ID   BIRC6_MOUSE             Reviewed;        4882 AA.
AC   O88738; E9PYU6; Q69ZM5; Q8BNX0; Q8BR72; Q8BRV7; Q8C737;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Baculoviral IAP repeat-containing protein 6;
DE            EC=2.3.2.27 {ECO:0000269|PubMed:15300255};
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   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 2), FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX   PubMed=9628897; DOI=10.1083/jcb.141.6.1415;
RA   Hauser H.P., Bardroff M., Pyrowolakis G., Jentsch S.;
RT   "A giant ubiquitin-conjugating enzyme related to IAP apoptosis
RT   inhibitors.";
RL   J. Cell Biol. 141:1415-1422(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-893; 3091-3912 AND 4121-4523.
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Corpora quadrigemina, Kidney, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1905-3034 (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15485903; DOI=10.1128/mcb.24.21.9339-9350.2004;
RA   Lotz K., Pyrowolakis G., Jentsch S.;
RT   "BRUCE, a giant E2/E3 ubiquitin ligase and inhibitor of apoptosis protein
RT   of the trans-Golgi network, is required for normal placenta development and
RT   mouse survival.";
RL   Mol. Cell. Biol. 24:9339-9350(2004).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INTERACTION WITH HTRA2; CASP9
RP   AND DIABLO/SMAC.
RX   PubMed=15300255; DOI=10.1038/ncb1159;
RA   Hao Y., Sekine K., Kawabata A., Nakamura H., Ishioka T., Ohata H.,
RA   Katayama R., Hashimoto C., Zhang X., Noda T., Tsuruo T., Naito M.;
RT   "Apollon ubiquitinates SMAC and caspase-9, and has an essential
RT   cytoprotection function.";
RL   Nat. Cell Biol. 6:849-860(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-483 AND SER-485, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. Required for normal placenta development.
CC       {ECO:0000269|PubMed:15300255, ECO:0000269|PubMed:15485903,
CC       ECO:0000269|PubMed:9628897}.
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:15300255};
CC   -!- ACTIVITY REGULATION: Inhibited by DIABLO/SMAC, HTRA2, CASP3, CASP6,
CC       CASP7 and CASP9. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Binds the activated, processed forms of CASP3,
CC       CASP6 and CASP7. Interacts with RNF41, KIF23/MKLP1, USP8/UBPY,
CC       BIRC5/survivin, MAP2K1/MEK1, RAB8A/RAB8, RAB11A/RAB11, PLK1, EXOC3/SEC6
CC       and EXOC4/SEC8 (By similarity). Interacts with CASP9, DIABLO/SMAC and
CC       HTRA2. {ECO:0000250, ECO:0000269|PubMed:15300255}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:Q9NR09}. Endosome
CC       {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q9NR09}. Midbody,
CC       Midbody ring {ECO:0000250|UniProtKB:Q9NR09}. Note=Exhibits cell cycle-
CC       dependent 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. In interphase cells, localizes to the trans-Golgi
CC       network membrane and endosomes. During cytokinesis, a fraction moves to
CC       the midzone where it specifically arrives at the midbody ring. After
CC       abscission completion, travels with the midbody remnant into one
CC       daughter cell, and remains bound to it until a new midbody ring is
CC       formed during the next cell division. {ECO:0000250|UniProtKB:Q9NR09}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O88738-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88738-2; Sequence=VSP_042537;
CC       Name=3;
CC         IsoId=O88738-3; Sequence=VSP_042536, VSP_042537;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the brain and
CC       kidney. {ECO:0000269|PubMed:9628897}.
CC   -!- DOMAIN: The BIR domain is essential for its antiapoptotic function and
CC       is important for binding to DIABLO/SMAC and CASP9. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit perinatal lethality and growth
CC       deficiencies, which are linked to a defect in proper placental
CC       development. {ECO:0000269|PubMed:15485903}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ubiquitin-
CC       conjugating enzyme family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32373.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC37801.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA76720.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y17267; CAA76720.1; ALT_INIT; mRNA.
DR   EMBL; AC098726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK041241; BAC30874.1; -; mRNA.
DR   EMBL; AK045446; BAC32373.1; ALT_INIT; mRNA.
DR   EMBL; AK052612; BAC35061.1; -; mRNA.
