ATAD5_MOUSE
ID ATAD5_MOUSE Reviewed; 1826 AA.
AC Q4QY64; Q3TMG5; Q3UW85; Q3V306; Q3V3T9; Q5SSK4; Q8BUH4; Q8CGG7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=ATPase family AAA domain-containing protein 5;
DE AltName: Full=Chromosome fragility-associated gene 1 protein;
GN Name=Atad5; Synonyms=Frag1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAD9A
RP AND RB1, AND TISSUE SPECIFICITY.
RX PubMed=15983387; DOI=10.1073/pnas.0504222102;
RA Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M., Mori M.,
RA Croce C.M., Huebner K., Ozawa K., Furukawa Y.;
RT "Frag1, a homolog of alternative replication factor C subunits, links
RT replication stress surveillance with apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-762 AND 1463-1826 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Eye, Lung, Stomach, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-472 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-727, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has an imporant role in DNA replication and in maintaining
CC genome integrity during replication stress. Involved in a RAD9A-related
CC damage checkpoint, a pathway that is important in determining whether
CC DNA damage is compatible with cell survival or whether it requires cell
CC elimination by apoptosis. Modulates the RAD9A interaction with BCL2 and
CC thereby induces DNA damage-induced apoptosis (PubMed:15983387).
CC Promotes PCNA deubiquitination by recruiting the ubiquitin-specific
CC protease 1 (USP1) and WDR48 thereby down-regulating the error-prone
CC damage bypass pathway. As component of the ATAD5 RFC-like complex,
CC regulates the function of the DNA polymerase processivity factor PCNA
CC by unloading the ring-shaped PCNA homotrimer from DNA after replication
CC during the S phase of the cell cycle. This seems to be dependent on its
CC ATPase activity. Plays important roles in restarting stalled
CC replication forks under replication stress, by unloading the PCNA
CC homotrimer from DNA and recruiting RAD51 possibly through an ATR-
CC dependent manner. Ultimately this enables replication fork regression,
CC breakage, and eventual fork restart. Both the PCNA unloading activity
CC and the interaction with WDR48 are required to efficiently recruit
CC RAD51 to stalled replication forks. Promotes the generation of MUS81-
CC mediated single-stranded DNA-associated breaks in response to
CC replication stress, which is an alternative pathway to restart
CC stalled/regressed replication forks (By similarity).
CC {ECO:0000250|UniProtKB:Q96QE3, ECO:0000269|PubMed:15983387}.
CC -!- SUBUNIT: Component of a heteropentameric replication factor ATAD5 RFC-
CC like complex composed of one large subunit (ATAD5) and four small
CC subunits (RFC2, RFC3, RFC4 and RFC5). Within the ATAD5 RFC-like
CC complex, interacts with RFC2, RFC4 and RFC5. Within the ATAD5 RFC-like
CC complex, interacts directly via-N terminal with RAD51; the interactions
CC is enhanced under replication stress (By similarity). Interacts with
CC RB1 predominantly in G1 phase via its LXCXE motif (PubMed:15983387).
CC Interacts with RAD9A in growing cells (PubMed:15983387). The
CC interaction with RAD9A is reduced after exposure to DNA replication-
CC inhibiting agents (PubMed:15983387). Interacts with BRD4. Interacts
CC with PCNA. Interacts with deubiquitinating enzyme USP1, and its
CC associated factor, WDR48 (By similarity).
CC {ECO:0000250|UniProtKB:Q96QE3, ECO:0000269|PubMed:15983387}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96QE3}.
CC Note=Accumulates in nuclear foci at sites of stalled DNA replication
CC forks in response to DNA damage. {ECO:0000250|UniProtKB:Q96QE3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4QY64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4QY64-2; Sequence=VSP_031098, VSP_031099;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in all cell lines like
CC teratocarcinoma, cell lymphoma, lymphoma.
CC {ECO:0000269|PubMed:15983387}.
CC -!- INDUCTION: Down-regulated by DNA replication-inhibiting agents.
CC -!- PTM: ATR may stimulate the RAD9A dissociation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38279.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=CAI24765.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI25200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI26037.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY557610; AAT52048.1; -; mRNA.
DR EMBL; AK032814; BAE20483.1; -; mRNA.
DR EMBL; AK053857; BAE20694.1; -; mRNA.
DR EMBL; AK085211; BAC39389.2; -; mRNA.
DR EMBL; AK136531; BAE23031.1; -; mRNA.
