BIRC6_MOUSE
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 03-AUG-2022, entry version 159.
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, Pancreas,
RC 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; 15.
DR CORUM; O88738; -.
DR IntAct; O88738; 9.
DR MINT; O88738; -.
DR STRING; 10090.ENSMUSP00000138333; -.
DR MEROPS; I32.006; -.
DR iPTMnet; O88738; -.
DR PhosphoSitePlus; O88738; -.
DR SwissPalm; O88738; -.
DR EPD; O88738; -.
DR jPOST; O88738; -.
DR MaxQB; O88738; -.
DR PaxDb; O88738; -.
DR PeptideAtlas; O88738; -.
DR PRIDE; O88738; -.
DR ProteomicsDB; 273619; -. [O88738-1]
DR ProteomicsDB; 273620; -. [O88738-2]
DR ProteomicsDB; 273621; -. [O88738-3]
DR Antibodypedia; 29188; 224 antibodies from 31 providers.
DR DNASU; 12211; -.
DR Ensembl; ENSMUST00000180037; ENSMUSP00000136329; ENSMUSG00000024073. [O88738-2]
DR Ensembl; ENSMUST00000182133; ENSMUSP00000138693; ENSMUSG00000024073. [O88738-3]
DR Ensembl; ENSMUST00000182597; ENSMUSP00000138333; ENSMUSG00000024073. [O88738-1]
DR GeneID; 12211; -.
DR KEGG; mmu:12211; -.
DR UCSC; uc033hfd.1; mouse. [O88738-2]
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; GPLDAQC; -.
DR OrthoDB; 1404665at2759; -.
DR PhylomeDB; O88738; -.
DR TreeFam; TF105357; -.
DR BioGRID-ORCS; 12211; 11 hits in 40 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 270 other tissues.
DR ExpressionAtlas; O88738; baseline and differential.
DR Genevisible; O88738; MM.
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; -; 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 Pfam; PF00653; BIR; 1.
DR Pfam; PF12356; BIRC6; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00238; BIR; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 1.
DR PROSITE; PS50127; UBC_2; 1.
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
