BRCA2_RAT
ID BRCA2_RAT Reviewed; 3343 AA.
AC O35923;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Breast cancer type 2 susceptibility protein homolog {ECO:0000305};
DE AltName: Full=Fanconi anemia group D1 protein homolog;
GN Name=Brca2 {ECO:0000312|RGD:2219}; Synonyms=Fancd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9242436;
RA McAllister K.A., Haugen-Strano A., Hagevik S., Brownlee H.A., Collins N.K.,
RA Futreal P.A., Bennett L.M., Wiseman R.W.;
RT "Characterization of the rat and mouse homologues of the BRCA2 breast
RT cancer susceptibility gene.";
RL Cancer Res. 57:3121-3125(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 2335-3151 IN COMPLEX WITH SEM1,
RP AND INTERACTION WITH SEM1.
RX PubMed=12228710; DOI=10.1126/science.297.5588.1837;
RA Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H.,
RA Zheng N., Chen P.L., Lee W.H., Pavletich N.P.;
RT "BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA
RT structure.";
RL Science 297:1837-1848(2002).
CC -!- FUNCTION: Involved in double-strand break repair and/or homologous
CC recombination. Binds RAD51 and potentiates recombinational DNA repair
CC by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts
CC by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to
CC displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-
CC ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded
CC HR complex containing RAD51C and which is thought to play a role in DNA
CC repair by HR. May participate in S phase checkpoint activation. Binds
CC selectively to ssDNA, and to ssDNA in tailed duplexes and replication
CC fork structures. May play a role in the extension step after strand
CC invasion at replication-dependent DNA double-strand breaks; together
CC with PALB2 is involved in both POLH localization at collapsed
CC replication forks and DNA polymerization activity. In concert with
CC NPM1, regulates centrosome duplication. Interacts with the TREX-2
CC complex (transcription and export complex 2) subunits PCID2 and SEM1,
CC and is required to prevent R-loop-associated DNA damage and thus
CC transcription-associated genomic instability, independently of its
CC known role in homologous recombination (By similarity).
CC {ECO:0000250|UniProtKB:P51587, ECO:0000250|UniProtKB:P97929}.
CC -!- SUBUNIT: Monomer and dimer. Interacts with RAD51; regulates RAD51
CC recruitment and function at sites of DNA repair. Interacts with SEM1,
CC WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with both
CC nonubiquitinated and monoubiquitinated FANCD2; this complex also
CC includes XRCC3 and phosphorylated FANCG. Part of a BRCA complex
CC containing BRCA1, BRCA2 and PALB2. Component of the homologous
CC recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2,
CC DSS1 and RAD51 (By similarity). Within the complex, interacts with
CC ERCC5/XPG and PALB2 (By similarity). Interacts directly with PALB2
CC which may serve as a scaffold for a HR complex containing PALB2, BRCA2,
CC RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only in the presence of
CC PALB2 which serves as the bridging protein. Interacts with POLH; the
CC interaction is direct. Interacts with the TREX-2 complex subunits PCID2
CC and SEM1 (By similarity). Interacts with HSF2BP and BRME1; the
CC interaction with HSF2BP is direct and allows the formation of a ternary
CC complex. The complex BRME1:HSF2BP:BRCA2 interacts with SPATA22, MEIOB
CC and RAD51 (By similarity). {ECO:0000250|UniProtKB:P51587,
CC ECO:0000250|UniProtKB:P97929, ECO:0000269|PubMed:12228710}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51587}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P51587}.
CC -!- TISSUE SPECIFICITY: Highest expression in testis. Also expressed in
CC spleen, skeletal muscle, thymus, mammary gland, heart, ovary, prostate,
CC liver, lung, kidney and brain.
CC -!- PTM: Phosphorylated by ATM upon irradiation-induced DNA damage.
CC Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51.
CC Phosphorylation at Ser-3222 by CDK1 and CDK2 is low in S phase when
CC recombination is active, but increases as cells progress towards
CC mitosis; this phosphorylation prevents homologous recombination-
CC dependent repair during S phase and G2 by inhibiting RAD51 binding.
CC {ECO:0000250|UniProtKB:P51587}.
CC -!- PTM: Ubiquitinated in the absence of DNA damage; this does not lead to
CC proteasomal degradation. In contrast, ubiquitination in response to DNA
CC damage leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P51587}.
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DR EMBL; U89653; AAB71378.1; -; mRNA.
DR PIR; T42207; T42207.
DR PDB; 1IYJ; X-ray; 3.40 A; B/D=2335-3151.
DR PDBsum; 1IYJ; -.
DR SMR; O35923; -.
DR STRING; 10116.ENSRNOP00000001475; -.
DR CarbonylDB; O35923; -.
DR PaxDb; O35923; -.
DR PRIDE; O35923; -.
DR UCSC; RGD:2219; rat.
