSNKGYSLA SLLAKVAAGK EKSSNVKNEN TSGTRKSENL RGCDLLQEVS VTIRRFKKTS ISKERVQRCA MLQFSEFHEK LLNTLCRKTD DGQITEHAQS LVLDTLCWLA GVHSNGPGSS KEGNENLLSK TRKFLSDIVR VCFFEAGRSI AHKCARFLAL CISNGKCDPC QPAFGPVLLK ALLDNMSFLP AATTGGSVYW YFVLLNYVKD EDLAGCSTAC ASLLTAVSRQ LQDRLTPMEA LLQTRYGLYS SPFDPVLFDL EMSGSSCKNV YNSSIGVQSD EIDLSDVLSG NGKVSSCTAA EGSFTSLTGL LEVEPLHFTC VSTSDGTRIE RDDAMSSFGV TPAVGGLSSG TVGEASTALS SAAQVALQSL SHAMASAEQQ LQVLQEKQQQ LLKLQQQKAK LEAKLHQTTA AAAAAASAVG PVHNSVPSNP VAAPGFFIHP SDVIPPTPKT TPLFMTPPLT PPNEAVSVVI NAELAQLFPG SVIDPPAVNL AAHNKNSNKS RMNPLGSGLA LAISHASHFL QPPPHQSIII ERMHSGARRF VTLDFGRPIL LTDVLIPTCG DLASLSIDIW TLGEEVDGRR LVVATDISTH SLILHDLIPP PVCRFMKITV IGRYGSTNAR AKIPLGFYYG HTYILPWESE LKLMHDPLKG EGESANQPEI DQHLAMMVAL QEDIQCRYNL ACHRLETLLQ SIDLPPLNSA NNAQYFLRKP DKAVEEDSRV FSAYQDCIQL QLQLNLAHNA VQRLKVALGA SRKMLSETSN PEDLIQTSST EQLRTIIRYL LDTLLSLLHA SNGHSVPAVL QSTFHAQACE ELFKHLCISG TPKIRLHTGL LLVQLCGGER WWGQFLSNVL QELYNSEQLL IFPQDRVFML LSCIGQRSLS NSGVLESLLN LLDNLLSPLQ PQLPMHRRTE GVLDIPMISW VVMLVSRLLD YVATVEDEAA AAKKPLNGNQ WSFINNNLHT QSLNRSSKGS SSLDRLYSRK IRKQLVHHKQ QLNLLKAKQK ALVEQMEKEK IQSNKGSSYK LLVEQAKLKQ ATSKHFKDLI RLRRTAEWSR SNLDTEVTTA KESPEIEPLP FTLAHERCIS VVQKLVLFLL SMDFTCHADL LLFVCKVLAR IANATRPTIH LCEIVNEPQL ERLLLLLVGT DFNRGDISWG GAWAQYSLTC MLQDILAGEL LAPVAAEAME EGTVGDDVGA TAGDSDDSLQ QSSVQLLETI DEPLTHDITG APPLSSLEKD KEIDLELLQD LMEVDIDPLD IDLEKDPLAA KVFKPISSTW YDYWGADYGT YNYNPYIGGL GIPVAKPPAN TEKNGSQTVS VSVSQALDAR LEVGLEQQAE LMLKMMSTLE ADSILQALTN TSPTLSQSPT GTDDSLLGGL QAANQTSQLI IQLSSVPMLN VCFNKLFSML QVHHVQLESL LQLWLTLSLN SSSTGNKENG ADIFLYNANR IPVISLNQAS ITSFLTVLAW YPNTLLRTWC LVLHSLTLMT NMQLNSGSSS AIGTQESTAH LLVSDPNLIH VLVKFLSGTS PHGTNQHSPQ VGPTATQAMQ EFLTRLQVHL SSTCPQIFSE FLLKLIHILS TERGAFQTGQ GPLDAQVKLL EFTLEQNFEV VSVSTISAVI ESVTFLVHHY ITCSDKVMSR SGSDSSVGAR ACFGGLFANL IRPGDAKAVC GEMTRDQLMF DLLKLVNILV QLPLSGNREY SARVSVTTNT TDSVSDEEKV SGGKDGNGSS TSVQGSPAYV ADLVLANQQI MSQILSALGL CNSSAMAMII GASGLHLTKH ENFHGGLDAI SVGDGLFTIL TTLSKKASTV HMMLQPILTY