ID   MUL1_MOUSE              Reviewed;         352 AA.
AC   Q8VCM5; A2AM82; A2AM84; B5M498; Q3TDK4; Q8BHF2; Q9DCV9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   09-APR-2025, entry version 172.
DE   RecName: Full=Mitochondrial ubiquitin ligase activator of NFKB 1;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q969V5};
DE   AltName: Full=E3 ubiquitin-protein ligase MUL1;
DE   AltName: Full=Growth inhibition and death E3 ligase;
DE   AltName: Full=Protein Hades {ECO:0000250|UniProtKB:Q969V5};
DE   AltName: Full=RING-type E3 ubiquitin transferase NFKB 1 {ECO:0000305};
GN   Name=Mul1; Synonyms=Gide;
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] (ISOFORM 1).
RX   PubMed=18591963; DOI=10.1038/cr.2008.75;
RA   Zhang B., Huang J., Li H.-L., Liu T., Wang Y.-Y., Waterman P., Mao A.-P.,
RA   Xu L.-G., Zhai Z., Liu D., Marrack P., Shu H.-B.;
RT   "GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and
RT   slows growth.";
RL   Cell Res. 18:900-910(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain cortex, Head, Kidney, Liver, and Thymus;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue;
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).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=24898855; DOI=10.7554/elife.01958;
RA   Yun J., Puri R., Yang H., Lizzio M.A., Wu C., Sheng Z.H., Guo M.;
RT   "MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin
RT   and compensates for loss of PINK1/parkin.";
RL   Elife 3:E01958-E01958(2014).
CC   -!- FUNCTION: Exhibits weak E3 ubiquitin-protein ligase activity (By
CC       similarity). E3 ubiquitin ligases accept ubiquitin from an E2
CC       ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfer the ubiquitin to targeted substrates (By similarity).
CC       Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-
CC       linked polyubiquitination and seems to be involved in regulation of Akt
CC       signaling by targeting phosphorylated Akt to proteasomal degradation
CC       (By similarity). Mediates polyubiquitination of cytoplasmic TP53 at
CC       'Lys-27' which targets TP53 for proteasomal degradation, thus reducing
CC       TP53 levels in the cytoplasm and mitochondrion (By similarity).
CC       Proposed to preferentially act as a SUMO E3 ligase at physiological
CC       concentrations (By similarity). Plays a role in the control of
CC       mitochondrial morphology by promoting mitochondrial fragmentation, and
CC       influences mitochondrial localization (By similarity). Likely to
CC       promote mitochondrial fission through negatively regulating the
CC       mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that
CC       is parallel to the PRKN/PINK1 regulatory pathway (PubMed:24898855). May
CC       also be involved in the sumoylation of the membrane fission protein
CC       DNM1L (By similarity). Inhibits cell growth (By similarity). When
CC       overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-
CC       dependent apoptosis (By similarity). Involved in the modulation of
CC       innate immune defense against viruses by inhibiting RIGI-dependent
CC       antiviral response (By similarity). Can mediate RIGI sumoylation and
CC       disrupt its polyubiquitination (By similarity).
CC       {ECO:0000250|UniProtKB:Q969V5, ECO:0000269|PubMed:24898855}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q969V5};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q969V5}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000250|UniProtKB:Q969V5}.
CC   -!- SUBUNIT: Homooligomer. Interacts with MAP3K7/TAK1. Interacts with UBC9.
CC       Interacts with and sumoylates DNM1L. Interacts with MAVS. Interacts
CC       with TP53 (via N-terminus); the interaction leads to ubiquitination and
CC       proteasomal degradation of TP53. {ECO:0000250|UniProtKB:Q969V5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q969V5}; Multi-pass membrane protein
CC       {ECO:0000255}. Peroxisome {ECO:0000250|UniProtKB:Q969V5}.
CC       Note=Transported in mitochondrion-derived vesicles from the
CC       mitochondrion to the peroxisome. {ECO:0000250|UniProtKB:Q969V5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VCM5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VCM5-2; Sequence=VSP_034454, VSP_034455;
CC       Name=3;
CC         IsoId=Q8VCM5-3; Sequence=VSP_034453;
CC   -!- TISSUE SPECIFICITY: Expressed in cortical neurons (at protein level).
CC       {ECO:0000269|PubMed:24898855}.
CC   -!- DOMAIN: The zinc finger domain is required for E3 ligase activity.
CC       {ECO:0000250|UniProtKB:Q969V5}.
CC   -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC       and enhancement of mitophagy. Deubiquitinated by USP30.
CC       {ECO:0000250|UniProtKB:Q969V5}.
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; EU935009; ACH72646.1; -; mRNA.
DR   EMBL; AK002416; BAB22084.1; -; mRNA.
DR   EMBL; AK044088; BAC31768.1; -; mRNA.
DR   EMBL; AK076419; BAC36332.1; -; mRNA.
DR   EMBL; AK083295; BAC38848.1; -; mRNA.
DR   EMBL; AK153956; BAE32279.1; -; mRNA.
DR   EMBL; AK170149; BAE41597.1; -; mRNA.
DR   EMBL; AL807249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC019516; AAH19516.1; -; mRNA.
DR   CCDS; CCDS18828.1; -. [Q8VCM5-1]
DR   RefSeq; NP_080965.2; NM_026689.3. [Q8VCM5-1]
DR   RefSeq; XP_006539197.1; XM_006539134.5. [Q8VCM5-3]
DR   AlphaFoldDB; Q8VCM5; -.
