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Breast cancer type 2 susceptibility protein homolog (Fanconi anemia group D1 protein homolog)

 BRCA2_MOUSE             Reviewed;        3329 AA.
P97929; F8VPU5; O35922; P97383;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 162.
RecName: Full=Breast cancer type 2 susceptibility protein homolog;
AltName: Full=Fanconi anemia group D1 protein homolog;
Name=Brca2; Synonyms=Fancd1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129;
PubMed=9063750; DOI=10.1093/hmg/6.2.291;
Connor F., Smith A., Wooster R., Stratton M., Dixon A., Campbell E.,
Tait T.M., Freeman T., Ashworth A.;
"Cloning, chromosomal mapping and expression pattern of the mouse
Brca2 gene.";
Hum. Mol. Genet. 6:291-300(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=9119389; DOI=10.1006/geno.1996.4573;
Sharan S.K., Bradley A.;
"Murine Brca2: sequence, map position, and expression pattern.";
Genomics 40:234-241(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/Sv;
PubMed=9242436;
McAllister K.A., Haugen-Strano A., Hagevik S., Brownlee H.A.,
Collins N.K., Futreal P.A., Bennett L.M., Wiseman R.W.;
"Characterization of the rat and mouse homologues of the BRCA2 breast
cancer susceptibility gene.";
Cancer Res. 57:3121-3125(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-200.
PubMed=8917547; DOI=10.1073/pnas.93.23.13078;
Rajan J.V., Wang M., Marquis S.T., Chodosh L.A.;
"Brca2 is coordinately regulated with Brca1 during proliferation and
differentiation in mammary epithelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 93:13078-13083(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 569-625.
PubMed=9196008; DOI=10.1007/s003359900497;
McAllister K.A., Ramachandran S., Haugen-Strano A., Fiedorek F.T. Jr.,
Wiseman R.W.;
"Genetic mapping of the Brca2 breast cancer susceptibility gene on
mouse chromosome 5.";
Mamm. Genome 8:540-541(1997).
[7]
PROTEIN SEQUENCE OF 784-790, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[8]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2378-3115 IN COMPLEX WITH
SEM1, AND INTERACTION WITH SEM1.
PubMed=12228710; DOI=10.1126/science.297.5588.1837;
Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H.,
Zheng N., Chen P.L., Lee W.H., Pavletich N.P.;
"BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-
ssDNA structure.";
Science 297:1837-1848(2002).
-!- FUNCTION: Involved in double-strand break repair and/or homologous
recombination. Binds RAD51 and potentiates recombinational DNA
repair by promoting assembly of RAD51 onto single-stranded DNA
(ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded
DNA, enabling RAD51 to displace replication protein-A (RPA) from
ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP
hydrolysis. Part of a PALB2-scaffolded HR complex containing
RAD51C and which is thought to play a role in DNA repair by HR.
May participate in S phase checkpoint activation. Binds
selectively to ssDNA, and to ssDNA in tailed duplexes and
replication fork structures. May play a role in the extension step
after strand invasion at replication-dependent DNA double-strand
breaks; together with PALB2 is involved in both POLH localization
at collapsed replication forks and DNA polymerization activity. In
concert with NPM1, regulates centrosome duplication. Interacts
with the TREX-2 complex (transcription and export complex 2)
subunits PCID2 and SEM1, and is required to prevent R-loop-
associated DNA damage and thus transcription-associated genomic
instability, independently of its known role in homologous
recombination (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P51587}.
-!- SUBUNIT: Monomer and dimer. Interacts with RAD51; regulates RAD51
recruitment and function at sites of DNA repair. Interacts with
SEM1, WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with both
nonubiquitinated and monoubiquitinated FANCD2; this complex also
includes XRCC3 and phosphorylated FANCG. Part of a BRCA complex
containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2
which may serve as a scaffold for a HR complex containing PALB2,
BRCA2, RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only in the
presence of PALB2 which serves as the bridging protein. Interacts
with POLH; the interaction is direct. Interacts with the TREX-2
complex subunits PCID2 and SEM1 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P51587, ECO:0000269|PubMed:12228710}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Highest expression in
cerebellum, testis, ileum, appendix, epididymis, ovary and mammary
gland. No expression in lung.
