ID   ERCC2_MOUSE             Reviewed;         760 AA.
AC   O08811; Q8C487; Q9DC01;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPD;
DE            Short=TFIIH subunit XPD;
DE            EC=3.6.4.12;
DE   AltName: Full=CXPD;
DE   AltName: Full=DNA excision repair protein ERCC-2;
DE   AltName: Full=DNA repair protein complementing XP-D cells;
DE   AltName: Full=Xeroderma pigmentosum group D-complementing protein;
GN   Name=Ercc2; Synonyms=Xpd;
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].
RX   PubMed=9426063;
RA   de Boer J., Donker I., de Wit J., Hoeijmakers J.H.J., Weeda G.;
RT   "Disruption of the mouse xeroderma pigmentosum group D DNA repair/basal
RT   transcription gene results in preimplantation lethality.";
RL   Cancer Res. 58:89-94(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
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].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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: ATP-dependent 5'-3' DNA helicase, component of the general
CC       transcription and DNA repair factor IIH (TFIIH) core complex, which is
CC       involved in general and transcription-coupled nucleotide excision
CC       repair (NER) of damaged DNA and, when complexed to CAK, in RNA
CC       transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA
CC       around the lesion to allow the excision of the damaged oligonucleotide
CC       and its replacement by a new DNA fragment. The ATP-dependent helicase
CC       activity of XPD/ERCC2 is required for DNA opening. In transcription,
CC       TFIIH has an essential role in transcription initiation. When the pre-
CC       initiation complex (PIC) has been established, TFIIH is required for
CC       promoter opening and promoter escape. Phosphorylation of the C-terminal
CC       tail (CTD) of the largest subunit of RNA polymerase II by the kinase
CC       module CAK controls the initiation of transcription. XPD/ERCC2 acts by
CC       forming a bridge between CAK and the core-TFIIH complex. Involved in
CC       the regulation of vitamin-D receptor activity. As part of the mitotic
CC       spindle-associated MMXD complex it plays a role in chromosome
CC       segregation. Might have a role in aging process and could play a
CC       causative role in the generation of skin cancers.
CC       {ECO:0000250|UniProtKB:P18074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC       XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which
CC       is active in NER. The core complex associates with the 3-subunit CDK-
CC       activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and
CC       MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC       transcription. The interaction with GTF2H2 results in the stimulation
CC       of the 5'-->3' helicase activity. Component of the MMXD complex, which
CC       includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with CIAO1
CC       and CIAO2B; the interaction WITH CIAO2B is direct. Interacts with
CC       ATF7IP. Interacts directly with MMS19. Part of TBP-based Pol II pre-
CC       initiation complex (PIC), in which Pol II core assembles with general
CC       transcription factors and other specific initiation factors including
CC       GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3,
CC       GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit
CC       PIC complex mediates DNA unwinding and targets Pol II core to the
CC       transcription start site where the first phosphodiester bond forms.
CC       {ECO:0000250|UniProtKB:P18074}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250}.
CC   -!- PTM: ISGylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB23443.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U97572; AAB58296.1; -; mRNA.
DR   EMBL; AK004652; BAB23443.1; ALT_INIT; mRNA.
DR   EMBL; AK082761; BAC38607.1; -; mRNA.
DR   EMBL; CH466639; EDL23140.1; -; Genomic_DNA.
DR   CCDS; CCDS20900.1; -.
DR   RefSeq; NP_031975.2; NM_007949.4.
DR   AlphaFoldDB; O08811; -.
DR   SMR; O08811; -.
DR   BioGRID; 199500; 1.
DR   IntAct; O08811; 1.
DR   MINT; O08811; -.
DR   STRING; 10090.ENSMUSP00000054380; -.
DR   iPTMnet; O08811; -.
DR   PhosphoSitePlus; O08811; -.
DR   SwissPalm; O08811; -.
DR   EPD; O08811; -.
DR   MaxQB; O08811; -.
DR   PaxDb; 10090-ENSMUSP00000054380; -.
DR   ProteomicsDB; 275672; -.
DR   Pumba; O08811; -.
DR   Antibodypedia; 17895; 315 antibodies from 37 providers.
DR   DNASU; 13871; -.
DR   Ensembl; ENSMUST00000062831.16; ENSMUSP00000054380.10; ENSMUSG00000030400.18.
DR   GeneID; 13871; -.
DR   KEGG; mmu:13871; -.
DR   UCSC; uc009flq.1; mouse.
DR   AGR; MGI:95413; -.
DR   CTD; 2068; -.
DR   MGI; MGI:95413; Ercc2.
DR   VEuPathDB; HostDB:ENSMUSG00000030400; -.
