DHX33_HUMAN
ID DHX33_HUMAN Reviewed; 707 AA.
AC Q9H6R0; B4DHF9; Q4G149; Q5CZ73; Q9H5M9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ATP-dependent RNA helicase DHX33 {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 33;
GN Name=DHX33 {ECO:0000312|HGNC:HGNC:16718}; Synonyms=DDX33;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Hepatoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 PROTEIN SEQUENCE OF 119-128; 130-138 AND 200-211, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-707.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, ASSOCIATION WITH RIBOSOMAL DNA LOCI, INTERACTION WITH UBTF, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21930779; DOI=10.1128/mcb.05832-11;
RA Zhang Y., Forys J.T., Miceli A.P., Gwinn A.S., Weber J.D.;
RT "Identification of DHX33 as a mediator of rRNA synthesis and cell growth.";
RL Mol. Cell. Biol. 31:4676-4691(2011).
RN [8]
RP FUNCTION, DOUBLE-STRANDED RNA-BINDING, MUTAGENESIS OF LYS-103, INTERACTION
RP WITH NLRP3, AND SUBCELLULAR LOCATION.
RX PubMed=23871209; DOI=10.1016/j.immuni.2013.07.001;
RA Mitoma H., Hanabuchi S., Kim T., Bao M., Zhang Z., Sugimoto N., Liu Y.J.;
RT "The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3
RT inflammasome.";
RL Immunity 39:123-135(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DDX3X; EIF3G; EIF3H; RPL3;
RP RPL7; RPL26 AND RPL27, AND RNA-BINDING.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
CC -!- FUNCTION: Implicated in nucleolar organization, ribosome biogenesis,
CC protein synthesis and cytoplasmic dsRNA sensing (By similarity)
CC (PubMed:21930779, PubMed:23871209, PubMed:26100019). Stimulates RNA
CC polymerase I transcription of the 47S precursor rRNA. Associates with
CC ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment
CC (PubMed:21930779). In the cytoplasm, promotes elongation-competent 80S
CC ribosome assembly at the late stage of mRNA translation initiation
CC (PubMed:26100019). Senses cytosolic dsRNA mediating NLRP3 inflammasome
CC formation in macrophages and type I interferon production in myeloid
CC dendritic cells (PubMed:23871209). Required for NLRP3 activation
CC induced by viral dsRNA and bacterial RNA (PubMed:23871209). In
CC dendritic cells, required for induction of type I interferon production
CC induced by cytoplasmic dsRNA via the activation of MAPK and NF-kappa-B
CC signaling pathways (By similarity). {ECO:0000250|UniProtKB:Q80VY9,
CC ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:23871209,
CC ECO:0000269|PubMed:26100019}.
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 UBTF (PubMed:21930779). Interacts with DDX3X,
CC EIF3G and EIF3H; the interaction is independent of RNA
CC (PubMed:26100019). Interacts (via HA2 region and Helicase C-terminal
CC domain) with the components of the large ribosomal subunit RPL3, RPL7,
CC RPL26 and RPL27 (PubMed:26100019). Interacts (via DEAH box) with NLRP3
CC (via NACHT domain) (PubMed:23871209). Binds to mRNA (PubMed:26100019).
CC Binds to double-stranded RNA (via the helicase C-terminal domain)
CC (PubMed:23871209). Interacts (via the helicase C-terminal domain) with
CC MAVS (By similarity). {ECO:0000250|UniProtKB:Q80VY9,
CC ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:23871209,
CC ECO:0000269|PubMed:26100019}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21930779,
CC ECO:0000269|PubMed:26100019}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:21930779}. Cytoplasm {ECO:0000269|PubMed:23871209,
CC ECO:0000269|PubMed:26100019}. Nucleus {ECO:0000269|PubMed:23871209}.
CC Inflammasome {ECO:0000269|PubMed:23871209}. Note=Predominantly in the
CC nucleolus. During mitosis, localizes with the nucleolar organizing
CC regions (PubMed:21930779). Upon dsRNA-binding, localizes in the
CC inflammasome (PubMed:23871209). {ECO:0000269|PubMed:21930779,
CC ECO:0000269|PubMed:23871209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H6R0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6R0-2; Sequence=VSP_016256;
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC Deubiquitinated by USP36. {ECO:0000250|UniProtKB:Q80VY9}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30017.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK025625; BAB15193.1; -; mRNA.
DR EMBL; AK026944; BAB15596.1; -; mRNA.
DR EMBL; AK295074; BAG58120.1; -; mRNA.
DR EMBL; AC004148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90332.1; -; Genomic_DNA.
DR EMBL; BC030017; AAH30017.1; ALT_INIT; mRNA.
DR EMBL; CR936655; CAI56793.1; -; mRNA.
DR CCDS; CCDS11072.1; -. [Q9H6R0-1]
DR RefSeq; NP_001186628.1; NM_001199699.1. [Q9H6R0-2]
DR RefSeq; NP_064547.2; NM_020162.3. [Q9H6R0-1]
DR RefSeq; XP_016880366.1; XM_017024877.1.
DR AlphaFoldDB; Q9H6R0; -.
DR SMR; Q9H6R0; -.
DR BioGRID; 121247; 69.
DR IntAct; Q9H6R0; 22.
DR MINT; Q9H6R0; -.
DR STRING; 9606.ENSP00000225296; -.
DR iPTMnet; Q9H6R0; -.
DR PhosphoSitePlus; Q9H6R0; -.