-!- DEVELOPMENTAL STAGE: In the mammary gland, expression increases
dramatically during pregnancy.
-!- PTM: Phosphorylation by CHEK1 and CHEK2 regulates interaction with
RAD51. Phosphorylation at Ser-3214 by CDK1 and CDK2 is low in S
phase when recombination is active, but increases as cells
progress towards mitosis; this phosphorylation prevents homologous
recombination-dependent repair during S phase and G2 by inhibiting
RAD51 binding (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated in the absence of DNA damage; this does not
lead to proteasomal degradation. In contrast, ubiquitination in
response to DNA damage leads to proteasomal degradation (By
similarity). {ECO:0000250}.
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EMBL; U82270; AAB48306.1; -; mRNA.
EMBL; U65594; AAC23702.1; -; mRNA.
EMBL; U89652; AAB71377.1; -; mRNA.
EMBL; AC154885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U72947; AAB40720.1; -; mRNA.
EMBL; U89503; AAC53276.1; -; Genomic_DNA.
CCDS; CCDS39411.1; -.
PIR; T30835; T30835.
PIR; T30904; T30904.
PIR; T42205; T42205.
RefSeq; NP_001074470.1; NM_001081001.2.
RefSeq; NP_033895.2; NM_009765.3.
RefSeq; XP_017176117.1; XM_017320628.1.
UniGene; Mm.236256; -.
PDB; 1MIU; X-ray; 3.10 A; A=2378-3115.
PDB; 1MJE; X-ray; 3.50 A; A=2378-3113.
PDBsum; 1MIU; -.
PDBsum; 1MJE; -.
ProteinModelPortal; P97929; -.
SMR; P97929; -.
BioGrid; 198384; 6.
IntAct; P97929; 2.
STRING; 10090.ENSMUSP00000038576; -.
iPTMnet; P97929; -.
PhosphoSitePlus; P97929; -.
EPD; P97929; -.
MaxQB; P97929; -.
PaxDb; P97929; -.
PeptideAtlas; P97929; -.
PRIDE; P97929; -.
Ensembl; ENSMUST00000044620; ENSMUSP00000038576; ENSMUSG00000041147.
Ensembl; ENSMUST00000202313; ENSMUSP00000144150; ENSMUSG00000041147.
GeneID; 12190; -.
KEGG; mmu:12190; -.
UCSC; uc009aty.2; mouse.
CTD; 675; -.
MGI; MGI:109337; Brca2.
eggNOG; KOG4751; Eukaryota.
eggNOG; ENOG410Y06W; LUCA.
GeneTree; ENSGT00390000003602; -.
HOGENOM; HOG000139693; -.
HOVERGEN; HBG050731; -.
InParanoid; P97929; -.
KO; K08775; -.
OMA; HRQMLND; -.
OrthoDB; EOG091G0C79; -.
TreeFam; TF105041; -.
Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-MMU-912446; Meiotic recombination.
Reactome; R-MMU-912497; Meiotic Recombination.
EvolutionaryTrace; P97929; -.
PRO; PR:P97929; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000041147; -.
CleanEx; MM_BRCA2; -.
ExpressionAtlas; P97929; baseline and differential.
Genevisible; P97929; MM.
GO; GO:0033593; C:BRCA2-MAGE-D1 complex; ISO:MGI.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000800; C:lateral element; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0030141; C:secretory granule; ISO:MGI.
GO; GO:0043015; F:gamma-tubulin binding; ISO:MGI.
GO; GO:0010484; F:H3 histone acetyltransferase activity; ISO:MGI.
GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0007569; P:cell aging; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0051298; P:centrosome duplication; ISO:MGI.
GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
GO; GO:0051276; P:chromosome organization; IMP:MGI.
GO; GO:0000910; P:cytokinesis; IEA:Ensembl.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:MGI.
