BRCA1_MACMU
ID BRCA1_MACMU Reviewed; 1863 AA.
AC Q6J6I9; O46487; Q28525;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Breast cancer type 1 susceptibility protein homolog;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P38398};
DE AltName: Full=RING-type E3 ubiquitin transferase BRCA1 {ECO:0000305};
GN Name=BRCA1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15385441; DOI=10.1093/hmg/ddh301;
RA Pavlicek A., Noskov V.N., Kouprina N., Barrett J.C., Jurka J., Larionov V.;
RT "Evolution of the tumor suppressor BRCA1 locus in primates: implications
RT for cancer predisposition.";
RL Hum. Mol. Genet. 13:2737-2751(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-1365.
RX PubMed=9462745; DOI=10.1038/ng0298-155;
RA Hacia J.G., Makalowski W., Edgemon K., Erdos M.R., Robbins C.M.,
RA Fodor S.P.A., Brody L.C., Collins F.S.;
RT "Evolutionary sequence comparisons using high-density oligonucleotide
RT arrays.";
RL Nat. Genet. 18:155-158(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1189-1253.
RA Thompson M.E., Holt J.T.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the
CC formation of 'Lys-6'-linked polyubiquitin chains and plays a central
CC role in DNA repair by facilitating cellular responses to DNA damage. It
CC is unclear whether it also mediates the formation of other types of
CC polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse
CC range of cellular pathways such as DNA damage repair, ubiquitination
CC and transcriptional regulation to maintain genomic stability. Regulates
CC centrosomal microtubule nucleation. Required for appropriate cell cycle
CC arrests after ionizing irradiation in both the S-phase and the G2 phase
CC of the cell cycle. Required for FANCD2 targeting to sites of DNA
CC damage. Inhibits lipid synthesis by binding to inactive phosphorylated
CC ACACA and preventing its dephosphorylation. Contributes to homologous
CC recombination repair (HRR) via its direct interaction with PALB2, fine-
CC tunes recombinational repair partly through its modulatory role in the
CC PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks.
CC Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation
CC and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-
CC mediated ubiquitination of RBBP8. Acts as a transcriptional activator.
CC {ECO:0000250|UniProtKB:P38398}.
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:0000250|UniProtKB:P38398};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated genome
CC surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1,
CC ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This
CC association could be a dynamic process changing throughout the cell
CC cycle and within subnuclear domains. Component of the BRCA1-A complex,
CC at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36,
CC BABAM2 and BABAM1/NBA1. Interacts (via the BRCT domains) with ABRAXAS1
CC (phosphorylated form); this is important for recruitment to sites of
CC DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1
CC (phosphorylated form). Component of the BRCA1-RBBP8 complex. Interacts
CC (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the
CC interaction ubiquitinates RBBP8, regulates CHEK1 activation, and
CC involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA
CC damage. Associates with RNA polymerase II holoenzyme. Interacts with
CC SMC1A, NELFB, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, UBXN1 and
CC PCLAF. Interacts (via BRCT domains) with BRIP1 (phosphorylated form).
CC Interacts with FANCD2 (ubiquitinated form). Interacts with H2AX
CC (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with
CC ACACA (phosphorylated form); the interaction prevents dephosphorylation
CC of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2.
CC Interacts directly with PALB2; the interaction is essential for its
CC function in HRR. Interacts directly with BRCA2; the interaction occurs
CC only in the presence of PALB2 which serves as the bridging protein.
CC Interacts (via the BRCT domains) with LMO4; the interaction represses
CC the transcriptional activity of BRCA1. Interacts (via the BRCT domains)
CC with CCAR2 (via N-terminus); the interaction represses the
CC transcriptional activator activity of BRCA1 (By similarity). Interacts
CC with EXD2 (By similarity). Interacts (via C-terminus) with DHX9; this
CC interaction is direct and links BRCA1 to the RNA polymerase II
CC holoenzyme (By similarity). {ECO:0000250|UniProtKB:P38398}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}.
CC Chromosome {ECO:0000250|UniProtKB:P48754}. Cytoplasm
CC {ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of DNA damage
CC at double-strand breaks (DSBs); recruitment to DNA damage sites is
CC mediated by the BRCA1-A complex. Translocated to the cytoplasm during
CC UV-induced apoptosis. {ECO:0000250|UniProtKB:P38398}.
CC -!- DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF motif
CC on proteins. The interaction with the phosphorylated pSXXF motif of
CC ABRAXAS1, recruits BRCA1 at DNA damage sites.
CC {ECO:0000250|UniProtKB:P38398}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
CC {ECO:0000250|UniProtKB:P38398}.
CC -!- PTM: Phosphorylated in response to IR, UV, and various stimuli that
CC cause checkpoint activation, probably by ATM or ATR. Phosphorylation at
CC Ser-987 by CHEK2 regulates mitotic spindle assembly. Phosphorylation by
CC AURKA regulates centrosomal microtubule nucleation.
CC {ECO:0000250|UniProtKB:P38398}.
CC -!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination.
CC 'Lys-6'-linked polyubiquitination does not promote degradation.
CC {ECO:0000250|UniProtKB:P38398}.
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DR EMBL; AY589041; AAT44833.1; -; Genomic_DNA.
DR EMBL; AF019078; AAC39586.1; -; Genomic_DNA.
DR EMBL; U44730; AAB03212.1; -; Genomic_DNA.
DR PIR; G02999; G02999.
DR RefSeq; NP_001108421.1; NM_001114949.1.
DR AlphaFoldDB; Q6J6I9; -.
DR BMRB; Q6J6I9; -.
DR SMR; Q6J6I9; -.