DR BioMuta; DHX33; -.
DR DMDM; 296434478; -.
DR EPD; Q9H6R0; -.
DR jPOST; Q9H6R0; -.
DR MassIVE; Q9H6R0; -.
DR MaxQB; Q9H6R0; -.
DR PaxDb; Q9H6R0; -.
DR PeptideAtlas; Q9H6R0; -.
DR PRIDE; Q9H6R0; -.
DR ProteomicsDB; 81012; -. [Q9H6R0-1]
DR ProteomicsDB; 81013; -. [Q9H6R0-2]
DR Antibodypedia; 23699; 81 antibodies from 11 providers.
DR DNASU; 56919; -.
DR Ensembl; ENST00000225296.8; ENSP00000225296.3; ENSG00000005100.13. [Q9H6R0-1]
DR GeneID; 56919; -.
DR KEGG; hsa:56919; -.
DR MANE-Select; ENST00000225296.8; ENSP00000225296.3; NM_020162.4; NP_064547.2.
DR UCSC; uc002gca.3; human. [Q9H6R0-1]
DR CTD; 56919; -.
DR DisGeNET; 56919; -.
DR GeneCards; DHX33; -.
DR HGNC; HGNC:16718; DHX33.
DR HPA; ENSG00000005100; Low tissue specificity.
DR MIM; 614405; gene.
DR neXtProt; NX_Q9H6R0; -.
DR OpenTargets; ENSG00000005100; -.
DR PharmGKB; PA27220; -.
DR VEuPathDB; HostDB:ENSG00000005100; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000156747; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; Q9H6R0; -.
DR OMA; HIHRTTP; -.
DR PhylomeDB; Q9H6R0; -.
DR TreeFam; TF354245; -.
DR PathwayCommons; Q9H6R0; -.
DR SignaLink; Q9H6R0; -.
DR BioGRID-ORCS; 56919; 602 hits in 1080 CRISPR screens.
DR ChiTaRS; DHX33; human.
DR GenomeRNAi; 56919; -.
DR Pharos; Q9H6R0; Tbio.
DR PRO; PR:Q9H6R0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H6R0; protein.
DR Bgee; ENSG00000005100; Expressed in secondary oocyte and 185 other tissues.
DR ExpressionAtlas; Q9H6R0; baseline and differential.
DR Genevisible; Q9H6R0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0000182; F:rDNA binding; IDA:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Helicase; Hydrolase; Inflammasome; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..707
FT /note="ATP-dependent RNA helicase DHX33"
FT /id="PRO_0000055164"
FT DOMAIN 84..252
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 277..450
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..80
FT /note="Required for nucleolar location"
FT /evidence="ECO:0000269|PubMed:26100019"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..562
FT /note="HA2; required for interaction with EIF3G and RPL26"
FT /evidence="ECO:0000269|PubMed:26100019"
FT MOTIF 194..197
FT /note="DEAH box"
FT MOTIF 547..558
FT /note="Critical for rDNA-binding"
FT /evidence="ECO:0000250"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016256"
FT VARIANT 118
FT /note="R -> C (in dbSNP:rs8069315)"
FT /id="VAR_057239"
FT VARIANT 483
FT /note="H -> D (in dbSNP:rs11653658)"
FT /id="VAR_057240"
FT MUTAGEN 103
FT /note="K->N: No effect on inflammasome activation upon
FT dsRNA-binding."
FT /evidence="ECO:0000269|PubMed:23871209"
FT CONFLICT 77
FT /note="F -> L (in Ref. 1; BAB15193)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="R -> G (in Ref. 1; BAB15193)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="A -> V (in Ref. 4; AAH30017)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="P -> S (in Ref. 6; CAI56793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78874 MW; E3515B12BD972431 CRC64;
MPEEAGFPPA KRFRPGSGPP SRAGSFPPGR QVVMLLTAGS GGRGGGGGRR QQPPLAQPSA
SPYPEAVELQ RRSLPIFQAR GQLLAQLRNL DNAVLIGETG SGKTTQIPQY LYEGGISRQG
IIAVTQPRRV AAISLATRVS DEKRTELGKL VGYTVRFDDV TSEDTRIKFL TDGMLLREAI
SDSLLRKYSC VILDEAHERT IHTDVLFGVV KAAQKRRKEL GKLPLKVIVM SATMDVDLFS
QYFNGAPVLY LEGRQHPIQV FYTKQPQNDY LHAALVSVFQ IHQEAPSSQD ILVFLTGQEE
IEAMSKTCRD IAKHLPDGCP AMLVLPLYAS LPYAQQLRVF QGAPKGYRKV IISTNIAETS
ITITGIKYVV DTGMVKAKKY NPDSGLEVLA VQRVSKTQAW QRTGRAGRED SGICYRLYTE
DEFEKFDKMT VPEIQRCNLA SVMLQLLAMK VPNVLTFDFM SKPSPDHIQA AIAQLDLLGA
LEHKDDQLTL TPMGRKMAAF PLEPKFAKTI LMSPKFHCTE EILTIVSLLS VDSVLHNPPS
RREEVQGVRK KFISSEGDHM TLLNIYRTFK NLGGNKDWCK ENFVNSKNMT LVAEVRAQLR
DICLKMSMPI ASSRGDVESV RRCLAHSLFM STAELQPDGT YATTDTHQPV AIHPSSVLFH
CKPACVVYTE LLYTNKCYMR DLCVIDAQWL YEAAPEYFRR KLRTARN