GO; GO:0006302; P:double-strand break repair; IMP:MGI.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
GO; GO:0070200; P:establishment of protein localization to telomere; IDA:BHF-UCL.
GO; GO:0008585; P:female gonad development; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IGI:MGI.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
GO; GO:0007141; P:male meiosis I; IMP:MGI.
GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; ISO:MGI.
GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:MGI.
GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI.
GO; GO:0001556; P:oocyte maturation; IMP:MGI.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0032465; P:regulation of cytokinesis; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0048478; P:replication fork protection; IMP:MGI.
GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
GO; GO:0010225; P:response to UV-C; IMP:MGI.
GO; GO:0010165; P:response to X-ray; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0000722; P:telomere maintenance via recombination; IGI:BHF-UCL.
CDD; cd04493; BRCA2DBD_OB1; 1.
CDD; cd04495; BRCA2DBD_OB3; 1.
InterPro; IPR015525; BRCA2.
InterPro; IPR015252; BRCA2_hlx.
InterPro; IPR036315; BRCA2_hlx_sf.
InterPro; IPR015187; BRCA2_OB_1.
InterPro; IPR015188; BRCA2_OB_3.
InterPro; IPR002093; BRCA2_repeat.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR015205; Tower_dom.
PANTHER; PTHR11289; PTHR11289; 1.
Pfam; PF09169; BRCA-2_helical; 1.
Pfam; PF09103; BRCA-2_OB1; 1.
Pfam; PF09104; BRCA-2_OB3; 1.
Pfam; PF00634; BRCA2; 7.
Pfam; PF09121; Tower; 1.
PIRSF; PIRSF002397; BRCA2; 1.
SMART; SM01341; Tower; 1.
SUPFAM; SSF50249; SSF50249; 4.
SUPFAM; SSF81872; SSF81872; 1.
PROSITE; PS50138; BRCA2_REPEAT; 6.
1: Evidence at protein level;
3D-structure; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Tumor suppressor; Ubl conjugation.
CHAIN 1 3329 Breast cancer type 2 susceptibility
protein homolog.
/FTId=PRO_0000064985.
REPEAT 981 1015 BRCA2 1.
REPEAT 1192 1226 BRCA2 2.
REPEAT 1394 1428 BRCA2 3.
REPEAT 1491 1525 BRCA2 4.
REPEAT 1623 1657 BRCA2 5.
REPEAT 1924 1958 BRCA2 6.
REPEAT 2004 2038 BRCA2 7.
REGION 1 40 Interaction with PALB2. {ECO:0000250}.
REGION 628 979 Interaction with NPM1. {ECO:0000250}.
REGION 2298 2466 Interaction with FANCD2. {ECO:0000250}.
REGION 2402 2753 Interaction with SEM1.
{ECO:0000250|UniProtKB:P51587}.
MOTIF 2603 2619 Nuclear export signal; masked by
interaction with SEM1.
{ECO:0000250|UniProtKB:P51587}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000250|UniProtKB:P51587}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000250|UniProtKB:P51587}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000250|UniProtKB:P51587}.
MOD_RES 2048 2048 Phosphoserine.
{ECO:0000250|UniProtKB:P51587}.
MOD_RES 3214 3214 Phosphoserine; by CDK1 and CDK2.
{ECO:0000250|UniProtKB:P51587}.
MOD_RES 3241 3241 Phosphoserine.
{ECO:0000250|UniProtKB:P51587}.
VARIANT 44 44 S -> F (in strain: C57BL/6 and 129/Sv).
VARIANT 340 340 T -> P (in strain: 129/Sv).
VARIANT 377 377 N -> H (in strain: C57BL/6).
VARIANT 407 407 H -> P (in strain: C57BL/6).
VARIANT 661 661 I -> V (in strain: C57BL/6).
VARIANT 739 739 P -> H (in strain: C57BL/6).
VARIANT 1198 1199 GF -> RI (in strain: C57BL/6).
VARIANT 1257 1257 Q -> P (in strain: C57BL/6).