MACGYMGRQG SLATCQLSEP LLWFILRVLD TSDALKAFHD MGGVQLICNN MVTSTRAIVN TARSMVSTIM KFLDSGPNKA VDSTLKTRIL ASEPDNAEGI HNFAPLGTIT SSSPTAQPAE VLLQATPPHR RARSAAWSYI FLPEEAWCDL TIHLPAAVLL KEIHIQPHLA SLATCPSSVS VEVSADGVNM LPLSTPVVTS GLTYIKIQLV KAEVASAVCL RLHRPRDAST LGLSQIKLLG LTAFGTTSSA TVNNPFLPSE DQVSKTSIGW LRLLHHCLTH ISDLEGMMAS AAAPTANLLQ TCAALLMSPY CGMHSPNIEV VLVKIGLQST RIGLKLIDIL LRNCAASGSD PTDLNSPLLF GRLNGLSSDS TIDILYQLGT TQDPGTKDRI QALLKWVSDS ARVAAMKRSG RMNYMCPNSS TVEYGLLMPS PSHLHCVAAI LWHSYELLVE YDLPALLDQE LFELLFNWSM SLPCNMVLKK AVDSLLCSMC HVHPNYFSLL MGWMGITPPP VQCHHRLSMT DDSKKQDLSS SLTDDSKNAQ APLALTESHL ATLASSSQSP EAIKQLLDSG LPSLLVRSLA SFCFSHISSS ESIAQSIDIS QDKLRRHHVP QQCNKMPITA DLVAPILRFL TEVGNSHIMK DWLGGSEVNP LWTALLFLLC HSGSTSGSHN LGAQQTSARS ASLSSAATTG LTTQQRTAIE NATVAFFLQC ISCHPNNQKL MAQVLCELFQ TSPQRGNLPT SGNISGFIRR LFLQLMLEDE KVTMFLQSPC PLYKGRINAT SHVIQHPMYG AGHKFRTLHL PVSTTLSDVL DRVSDTPSIT AKLISEQKDD KEKKNHEEKE KVKAENGFQD NYSVVVASGL KSQSKRAVSA TPPRPPSRRG RTIPDKIGST SGAEAANKII TVPVFHLFHK LLAGQPLPAE MTLAQLLTLL YDRKLPQGYR SIDLTVKLGS RVITDPSLSK TDSYKRLHPE KDHGDLLASC PEDEALTPGD ECMDGILDES LLETCPIQSP LQVFAGMGGL ALIAERLPML YPEVIQQVSA PVVTSTTQEK PKDSDQFEWV TIEQSGELVY EAPETVAAEP PPIKSAVQTM SPIPAHSLAA FGLFLRLPGY AEVLLKERKH AQCLLRLVLG VTDDGEGSHI LQSPSANVLP TLPFHVLRSL FSTTPLTTDD GVLLRRMALE IGALHLILVC LSALSHHSPR VPNSSVNQTE PQVSSSHNPT STEEQQLYWA KGTGFGTGST ASGWDVEQAL TKQRLEEEHV TCLLQVLASY INPVSSAVNG EAQSSHETRG QNSNALPSVL LELLSQSCLI PAMSSYLRND SVLDMARHVP LYRALLELLR AIASCAAMVP LLLPLSTENG EEEEEQSECQ TSVGTLLAKM KTCVDTYTNR LRSKRENVKT GVKPDASDQE PEGLTLLVPD IQKTAEIVYA ATTSLRQANQ EKKLGEYSKK AAMKPKPLSV LKSLEEKYVA VMKKLQFDTF EMVSEDEDGK LGFKVNYHYM SQVKNANDAN SAARARRLAQ EAVTLSTSLP LSSSSSVFVR CDEERLDIMK VLITGPADTP YANGCFEFDV YFPQDYPSSP PLVNLETTGG HSVRFNPNLY NDGKVCLSIL NTWHGRPEEK WNPQTSSFLQ VLVSVQSLIL VAEPYFNEPG YERSRGTPSG TQSSREYDGN IRQATVKWAM LEQIRNPSPC FKEVIHKHFY LKRVEIMAQC EEWIADIQQY SSDKRVGRTM SHHAAALKRH TAQLREELLK LPCPEGLDPD TDDAPEVCRA TTGAEETLMH DQVKPSSSKE LPSDFQL //