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Description:
Mediator of DNA damage checkpoint protein 1 (Nuclear factor with BRCTdomains 1).
Molecular weight: 2266
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 3.
07-MAR-2006, entry version 42.
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 MDC1_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | D79992 | BAA11487.2.1 | ALT_INIT |
| EMBL | CR749828 | CAH18685.1 | ALT_TERM |
| EMBL | BA000025 | BAB63322.1 | - |
| EMBL | AB088099 | BAC54931.1 | - |
| EMBL | AL662848 | CAI17440.1 | - |
| EMBL | AL662797 | CAI18195.1 | - |
| EMBL | AL845353 | CAI41890.1 | ALT_SEQ |
| EMBL | AL845353 | CAI41891.1 | - |
| PDB | 2ADO | X-ray | A/B=1891-2086. |
| PDB | 2AZM | X-ray | A/B=1883-2089. |
| PDB | 2ETX | X-ray | A/B=1884-2089. |
| IntAct | Q14676 | -.1 | |
| Ensembl | ENSG00000137337 | Homo sapiens.1 | |
| HGNC | HGNC:21163 | MDC1.1 | |
| MIM | 607593 | gene. | |
| Reactome | Q14676 | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| InterPro | IPR001357 | BRCT. | |
| InterPro | IPR000253 | FHA. | |
| Pfam | PF00533 | BRCT | 2. |
| Pfam | PF00498 | FHA | 1. |
| SMART | SM00240 | FHA | 1. |
| PROSITE | PS50172 | BRCT | 1. |
| PROSITE | PS50006 | FHA_DOMAIN | 1. |
Keywords:
3D-structure; Alternative splicing; Cell cycle; DNA damage; DNA repair; Nuclear protein; Phosphorylation; Polymorphism; Repeat.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP PRO-1540.
RC TISSUE=Bone marrow;
RX MEDLINE=96281124; PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V.
RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP LYS-268.
RC TISSUE=Testis;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-251;
RP ALA-586; ASP-1509 AND PRO-1540.
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-1509.
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-268.
RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RA Mochan T.A., Venere M., DiTullio R.A. Jr., Halazonetis T.D.;
RT "53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways
RT activating ataxia-telangiectasia mutated (ATM) in response to DNA
RT damage.";
RL Cancer Res. 63:8586-8591(2003).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12475977; DOI=10.1074/jbc.M210749200;
RA Shang Y.L., Bodero A.J., Chen P.-L.;
RT "NFBD1, a novel nuclear protein with signature motifs of FHA and BRCT,
RT and an internal 41-amino acid repeat sequence, is an early participant
RT in DNA damage response.";
RL J. Biol. Chem. 278:6323-6329(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ATM- AND CELL
RP CYCLE-DEPENDENT PHOSPHORYLATION, AND REGIONS NLS1 AND NLS2.
RX PubMed=12499369; DOI=10.1074/jbc.M211392200;
RA Xu X., Stern D.F.;
RT "NFBD1/KIAA0170 is a chromatin-associated protein involved in DNA
RT damage signaling pathways.";
RL J. Biol. Chem. 278:8795-8803(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHEK2.
RX PubMed=12551934; DOI=10.1074/jbc.C300001200;
RA Peng A., Chen P.-L.;
RT "NFBD1, like 53BP1, is an early and redundant transducer mediating
RT Chk2 phosphorylation in response to DNA damage.";
RL J. Biol. Chem. 278:8873-8876(2003).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTIONS WITH BRCA1 AND BARD1.
RX PubMed=12611903; DOI=10.1074/jbc.C300060200;
RA Lou Z., Chini C.C.S., Minter-Dykhouse K., Chen J.;
RT "Mediator of DNA damage checkpoint protein 1 regulates BRCA1
RT localization and phosphorylation in DNA damage checkpoint control.";
RL J. Biol. Chem. 278:13599-13602(2003).
RN [11]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP INTERACTION WITH THE MRN COMPLEX, ATM-DEPENDENT PHOSPHORYLATION, AND
RP MUTAGENESIS OF ARG-58.
RX PubMed=12607003; DOI=10.1038/nature01445;
RA Goldberg M., Stucki M., Falck J., D'Amours D., Rahman D., Pappin D.,
RA Bartek J., Jackson S.P.;
RT "MDC1 is required for the intra-S-phase DNA damage checkpoint.";
RL Nature 421:952-956(2003).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK2,
RP ATM/CHEK2-DEPENDENT PHOSPHORYLATION, AND MUTAGENESIS OF ARG-58;
RP SER-72; ASN-96; GLY-97 AND THR-98.