VARIANT 1392 1392 Q -> R (in strain: C57BL/6).
VARIANT 1520 1521 FD -> CG (in strain: C57BL/6).
VARIANT 1583 1583 R -> W (in strain: C57BL/6).
VARIANT 1613 1613 C -> W (in strain: C57BL/6).
VARIANT 1686 1686 S -> R (in strain: C57BL/6).
VARIANT 1799 1799 S -> F (in strain: 129/Sv).
VARIANT 1881 1881 P -> L (in strain: C57BL/6).
VARIANT 1894 1894 S -> F (in strain: 129/Sv).
VARIANT 2141 2141 Q -> K (in strain: C57BL/6).
VARIANT 2392 2392 S -> R (in strain: C57BL/6).
VARIANT 2605 2605 K -> Q (in strain: C57BL/6).
VARIANT 2648 2648 A -> P (in strain: C57BL/6).
VARIANT 2717 2717 R -> C (in strain: 129/Sv).
VARIANT 2729 2729 L -> M (in strain: 129/Sv).
VARIANT 2814 2814 Q -> H (in strain: C57BL/6).
VARIANT 2827 2827 A -> P (in strain: C57BL/6).
VARIANT 2907 2907 S -> I (in strain: 129/Sv).
VARIANT 2929 2929 H -> L (in strain: 129/Sv).
VARIANT 3058 3058 A -> G (in strain: C57BL/6).
VARIANT 3071 3071 A -> G (in strain: C57BL/6).
VARIANT 3081 3081 K -> E (in strain: C57BL/6).
VARIANT 3089 3089 T -> S (in strain: C57BL/6).
VARIANT 3105 3109 DSPKW -> SQSQV (in strain: C57BL/6).
VARIANT 3220 3220 A -> G (in strain: 129/Sv).
VARIANT 3238 3238 E -> K (in strain: 129/Sv).
VARIANT 3243 3243 Missing (in strain: C57BL/6).
VARIANT 3245 3245 R -> K (in strain: 129/Sv).
CONFLICT 1038 1038 L -> I (in Ref. 1; AAB48306).
{ECO:0000305}.
HELIX 2404 2420 {ECO:0000244|PDB:1MIU}.
HELIX 2430 2435 {ECO:0000244|PDB:1MIU}.
HELIX 2446 2448 {ECO:0000244|PDB:1MIU}.
STRAND 2456 2458 {ECO:0000244|PDB:1MJE}.
STRAND 2462 2464 {ECO:0000244|PDB:1MIU}.
STRAND 2468 2472 {ECO:0000244|PDB:1MIU}.
TURN 2475 2480 {ECO:0000244|PDB:1MIU}.
HELIX 2486 2489 {ECO:0000244|PDB:1MIU}.
TURN 2490 2492 {ECO:0000244|PDB:1MIU}.
STRAND 2495 2497 {ECO:0000244|PDB:1MJE}.
STRAND 2503 2505 {ECO:0000244|PDB:1MJE}.
TURN 2512 2514 {ECO:0000244|PDB:1MJE}.
HELIX 2518 2527 {ECO:0000244|PDB:1MIU}.
HELIX 2538 2554 {ECO:0000244|PDB:1MIU}.
TURN 2560 2562 {ECO:0000244|PDB:1MIU}.
STRAND 2564 2569 {ECO:0000244|PDB:1MIU}.
HELIX 2570 2584 {ECO:0000244|PDB:1MIU}.
TURN 2585 2587 {ECO:0000244|PDB:1MJE}.
HELIX 2592 2597 {ECO:0000244|PDB:1MIU}.
STRAND 2606 2608 {ECO:0000244|PDB:1MIU}.
STRAND 2640 2643 {ECO:0000244|PDB:1MJE}.
STRAND 2648 2653 {ECO:0000244|PDB:1MJE}.
HELIX 2655 2662 {ECO:0000244|PDB:1MIU}.
STRAND 2671 2674 {ECO:0000244|PDB:1MJE}.