DR EMBL; AK165945; BAE38477.1; -; mRNA.
DR EMBL; AL591113; CAI24765.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL663057; CAI24765.1; JOINED; Genomic_DNA.
DR EMBL; AL672178; CAI24765.1; JOINED; Genomic_DNA.
DR EMBL; AL672178; CAI25200.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL591113; CAI25200.1; JOINED; Genomic_DNA.
DR EMBL; AL663057; CAI25200.1; JOINED; Genomic_DNA.
DR EMBL; AL663057; CAI26037.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL591113; CAI26037.1; JOINED; Genomic_DNA.
DR EMBL; AL672178; CAI26037.1; JOINED; Genomic_DNA.
DR EMBL; BC038279; AAH38279.2; ALT_SEQ; mRNA.
DR CCDS; CCDS25127.1; -. [Q4QY64-1]
DR RefSeq; NP_001025027.1; NM_001029856.2. [Q4QY64-1]
DR AlphaFoldDB; Q4QY64; -.
DR SMR; Q4QY64; -.
DR BioGRID; 231918; 4.
DR IntAct; Q4QY64; 1.
DR STRING; 10090.ENSMUSP00000017694; -.
DR iPTMnet; Q4QY64; -.
DR PhosphoSitePlus; Q4QY64; -.
DR EPD; Q4QY64; -.
DR jPOST; Q4QY64; -.
DR MaxQB; Q4QY64; -.
DR PaxDb; Q4QY64; -.
DR PeptideAtlas; Q4QY64; -.
DR PRIDE; Q4QY64; -.
DR ProteomicsDB; 277058; -. [Q4QY64-1]
DR ProteomicsDB; 277059; -. [Q4QY64-2]
DR Antibodypedia; 15166; 161 antibodies from 28 providers.
DR DNASU; 237877; -.
DR Ensembl; ENSMUST00000017694; ENSMUSP00000017694; ENSMUSG00000017550. [Q4QY64-1]
DR GeneID; 237877; -.
DR KEGG; mmu:237877; -.
DR UCSC; uc007klf.2; mouse. [Q4QY64-2]
DR UCSC; uc007klg.2; mouse. [Q4QY64-1]
DR CTD; 79915; -.
DR MGI; MGI:2442925; Atad5.
DR VEuPathDB; HostDB:ENSMUSG00000017550; -.
DR eggNOG; KOG1968; Eukaryota.
DR GeneTree; ENSGT00940000153469; -.
DR InParanoid; Q4QY64; -.
DR OMA; ANLDNAW; -.
DR OrthoDB; 162624at2759; -.
DR PhylomeDB; Q4QY64; -.
DR TreeFam; TF329112; -.
DR BioGRID-ORCS; 237877; 7 hits in 111 CRISPR screens.
DR ChiTaRS; Atad5; mouse.
DR PRO; PR:Q4QY64; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q4QY64; protein.
DR Bgee; ENSMUSG00000017550; Expressed in humerus cartilage element and 196 other tissues.
DR ExpressionAtlas; Q4QY64; baseline and differential.
DR Genevisible; Q4QY64; MM.
DR GO; GO:0031391; C:Elg1 RFC-like complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0061860; F:DNA clamp unloader activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0090618; P:DNA clamp unloading; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IGI:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IGI:MGI.
DR GO; GO:0045190; P:isotype switching; IMP:MGI.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0033260; P:nuclear DNA replication; IMP:MGI.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IMP:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IMP:MGI.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:MGI.