RX PubMed=12607004; DOI=10.1038/nature01447;
RA Lou Z., Minter-Dykhouse K., Wu X., Chen J.;
RT "MDC1 is coupled to activated CHK2 in mammalian DNA damage response
RT pathways.";
RL Nature 421:957-961(2003).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTIONS WITH THE MRN COMPLEX;
RP ATM; FANCD2; H2AFX; SMC1L1 AND TP53BP1, AND ATM1- AND NBS1-DEPENDENT
RP PHOSPHORYLATION.
RX PubMed=12607005; DOI=10.1038/nature01446;
RA Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.;
RT "MDC1 is a mediator of the mammalian DNA damage checkpoint.";
RL Nature 421:961-966(2003).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH H2AFX.
RX PubMed=15201865; DOI=10.1038/sj.emboj.7600269;
RA Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S.,
RA Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.;
RT "Mdc1 couples DNA double-strand break recognition by Nbs1 with its
RT H2AX-dependent chromatin retention.";
RL EMBO J. 23:2674-2683(2004).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE PRKDC
RP COMPLEX.
RX PubMed=15377652; DOI=10.1074/jbc.C400375200;
RA Lou Z., Chen B.P.-C., Asaithamby A., Minter-Dykhouse K., Chen D.J.,
RA Chen J.;
RT "MDC1 regulates DNA-PK autophosphorylation in response to DNA
RT damage.";
RL J. Biol. Chem. 279:46359-46362(2004).
RN [16]
RP PHOSPHORYLATION SITES SER-168; SER-329; SER-964; SER-988; SER-995;
RP THR-1425 AND THR-1461.
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 [17]
RP REVIEW.
RX PubMed=15279781; DOI=10.1016/j.dnarep.2004.03.007;
RA Stucki M., Jackson S.P.;
RT "MDC1/NFBD1: a key regulator of the DNA damage response in higher
RT eukaryotes.";
RL DNA Repair 3:953-957(2004).
Feature:
CHAIN 1 2089 Mediator of DNA damage checkpoint protein
1.
/FTId=PRO_0000096316.
DOMAIN 54 105 FHA.
DOMAIN 1892 1970 BRCT 1.
DOMAIN 1991 2082 BRCT 2.
REGION 1 150 Interaction with CHEK2.
REGION 2 220 Interaction with the MRN complex.
REGION 145 568 Required for nuclear localization (NLS1).
REGION 1148 1610 Interaction with the PRKDC complex.
REGION 1698 2089 Required for nuclear localization (NLS2).
COMPBIAS 1034 1469 Pro-rich.
MOD_RES 168 168 Phosphoserine.
MOD_RES 329 329 Phosphoserine.
MOD_RES 964 964 Phosphoserine.
MOD_RES 988 988 Phosphoserine.
MOD_RES 995 995 Phosphoserine.
MOD_RES 1425 1425 Phosphothreonine.
MOD_RES 1461 1461 Phosphothreonine.
VARSPLIC 741 1004 Missing (in isoform 2).
/FTId=VSP_014593.
VARIANT 251 251 E -> K (in dbSNP:2517560).
/FTId=VAR_022843.
VARIANT 268 268 R -> K (in dbSNP:9262152).
/FTId=VAR_022844.
VARIANT 371 371 E -> K (in dbSNP:2075015).
/FTId=VAR_022845.
VARIANT 586 586 S -> A (in dbSNP:2844707).
/FTId=VAR_022846.
VARIANT 1509 1509 E -> D (in dbSNP:3132589).
/FTId=VAR_022847.
VARIANT 1540 1540 S -> P (in dbSNP:3130645).
/FTId=VAR_022848.
MUTAGEN 58 58 R->A: Abrogates binding to the MRE11
complex and to CHEK2.
MUTAGEN 72 72 S->A: Abrogates binding to CHEK2.
MUTAGEN 96 96 N->A: Abrogates binding to CHEK2; when
associated with A-97 and A-98.
MUTAGEN 97 97 G->A: Abrogates binding to CHEK2; when
associated with A-96 and A-98.
MUTAGEN 98 98 T->A: Abrogates binding to CHEK2; when
associated with A-96 and A-97.
CONFLICT 536 536 I -> M (in Ref. 1).
CONFLICT 638 638 L -> P (in Ref. 2).
CONFLICT 645 1326 Missing (in Ref. 2).