DR   SMR; Q8VCM5; -.
DR   BioGRID; 212817; 2.
DR   STRING; 10090.ENSMUSP00000039604; -.
DR   iPTMnet; Q8VCM5; -.
DR   PhosphoSitePlus; Q8VCM5; -.
DR   PaxDb; 10090-ENSMUSP00000039604; -.
DR   PeptideAtlas; Q8VCM5; -.
DR   ProteomicsDB; 290221; -. [Q8VCM5-1]
DR   ProteomicsDB; 290222; -. [Q8VCM5-2]
DR   ProteomicsDB; 290223; -. [Q8VCM5-3]
DR   Pumba; Q8VCM5; -.
DR   Antibodypedia; 2986; 344 antibodies from 30 providers.
DR   DNASU; 68350; -.
DR   Ensembl; ENSMUST00000044058.11; ENSMUSP00000039604.5; ENSMUSG00000041241.13. [Q8VCM5-1]
DR   Ensembl; ENSMUST00000105813.8; ENSMUSP00000101439.2; ENSMUSG00000041241.13. [Q8VCM5-3]
DR   Ensembl; ENSMUST00000105815.2; ENSMUSP00000101441.2; ENSMUSG00000041241.13. [Q8VCM5-2]
DR   GeneID; 68350; -.
DR   KEGG; mmu:68350; -.
DR   UCSC; uc008vky.1; mouse. [Q8VCM5-1]
DR   AGR; MGI:1915600; -.
DR   CTD; 79594; -.
DR   MGI; MGI:1915600; Mul1.
DR   VEuPathDB; HostDB:ENSMUSG00000041241; -.
DR   eggNOG; KOG1571; Eukaryota.
DR   GeneTree; ENSGT00390000012141; -.
DR   HOGENOM; CLU_050604_1_0_1; -.
DR   InParanoid; Q8VCM5; -.
DR   OMA; YILWKQY; -.
DR   OrthoDB; 66726at2759; -.
DR   PhylomeDB; Q8VCM5; -.
DR   TreeFam; TF325195; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR   UniPathway; UPA00143; -.
DR   UniPathway; UPA00886; -.
DR   BioGRID-ORCS; 68350; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Mul1; mouse.
DR   PRO; PR:Q8VCM5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8VCM5; protein.
DR   Bgee; ENSMUSG00000041241; Expressed in facial nucleus and 254 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0019789; F:SUMO transferase activity; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR   GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; ISS:UniProtKB.
DR   GO; GO:0050689; P:negative regulation of defense response to virus by host; ISS:UniProtKB.
DR   GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
DR   GO; GO:0010637; P:negative regulation of mitochondrial fusion; IEA:Ensembl.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR   GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:Ensembl.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; IEA:Ensembl.
DR   GO; GO:1905091; P:positive regulation of type 2 mitophagy; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IGI:ParkinsonsUK-UCL.
DR   GO; GO:1901028; P:regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
DR   CDD; cd16648; mRING-HC-C3HC5_MAPL; 1.
DR   FunFam; 3.30.40.10:FF:000351; Mitochondrial ubiquitin ligase activator of NFKB 1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR051652; MDM2_MDM4_MUL1.
DR   InterPro; IPR022170; MUL1-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12183; MITOCHONDRIAL UBIQUITIN LIGASE ACTIVATOR OF NFKB 1; 1.
DR   PANTHER; PTHR12183:SF4; MITOCHONDRIAL UBIQUITIN LIGASE ACTIVATOR OF NFKB 1; 1.
DR   Pfam; PF12483; GIDE; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Isopeptide bond; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion outer membrane; Peroxisome;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..352
FT                   /note="Mitochondrial ubiquitin ligase activator of NFKB 1"
FT                   /id="PRO_0000277662"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..238
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         302..340
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   CROSSLNK        52
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969V5"
FT   CROSSLNK        299
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q969V5"
FT   VAR_SEQ         1..40
FT                   /note="MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELK -> MVVVLCWL
FT                   EFHSPSAKDLFWQLYGRWTLEPKSYHQ (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034453"
FT   VAR_SEQ         111..123
FT                   /note="NDYSKIIHQRTNT -> CVSSGFYTSEVVV (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034454"
FT   VAR_SEQ         124..352
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034455"
FT   CONFLICT        38
FT                   /note="E -> V (in Ref. 2; BAE41597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="V -> F (in Ref. 2; BAB22084)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="I -> V (in Ref. 1; ACH72646 and 4; AAH19516)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  39835 MW;  252530F1BD917871 CRC64;
     MESGSRPSLG QVILLGTSSM VTAVLYSIYR QKAQVAQELK GAKKIHLGED LKGILSEAPG
     KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLSLQEHK MVWNRTTHLW NDYSKIIHQR
     TNTVPFDLVP HEDGVAVSVR VLKPLDSVDL GLETVYEKFH PSVQSFTDAI GHYISGERPK
     GIQETEEMLK VGATLTGIGE LVLDNNAVRL QPPKQGMQYY LSSQDFDSLL HRQESSVRLW
     KILVLVFGFA TCATLFFILR KQYLHRQERL RQQQLQEEFL EHEAQLLSQA SPEDRESLKS
     ACVVCLSNFK SCVFLECGHV CSCRQCYLAL PEPKRCPICR REITRVIPLY NS
//