DR   EMBL; AK079995; BAC37801.1; ALT_INIT; mRNA.
DR   EMBL; AK173143; BAD32421.1; -; Transcribed_RNA.
DR   CCDS; CCDS37693.2; -. [O88738-2]
DR   PIR; T31067; T31067.
DR   RefSeq; NP_031592.3; NM_007566.3. [O88738-2]
DR   SMR; O88738; -.
DR   BioGRID; 198389; 19.
DR   CORUM; O88738; -.
DR   IntAct; O88738; 9.
DR   MINT; O88738; -.
DR   STRING; 10090.ENSMUSP00000136329; -.
DR   ChEMBL; CHEMBL4879421; -.
DR   MEROPS; I32.006; -.
DR   iPTMnet; O88738; -.
DR   PhosphoSitePlus; O88738; -.
DR   SwissPalm; O88738; -.
DR   EPD; O88738; -.
DR   jPOST; O88738; -.
DR   MaxQB; O88738; -.
DR   PaxDb; 10090-ENSMUSP00000138333; -.
DR   PeptideAtlas; O88738; -.
DR   ProteomicsDB; 273619; -. [O88738-1]
DR   ProteomicsDB; 273620; -. [O88738-2]
DR   ProteomicsDB; 273621; -. [O88738-3]
DR   Pumba; O88738; -.
DR   Antibodypedia; 29188; 252 antibodies from 31 providers.
DR   DNASU; 12211; -.
DR   Ensembl; ENSMUST00000180037.8; ENSMUSP00000136329.2; ENSMUSG00000024073.17. [O88738-2]
DR   Ensembl; ENSMUST00000182133.8; ENSMUSP00000138693.2; ENSMUSG00000024073.17. [O88738-3]
DR   Ensembl; ENSMUST00000182597.8; ENSMUSP00000138333.2; ENSMUSG00000024073.17. [O88738-1]
DR   GeneID; 12211; -.
DR   KEGG; mmu:12211; -.
DR   UCSC; uc033hfd.1; mouse. [O88738-2]
DR   AGR; MGI:1276108; -.
DR   CTD; 57448; -.
DR   MGI; MGI:1276108; Birc6.
DR   VEuPathDB; HostDB:ENSMUSG00000024073; -.
DR   eggNOG; KOG0895; Eukaryota.
DR   eggNOG; KOG1101; Eukaryota.
DR   GeneTree; ENSGT00940000156126; -.
DR   InParanoid; O88738; -.
DR   OMA; LDAQCKL; -.
DR   OrthoDB; 117123at2759; -.
DR   PhylomeDB; O88738; -.
DR   TreeFam; TF105357; -.
DR   BioGRID-ORCS; 12211; 11 hits in 45 CRISPR screens.
DR   ChiTaRS; Birc6; mouse.
DR   PRO; PR:O88738; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; O88738; Protein.
DR   Bgee; ENSMUSG00000024073; Expressed in embryonic post-anal tail and 272 other cell types or tissues.
DR   ExpressionAtlas; O88738; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000922; C:spindle pole; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
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; IMP:MGI.
DR   GO; GO:0060711; P:labyrinthine layer development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0001890; P:placenta development; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; IC:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0060712; P:spongiotrophoblast layer development; IMP:MGI.
DR   CDD; cd00022; BIR; 1.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR001370; BIR_rpt.