CONFLICT 1005 1005 G -> GS (in Ref. 3).
CONFLICT 1041 1041 T -> A (in Ref. 1).
CONFLICT 1533 1533 A -> T (in Ref. 4).
CONFLICT 1545 1545 Q -> R (in Ref. 1).
CONFLICT 1668 1668 Q -> R (in Ref. 2).
CONFLICT 1843 1843 E -> K (in Ref. 2).
CONFLICT 2048 2048 H -> R (in Ref. 2).
STRAND 1894 1897
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HELIX 2063 2071
TURN 2072 2072
HELIX 2076 2079
STRAND 2080 2080
TURN 2083 2084
Comments:
-!- FUNCTION: Required for checkpoint mediated cell cycle arrest in
response to DNA damage within both the S phase and G2/M phases of
the cell cycle. May serve as a scaffold for the recruitment of DNA
repair and signal transduction proteins to discrete foci of DNA
damage marked by Ser-139 phosphorylation of histone H2AFX. Also
required for downstream events subsequent to the recruitment of
these proteins. These include phosphorylation and activation of
the ATM, CHEK1/CHK1 and CHEK2/CHK2/CDS1 kinases, and stabilization
of TP53 and apoptosis. ATM and CHEK2 may also be activated
independently by a parallel pathway mediated by TP53BP1.
-!- SUBUNIT: Interacts with several proteins involved in the DNA
damage response, although not all these interactions may be
direct. Interacts with H2AFX, which requires phosphorylation of
H2AFX on Ser-139. Interacts with the MRN complex, composed of
MRE11A/MRE11, RAD50, and NBS1. Interacts with CHEK2/CHK2/CDS1,
which requires ATM-mediated phosphorylation of Thr-68 within the
FHA domain of CHEK2. Interacts constitutively with the BRCA1-BARD1
complex, SMC1L1 and TP53BP1. Interacts with ATM and FANCD2, and
these interactions are reduced upon DNA damage. Also interacts
with the PRKDC complex, composed of G22P1/KU70, XRCC5/KU80 and
PRKDC/XRCC7. This interaction may be required for PRKDC
autophosphorylation, which is essential for DNA double strand
break (DSB) repair.
-!- INTERACTION:
Q13315:ATM; NbExp=1; IntAct=EBI-495453, EBI-495465;
O60934:NBS; NbExp=1; IntAct=EBI-495453, EBI-494844;
-!- SUBCELLULAR LOCATION: Nuclear; associated with chromatin.
Relocalizes to discrete nuclear foci following DNA damage; this
requires Ser-139 phosphorylation of H2AFX.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14676-1; Sequence=Displayed;
Name=2;
IsoId=Q14676-2; Sequence=VSP_014593;
Note=Gene prediction based on EST data. No experimental
confirmation available;
-!- TISSUE SPECIFICITY: Highly expressed in testis.
-!- DOMAIN: Tandemly repeated BRCT domains are characteristic of
proteins involved in DNA damage signaling. In MDC1, these repeats
are required for localization to chromatin which flanks sites of
DNA damage marked by Ser-139 phosphorylation of H2AFX.
-!- PTM: Phosphorylated on undefined residues upon exposure to
ionizing radiation (IR), ultraviolet radiation (UV), and
hydroxyurea (HU). Phosphorylation in response to IR requires ATM,
NBS1, and possibly CHEK2. Also phosphorylated during the G2/M
phase of the cell cycle and during activation of the mitotic
spindle checkpoint.
-!- SIMILARITY: Contains 2 BRCT domains.
-!- SIMILARITY: Contains 1 FHA domain.
-!- CAUTION: Ref.2 sequence differs from that shown due to the
presence of a stop codon at position 1804 which was translated as
Gln to extend the sequence.
-!- CAUTION: Ref.5 (CAI41890) sequence differs from that shown due to
erroneous gene model prediction.