STRAND 2675 2677 {ECO:0000244|PDB:1MIU}.
STRAND 2679 2681 {ECO:0000244|PDB:1MIU}.
STRAND 2696 2699 {ECO:0000244|PDB:1MJE}.
HELIX 2701 2703 {ECO:0000244|PDB:1MIU}.
STRAND 2704 2707 {ECO:0000244|PDB:1MJE}.
STRAND 2713 2715 {ECO:0000244|PDB:1MIU}.
HELIX 2726 2728 {ECO:0000244|PDB:1MIU}.
STRAND 2731 2733 {ECO:0000244|PDB:1MIU}.
STRAND 2736 2746 {ECO:0000244|PDB:1MIU}.
STRAND 2751 2754 {ECO:0000244|PDB:1MJE}.
STRAND 2756 2758 {ECO:0000244|PDB:1MIU}.
STRAND 2760 2763 {ECO:0000244|PDB:1MJE}.
HELIX 2767 2778 {ECO:0000244|PDB:1MIU}.
HELIX 2782 2791 {ECO:0000244|PDB:1MIU}.
HELIX 2813 2817 {ECO:0000244|PDB:1MIU}.
HELIX 2822 2830 {ECO:0000244|PDB:1MIU}.
STRAND 2833 2835 {ECO:0000244|PDB:1MIU}.
TURN 2836 2840 {ECO:0000244|PDB:1MIU}.
STRAND 2848 2850 {ECO:0000244|PDB:1MIU}.
TURN 2851 2853 {ECO:0000244|PDB:1MIU}.
HELIX 2855 2858 {ECO:0000244|PDB:1MIU}.
HELIX 2861 2871 {ECO:0000244|PDB:1MIU}.
HELIX 2873 2876 {ECO:0000244|PDB:1MIU}.
TURN 2877 2881 {ECO:0000244|PDB:1MIU}.
STRAND 2889 2900 {ECO:0000244|PDB:1MIU}.
STRAND 2904 2910 {ECO:0000244|PDB:1MIU}.
HELIX 2913 2918 {ECO:0000244|PDB:1MIU}.
STRAND 2924 2930 {ECO:0000244|PDB:1MIU}.
STRAND 2938 2940 {ECO:0000244|PDB:1MIU}.
STRAND 2945 2957 {ECO:0000244|PDB:1MIU}.
HELIX 2961 2964 {ECO:0000244|PDB:1MIU}.
TURN 2965 2967 {ECO:0000244|PDB:1MIU}.
HELIX 2977 2980 {ECO:0000244|PDB:1MIU}.
STRAND 2981 2983 {ECO:0000244|PDB:1MIU}.
TURN 2986 2989 {ECO:0000244|PDB:1MIU}.
STRAND 2990 3001 {ECO:0000244|PDB:1MIU}.
STRAND 3004 3006 {ECO:0000244|PDB:1MJE}.
STRAND 3009 3013 {ECO:0000244|PDB:1MIU}.
STRAND 3015 3017 {ECO:0000244|PDB:1MIU}.
STRAND 3019 3026 {ECO:0000244|PDB:1MIU}.
STRAND 3037 3044 {ECO:0000244|PDB:1MIU}.
STRAND 3050 3052 {ECO:0000244|PDB:1MIU}.
STRAND 3056 3058 {ECO:0000244|PDB:1MIU}.
STRAND 3063 3067 {ECO:0000244|PDB:1MIU}.
TURN 3071 3073 {ECO:0000244|PDB:1MIU}.
HELIX 3074 3080 {ECO:0000244|PDB:1MIU}.
HELIX 3082 3085 {ECO:0000244|PDB:1MIU}.
HELIX 3090 3102 {ECO:0000244|PDB:1MIU}.
