DDX31_HUMAN
ID DDX31_HUMAN Reviewed; 851 AA.
AC Q9H8H2; Q5K6N2; Q5K6N3; Q5K6N4; Q5VZJ4; Q5VZJ9; Q96E91; Q96NY2; Q96SX5;
AC Q9H5K6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX31;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 31;
DE AltName: Full=Helicain;
GN Name=DDX31;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12782131; DOI=10.1016/s0888-7543(03)00049-1;
RA Abdelhaleem M., Maltais L., Wain H.;
RT "The human DDX and DHX gene families of putative RNA helicases.";
RL Genomics 81:618-622(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT VAL-799.
RA Sugihara T.T., Wadhwa R.R.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 90-851 (ISOFORM 1), AND VARIANT VAL-799.
RC TISSUE=Hepatoma, Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-851 (ISOFORM 1), AND VARIANT
RP VAL-799.
RC TISSUE=Lung;
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH NPM1, AND
RP FUNCTION.
RX PubMed=23019224; DOI=10.1158/0008-5472.can-12-1645;
RA Fukawa T., Ono M., Matsuo T., Uehara H., Miki T., Nakamura Y.,
RA Kanayama H.O., Katagiri T.;
RT "DDX31 regulates the p53-HDM2 pathway and rRNA gene transcription through
RT its interaction with NPM1 in renal cell carcinomas.";
RL Cancer Res. 72:5867-5877(2012).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-828, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase (By similarity). Plays a
CC role in ribosome biogenesis and TP53/p53 regulation through its
CC interaction with NPM1 (PubMed:23019224). {ECO:0000250,
CC ECO:0000269|PubMed:23019224}.
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=3.6.4.13;
CC -!- SUBUNIT: Interacts with NPM1; this interaction prevents interaction
CC between NPM1 and HDM2. {ECO:0000269|PubMed:23019224}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:23019224}. Note=Colocalized with NPM1 in the
CC nucleoli. {ECO:0000269|PubMed:23019224}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Helicain B;
CC IsoId=Q9H8H2-1; Sequence=Displayed;
CC Name=2; Synonyms=Helicain C;
CC IsoId=Q9H8H2-2; Sequence=VSP_014790;
CC Name=3; Synonyms=Helicain A;
CC IsoId=Q9H8H2-3; Sequence=VSP_014787, VSP_014788;
CC Name=4;
CC IsoId=Q9H8H2-4; Sequence=VSP_014789;
CC -!- TISSUE SPECIFICITY: Weakly or undetectably expressed in normal organs.
CC Up-regulated in renal cell carcinoma. {ECO:0000269|PubMed:23019224}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ14889.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ14890.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15620.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF427339; AAL26549.1; -; mRNA.
DR EMBL; AF335567; AAQ14888.1; -; mRNA.
DR EMBL; AF335568; AAQ14889.1; ALT_FRAME; mRNA.
DR EMBL; AF335569; AAQ14890.1; ALT_FRAME; mRNA.
DR EMBL; AK023695; BAB14644.1; ALT_INIT; mRNA.
DR EMBL; AK027002; BAB15620.1; ALT_FRAME; mRNA.
DR EMBL; AK027484; BAB55146.1; -; mRNA.
DR EMBL; AL160165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012726; AAH12726.2; -; mRNA.
DR RefSeq; NP_001309269.1; NM_001322340.1. [Q9H8H2-2]
DR RefSeq; NP_001309273.1; NM_001322344.1. [Q9H8H2-3]
DR RefSeq; NP_073616.6; NM_022779.8. [Q9H8H2-1]
DR RefSeq; NP_619526.1; NM_138620.1. [Q9H8H2-4]
DR AlphaFoldDB; Q9H8H2; -.
DR SMR; Q9H8H2; -.
DR BioGRID; 122302; 262.
DR IntAct; Q9H8H2; 120.
DR MINT; Q9H8H2; -.
DR STRING; 9606.ENSP00000361232; -.
DR iPTMnet; Q9H8H2; -.
DR PhosphoSitePlus; Q9H8H2; -.
DR BioMuta; DDX31; -.
DR DMDM; 71153334; -.
DR SWISS-2DPAGE; Q9H8H2; -.
DR EPD; Q9H8H2; -.
DR jPOST; Q9H8H2; -.
DR MassIVE; Q9H8H2; -.
DR MaxQB; Q9H8H2; -.
DR PaxDb; Q9H8H2; -.
DR PeptideAtlas; Q9H8H2; -.
DR PRIDE; Q9H8H2; -.
DR ProteomicsDB; 81209; -. [Q9H8H2-1]
DR ProteomicsDB; 81210; -. [Q9H8H2-2]
DR ProteomicsDB; 81211; -. [Q9H8H2-3]
DR ProteomicsDB; 81212; -. [Q9H8H2-4]
DR Antibodypedia; 18198; 68 antibodies from 16 providers.
DR DNASU; 64794; -.
DR Ensembl; ENST00000310532.7; ENSP00000310539.2; ENSG00000125485.18.
DR Ensembl; ENST00000372159.8; ENSP00000361232.4; ENSG00000125485.18.
DR Ensembl; ENST00000480876.3; ENSP00000479697.2; ENSG00000125485.18.