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Sequence length: 2089
MEDTQAIDWD VEEEEETEQS SESLRCNVEP VGRLHIFSGA HGPEKDFPLH LGKNVVGRMP
DCSVALPFPS ISKQHAEIEI LAWDKAPILR DCGSLNGTQI LRPPKVLSPG VSHRLRDQEL
ILFADLLCQY HRLDVSLPFV SRGPLTVEET PRVQGETQPQ RLLLAEDSEE EVDFLSERRM
VKKSRTTSSS VIVPESDEEG HSPVLGGLGP PFAFNLNSDT DVEEGQQPAT EEASSAARRG
ATVEAKQSEA EVVTEIQLEK DQPLVKERDN DTKVKRGAGN GVVPAGVILE RSQPPGEDSD
TDVDDDSRPP GRPAEVHLER AQPFGFIDSD TDAEEERIPA TPVVIPMKKR KIFHGVGTRG
PGAPGLAHLQ ESQAGSDTDV EEGKAPQAVP LEKSQASMVI NSDTDDEEEV SAALTLAHLK
ESQPAIWNRD AEEDMPQRVV LLQRSQTTTE RDSDTDVEEE ELPVENREAV LKDHTKIRAL
VRAHSEKDQP PFGDSDDSVE ADKSSPGIHL ERSQASTTVD INTQVEKEVP PGSAIIHIKK
HQVSVEGTNQ TDVKAVGGPA KLLVVSLEEA WPLHGDCETD AEEGTSLTAS VVADVRKSQL
PAEGDAGAEW AAAVLKQERA HEVGAQGGPP VAQVEQDLPI SRENLTDLVV DTDTLGESTQ
PQREGAQVPT GREREQHVGG TKDSEDNYGD SEDLDLQATQ CFLENQGLEA VQSMEDEPTQ
AFMLTPPQEL GPSHCSFQTT GTLDEPWEVL ATQPFCLRES EDSETQPFDT HLEAYGPCLS
PPRAIPGDQH PESPVHTEPM GIQGRGRQTV DKVMGIPKET AERVGPERGP LERETEKLLP
ERQTDVTGEE ELTKGKQDRE QKQLLARDTQ RQESDKNGES ASPERDRESL KVEIETSEEI
QEKQVQKQTL PSKAFEREVE RPVANRECDP AELEEKVPKV ILERDTQRGE PEGGSQDQKG
QASSPTPEPG VGAGDLPGPT SAPVPSGSQS GGRGSPVSPR RHQKGLLNCK MPPAEKASRI
RAAEKVSRGD QESPDACLPP TVPEAPAPPQ KPLNSQSQKH LAPPPLLSPL LPSIKPTVRK
TRQDGSQEAP EAPLSSELEP FHPKPKIRTR KSSRMTPFPA TSAAPEPHPS TSTAQPVTPK
PTSQATRSRT NRSSVKTPEP VVPTAPELQP STSTDQPVTS EPTSQVTRGR KSRSSVKTPE
TVVPTALELQ PSTSTDRPVT SEPTSQATRG RKNRSSVKTP EPVVPTAPEL QPSTSTDQPV
TSEPTYQATR GRKNRSSVKT PEPVVPTAPE LRPSTSTDRP VTPKPTSRTT RSRTNMSSVK
TPETVVPTAP ELQISTSTDQ PVTPKPTSRT TRSRTNMSSV KNPESTVPIA PELPPSTSTE
QPVTPEPTSR ATRGRKNRSS GKTPETLVPT APKLEPSTST DQPVTPEPTS QATRGRTNRS
SVKTPETVVP TAPELQPSTS TDQPVTPEPT SQATRGRTDR SSVKTPETVV PTAPELQASA
STDQPVTSEP TSRTTRGRKN RSSVKTPETV VPAAPELQPS TSTDQPVTPE PTSRATRGRT
NRSSVKTPES IVPIAPELQP STSRNQLVTP EPTSRATRCR TNRSSVKTPE PVVPTAPEPH
PTTSTDQPVT PKLTSRATRR KTNRSSVKTP KPVEPAASDL EPFTPTDQSV TPEAIAQGGQ
SKTLRSSTVR AMPVPTTPEF QSPVTTDQPI SPEPITQPSC IKRQRAAGNP GSLAAPIDHK
PCSAPLEPKS QASRNQRWGA VRAAESLTAI PEPASPQLLE TPIHASQIQK VEPAGRSRFT
PELQPKASQS RKRSLATMDS PPHQKQPQRG EVSQKTVIIK EEEEDTAEKP GKEEDVVTPK
PGKRKRDQAE EEPNRIPSRS LRRTKLNQES TAPKVLFTGV VDARGERAVL ALGGSLAGSA
AEASHLVTDR IRRTVKFLCA LGRGIPILSL DWLHQSRKAG FFLPPDEYVV TDPEQEKNFG
FSLQDALSRA RERRLLEGYE IYVTPGVQPP PPQMGEIISC CGGTYLPSMP RSYKPQRVVI
TCPQDFPHCS IPLRVGLPLL SPEFLLTGVL KQEAKPEAFV LSPLEMSST