SEQUENCE 3329 AA; 370664 MW; 50A32E8BADE2CF7E CRC64;
MPVEYKRRPT FWEIFKARCS TADLGPISLN WFEELSSEAP PYNSEPPEES EYKPHGYEPQ
LFKTPQRNPP YHQFASTPIM FKERSQTLPL DQSPFRELGK VVASSKHKTH SKKKTKVDPV
VDVASPPLKS CLSESPLTLR CTQAVLQREK PVVSGSLFYT PKLKEGQTPK PISESLGVEV
DPDMSWTSSL ATPPTLSSTV LIARDEEARS SVTPADSPAT LKSCFSNHNE SPQKNDRSVP
SVIDSENKNQ QEAFSQGLGK MLGDSSGKRN SFKDCLRKPI PNILEDGETA VDTSEEDSFS
LCFPKRRTRN LQKMRMGKTR KKIFSETRTD ELSEEARRQT DDKNSFVFEM ELRESDPLDP
GVTSQKPFYS QNEEICNEAV QCSDSRWSQS NLSGLNETQT GKITLPHISS HSQNISEDFI
DMKKEGTGSI TSEKSLPHIS SLPEPEKMFS EETVVDKEHE GQHFESLEDS IAGKQMVSRT
SQAACLSPSI RKSIFKMREP LDETLGTVFS DSMTNSTFTE EHEASACGLG ILTACSQRED
SICPSSVDTG SWPTTLTDTS ATVKNAGLIS TLKNKKRKFI YSVSDDASLQ GKKLQTHRQL
ELTNLSAQLE ASAFEVPLTF TNVNSGIPDS SDKKRCLPND PEEPSLTNSF GTATSKEISY
IHALISQDLN DKEAIVIEEK PQPYTAREAD FLLCLPERTC ENDQKSPKVS NGKEKVLVSA
CLPSAVQLSS ISFESQENPL GDHNGTSTLK LTPSSKLPLS KADMVSREKM CKMPEKLQCE
SCKVNIELSK NILEVNEICI LSENSKTPGL LPPGENIIEV ASSMKSQFNQ NAKIVIQKDQ
KGSPFISEVA VNMNSEELFP DSGNNFAFQV TNKCNKPDLG SSVELQEEDL SHTQGPSLKN
SPMAVDEDVD DAHAAQVLIT KDSDSLAVVH DYTEKSRNNI EQHQKGTEDK DFKSNSSLNM
KSDGNSDCSD KWSEFLDPVL NHNFGGSFRT ASNKEIKLSE HNVKKSKMFF KDIEEQYPTR
LACIDIVNTL PLANQKKLSE PHIFDLKSVT TVSTQSHNQS SVSHEDTDTA PQMLSSKQDF
HSNNLTTSQK AEITELSTIL EESGSQFEFT QFRKPSHIAQ NTSEVPGNQM VVLSTASKEW
KDTDLHLPVD PSVGQTDHSK QFEGSAGVKQ SFPHLLEDTC NKNTSCFLPN INEMEFGGFC
SALGTKLSVS NEALRKAMKL FSDIENSEEP SAKVGPRGFS SSAHHDSVAS VFKIKKQNTE
KSFDEKSSKC QVTLQNNIEM TTCIFVGRNP EKYIKNTKHE DSYTSSQRNN LENSDGSMSS
TSGPVYIHKG DSDLPADQGS KCPESCTQYA REENTQIKEN ISDLTCLEIM KAEETCMKSS
DKKQLPSDKM EQNIKEFNIS FQTASGKNTR VSKESLNKSV NIFNRETDEL TVISDSLNSK
ILHGINKDKM HTSCHKKAIS IKKVFEDHFP IVTVSQLPAQ QHPEYEIEST KEPTLLSFHT
ASGKKVKIMQ ESLDKVKNLF DETQYVRKTA SFSQGSKPLK DSKKELTLAY EKIEVTASKC
EEMQNFVSKE TEMLPQQNYH MYRQTENLKT SNGTSSKVQE NIENNVEKNP RICCICQSSY
PVTEDSALAY YTEDSRKTCV RESSLSKGRK WLREQGDKLG TRNTIKIECV KEHTEDFAGN