DR   eggNOG; KOG1131; Eukaryota.
DR   GeneTree; ENSGT00950000182970; -.
DR   InParanoid; O08811; -.
DR   OMA; IREQFFR; -.
DR   OrthoDB; 124793at2759; -.
DR   PhylomeDB; O08811; -.
DR   TreeFam; TF101232; -.
DR   Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-72086; mRNA Capping.
DR   Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   BioGRID-ORCS; 13871; 32 hits in 120 CRISPR screens.
DR   PRO; PR:O08811; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O08811; Protein.
DR   Bgee; ENSMUSG00000030400; Expressed in spermatocyte and 152 other cell types or tissues.
DR   ExpressionAtlas; O08811; baseline and differential.
DR   GO; GO:0070516; C:CAK-ERCC2 complex; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0071817; C:MMXD complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:MGI.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR   GO; GO:0032289; P:central nervous system myelin formation; IMP:MGI.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; IMP:MGI.
DR   GO; GO:0040016; P:embryonic cleavage; IMP:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR   GO; GO:0043249; P:erythrocyte maturation; IMP:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0035315; P:hair cell differentiation; IMP:MGI.
DR   GO; GO:0022405; P:hair cycle process; IMP:MGI.
DR   GO; GO:0048820; P:hair follicle maturation; IMP:MGI.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:MGI.
DR   GO; GO:0045951; P:positive regulation of mitotic recombination; IBA:GO_Central.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   GO; GO:0009411; P:response to UV; IMP:MGI.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0021510; P:spinal cord development; IMP:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006362; P:transcription elongation by RNA polymerase I; IMP:MGI.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR   GO; GO:0009650; P:UV protection; IMP:MGI.
DR   CDD; cd17969; DEAHc_XPD; 1.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR010643; HBB.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   InterPro; IPR001945; RAD3/XPD.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF1; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF06777; HBB; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   PRINTS; PR00852; XRODRMPGMNTD.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR   Genevisible; O08811; MM.
PE   1: Evidence at protein level;
KW   4Fe-4S; ATP-binding; Chromosome partition; Cytoplasm; Cytoskeleton;
KW   DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase; Iron;
KW   Iron-sulfur; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..760
FT                   /note="General transcription and DNA repair factor IIH
FT                   helicase subunit XPD"
FT                   /id="PRO_0000101981"
FT   DOMAIN          7..283
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          438..637
FT                   /note="Mediates interaction with MMS19"
FT                   /evidence="ECO:0000250"
FT   MOTIF           234..237
FT                   /note="DEAH box"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         116
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        285
FT                   /note="Y -> C (in Ref. 2; BAB23443)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595
FT                   /note="I -> V (in Ref. 1; AAB58296)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   760 AA;  86842 MW;  02B2E116792D4E44 CRC64;
     MKLNVDGLLV YFPYDYIYPE QFSYMLELKR TLDAKGHGVL EMPSGTGKTV SLLALIVAYQ
     RAYPLEVTKL IYCSRTVPEI EKVIEELRKL LSFYEQQEGE KLPFLGLALS SRKNLCIHPE
     VTPLRFGKDV DGKCHSLTAS YVRAQYQQDA SLPHCRFYEE FDIHGRQMPL PAGIYNLDDL
     KALGQRQGWC PYFLARYSIL HANVVVYSYH YLLDPKIADL VSKELARKAV VVFDEAHNID
     NVCIDSMSVN LTRRTLDRCQ SNLDTLQKTV LRIKETDEQR LRDEYRRLVE GLREASVARE
     TDAHLANPVL PDEVLQEAVP GSIRTAEHFL GFLRRLLEYV KWRLRVQHVV QESPPAFLSG
     LAQRVCIQRK PLRFCAERLR SLLHTLEIAD LADFSPLTLL ANFATLVSTY AKGFTIIIEP
     FDDRTPTIAN PVLHFSCMDA SLAIKPVFER FQSVIITSGT LSPLDIYPKI LDFHPVTMAT
     FTMTLARVCL CPMIIGRGND QVAISSKFET REDIAVIRNY GNLLLEMSAV VPDGIVAFFT
     SYQYMESTVA SWYEQGILEN IQRNKLLFIE TQDGAETSVA LEKYQEACEN GRGAILLSVA
     RGKVSEGIDF VHHYGRAVIM FGVPYVYTQS RILKARLEYL RDQFQIREND FLTFDAMRHA
     AQCVGRAIRG KTDYGLMVFA DKRFARADKR GKLPRWIQEH LTDSNLNLTV DEGVQVAKYF
     LRQMAQPFHR EDQLGLSLLS LEQLQSEETL QRIEQIAQQL
//