DR STRING; 9544.ENSMMUP00000034386; -.
DR GeneID; 712634; -.
DR KEGG; mcc:712634; -.
DR CTD; 672; -.
DR eggNOG; KOG4362; Eukaryota.
DR InParanoid; Q6J6I9; -.
DR OrthoDB; 496760at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0070531; C:BRCA1-A complex; IBA:GO_Central.
DR GO; GO:0031436; C:BRCA1-BARD1 complex; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043009; P:chordate embryonic development; IBA:GO_Central.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR011364; BRCA1.
DR InterPro; IPR031099; BRCA1-associated.
DR InterPro; IPR025994; BRCA1_serine_dom.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13763; PTHR13763; 1.
DR Pfam; PF00533; BRCT; 2.
DR Pfam; PF12820; BRCT_assoc; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PIRSF; PIRSF001734; BRCA1; 1.
DR PRINTS; PR00493; BRSTCANCERI.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; Cell cycle; Chromosome; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Fatty acid biosynthesis;
KW Fatty acid metabolism; Isopeptide bond; Lipid biosynthesis;
KW Lipid metabolism; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Tumor suppressor; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..1863
FT /note="Breast cancer type 1 susceptibility protein homolog"
FT /id="PRO_0000055831"
FT DOMAIN 1642..1736
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 1756..1855
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ZN_FING 24..65
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 231..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1424
FT /note="Interaction with PALB2"
FT /evidence="ECO:0000250"
FT REGION 1440..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1360
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48754"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48754"
FT MOD_RES 987
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 518
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 582
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 733
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 917
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 986
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 1079
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CONFLICT 366
FT /note="A -> T (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="A -> P (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="Missing (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="M -> I (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="D -> G (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="E -> Q (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="E -> K (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="P -> S (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="A -> E (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="Q -> R (in Ref. 2; AAC39586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1863 AA; 207790 MW; 6AA0DE2AA9A983BC CRC64;
MDLSAVRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCRFCMLK LLNQKKGPSQ
CPLCKNDITK RSLQESTRFS QLVEELLKII HAFQLDTGLQ FANSYNFAKK ENHSPEHLKD
EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVPLSNLG IVRTLRTKQQ IQPQKKSVYI
ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDETSLDS AKKAACEFSE KDITNTEHHQ
SSNNDLNTTE KHATERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSLL LTKDRMNVEK
AEFCNKSKQP GLARSQHNRW TGSKETCNDR QTPSTEKKVD LNANALYERK EWNKQKLPCS
ENPRDAEDVP WITLNSSIQK VNEWFSRSDE LLSSDDSHDG GSESNAKVAD VLDVLNEVDE
YSGSSEKIDL LASDPHEPLI CKSERVHSSS VESNIKDKIF GKTYRRKANL PNLSHVTENL
IIGALVTESQ IMQERPLTNK LKRKRRTTSG LHPEDFIKKA DLAVQKTPEI INQGTNQMEQ
NGQVMNITNS AHENKTKGDS IQNEKNPNAI ESLEEESAFK TKAEPISSSI NNMELELNIH
NSKAPKKNRL RRKSSTRHIH ALELVVSRNL SPPNCTELQI DSCSSSEEIK KKNYNQMPVR
HSRNLQLMED KESATGAKKS NKPNEQTSKR HASDTFPELK LTKVPGSFTN CSNTSELKEF
VNPSLSREEK EEKLETVKVS NNAKDPKDLM LSGERVLQTE RSVESSSISL VPDTDYGTQE
SISLLEVSTL GKAKTERNKC MSQCAAFENP KELIHGCSED TRNDTEGFKY PLGSEVNHSQ
ETSIEIEESE LDTQYLQNTF KVSKRQSFAL FSNPGNPEEE CATFSAHSRS LKKQSPKVTS
ECEQKEENQG KKESNIKPVQ TVNITAGFSV VCQKDKPVDN AKCSIKGGSR FCLSSQFRGN
ETGLITPNKH GLLQNPYHIP PLFPVKSFVK TKCNKNLLEE NSEEHSVSPE RAVGNENIIP
STVSTISHNN IRENAFKEAS SSNINEVGSS TNEVGSSINE VGPSDENIQA ELGRNRGPKL
NAVLRLGLLQ PEVCKQSLPI SNCKHPEIKK QEHEELVQTV NTDFSPCLIS DNLEQPMGSS
HASEVCSETP DDLLDDGEIK EDTSFAANDI KESSAVFSKS IQRGELSRSP SPFTHTHLAQ
GYQKEAKKLE SSEENLSSED EELPCFQHLL FGKVSNIPSQ TTRHSTVATE CLSKNTEENL
LSLKNSLTDC SNQVILAKAS QEHHLSEETK CSGSLFSSQC SELEDLTANT NTQDPFLIGS
SKRMRHQSES QGVGLSDKEL VSDDEERGTG LEEDNQEEQS VDSNLGEAAS GYESETSVSE
DCSRLSSQSE ILTTQQRDTM QDNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIITDSSALE
DLRNPEQSTS EKAVLTSQKS SEYPINQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK
CQSLEDRWYV HSSSGSLQNG NYPSQEELIK VVDVETQQLE KSGPHDLMEP SYLPRQDLDG
TPYLESGISL FSDDPESDPS EDRAPESAHV GSIPSSTSAL KVPQWQVAES AQSPAAAHNT
NTAGYNAMEE SVSRENPKLT ASTERVNKRM SLVVSGLTPE EFMLVYKFAR RYHIALTNLI
SEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV
VNGRNHQGPK RARESPDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL
GTGFHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH
SHY