DR RGD; 2219; Brca2.
DR eggNOG; KOG4751; Eukaryota.
DR InParanoid; O35923; -.
DR PhylomeDB; O35923; -.
DR Reactome; R-RNO-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-RNO-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-RNO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-RNO-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-RNO-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR EvolutionaryTrace; O35923; -.
DR PRO; PR:O35923; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0033593; C:BRCA2-MAGE-D1 complex; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISO:RGD.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:1990391; C:DNA repair complex; ISO:RGD.
DR GO; GO:0000800; C:lateral element; ISO:RGD.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0043015; F:gamma-tubulin binding; ISO:RGD.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; ISO:RGD.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; ISO:RGD.
DR GO; GO:0051298; P:centrosome duplication; ISO:RGD.
DR GO; GO:0043009; P:chordate embryonic development; ISO:RGD.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:RGD.
DR GO; GO:0006310; P:DNA recombination; IDA:RGD.
DR GO; GO:0006302; P:double-strand break repair; ISO:RGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0070200; P:establishment of protein localization to telomere; ISO:RGD.
DR GO; GO:0008585; P:female gonad development; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:RGD.
DR GO; GO:0031619; P:homologous chromosome orientation involved in meiotic metaphase I plate congression; IMP:RGD.
DR GO; GO:0001833; P:inner cell mass cell proliferation; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR GO; GO:0007141; P:male meiosis I; ISO:RGD.
DR GO; GO:0030879; P:mammary gland development; IMP:RGD.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; IMP:RGD.
DR GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:RGD.
DR GO; GO:0006289; P:nucleotide-excision repair; ISO:RGD.
DR GO; GO:0001556; P:oocyte maturation; ISO:RGD.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048478; P:replication fork protection; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0010225; P:response to UV-C; ISO:RGD.
DR GO; GO:0010165; P:response to X-ray; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IMP:RGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISO:RGD.
DR CDD; cd04493; BRCA2DBD_OB1; 1.
DR CDD; cd04495; BRCA2DBD_OB3; 1.
DR Gene3D; 2.40.50.140; -; 3.
DR InterPro; IPR015525; BRCA2.
DR InterPro; IPR015252; BRCA2_hlx.
DR InterPro; IPR036315; BRCA2_hlx_sf.
DR InterPro; IPR015187; BRCA2_OB_1.
DR InterPro; IPR015188; BRCA2_OB_3.
DR InterPro; IPR002093; BRCA2_repeat.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR015205; Tower_dom.
DR PANTHER; PTHR11289; PTHR11289; 1.
DR Pfam; PF09169; BRCA-2_helical; 1.
DR Pfam; PF09103; BRCA-2_OB1; 1.
DR Pfam; PF09104; BRCA-2_OB3; 1.
DR Pfam; PF00634; BRCA2; 7.
DR Pfam; PF09121; Tower; 1.
DR PIRSF; PIRSF002397; BRCA2; 1.
DR SMART; SM01341; Tower; 1.
DR SUPFAM; SSF50249; SSF50249; 3.
DR SUPFAM; SSF81872; SSF81872; 1.
DR PROSITE; PS50138; BRCA2_REPEAT; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..3343
FT /note="Breast cancer type 2 susceptibility protein homolog"
FT /id="PRO_0000064986"
FT REPEAT 984..1018
FT /note="BRCA2 1"
FT REPEAT 1197..1231
FT /note="BRCA2 2"
FT REPEAT 1405..1439
FT /note="BRCA2 3"
FT REPEAT 1503..1537
FT /note="BRCA2 4"
FT REPEAT 1645..1669
FT /note="BRCA2 5"
FT REPEAT 1828..1845
FT /note="BRCA2 6"
FT REPEAT 1939..1973
FT /note="BRCA2 7"
FT REPEAT 2019..2053
FT /note="BRCA2 8"
FT REGION 1..40
FT /note="Interaction with PALB2"
FT /evidence="ECO:0000250"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..982
FT /note="Interaction with NPM1"
FT /evidence="ECO:0000250"
FT REGION 985..2050
FT /note="Interaction with RAD51"
FT /evidence="ECO:0000250|UniProtKB:P97929"
FT REGION 2059..2138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2233..2300
FT /note="Interaction with HSF2BP"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT REGION 2297..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2313..2475
FT /note="Interaction with FANCD2"
FT /evidence="ECO:0000250"
FT REGION 2377..2407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2411..2762