DR GO; GO:0042770; P:signal transduction in response to DNA damage; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; DNA damage; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1826
FT /note="ATPase family AAA domain-containing protein 5"
FT /id="PRO_0000317619"
FT REGION 170..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..381
FT /note="Interaction with WDR48"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT REGION 398..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1701
FT /note="Interaction with RAD51 and RFC5"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT MOTIF 1415..1419
FT /note="LXCXE motif"
FT COMPBIAS 172..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1119..1126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QE3"
FT VAR_SEQ 775..814
FT /note="KMKIAPLFLAKRTKRAAIPVFDLDESSQDSSEQTQDCDVQ -> NWIHYCFM
FT DTLLLSTVLWITIHKCLGAIHPEYSGVLSQKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031098"
FT VAR_SEQ 815..1826
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031099"
FT CONFLICT 330
FT /note="P -> H (in Ref. 2; BAE38477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1826 AA; 203909 MW; 8830CAF65BCDDA81 CRC64;
MVGVLSMAAA AAPLPVKDYE IEPCKKRRKD DDNSSCETIT KYLSPIGKTG DKVFSPPKPS
NILHYFRKTS LTTEKPQSTK AYKIKPSPPL LVGNSKDCKT PLEVFSNREF KRKRKRVSLS
SQLNDIKIQD ECPVEISNND SKEDGGLSDC VESSASVSLY KEHVEVLAES IEDSRNQPNT
KSSKKKVNPK QCTTKSDDRI LRKRKRSKVT GQSESVPLAD ELSLPEDGGK DSKLTKPSLA
EENDSRTHAT KRADLKESTI TVSYEEFVKS HKAAKVEEIP DPAVPACVPS GPGEAVKSGS
EGELSGSCEP SPQLHLKTVT VLAQVHPTPP KKKGKIPPIF LKQKQPELEN SLSDPENEQP
VQKRKSNVVI QEGQLELAVL EAWNSEASVP KCSMEERQQF MRAFRQPPPD TLKNGFKKPL
EKQKDPSEKS VHEGDSSSEK IIENPNIQRV SSQGCLQSHA DRGSFPKEKS KKPNKKGKKT
RTTAGGNREE NIQKEKTAFS LKDEQDQNSL RRSVRQKSEV LKSNALLNSE NLVCEDTAHD
SVQMSLCNRN KSRSSSTPTR DMVTHHRAEP GSSLEYVSTR QPIRRSLRSC STPATNALGG
TESEDAQDTI PVKASTPKSA RTSEKHNLYT AELIIVSSDS ESPIRMKFTR ISTPKKSKKS
SKKSETTEEE LTSQKKKANS TSKNISKAKE LIEEAKAFQI GGSKTEETVV PLRRSSRHQA
RSAKEKSPEI DDSVIVIDSS PTSIREPEKS QKKLQNLNDV LGKKLNKSSK NVPGKMKIAP
LFLAKRTKRA AIPVFDLDES SQDSSEQTQD CDVQFKAKRD FLMSGLPDLL KRQIAKKAAA
LDVYNAVSTS FQRVVHVQQK DDEYWLWHLK PPSCPLLTEF KELNTKVTDL SEYVVAFGEF
STLNPNPRSN PAAVMMRTRK DFTKEVRNLL LEEIKCSNPE FSLEKYFPLL LKKRIEHQVL
CEGHGKQASP QLQPDVSQKE TKRKQVATGN QKSKRKRQNE YSVSPEEMKG RSKDLDERIS
SSCTNLDPSR DSGTEDMLWT EKYQPQNSNE LIGNELAVKK LHSWLKDWKR RAELEERHNL
KGKRDEKEEG ILDLSDSTDF KGSSDDEENR LCNTVLITGP TGVGKTAAVY ACAQELGFKI
FEVNASSQRS GRQILSQLKE ATQSHQVDKQ GVNSQKPCFF NNYNIGKSPK KLNSPGKVVT
SPRKLPPSSP KTSGQKRALL PKTLANYFKV SSKSKSNDDV GALMGDDKGV KNSSLEQRQL
IQTKSTNANN SHIKDVGAEE SNRKKATSLI LFEEVDVIFD EDAGFLNAVK TFMATTKRPV
ILTTSDPTFS LVFDGCFEEI NFSIPSLLNV ASYLQVICLV ENFRTDFKDF VTLLTANACD
IRKSILYLQF WIRSGGGILE ERPLSHCREN SRNTLVCSED GSDANINSKK PKRNRVALPR
CDTGCAEALF GLKNIASPSQ DLLSLLKHKI TTKEEWQKLI QVLTEFHVQN IDLLHSNLEV
ILPLPVHVVP DVRGAYGFPV TTQASAPASM GHLTRKQSKD QPLRKSQKRK QKKMVILDDS
DLFDTGLDFS GELPSLSPAP SLSVEDNIRR DSNPEIKTQN SGFKPHSVPQ PPKTLAEKKC
CMLVSHCLNS LSEFMENMSF IDALLTDPGE QNELGRSAFH WTNGRVKSGL CDEFSLENRD
RWAPQSAGEL KATAEALSFT ECSSTISKAL ESLNSCKQLE RDPTNELTVC VSQRRHDACF
RQSAANLDNA DKRMAVIKSV FSSRSFLTLG NKQASIIDYL PTLRNICRTE KLKEQEKNKR
RFLHYFEGIH LEIPEETITT LAADFP
