|
|
|
|
|
|
Description:
ATP-dependent DNA helicase 2 subunit 1 (EC 3.6.1.-) (ATP-dependent DNAhelicase II 70 kDa subunit) (Lupus Ku autoantigen protein p70) (Ku70)(70 kDa subunit of Ku antigen) (Thyroid-lupus autoantigen) (TLAA) (CTCbox-binding factor 75 kDa subunit) (CTCBF) (CTC75) (DNA-repair proteinXRCC6).
Molecular weight: 69712
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA ligation( GO:0006266 ) DNA repair( GO:0006281 ) double-strand break repair via nonhomologous end-joining( GO:0006303 )
Important dates:
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
07-MAR-2006, entry version 78.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein KU70_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | J04611 | AAA51733.1 | - |
| EMBL | J04607 | AAA61177.1 | - |
| EMBL | M32865 | AAA36155.1 | - |
| EMBL | S38729 | AAB22381.1 | - |
| EMBL | AY870329 | AAW34364.1 | - |
| EMBL | Z83840 | CAB46206.1 | - |
| EMBL | BC008343 | AAH08343.1 | - |
| EMBL | BC010034 | AAH10034.1 | - |
| EMBL | BC012154 | AAH12154.1 | - |
| EMBL | BC018259 | AAH18259.1 | - |
| EMBL | BC072449 | AAH72449.1 | - |
| PIR | A30299 | A30894. | |
| PDB | 1JEQ | X-ray | A=1-608. |
| PDB | 1JEY | X-ray | A=1-608. |
| PDB | 1JJR | NMR | A=-. |
| IntAct | P12956 | -.1 | |
| TRANSFAC | T05110 | -. | |
| SWISS-2DPAGE | P12956 | HUMAN. | |
| Ensembl | ENSG00000196419 | Homo sapiens.1 | |
| H-InvDB | HIX0016526 | -.1 | |
| HGNC | HGNC:4055 | XRCC6.1 | |
| MIM | 152690 | gene. | |
| Reactome | P12956 | -.1 | |
| LinkHub | P12956 | -.1 | |
| GO | GO:0005624 | C:membrane fraction | TAS. |
| GO | GO:0005634 | C:nucleus | TAS. |
| GO | GO:0005667 | C:transcription factor complex | IDA. |
| GO | GO:0004003 | F:ATP-dependent DNA helicase activity | TAS. |
| GO | GO:0003690 | F:double-stranded DNA binding | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006266 | P:DNA ligation | TAS. |
| GO | GO:0006303 | P:double-strand break repair via nonhomologou... | TAS. |
| GO | GO:0045893 | P:positive regulation of transcription, DNA-d... | IDA. |
| InterPro | IPR006164 | Ku. | |
| InterPro | IPR006165 | Ku70. | |
| InterPro | IPR005160 | Ku_C. | |
| InterPro | IPR005161 | Ku_N. | |
| InterPro | IPR003034 | SAP_DNA_bd. | |
| Pfam | PF02735 | Ku | 1. |
| Pfam | PF03730 | Ku_C | 1. |
| Pfam | PF03731 | Ku_N | 1. |
| Pfam | PF02037 | SAP | 1. |
| PIRSF | PIRSF003033 | Ku70 | 1. |
| SMART | SM00559 | Ku78 | 1. |
| SMART | SM00513 | SAP | 1. |
| TIGRFAMs | TIGR00578 | ku70 | 1. |
| PROSITE | PS50800 | SAP | 1. |
Keywords:
3D-structure; Acetylation; Antigen; ATP-binding; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase; Hydrolase; Nuclear protein; Nucleotide-binding; Phosphorylation; Systemic lupus erythematosus.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX MEDLINE=89174787; PubMed=2466842;
RA Reeves W.H., Sthoeger Z.M.;
RT "Molecular cloning of cDNA encoding the p70 (Ku) lupus autoantigen.";
RL J. Biol. Chem. 264:5047-5052(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX MEDLINE=89139411; PubMed=2917966;
RA Chan J.Y., Lerman M.I., Prabhakar B.S., Isozaki O., Santisteban P.,
RA Kuppers R.C., Oates E.L., Notkins A.L., Kohn L.D.;
RT "Cloning and characterization of a cDNA that encodes a 70-kDa novel
RT human thyroid autoantigen.";
RL J. Biol. Chem. 264:3651-3654(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=92301477; PubMed=1608402;
RA Griffith A.J., Craft J., Evans J., Mimori T., Hardin J.A.;
RT "Nucleotide sequence and genomic structure analyses of the p70 subunit
RT of the human Ku autoantigen: evidence for a family of genes encoding
RT Ku (p70)-related polypeptides.";
RL Mol. Biol. Rep. 16:91-97(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Livingston R.J., Rieder M.J., Chung M.-W., Downing T.K., Olson A.N.,
RA Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J.,
RA Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, Lung, Placenta, and Skin;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [7]
RP PROTEIN SEQUENCE OF 9-29 AND 298-316.
