FBX44_HUMAN
ID FBX44_HUMAN Reviewed; 255 AA.
AC Q9H4M3; B3KNZ2; B7Z743; Q5TGX2; Q5TGX4; Q5TGX5; Q68DJ9; Q8WWY2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=F-box only protein 44;
DE AltName: Full=F-box protein FBX30;
DE AltName: Full=F-box/G-domain protein 3;
GN Name=FBXO44; Synonyms=FBG3, FBX30, FBX44, FBX6A, FBXO6A;
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 2).
RC TISSUE=Brain;
RA Paulson H.L., Koppenhafer S.L.;
RT "Fbx30: a novel member of NFB42 class of Fbx genes.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12383498; DOI=10.1016/s0378-1119(02)00867-3;
RA Ilyin G.P., Serandour A.L., Pigeon C., Rialland M., Glaise D.,
RA Guguen-Guillouzo C.;
RT "A new subfamily of structurally related human F-box proteins.";
RL Gene 296:11-20(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Synovium;
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 MRNA] (ISOFORM 1).
RC TISSUE=Retina;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=B-cell;
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 [8]
RP LACK OF SUGAR-BINDING, INTERACTION WITH CUL1 AND SKP1, AND IDENTIFICATION
RP IN SCF-COMPLEX.
RX PubMed=18203720; DOI=10.1074/jbc.m709508200;
RA Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
RT "Diversity in tissue expression, substrate binding, and SCF complex
RT formation for a lectin family of ubiquitin ligases.";
RL J. Biol. Chem. 283:12717-12729(2008).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC Interacts with SKP1 and CUL1. {ECO:0000269|PubMed:18203720}.
CC -!- INTERACTION:
CC Q9H4M3; Q96GS4: BORCS6; NbExp=4; IntAct=EBI-2322644, EBI-10193358;
CC Q9H4M3; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-2322644, EBI-748621;
CC Q9H4M3; P63208: SKP1; NbExp=5; IntAct=EBI-2322644, EBI-307486;
CC Q9H4M3-2; P78537: BLOC1S1; NbExp=3; IntAct=EBI-12104696, EBI-348630;
CC Q9H4M3-2; Q96GS4: BORCS6; NbExp=8; IntAct=EBI-12104696, EBI-10193358;
CC Q9H4M3-2; Q8TAV5: C11orf45; NbExp=3; IntAct=EBI-12104696, EBI-12810853;
CC Q9H4M3-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-12104696, EBI-7116203;
CC Q9H4M3-2; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-12104696, EBI-18398632;
CC Q9H4M3-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12104696, EBI-16439278;
CC Q9H4M3-2; Q9NQX1-2: PRDM5; NbExp=3; IntAct=EBI-12104696, EBI-12859340;
CC Q9H4M3-2; P63208: SKP1; NbExp=6; IntAct=EBI-12104696, EBI-307486;
CC Q9H4M3-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-12104696, EBI-742688;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4M3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4M3-2; Sequence=VSP_011346, VSP_011347;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain and kidney. Expressed
CC at lower levels in heart, spleen and liver.
CC {ECO:0000269|PubMed:12383498}.
CC -!- MISCELLANEOUS: In contrast to other FBA domain containing proteins,
CC FBXO44 demonstrates no significant binding to any of the 200 glycans
CC tested.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=FLAG-FBG3;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Fusion_411";
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DR EMBL; AY007380; AAG09623.1; -; mRNA.
DR EMBL; AY040878; AAK77940.1; -; mRNA.
DR EMBL; AK301418; BAH13479.1; -; mRNA.
DR EMBL; AK055344; BAG51504.1; -; mRNA.
DR EMBL; CR749368; CAH18221.1; -; mRNA.
DR EMBL; AL031731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71690.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71691.1; -; Genomic_DNA.
DR EMBL; BC007832; AAH07832.1; -; mRNA.
DR CCDS; CCDS131.1; -. [Q9H4M3-2]
DR CCDS; CCDS132.1; -. [Q9H4M3-1]
DR RefSeq; NP_001014765.1; NM_001014765.1. [Q9H4M3-1]
DR RefSeq; NP_001291719.1; NM_001304790.1. [Q9H4M3-2]
DR RefSeq; NP_001291720.1; NM_001304791.1. [Q9H4M3-1]
DR RefSeq; NP_149438.2; NM_033182.5. [Q9H4M3-1]
DR RefSeq; NP_904319.1; NM_183412.2. [Q9H4M3-2]
DR RefSeq; NP_904320.1; NM_183413.2. [Q9H4M3-2]
DR RefSeq; XP_006711108.1; XM_006711045.2. [Q9H4M3-1]
DR RefSeq; XP_016858332.1; XM_017002843.1. [Q9H4M3-1]
DR RefSeq; XP_016858333.1; XM_017002844.1. [Q9H4M3-2]
DR PDB; 3WSO; X-ray; 2.60 A; A=1-255.
DR PDB; 5B4N; X-ray; 2.30 A; A/B=94-191, A/B=194-247.
DR PDBsum; 3WSO; -.
DR PDBsum; 5B4N; -.
DR AlphaFoldDB; Q9H4M3; -.
DR SMR; Q9H4M3; -.
DR BioGRID; 125038; 39.
