NDUF4_HUMAN
ID NDUF4_HUMAN Reviewed; 175 AA.
AC Q9P032; B2R4J5;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4;
DE AltName: Full=Hormone-regulated proliferation-associated protein of 20 kDa {ECO:0000303|PubMed:17001319};
GN Name=NDUFAF4 {ECO:0000312|HGNC:HGNC:21034};
GN Synonyms=C6orf66 {ECO:0000303|PubMed:18179882},
GN HRPAP20 {ECO:0000303|PubMed:17001319}; ORFNames=HSPC125, My013;
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].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Lin Q., Li Y., Dai J.L., Ying K.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone;
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 [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=14871833; DOI=10.1158/0008-5472.can-03-0023;
RA Karp C.M., Pan H., Zhang M., Buckley D.J., Schuler L.A., Buckley A.R.;
RT "Identification of HRPAP20: a novel phosphoprotein that enhances growth and
RT survival in hormone-responsive tumor cells.";
RL Cancer Res. 64:1016-1025(2004).
RN [8]
RP FUNCTION, INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF LYS-73.
RX PubMed=17001319; DOI=10.1038/sj.onc.1209980;
RA Karp C.M., Shukla M.N., Buckley D.J., Buckley A.R.;
RT "HRPAP20: a novel calmodulin-binding protein that increases breast cancer
RT cell invasion.";
RL Oncogene 26:1780-1788(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN MC1DN15, AND VARIANT MC1DN15
RP PRO-65.
RX PubMed=18179882; DOI=10.1016/j.ajhg.2007.08.003;
RA Saada A., Edvardson S., Rapoport M., Shaag A., Amry K., Miller C.,
RA Lorberboum-Galski H., Elpeleg O.;
RT "C6ORF66 is an assembly factor of mitochondrial complex I.";
RL Am. J. Hum. Genet. 82:32-38(2008).
RN [10]
RP INTERACTION WITH NDUFAF3.
RX PubMed=19463981; DOI=10.1016/j.ajhg.2009.04.020;
RA Saada A., Vogel R.O., Hoefs S.J., van den Brand M.A., Wessels H.J.,
RA Willems P.H., Venselaar H., Shaag A., Barghuti F., Reish O., Shohat M.,
RA Huynen M.A., Smeitink J.A.M., van den Heuvel L.P., Nijtmans L.G.;
RT "Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting
RT complex I assembly protein, cause fatal neonatal mitochondrial disease.";
RL Am. J. Hum. Genet. 84:718-727(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP INTERACTION WITH VSIV PROTEIN M (MICROBIAL INFECTION).
RX PubMed=33635491; DOI=10.1007/s11262-021-01833-0;
RA Pan W., Shen Z., Wang H., He H.;
RT "The host cellular protein Ndufaf4 interacts with the vesicular stomatitis
RT virus M protein and affects viral propagation.";
RL Virus Genes 57:250-257(2021).
RN [16]
RP FUNCTION, INVOLVEMENT IN MC1DN15, VARIANT MC1DN15 PRO-3, AND
RP CHARACTERIZATION OF VARIANT MC1DN15 PRO-3.
RX PubMed=28853723; DOI=10.1038/ejhg.2017.133;
RA Baertling F., Sanchez-Caballero L., van den Brand M.A.M., Wintjes L.T.,
RA Brink M., van den Brandt F.A., Wilson C., Rodenburg R.J.T.,
RA Nijtmans L.G.J.;
RT "NDUFAF4 variants are associated with Leigh syndrome and cause a specific
RT mitochondrial complex I assembly defect.";
RL Eur. J. Hum. Genet. 25:1273-1277(2017).
CC -!- FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone
CC oxidoreductase complex (complex I) (PubMed:18179882, PubMed:28853723).
CC May be involved in cell proliferation and survival of hormone-dependent
CC tumor cells. May be a regulator of breast tumor cell invasion.
CC {ECO:0000269|PubMed:14871833, ECO:0000269|PubMed:17001319,
CC ECO:0000269|PubMed:18179882, ECO:0000269|PubMed:28853723}.
CC -!- SUBUNIT: Binds calmodulin. Interacts with NDUFAF3.
CC {ECO:0000269|PubMed:17001319, ECO:0000269|PubMed:19463981}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the vesicular stomatitis
CC virus matrix protein/M; the interaction inhibits viral propagation.
CC {ECO:0000269|PubMed:33635491}.
CC -!- INTERACTION:
CC Q9P032; P28799: GRN; NbExp=3; IntAct=EBI-2606839, EBI-747754;
CC Q9P032; Q9BU61: NDUFAF3; NbExp=10; IntAct=EBI-2606839, EBI-2114801;
CC Q9P032; Q9BU61-2: NDUFAF3; NbExp=8; IntAct=EBI-2606839, EBI-10298649;
CC Q9P032; O76024: WFS1; NbExp=3; IntAct=EBI-2606839, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18179882}.
CC Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC -!- INDUCTION: Expression is low in quiescent cells and is induced in
CC exponentially proliferating cultures. Expression is also induced when
CC prolactin is added to stationary cells. Induced by dietary
CC differentiating agents such as butyrate and retinoic acid.
CC {ECO:0000269|PubMed:14871833}.
CC -!- PTM: Phosphorylated on serine. Prolactin stimulate serine
CC phosphorylation (By similarity). {ECO:0000250}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 15 (MC1DN15)
CC [MIM:618237]: A form of mitochondrial complex I deficiency, the most
CC common biochemical signature of mitochondrial disorders, a group of
CC highly heterogeneous conditions characterized by defective oxidative
CC phosphorylation, which collectively affects 1 in 5-10000 live births.