RX MEDLINE=92165807; PubMed=1537839;
RA Wedrychowski A., Henzel W., Huston L., Paslidis N., Ellerson D.,
RA McRae M., Seong D., Howard O.M.Z., Deisseroth A.;
RT "Identification of proteins binding to interferon-inducible
RT transcriptional enhancers in hematopoietic cells.";
RL J. Biol. Chem. 267:4533-4540(1992).
RN [8]
RP PROTEIN SEQUENCE OF 345-351, AND FUNCTION.
RX MEDLINE=95045391; PubMed=7957065;
RA Tuteja N., Tuteja R., Ochem A., Taneja P., Huang N.W., Simoncsits A.,
RA Susic S., Rahman K., Marusic L., Chen J., Zhang J., Wang S.,
RA Pongor S., Falaschi A.;
RT "Human DNA helicase II: a novel DNA unwinding enzyme identified as the
RT Ku autoantigen.";
RL EMBO J. 13:4991-5001(1994).
RN [9]
RP PROTEIN SEQUENCE OF 300-307 AND 555-564.
RX MEDLINE=95188883; PubMed=7882982;
RA Genersch E., Eckerskorn C., Lottspeich F., Herzog C., Kuehn K.,
RA Poeschl E.;
RT "Purification of the sequence-specific transcription factor CTCBF,
RT involved in the control of human collagen IV genes: subunits with
RT homology to Ku antigen.";
RL EMBO J. 14:791-800(1995).
RN [10]
RP PHOSPHORYLATION SITE SER-50.
RX PubMed=9362500; DOI=10.1093/emboj/16.22.6874;
RA Jin S., Weaver D.T.;
RT "Double-strand break repair by Ku70 requires heterodimerization with
RT Ku80 and DNA binding functions.";
RL EMBO J. 16:6874-6885(1997).
RN [11]
RP PHOSPHORYLATION SITE SER-5.
RX PubMed=10026262; DOI=10.1021/bi982584b;
RA Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P.;
RT "DNA-dependent protein kinase phosphorylation sites in Ku 70/80
RT heterodimer.";
RL Biochemistry 38:1819-1828(1999).
RN [12]
RP REVIEW.
RX MEDLINE=99305707; PubMed=10377944; DOI=10.1016/S0921-8777(99)00006-3;
RA Featherstone C., Jackson S.P.;
RT "Ku, a DNA repair protein with multiple cellular functions?";
RL Mutat. Res. 434:3-15(1999).
RN [13]
RP FUNCTION, AND INTERACTION WITH PRKDC.
RX MEDLINE=98414607; PubMed=9742108;
RA West R.B., Yaneva M., Lieber M.R.;
RT "Productive and nonproductive complexes of Ku and DNA-dependent
RT protein kinase at DNA termini.";
RL Mol. Cell. Biol. 18:5908-5920(1998).
RN [14]
RP INTERACTION WITH PRKDC.
RX MEDLINE=22397538; PubMed=12509254; DOI=10.1016/S1568-7864(01)00018-0;
RA Hsu H.-L., Yannone S.M., Chen D.J.;
RT "Defining interactions between DNA-PK and ligase IV/XRCC4.";
RL DNA Repair 1:225-235(2002).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH G22P2; PRKDC AND XRCC4, AND
RP PHOSPHORYLATION.