DR GeneID; 64794; -.
DR KEGG; hsa:64794; -.
DR UCSC; uc004cbq.1; human. [Q9H8H2-1]
DR CTD; 64794; -.
DR DisGeNET; 64794; -.
DR GeneCards; DDX31; -.
DR HGNC; HGNC:16715; DDX31.
DR HPA; ENSG00000125485; Low tissue specificity.
DR MIM; 616533; gene.
DR neXtProt; NX_Q9H8H2; -.
DR PharmGKB; PA27218; -.
DR VEuPathDB; HostDB:ENSG00000125485; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; Q9H8H2; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q9H8H2; -.
DR TreeFam; TF323273; -.
DR PathwayCommons; Q9H8H2; -.
DR SignaLink; Q9H8H2; -.
DR BioGRID-ORCS; 64794; 15 hits in 1084 CRISPR screens.
DR ChiTaRS; DDX31; human.
DR GeneWiki; DDX31; -.
DR GenomeRNAi; 64794; -.
DR Pharos; Q9H8H2; Tbio.
DR PRO; PR:Q9H8H2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H8H2; protein.
DR Bgee; ENSG00000125485; Expressed in right lobe of thyroid gland and 143 other tissues.
DR ExpressionAtlas; Q9H8H2; baseline and differential.
DR Genevisible; Q9H8H2; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Helicase; Hydrolase; Methylation;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..851
FT /note="Probable ATP-dependent RNA helicase DDX31"
FT /id="PRO_0000055049"
FT DOMAIN 262..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 480..659
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 230..259
FT /note="Q motif"
FT MOTIF 388..391
FT /note="DEAD box"
FT COMPBIAS 122..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 828
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 302..319
FT /note="RSDGPYALVLVPTRELAL -> VLLLSTFYEEEQRLRKVK (in isoform
FT 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014787"
FT VAR_SEQ 320..851
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014788"
FT VAR_SEQ 586..851
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014789"
FT VAR_SEQ 603..714
FT /note="YNAPSSPAEYIHRIGRTARIGCHGSSLLILAPSEAEYVNSLASHKINVSEIK
FT MEDILCVLTRDDCFKGKRWGAQKSHAVGPQEIRERATVLQTVFEDYVHSSERRVSWAKK
FT A -> NTSTGLEEPPGLAAMGAACSFWLLRRQNMSTRWLLTKST (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014790"
FT VARIANT 153
FT /note="E -> K (in dbSNP:rs17402080)"
FT /id="VAR_052164"
FT VARIANT 687
FT /note="R -> Q (in dbSNP:rs34246652)"
FT /id="VAR_052165"
FT VARIANT 799
FT /note="I -> V (in dbSNP:rs306547)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_023065"
FT VARIANT 843
FT /note="R -> Q (in dbSNP:rs306548)"
FT /id="VAR_023066"
FT CONFLICT 206
FT /note="K -> L (in Ref. 3; BAB15620)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="L -> P (in Ref. 3; BAB15620)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="Y -> C (in Ref. 3; BAB15620)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="M -> K (in Ref. 3; BAB55146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 851 AA; 94087 MW; E3C73701FF2F37E7 CRC64;
MAPDLASQRH SESFPSVNSR PNVILPGREG RREGLPPGGG TRGSLVPTRP VPPSPAPLGT
SPYSWSRSGP GRGGGAGSSR VPRGVPGPAV CAPGSLLHHA SPTQTMAAAD GSLFDNPRTF
SRRPPAQASR QAKATKRKYQ ASSEAPPAKR RNETSFLPAK KTSVKETQRT FKGNAQKMFS
PKKHSVSTSD RNQEERQCIK TSSLFKNNPD IPELHRPVVK QVQEKVFTSA AFHELGLHPH
LISTINTVLK MSSMTSVQKQ SIPVLLEGRD ALVRSQTGSG KTLAYCIPVV QSLQAMESKI
QRSDGPYALV LVPTRELALQ SFDTVQKLLK PFTWIVPGVL MGGEKRKSEK ARLRKGINIL
ISTPGRLVDH IKSTKNIHFS RLRWLVFDEA DRILDLGFEK DITVILNAVN AECQKRQNVL
LSATLTEGVT RLADISLHDP VSISVLDKSH DQLNPKDKAV QEVCPPPAGD KLDSFAIPES
LKQHVTVVPS KLRLVCLAAF ILQKCKFEED QKMVVFFSSC ELVEFHYSLF LQTLLSSSGA
PASGQLPSAS MRLKFLRLHG GMEQEERTAV FQEFSHSRRG VLLCTDVAAR GLDLPQVTWI
VQYNAPSSPA EYIHRIGRTA RIGCHGSSLL ILAPSEAEYV NSLASHKINV SEIKMEDILC
VLTRDDCFKG KRWGAQKSHA VGPQEIRERA TVLQTVFEDY VHSSERRVSW AKKALQSFIQ
AYATYPRELK HIFHVRSLHL GHVAKSFGLR DAPRNLSALT RKKRKAHVKR PDLHKKTQSK
HSLAEILRSE YSSGMEADIA KVKKQNAPGE PGGRPLQHSL QPTPCFGRGK TLKWRKTQKG
VQRDSKTSQK V
