BRCA1_PONPY
ID BRCA1_PONPY Reviewed; 1863 AA.
AC Q6J6J0; O46486;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 123.
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 Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
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).
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-988 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; AY589040; AAT44834.1; -; Genomic_DNA.
DR EMBL; AF019077; AAC39585.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6J6J0; -.
DR BMRB; Q6J6J0; -.
DR SMR; Q6J6J0; -.
DR PRIDE; Q6J6J0; -.
DR UniPathway; UPA00143; -.
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: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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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: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; Repeat;
KW Transcription; Transcription regulation; Transferase; Tumor suppressor;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1863
FT /note="Breast cancer type 1 susceptibility protein homolog"
FT /id="PRO_0000055834"
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..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1394
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..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1394
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..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1628
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 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48754"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48754"
FT MOD_RES 988
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT MOD_RES 1009
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 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 519
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 739
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 918
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38398"
FT CROSSLNK 987
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 755
FT /note="E -> G (in Ref. 2; AAC39585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1863 AA; 207954 MW; D2C2569CEB3EA83B CRC64;
MDLSAVRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ
CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLQ YANSYNFAKK ENNSPEHLKD
EVSIIQSMGY RNRAKRLLQS EPENPSLQET SPSVQLSNLG TVRTLRTKQR IQPQKKSVYI
ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTSDEISLDS AKKAACEFSE TDVTNTEHHQ
PSNNDLNTTE KRATERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE
KAEFCNKSKQ PGLARSQHNR WAGSKETCND RQTPSTEKKV DLNADPLCER KEWNKQKLPC
SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GRSESNAKVA DVLDVLNEVD
EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNIEDKI FGKTYRRKAS LPNLSHVTEN
LIIGAFVTEP QIIQERPLTN KLKRKRRATS GLHPEDFIKK ADLAVQKTPE MINQGTNQME
QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI
HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV
RHSRNLQLME DKEPATGAKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT NCSNTSELKE
FVNPSLPREE KEEKLGTVKV SNNAKDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ
ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKELIHGCFK DTRNDTEGFK YPLGHEVNHS
QETSIEMEES ELDTQYLQNT FKVSKRQSFA LFSNPGNPEE ECATFSAHSR SLKKQSPKVT
FECEQKEENQ GKNESNIKPV QTANITAGFP VVCQKDKPVD YAKCSIKGGS RFCLSSQFRG
NETGLITPNK HGLSQNPYHI PPLFPIKSFV KTKCKKNLLE ENSEEHSMSP EREMGNENIP
STVSIISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE VGSSDENIQA ELGRSRGPKL
NAMLRLGVLQ PEVYKQSFPG SNGKHPEIKK QEYEEVLQTV NTDFSPCLIS DNLEQPMRSS
HASQVCSETP NDLLDDGEIK EDTSFAENDI KESSAVFSKS VQRGELSRSP SPFTHTHLAQ
GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVSNIPSQ STRHSTVATE CLSKNTEENL
LSLKNSLNDY SNQVILVKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDRFFIGS
SKQMRHQSES QGVGLSDKEL VSDDEERGTD LEENNQEEQG VDSNLGEAAS GYESETSVSE
DCSGLSSQSD ILTTQQRDTM QDNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE
DLRNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTNKNKE PGVERSSPSK
CPSLDDRWYM HSCSGSLQNG NYPSQEELIK VVDVEKQQLE ESGPHDLTEP SYLPRQDLEG
TPYLESGISL FSDDPESDAS EDRAPESAHV GSIPSSTSAL KVPQLKVAES AQSPAAAQTT
NTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI
TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV
VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWIVQLCGAS VVKELSSFTL
GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH
SHY