CC Clinical disorders have variable severity, ranging from lethal neonatal
CC disease to adult-onset neurodegenerative disorders. Phenotypes include
CC macrocephaly with progressive leukodystrophy, non-specific
CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC syndrome, Leber hereditary optic neuropathy, and some forms of
CC Parkinson disease. MC1DN15 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:18179882,
CC ECO:0000269|PubMed:28853723}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the NDUFAF4 family. {ECO:0000305}.
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DR EMBL; AF161474; AAF29089.1; -; mRNA.
DR EMBL; AF060508; AAG43126.1; -; mRNA.
DR EMBL; AK311850; BAG34792.1; -; mRNA.
DR EMBL; AL159985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48501.1; -; Genomic_DNA.
DR EMBL; BC039464; AAH39464.1; -; mRNA.
DR CCDS; CCDS5037.1; -.
DR RefSeq; NP_054884.1; NM_014165.3.
DR AlphaFoldDB; Q9P032; -.
DR SMR; Q9P032; -.
DR BioGRID; 118848; 179.
DR IntAct; Q9P032; 57.
DR MINT; Q9P032; -.
DR STRING; 9606.ENSP00000358272; -.
DR BindingDB; Q9P032; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugCentral; Q9P032; -.
DR GlyGen; Q9P032; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P032; -.
DR PhosphoSitePlus; Q9P032; -.
DR BioMuta; NDUFAF4; -.
DR DMDM; 30912745; -.
DR EPD; Q9P032; -.
DR jPOST; Q9P032; -.
DR MassIVE; Q9P032; -.
DR MaxQB; Q9P032; -.
DR PaxDb; Q9P032; -.
DR PeptideAtlas; Q9P032; -.
DR PRIDE; Q9P032; -.
DR ProteomicsDB; 83539; -.
DR TopDownProteomics; Q9P032; -.
DR Antibodypedia; 48392; 126 antibodies from 25 providers.
DR DNASU; 29078; -.
DR Ensembl; ENST00000316149.8; ENSP00000358272.4; ENSG00000123545.6.
DR GeneID; 29078; -.
DR KEGG; hsa:29078; -.
DR MANE-Select; ENST00000316149.8; ENSP00000358272.4; NM_014165.4; NP_054884.1.
DR UCSC; uc003pow.4; human.
DR CTD; 29078; -.
DR DisGeNET; 29078; -.
DR GeneCards; NDUFAF4; -.
DR HGNC; HGNC:21034; NDUFAF4.
DR HPA; ENSG00000123545; Low tissue specificity.
DR MalaCards; NDUFAF4; -.
DR MIM; 611776; gene.
DR MIM; 618237; phenotype.
DR neXtProt; NX_Q9P032; -.
DR OpenTargets; ENSG00000123545; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR PharmGKB; PA164723808; -.
DR VEuPathDB; HostDB:ENSG00000123545; -.
DR eggNOG; KOG4481; Eukaryota.
DR GeneTree; ENSGT00390000001627; -.
DR HOGENOM; CLU_054693_2_0_1; -.
DR InParanoid; Q9P032; -.
DR OMA; IPDQKYK; -.
DR OrthoDB; 1395543at2759; -.
DR PhylomeDB; Q9P032; -.
DR TreeFam; TF323532; -.
DR PathwayCommons; Q9P032; -.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; Q9P032; -.
DR BioGRID-ORCS; 29078; 116 hits in 1077 CRISPR screens.
DR ChiTaRS; NDUFAF4; human.
DR GenomeRNAi; 29078; -.
DR Pharos; Q9P032; Tclin.
DR PRO; PR:Q9P032; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9P032; protein.
DR Bgee; ENSG00000123545; Expressed in pons and 198 other tissues.
DR Genevisible; Q9P032; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR InterPro; IPR009622; NDUFAF4.
DR PANTHER; PTHR13338; PTHR13338; 1.
DR Pfam; PF06784; UPF0240; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Disease variant; Host-virus interaction; Lipoprotein;
KW Membrane; Mitochondrion; Myristate; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..175
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT assembly factor 4"
FT /id="PRO_0000220988"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT VARIANT 3
FT /note="A -> P (in MC1DN15; results in altered complex I
FT assembly; dbSNP:rs1554197721)"
FT /evidence="ECO:0000269|PubMed:28853723"
FT /id="VAR_081426"
FT VARIANT 65
FT /note="L -> P (in MC1DN15; dbSNP:rs63751061)"
FT /evidence="ECO:0000269|PubMed:18179882"
FT /id="VAR_044329"
FT MUTAGEN 73
FT /note="K->A: Reduces interaction with calmodulin. Does not
FT promote MMP-9 secretion."
FT /evidence="ECO:0000269|PubMed:17001319"
SQ SEQUENCE 175 AA; 20266 MW; B6445B0B4AA905D0 CRC64;
MGALVIRGIR NFNLENRAER EISKMKPSVA PRHPSTNSLL REQISLYPEV KGEIARKDEK
LLSFLKDVYV DSKDPVSSLQ VKAAETCQEP KEFRLPKDHH FDMINIKSIP KGKISIVEAL
TLLNNHKLFP ETWTAEKIMQ EYQLEQKDVN SLLKYFVTFE VEIFPPEDKK AIRSK