RX MEDLINE=22435910; PubMed=12547193; DOI=10.1016/S0022-2836(02)01328-1;
RA Calsou P., Delteil C., Frit P., Drouet J., Salles B.;
RT "Coordinated assembly of Ku and p460 subunits of the DNA-dependent
RT protein kinase on DNA ends is necessary for XRCC4-ligase IV
RT recruitment.";
RL J. Mol. Biol. 326:93-103(2003).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTIONS WITH
RP NARG1; MSX2; RUNX2 AND DLX5.
RC TISSUE=Heart, and Osteoblast;
RX MEDLINE=22241900; PubMed=12145306; DOI=10.1074/jbc.M206482200;
RA Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S.,
RA Ornitz D.M., Towler D.A.;
RT "Regulation of osteocalcin gene expression by a novel Ku antigen
RT transcription factor complex.";
RL J. Biol. Chem. 277:37280-37291(2002).
RN [17]
RP PHOSPHORYLATION SITE SER-26.
RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN [18]
RP STRUCTURE BY NMR OF 556-609.
RX MEDLINE=21474285; PubMed=11457852; DOI=10.1074/jbc.M105238200;
RA Zhang Z., Zhu L., Lin D., Chen F., Chen D.J., Chen Y.;
RT "The three-dimensional structure of the C-terminal DNA-binding domain
RT of human Ku70.";
RL J. Biol. Chem. 276:38231-38236(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 35-608 IN COMPLEX WITH G22P2.
RX MEDLINE=21385640; PubMed=11493912; DOI=10.1038/35088000;
RA Walker J.R., Corpina R.A., Goldberg J.;
RT "Structure of the Ku heterodimer bound to DNA and its implications for
RT double-strand break repair.";
RL Nature 412:607-614(2001).
Feature:
INIT_MET 0 0
CHAIN 1 608 ATP-dependent DNA helicase 2 subunit 1.
/FTId=PRO_0000210179.
DOMAIN 572 606 SAP.
COMPBIAS 1 60 Ser-rich (potentially targets for
phosphorylation).
COMPBIAS 10 28 Asp/Glu-rich (acidic).
COMPBIAS 329 341 Asp/Glu-rich (acidic).
MOD_RES 1 1 N-acetylserine (Potential).
MOD_RES 5 5 Phosphoserine (by PRKDC).
MOD_RES 26 26 Phosphoserine.
MOD_RES 50 50 Phosphoserine (by PRKDC).
CONFLICT 19 19 Q -> D (in Ref. 7).
STRAND 34 42
STRAND 44 44
HELIX 45 48
STRAND 52 55
HELIX 58 75
TURN 76 77
STRAND 81 88
STRAND 90 91
STRAND 93 94
TURN 95 96
TURN 99 100
STRAND 101 108
HELIX 112 119
TURN 120 121
STRAND 122 122
HELIX 123 134
STRAND 137 137
HELIX 142 154
TURN 155 155
STRAND 157 158
STRAND 160 170
STRAND 172 172
TURN 174 177
HELIX 179 195
TURN 196 196
STRAND 197 204
TURN 207 208
TURN 212 215
HELIX 216 218
TURN 219 219
STRAND 235 235
STRAND 237 237
HELIX 238 249
STRAND 250 250
STRAND 255 265
STRAND 267 273
STRAND 275 276
STRAND 285 288
TURN 289 291
STRAND 294 303
TURN 304 306
STRAND 309 309
HELIX 312 314
STRAND 315 321
TURN 322 323
STRAND 324 328
HELIX 330 335
TURN 336 337
STRAND 340 340
STRAND 342 351
HELIX 352 354
STRAND 355 355
HELIX 357 359
STRAND 362 362
STRAND 365 369
TURN 371 373
STRAND 374 375
TURN 376 376
HELIX 377 390
TURN 391 392
STRAND 393 400
STRAND 402 404
STRAND 408 415
STRAND 418 419
TURN 421 422
STRAND 425 427
STRAND 429 435
HELIX 439 441
STRAND 442 442
HELIX 455 467
TURN 468 468
STRAND 469 469
TURN 474 475
STRAND 476 476
HELIX 480 493
TURN 494 495
STRAND 497 498
TURN 505 506
STRAND 507 507
HELIX 510 517
TURN 518 519
HELIX 520 528
STRAND 529 529
STRAND 531 531
Comments:
-!- FUNCTION: Single stranded DNA-dependent ATP-dependent helicase.