FT /note="Interaction with SEM1"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT REGION 3114..3163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3231..3255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3289..3343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2612..2628
FT /note="Nuclear export signal; masked by interaction with
FT SEM1"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT COMPBIAS 356..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2081..2138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2300..2346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3115..3163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3289..3313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3314..3335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT MOD_RES 2063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT MOD_RES 3222
FT /note="Phosphoserine; by CDK1 and CDK2"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT MOD_RES 3250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51587"
FT TURN 2407..2409
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2410..2428
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2441..2443
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2444..2446
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2453..2457
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2467..2469
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2470..2473
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2479..2481
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2484..2489
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2494..2498
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2500..2502
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2503..2505
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2509..2511
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2512..2514
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2515..2517
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2527..2535
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2542..2544
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2547..2567
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2569..2571
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2573..2575
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2576..2578
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2579..2593
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2601..2606
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2615..2622
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2649..2652
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2657..2660
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2664..2671
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2680..2684
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2687..2690
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2697..2699
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2705..2707
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2710..2712
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2713..2715
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2718..2720
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2722..2724
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2746..2748
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2759..2763
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2765..2772
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2774..2782
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2895..2903
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2905..2909
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2913..2919
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2922..2927
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2934..2938
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2962..2965
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2970..2973
FT /evidence="ECO:0007829|PDB:1IYJ"
FT TURN 2974..2976
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2985..2989
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 2996..2998
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 2999..3005