DR CORUM; Q9H4M3; -.
DR IntAct; Q9H4M3; 17.
DR STRING; 9606.ENSP00000365961; -.
DR iPTMnet; Q9H4M3; -.
DR BioMuta; FBXO44; -.
DR DMDM; 61252661; -.
DR EPD; Q9H4M3; -.
DR jPOST; Q9H4M3; -.
DR MassIVE; Q9H4M3; -.
DR MaxQB; Q9H4M3; -.
DR PaxDb; Q9H4M3; -.
DR PeptideAtlas; Q9H4M3; -.
DR PRIDE; Q9H4M3; -.
DR ProteomicsDB; 80863; -. [Q9H4M3-1]
DR ProteomicsDB; 80864; -. [Q9H4M3-2]
DR Antibodypedia; 1239; 229 antibodies from 28 providers.
DR DNASU; 93611; -.
DR Ensembl; ENST00000251546.8; ENSP00000251546.4; ENSG00000132879.14. [Q9H4M3-2]
DR Ensembl; ENST00000251547.10; ENSP00000251547.5; ENSG00000132879.14. [Q9H4M3-1]
DR Ensembl; ENST00000376760.5; ENSP00000365951.1; ENSG00000132879.14. [Q9H4M3-2]
DR Ensembl; ENST00000376762.8; ENSP00000365953.4; ENSG00000132879.14. [Q9H4M3-2]
DR Ensembl; ENST00000376770.5; ENSP00000365961.1; ENSG00000132879.14. [Q9H4M3-1]
DR GeneID; 93611; -.
DR KEGG; hsa:93611; -.
DR MANE-Select; ENST00000251547.10; ENSP00000251547.5; NM_033182.7; NP_149438.2.
DR UCSC; uc001ask.4; human. [Q9H4M3-1]
DR CTD; 93611; -.
DR DisGeNET; 93611; -.
DR GeneCards; FBXO44; -.
DR HGNC; HGNC:24847; FBXO44.
DR HPA; ENSG00000132879; Tissue enhanced (brain).
DR MIM; 609111; gene.
DR neXtProt; NX_Q9H4M3; -.
DR OpenTargets; ENSG00000132879; -.
DR PharmGKB; PA134863106; -.
DR VEuPathDB; HostDB:ENSG00000132879; -.
DR eggNOG; ENOG502RZA6; Eukaryota.
DR GeneTree; ENSGT00940000159408; -.
DR HOGENOM; CLU_068548_0_0_1; -.
DR InParanoid; Q9H4M3; -.
DR OMA; QKSDARW; -.
DR PhylomeDB; Q9H4M3; -.
DR TreeFam; TF320527; -.
DR PathwayCommons; Q9H4M3; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9H4M3; -.
DR BioGRID-ORCS; 93611; 9 hits in 1111 CRISPR screens.
DR ChiTaRS; FBXO44; human.
DR GenomeRNAi; 93611; -.
DR Pharos; Q9H4M3; Tbio.
DR PRO; PR:Q9H4M3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H4M3; protein.
DR Bgee; ENSG00000132879; Expressed in right hemisphere of cerebellum and 160 other tissues.
DR ExpressionAtlas; Q9H4M3; baseline and differential.
DR Genevisible; Q9H4M3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR007397; F-box-assoc_dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR039752; F-box_only.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR12125; PTHR12125; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF04300; FBA; 1.
DR SMART; SM01198; FBA; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS51114; FBA; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..255
FT /note="F-box only protein 44"
FT /id="PRO_0000119945"
FT DOMAIN 3..50
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 71..252
FT /note="FBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT VAR_SEQ 123..224
FT /note="KKYFVTSYYTCLKSQVVDLKAEGYWEELMDTTRPDIEVKDWFAARPDCGSKY
FT QLCVQLLSSAHAPLGTFQPDPATIQQKSDAKWREVSHTFSNYPPGVRYIW -> RSQAR
FT LRVQVPAVRSAPVVRARASGDLPARPGDHPAEERCQVEGGLPHILQLPARRPLHLVSAR
FT RRGHSLLGRLVRPEGHQQQHHHRAPAALTPPEPPSAEP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_011346"
FT VAR_SEQ 225..255
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_011347"
FT CONFLICT 101
FT /note="G -> D (in Ref. 4; CAH18221)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="G -> R (in Ref. 2; AAK77940)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3WSO"
FT TURN 88..93
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5B4N"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5B4N"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:5B4N"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5B4N"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:5B4N"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3WSO"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5B4N"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:5B4N"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:3WSO"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:5B4N"
SQ SEQUENCE 255 AA; 29747 MW; 3DA167B70E22A7E8 CRC64;
MAVGNINELP ENILLELFTH VPARQLLLNC RLVCSLWRDL IDLVTLWKRK CLREGFITED
WDQPVADWKI FYFLRSLHRN LLHNPCAEEG FEFWSLDVNG GDEWKVEDLS RDQRKEFPND
QVKKYFVTSY YTCLKSQVVD LKAEGYWEEL MDTTRPDIEV KDWFAARPDC GSKYQLCVQL
LSSAHAPLGT FQPDPATIQQ KSDAKWREVS HTFSNYPPGV RYIWFQHGGV DTHYWAGWYG
PRVTNSSITI GPPLP