ASYEHSLVII RTEIDTNHVS ENQVSTLLSD PNVCHSYLSQ SSFCHCDDMH NDSGYFLKNK
IDSDVPPDMK NAEGNTISPR VSATKERNLH PQTINEYCVQ KLETNTSPHA NKDVAIDPSL
LDSRNCKVGS LVFITAHSQE TERTKEIVTD NCYKIVEQNR QSKPDTCQTS CHKVLDDSKD
FICPSSSGDV CINSRKDSFC PHNEQILQHN QSMSGLKKAA TPPVGLETWD TSKSIREPPQ
AAHPSRTYGI FSTASGKAIQ VSDASLEKAR QVFSEMDGDA KQLSSMVSLE GNEKPHHSVK
RENSVVHSTQ GVLSLPKPLP GNVNSSVFSG FSTAGGKLVT VSESALHKVK GMLEEFDLIR
TEHTLQHSPI PEDVSKILPQ PCAEIRTPEY PVNSKLQKTY NDKSSLPSNY KESGSSGNTQ
SIEVSLQLSQ MERNQDTQLV LGTKVSHSKA NLLGKEQTLP QNIKVKTDEM KTFSDVPVKT
NVGEYYSKES ENYFETEAVE SAKAFMEDDE LTDSEQTHAK CSLFTCPQNE TLFNSRTRKR
GGVTVDAVGQ PPIKRSLLNE FDRIIESKGK SLTPSKSTPD GTVKDRSLFT HHMSLEPVTC
GPFCSSKERQ GAQRPHLTSP AQELLSKGHP WRHSALEKSP SSPIVSILPA HDVSATRTER
TRHSGKSTKV FVPPFKMKSQ FHGDEHFNSK NVNLEGKNQK STDGDREDGN DSHVRQFNKD
LMSSLQSARD LQDMRIKNKE RRHLRLQPGS LYLTKSSTLP RISLQAAVGD RAPSACSPKQ
LYIYGVSKEC INVNSKNAEY FQFDIQDHFG KEDLCAGKGF QLADGGWLIP SNDGKAGKEE
FYRALCDTPG VDPKLISSIW VANHYRWIVW KLAAMEFAFP KEFANRCLNP ERVLLQLKYR
YDVEIDNSRR SALKKILERD DTAAKTLVLC ISDIISPSTK VSETSGGKTS GEDANKVDTI
ELTDGWYAVR AQLDPPLMAL VKSGKLTVGQ KIITQGAELV GSPDACAPLE APDSLRLKIS
ANSTRPARWH SRLGFFRDPR PFPLPLSSLF SDGGNVGCVD IIVQRVYPLQ WVEKTVSGLY
IFRSEREEEK EALRFAEAQQ KKLEALFTKV HTEFKDHEED TTQRCVLSRT LTRQQVHALQ
DGAELYAAVQ YASDPDHLEA CFSEEQLRAL NNYRQMLNDK KQARIQSEFR KALESAEKEE
GLSRDVTTVW KLRVTSYKKK EKSALLSIWR PSSDLSSLLT EGKRYRIYHL AVSKSKSKFE
RPSIQLTATK RTQYQQLPVS SETLLQVYQP RESLHFSRLS DPAFQPPCSE VDVVGVVVSV
VKPIGLAPLV YLSDECLNLL VVKFGIDLNE DIKPRVLIAA SNLQCQPEST SGVPTLFAGH
FSIFSASPKE AYFQEKVNNL KHAIENIDTF YKEAEKKLIH VLEGDSPKWS TPNKDPTREP
HAASTCCASD LLGSGGQFLR ISPTGQQSYQ SPLSHCTLKG KSMPLAHSAQ MAAKSWSGEN
EIDDPKTCRK RRALDFLSRL PLPSPVSPIC TFVSPAAQKA FQPPRSCGTK YATPIKKEPS
SPRRRTPFQK TSGVSLPDCD SVADEELALL STQALTPDSV GGNEQAFPGD STRNPQPAQR
PDQQVGPRSR KESLRDCRGD SSEKLAVES


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