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 3008..3010
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 3013..3015
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 3018..3022
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 3028..3035
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 3046..3054
FT /evidence="ECO:0007829|PDB:1IYJ"
FT STRAND 3064..3076
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 3080..3097
FT /evidence="ECO:0007829|PDB:1IYJ"
FT HELIX 3101..3110
FT /evidence="ECO:0007829|PDB:1IYJ"
SQ SEQUENCE 3343 AA; 372216 MW; 653DB110D2302A8D CRC64;
MTVEYKRRPT FWEIFKARCS TADLGPISLN WFEELFSEAP PYNTEHPEES EYKPQGHEPQ
LFKTPQRNPS YHQFASTPIM FKEQSQTLPL DQSPFKELGN VVANSKRKHH SKKKARKDPV
VDVASLPLKA CPSESPCTPR CTQVAPQRRK PVVSGSLFYT PKLEETPKHI SESLGVEVDP
DMSWTSSLAT PPTLSSTVLI ARDEEAHRNA FPADSPASLK SYFSNHNESL KKNDRFIPSV
SDSENKSQQE AFSQGLEKML GDSSSKINRF RDCLRKPIPN VLEDGETAVD TSGEDSFSLC
FPKRRTRNLQ KTRMGKMKKK IFSETRTDGL SEEARGQADD KNSFALEIEP RDSEPLDPSV
TNQKPLYSQS GDISSEAGQC SDSIWSQPDP SGLNGTQTRK IPLLHISFHK QSILEDFIDM
KKEGTGSITF PHISSLPEPE KMFSEETLVD KEHEGQHLES LEDSISGKQM VSGTSQTACL
SPSIRKSIVK MREPLEETLD TVFSDSMTSS AFTEELDASA GGLEIHTACS QREDSLCPSS
VDTGSWPTTL TDTSATVKNA GLITTLKNKR RKFIYSVSDD ASHQGKKLQT QRQSELTNLS
APFEASAFEV PFPFTNVDSG IPDSSIKRSN LPNDPEEPSL SLTNSFVTAA SKEISYIHAL
ISQDLNDKEA ILSEEKPQPY TALEADFLSC LPERSCENDQ KSPKVSDRKE KVLVSACRPS
GRLAAAVQLS SISFDSQENP LGSHNVTSTL KLTPSPKTPL SKPVVVSRGK MCKMPEKLQC
KSCKDNIELS KNIPLGVNEM CVLSENSETP ELLPPLEYIT EVSSSVKSQF NQNTKIAVVQ
KDQKDSTFIS EVTVHMNSEE LFPEKENNFA FQVTNESNKP NIGSTVEFQE EDLSHAKGHS
LKNSPMTVDR DLDDEQAGQV LITEDSDSLA VVHDCTKKSR NTIEQHQKGT ADKDFKSNSS
LYLKSDGNND YLDKWSEFLD PLMNHKLGGS FRTASNKEIK LSEDNVKKSK MFFKDIEEQY
PTSLDCIDTV STLQLANKKR LSEPHTFDLK SGTTVSTQCH SQSSVSHEDT HTAPQMLSSK
QDFHSSHNLT PSQKAEITEL STILEESGSQ FEFTQFKNPS HIAQNNTSAV LGNQMAVVRT
ASEEWKDVDL HLPLNPSSVG QIDHNKKFEC LVGVKQSSSH LLEDTCNQNT SCFLPIKEME
FGGFCSALGT KLSVSNEALR KAMKLFSDIE NISEEPSTKV GPRGFSSCAH HDSVASVFKI
KKQNTDKSFD EKSSKCQVTV QNNKEMTTCI LVDENPENYV KNIKQDNNYT GSQRNAYKLE
NSDVSKSSTS GTVYINKGDS DLPFAAEKGN KYPESCTQYV REENAQIKES VSDLTCLEVM
KAEETCHMKS SDKEQLPSDK MEQNMKEFNI SFQTASGKNI RVSKESLNKS VNILDQETED
LTVTSDSLNS KILCGINKDK MHISCHKKSI NIKKVFEEHF PIGTVSQLPA LQQYPEYEIE
SIKEPTLLSF HTASGKKVKI MQESLDKVKN LFDETQYVRK TTNFGHQESK PLKDREDYKE
RLTLAYEKIE VTASKCEEMQ NFVSKQTEML PQQNDHMYRQ TENLTSNGSS PKVHGNIENK
IEKNPRICCI CQSSYFVTED SALACYTGDS RKTCVGESSL SKGKKWLREQ SDKLGTRNTI
EIQCVKEHTE DFAGNALYEH SLVIIRTEID TSHVSENQAS TLFSDPNVCH SYLSHSSFCH
HDDMHNDSGY FLKDKIDSDV QPDMKNTEGN AIFPKISATK EIKLHPQTVN EECVQKLETN
ASPYANKNIA IDSAMLDLRN CKVGSPVFIT THSQETVRMK EIFTDNCSKI VEQNRESKPD
TCQTSCHKAL DNSEDFICPS SSGDVCINSP MAIFYPQSEQ ILQHNQSVSG LKKAATPPVS
LETWDTCKSI RGSPQEVHPS RTYGFFSTAS GKAVQVSDAS LEKARQVFSE IDGDAKQLAS
MVSLEGNEKS HHSVKRESSV VHNTHGVLSL RKTLPGNVSS FVFSGFSTAG GKLVTVSESA
LHKVKGMLEE FDLIRTEHTL QHSPTPEDVS KIPPQPCLES RTPEYSVSSK LQKTYNDKSR
SPSNYKESGS SGNTQSLEVS PQLSQMERKQ ETQSVLGTKV SQRKTNILEK KQNLPQNIKI
ESNKMETFSD VSMKTNVGEY YSKEPENYFE TEAVEIAKAF MEDDELTDSE QTHAKCSLFA
CPQNEALLNS RTRKRGGMAG VAVGQPPIKR SLLNEFDRII ESKGKSLTPS KSTPDGTIKD
RRLFTHHMSL EPVTCGPFCS SKERQETQSP HVTSPAQGLQ SKEHPSRHSA VGKSSSNPTV
SALRSERTRH SVSDKSTKVF VPPFKVKSRF HRDEHFDSKN VNLEGKNQKS ADGVSEDGND
SDFPQFNKDL MSSLQNARDL QDIRIKNKER HHLCPQPGSL YLTKSSTLPR ISLQAAVGDS
VPSACSPKQL YMYGVSKACI SVNSKNAEYF QFAIEDHFGK EALCAGKGFR LADGGWLIPS
DDGKAGKEEF YRALCDTPGV DPKLISSVWV SNHYRWIVWK LAAMEFAFPK EFANRCLNPE
RVLLQLKYRY DVEIDNSSRS ALKKILERDD TAAKTLVLCV SDIISLSTNV SETSGSKASS
EDSNKVDTIE LTDGWYAVKA QLDPPLLALV KSGRLTVGQK IITQGAELVG SPDACAPLEA
PDSLRLKISA NSTRPARWHS KLGFFHDPRP FPLPLSSLFS DGGNVGCVDV IVQRVYPLQW
VEKTVSGSYI FRNEREEEKE ALRFAEAQQK KLEALFTKVH TELKEHEEDI AQRRVLSRAL
TRQQVHALQD GAELYAAVQD ASDPEHLETC FSEEQLRALN NYRQMLSDKK QARIQSEFRK
ALEAAEKEEG LSRDVSTVWK LRVTSYKKRE KSALLSIWRP SSDLPSLLTE GQRYRIYHLS
VSKSKNKFEW PSIQLTATKR TQYQQLPVSS ETLLQLYQPR ELLPFSKLSD PAFQPPCSEV
DVVGVVVSVV KPIGLAPLVY LSDECLHLLV VKFGIDLNED IKPRVLIAAS NLQWRPESTS
RVPTLFAGNF SVFSASPKEA HFQERVTNMK HAIENIDTFY KEAEKKLIQV LKGDSPKWST
PNKDPTREPY PASTCSASDL ASGGQLPRSS PTDQQSYRSP LSCCTPTGKS TPLAHSAWMA
AKSCSGENEI EDPKTCRKKR ALDLLSRLPL PPPLSPVCTF VSPAAQKAFQ PPRSCGTKYP
TPLKKEGPSS PWSRAPFQKA SGVSLLDCDS VADEELALLS TQALVPHSVG GSEQVFPSDS
TRTEGPSAST EARPANRSKR ESLRDCRDDS DGKLAAETVP DYS