DR   InterPro; IPR022103; BIRC6.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
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   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50143; BIR_REPEAT_2; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; O88738; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; 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..4882
FT                   /note="Baculoviral IAP repeat-containing protein 6"
FT                   /id="PRO_0000416247"
FT   REPEAT          292..362
FT                   /note="BIR"
FT   DOMAIN          4598..4765
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          468..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2969..2998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3908..3927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3943..3973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4285..4304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4857..4882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4865..4882
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4691
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         584
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR09"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR09"
FT   MOD_RES         1724
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR09"
FT   MOD_RES         2245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR09"
FT   MOD_RES         2978
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR09"
FT   MOD_RES         3954
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR09"
FT   MOD_RES         4047
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR09"
FT   VAR_SEQ         2057..2062
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15368895"
FT                   /id="VSP_042536"
FT   VAR_SEQ         2212..2220
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:9628897"
FT                   /id="VSP_042537"
FT   CONFLICT        206
FT                   /note="T -> I (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="S -> R (in Ref. 3; BAC37801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        718
FT                   /note="A -> T (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2107
FT                   /note="G -> R (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2455
FT                   /note="C -> G (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2996
FT                   /note="T -> I (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3214
FT                   /note="R -> K (in Ref. 3; BAC35061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3263
FT                   /note="S -> T (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3951
FT                   /note="M -> V (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3966
FT                   /note="I -> V (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4383