Has a role in chromosome translocation. The DNA helicase II
complex binds preferentially to fork-like ends of double-stranded
DNA in a cell cycle-dependent manner. It works in the 3'-5'
direction. Binding to DNA may be mediated by p70. Involved in DNA
nonhomologous end joining (NHEJ) required for double-strand break
repair and V(D)J recombination. The Ku p70/p86 dimer acts as
regulatory subunit of the DNA-dependent protein kinase complex
DNA-PK by increasing the affinity of the catalytic subunit PRKDC
to DNA by 100-fold. The Ku p70/p86 dimer is probably involved in
stabilizing broken DNA ends and bringing them together. The
assembly of the DNA-PK complex to DNA ends is required for the
NHEJ ligation step. Required for osteocalcin gene expression (By
similarity).
-!- SUBUNIT: Heterodimer of a 70 kDa and a 80 kDa subunit. The dimer
associates in a DNA-dependent manner with PRKDC to form the DNA-
dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4
complex. The dimer also associates with NARG1, and this complex
binds to the osteocalcin promoter and activates osteocalcin
expression. In addition, the 70 kDa subunit binds to the
osteoblast-specific transcription factors MSX2, RUNX2 and DLX5.
-!- INTERACTION:
Q96P48:CENTD2; NbExp=1; IntAct=EBI-353208, EBI-710003;
P42858:HD; NbExp=1; IntAct=EBI-353208, EBI-466029;
P13010:XRCC5; NbExp=1; IntAct=EBI-353208, EBI-357997;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- INDUCTION: In osteoblasts, by FGF2.
-!- PTM: Phosphorylation by PRKDC may enhance helicase activity.
Phosphorylation of Ser-50 does not affect DNA repair.
-!- DISEASE: Individuals with systemic lupus erythematosus (SLE) and
related disorders produce extremely large amounts of
autoantibodies to p70 and p86. Existence of a major autoantigenic
epitope or epitopes on the C-terminal 190 amino acids of p70
containing the leucine repeat. The majority of autoantibodies to
p70 in most sera from patients with SLE seem to be reactive with
this region.
-!- SIMILARITY: Belongs to the ATP-dependent DNA helicase II 70 kDa
subunit family.
-!- SIMILARITY: Contains 1 SAP domain.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
Sequence length: 608
SGWESYYKTE GDEEAEEEQE ENLEASGDYK YSGRDSLIFL VDASKAMFES QSEDELTPFD
MSIQCIQSVY ISKIISSDRD LLAVVFYGTE KDKNSVNFKN IYVLQELDNP GAKRILELDQ
FKGQQGQKRF QDMMGHGSDY SLSEVLWVCA NLFSDVQFKM SHKRIMLFTN EDNPHGNDSA
KASRARTKAG DLRDTGIFLD LMHLKKPGGF DISLFYRDII SIAEDEDLRV HFEESSKLED
LLRKVRAKET RKRALSRLKL KLNKDIVISV GIYNLVQKAL KPPPIKLYRE TNEPVKTKTR
TFNTSTGGLL LPSDTKRSQI YGSRQIILEK EETEELKRFD DPGLMLMGFK PLVLLKKHHY
LRPSLFVYPE ESLVIGSSTL FSALLIKCLE KEVAALCRYT PRRNIPPYFV ALVPQEEELD
DQKIQVTPPG FQLVFLPFAD DKRKMPFTEK IMATPEQVGK MKAIVEKLRF TYRSDSFENP
VLQQHFRNLE ALALDLMEPE QAVDLTLPKV EAMNKRLGSL VDEFKELVYP PDYNPEGKVT
KRKHDNEGSG SKRPKVEYSE EELKTHISKG TLGKFTVPML KEACRAYGLK SGLKKQELLE
ALTKHFQD