FT                   /note="V -> M (in Ref. 1; CAA76720)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   4882 AA;  532170 MW;  6F804ACFA3AFA211 CRC64;
     MVTGCGAAPP GTVTERLPSV IVLSAGRKMA AAAAEASGPS CSSAAAAAGA GAAGVSEWLV
     LRDGCMRCDA DGLHSLSYHP ALNAILAVTS RGTIKVIDGT SGATLQASAL SAKPGGQVKC
     QYISAVDKVI FVDDYAVGCR KDLNGILLLD TALQTPVSKQ DDVVQLELPV TEAQQLLSAC
     IEKIDVSSTE GYDLFITQLK DGLKNTSHET AANHKVAKWA TVTFHLPHHV LKSIASAIVN
     ELKKINQNVA ALPVASSVMD RLSYLLPSAR PELGVGPGRS VDRALMYSEA NRRETFTSWP
     HVGYRWAQPD PMAQAGFYHQ PASSGDDRAM CFTCSVCLVC WEPTDEPWSE HERHSPNCPF
     VKGEHTQNVP LSVTLATSPA QLPSADGADR IACFGSGSCP QFLAAATKRG KICIWDVSKL
     MKVHLKFEIN AYDPAIVQQL ILSGDPSSGV DSRRPTLAWL EDSSSCSDIP KLEGDSDDLL
     EDSDSEEHSR SDSVTGHTSQ KEAMEVSLDI TALSILQQPE KLQWEIVANV LEDTVKDLEE
     LGANPSLTNS KSEKTKEKHQ EQHNIPFPCL LAGGLLTYKS PATSPISSNS HRSLDGLSRT
     QGESISEQGS TDNESCTNSE LNSPLVRRTL PVLLLYSIKE SDEKAGKIFS QMNNIMSKSL
     HDDGFTVPQI IEMELDNQEQ LLLQDPPVTY IQQFADAAAS LTSPDSEKWN SVFPKPGALV
     QCLRLPKFAE EETLCIDSIT PCADGIHLLV GLRTCSVESL SAINQVEALN NLNKLNSALC
     NRRKGDLESN LAVVNGANIS VIQHESPADV PEHLLIRPEQ RNVVSGGYLV LYKMNYTTRI
     VTLEEEPVKI QHIKDPQDTI TSLILLPPDI LDNREDDCEE PAEEMQLASK NGIEREKKSD
     ISTLGHLVVT TQGGYVKVLD LSNFEILAKV EPPKKEGTEE QDTFVSVIYC SGTDRLCACT
     KGGELHFLQI GGTCDDIDEA DILVDGSLSK GIEPALEGSR PLSNPSSPGI SGVELLVDQP
     FTLEILTSLV ELTRFETLTP RFSATVPPCW VEVQQEQQQR RHPQHLHQQH HGDAAQHTRT
     WKLQTDSNSW DEHVFELVLP KACMVGHVDF KFVLNSNITS VPQIQVTLLK NKAPGLGKAN
     ALNIEVEHNG NPSLVDLNEE MHHMDVEESQ CLRLCPFLED HKEDILCGPV WLASGLDLSG
     HAGMLTLTSP KLVKGMAGGK YRSFLIHVKA VSDRGAADEM CSSGLRPVVR LPSLKQQGHK
     GYSLASLLAK VAAGKEKSSN VKNENAGGTR KSENLRGCDL LQEVSVTIRR FKKTSICKER
     VQRCAMLQFS EFHEKLLNTL CRRSDDGQVT EHAQSLVLDA LCWLAGVHSN GSGSSKEGNE
     CLLSKTRKCL SDIVRVCFFE AGRSIAHKCA RFLALCISNG KCEPCQPGFG SVLLKALLDN
     MCFLPAAATG GSVYWYFVLL NYVKDEDLAG CSTACAALLT AVSRQLQDRL TPLEALLQTR
     YGLYSSPFDP VLFDLEMSGS SWKTVYSSST AVQSDEIDLS DVLSGNGRVS SCTAAEGSFT
     SLTGLLEVEP LHFTCVSTSD GTRIERDDAS TFTVSSFGVP PAVGGLSSGT VGEASTALSS
     AAQVALQSLS HAMASAEQQL QVLQEKQQQL LKLQQQKAKL EAKLHQTTAA AAAAASAAAA
     AAAGPVHNAV PSNPVAAPGF FIHPSDVIPP TPKTTPLFMT PPLTPPNEAV SVVINAELAQ
     LFPGSVIDPP AVNLAAQNKN SSKSRMNPLG SGLALAISHA SHFLQPPPHQ SIIIERMHSG
     ARRFVTLDFG RPILLTDVLI PTCGDLASLS IDIWTLGEEV DGRRLVVATD ISTHSLILHD
     LIPPPVCRFM KITVIGRYGS TNARAKIPLG FYYGHSYILP WESELKLMHD PLRGEGESAS
     QPEIDQHLAM MVALQEDIQC RYNLACHRLE ALLQSIDLPP LNSANNAQYF LRKPDKAVEE
     DSRVFSAYQD CIQLQLQLNL AHNAVQRLKV AIGASRKLLN ETSGPEDLIQ TSSTEQLRTI
     VRYLLDTLLS LLHSSNGHSV PAVLQSTFHA QACEELFKHL CISGTPKIRL HTGLLLVQLC
     GGERWWGQFL SNVLQELYNS EQLLIFPQDR VFMLLSCIGQ RSLSNSGVLE SLLNLLDNLL
     SPLQPELSMH RRTEGVLDIP MISWVVMLVS RLLDYVATVE DEAAAAKKPL NGKDRERFLT
     GNQWSFINNN LHTQNLNRSS KGGSSLDRLY SRKIRKQLVH HKQQLNLLKA KQKALVEQME
     KEKIQSNKGS SYKLLVEQAK LKQATSKHFK DLIRLRRTAE WSRSNLDTEV TTTKESPEIE
     PLPFTLAHDR CISVVQKLVL FLLSMDFTCH ADLLLFVCKV LARIANATRP TIHLCEIVNE
     PQLERLLLLL VGTDFNRGDI SWGGAWAQYS LTCMLQDILA GELLAPVAAE AMEECTVSED
     VGATAGDSDD SLQQSPAQLL ETIDEPLTHE IAGTPPLSSL EKDKEIDLEL LQDLMEVDID
     PLDIDLEKDP LAAKVFKPIS STWYDYWGAD YGTYNYNPYI GGLGMPVAKP PSNTEKNGSQ
     TVSVSVSQAL DARLEVGLEQ QAELMLKMMS TLEADSILQA LTNTSPTFSQ SPTGTDDSLL
     GNLQPANQNS QLMIQLSSVP MLNVCFNKLF SMLQVHHVQL ESLLQLWLTL SLNSSSSGNK
     ENGADIFLYN ANRIPVISLN QASIASFLTV LAWYPNTLLR TWCLVLHSLT LMTNMQLNSG
     SSSSIGIQET TAHLLVSDPN LIHVLVKFLS GTSPHGTNQH SPQVGPTATQ AMQEFLTRLQ
     VHLSSTCPQI FSELLLKLIH ILSTERGAFQ TGQGPLDAQV KLLEFTLEQN FEVVSVSTIS
     AVIESVTFLV HHYITCSDKV MSRSGSDSSA GARACFGGLF ANLIRPGDAK AVCGEMTRDQ
     LMFDLLKLVN ILVQLPLSSN REYSARVSVT TNTTDSVSDE EKVSGGKDVN GSSASTPGSP
     ACVADLVLAN QQIMSQILSA LGLCNSSAMA MIIGASGLHL TKHENFHGGL DAISVGDGLF
     TILTTLSKKA STVHMMLQPI LTYMACGYMG RQGSLATCQL SEPLLWFILR VLDTSDALKA
     FHDMGGVQLI CNNMVTSTRA IVNTARSMVS TIMKFLDSGP NKAVDSTLKT RILASEPDNA
     EGIHNFAPLG TITSSSPTAQ PAEVLLQATP PHRRARSAAW SYIFLPEEAW CDLTIHLPSA
     VLLKEIHIQP HLASLATCPS SVSVEVSADG VNMLPLSTPV VTSGLTYIKI QLVKAEVASA
     VCLRLHRPRD ASTLGLSQIK LLGLTAFGTT SSATVNNPFL PSEDQVSKTS IGWLRLLHHC
     LTHISDLEGM MASAAAPTAN LLQTCAALLM SPYCGMHSPN IEVVLVKIGL QSTRIGLKLI
     DILLRNCAAS GSDPTDLNSP LLFGRLNGLS SDSTIDILYQ LGTTQDPGTK DRIQALLKWV
     SDSAKMAALK RSGRMNYMCP SSSAVEYGLL MPSPSHLHCV AAILWHSYEL LVEYDLPALL
     DRELFELLFN WSMSLPCNVV LKKAVDSLLC SMCHIHPNYF SLLMGWMGII PPPVQCHHRL
     SMTDDSKKQD LSSSLTDDSK NAQAPLSLTE SHLATLASSS QSPEAIKQLL DSGLPSLLVR
     SLASFCFSHI SYSESIAQSV DNSQDKLRRH HVPQHCNKMP ITADLVAPIL RFLTEVGNSH
     IMKDWLGGSE VNPLWTALLF LLCHSGSTAG GHNLGAQQSS TRSASHSSAT TTVLTTQQRT
     AIENATVAFF LQCISCHPNN QKLMAQVLCE LFQTAPQRGS LPTSGNISGF VRRLFLQLML
     EDEKVTMFLQ SPCPLYKGRI NATSHVIQHP MFGAGHKFRT LHLPVSTTLS DVLDRVSDTP
     SITAKLISEQ KDDKEKKNHE EKEKVKAENG FQDNYSVVVA SGLKSQSKRA MASTPPRPPS
     RRGRTIPDKI GSASSSADAA SKIITVPVFH LFHRLLAGQP LPAEMTLAQL LTLLYDRKLP
     QGYRSIDLTV KLGSKVITDP SLSKTDSFKR LHPEKDHGDL VGSCPEDEAL TPSDECMDGV
     LDESLLETCP IQSPLQVFAG MGGLALIAER LPMLYPEVIQ QVSAPVIAST TQEKPKDSDQ
     FEWVTIEQSG ELVYEAPETI AAEPPPVKSA VQATSPIPAH SLAAFGLFLR LPGYAEVLLK
     ERKHAQCLLR LVLGVTDDGE GSHILQSPSA NVLPTLPFHV LRSLFSATPL TTDDGVLLRR
     MALEIGALHL ILVCLSALSH HAPRVPNSSL SQTEPQVSNS HNPTSAEEQQ LYWAKGTGFG
     TGSTASGWDV EQALTKQRLE EEHVTCLLQV LASYINPMSG AVNGEAQASP ESRAQNSSAL
     PSVLLELLSQ SCLIPAMSSY LRNDSVLDMA RHVPLYRALL ELLRAIASCT SMVPLLLPLS
     TENGEEEEDE QSECQTSVGT LLAKMKTCVD TYTNRLRSKR ENVKAGVKPD APDQEPEGLA
     LLVPDIQRTA EIVHAATANL RQANQEKKLG EYSKKVVMKP KPLSVLKSLE EKYVAVMKKL
     QFDTFEMVSE DDDGKLGFKV NYHYMSQVKN ANDANSAARA RRLAQEAVTL STSLPLSSSS
     SVFVRCDEER LDIMKVLITG PADTPYANGC FEFDVYFPQD YPSSPPLVNL ETTGGHSVRF
     NPNLYNDGKV CLSILNTWHG RPEEKWNPQT SSFLQVLVSV QSLILVAEPY FNEPGYERSR
     GTPSGTQSSR EYDGNIRQAT VKWAMLEQIR NPSPCFKEVI HKHFYLKRIE LMAQCEEWIA
     DIQQYSSDKR VGRTMSHHAA ALKRHTAQLR EELLKLPCPE GLDPDIEDAS PVCRATAGAE
     DTLTHDHVNP SSSKDLPSDF QL
//