MIB2_MOUSE
ID MIB2_MOUSE Reviewed; 973 AA.
AC Q8R516; A2A9P9; Q52QU8; Q6PEF6; Q8C1N7; Q8VIB4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=E3 ubiquitin-protein ligase MIB2;
DE EC=2.3.2.27;
DE AltName: Full=Dystrophin-like protein;
DE Short=Dyslike;
DE AltName: Full=Mind bomb homolog 2;
DE Short=Mind bomb-2;
DE AltName: Full=RING-type E3 ubiquitin transferase MIB2 {ECO:0000305};
DE AltName: Full=Skeletrophin;
GN Name=Mib2; Synonyms=Skd;
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), ENZYME ACTIVITY, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP UBIQUITINATION, AND MUTAGENESIS OF CYS-874 AND CYS-951.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
RX PubMed=15824097; DOI=10.1074/jbc.m501631200;
RA Koo B.-K., Yoon K.-J., Yoo K.-W., Lim H.-S., Song R., So J.-H., Kim C.-H.,
RA Kong Y.-Y.;
RT "Mind bomb-2 is an E3 ligase for Notch ligand.";
RL J. Biol. Chem. 280:22335-22342(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RA Takeuchi T.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-750.
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [7]
RP PROTEIN SEQUENCE OF 920-926, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC Delta receptors, which act as ligands of Notch proteins. Positively
CC regulates the Delta-mediated Notch signaling by ubiquitinating the
CC intracellular domain of Delta, leading to endocytosis of Delta
CC receptors. {ECO:0000269|PubMed:15824097}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with actin monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15824097}. Endosome
CC {ECO:0000269|PubMed:15824097}. Note=Colocalizes with endosomal
CC compartments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8R516-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R516-2; Sequence=VSP_014397, VSP_014400, VSP_014401;
CC Name=3;
CC IsoId=Q8R516-3; Sequence=VSP_014398, VSP_014399;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, liver and kidney.
CC {ECO:0000269|PubMed:15824097}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in neonate and adult, but only
CC slightly in embryos. In 10.5 dpc embryos, it is weakly expressed in the
CC tail bud and limb buds. Expressed in the same pattern than MIB1 in the
CC skin and intestine at postnatal day 1 (P1) and in the hair follicle in
CC the skin in the adult. {ECO:0000269|PubMed:15824097}.
CC -!- PTM: Ubiquitinated. Possibly via autoubiquitination.
CC {ECO:0000269|PubMed:15824097}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB79447.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB86856.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY974090; AAX84652.1; -; mRNA.
DR EMBL; AB063290; BAB79447.1; ALT_FRAME; mRNA.
DR EMBL; AB072336; BAB86856.1; ALT_FRAME; mRNA.
DR EMBL; AL627405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL15023.1; -; Genomic_DNA.
DR EMBL; BC058086; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK008671; BAC25227.1; -; mRNA.
DR CCDS; CCDS19035.1; -. [Q8R516-2]
DR RefSeq; NP_001243037.2; NM_001256108.2. [Q8R516-2]
DR RefSeq; NP_660106.2; NM_145124.3. [Q8R516-2]
DR AlphaFoldDB; Q8R516; -.
DR SMR; Q8R516; -.
DR BioGRID; 218188; 14.
DR IntAct; Q8R516; 1.
DR STRING; 10090.ENSMUSP00000099465; -.
DR iPTMnet; Q8R516; -.
DR PhosphoSitePlus; Q8R516; -.
DR MaxQB; Q8R516; -.
DR PRIDE; Q8R516; -.
DR ProteomicsDB; 290231; -. [Q8R516-1]
DR ProteomicsDB; 290232; -. [Q8R516-2]
DR ProteomicsDB; 290233; -. [Q8R516-3]
DR Antibodypedia; 26451; 112 antibodies from 25 providers.
DR DNASU; 76580; -.
DR Ensembl; ENSMUST00000103176; ENSMUSP00000099465; ENSMUSG00000029060. [Q8R516-2]
DR GeneID; 76580; -.
DR KEGG; mmu:76580; -.
DR UCSC; uc008wee.2; mouse. [Q8R516-1]
DR UCSC; uc008wef.2; mouse. [Q8R516-2]
DR CTD; 142678; -.
DR MGI; MGI:2679684; Mib2.
DR VEuPathDB; HostDB:ENSMUSG00000029060; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00940000158097; -.
DR HOGENOM; CLU_007287_2_0_1; -.
DR InParanoid; Q8R516; -.
DR OMA; ATCGGHY; -.
DR OrthoDB; 220300at2759; -.
DR PhylomeDB; Q8R516; -.
DR TreeFam; TF324147; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76580; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Mib2; mouse.
DR PRO; PR:Q8R516; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8R516; protein.
DR Bgee; ENSMUSG00000029060; Expressed in embryonic brain and 243 other tissues.
DR ExpressionAtlas; Q8R516; baseline and differential.
DR Genevisible; Q8R516; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042056; MIB1/2_ZZ.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF159034; SSF159034; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ANK repeat; Cytoplasm;
KW Direct protein sequencing; Endosome; Metal-binding;
KW Notch signaling pathway; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..973
FT /note="E3 ubiquitin-protein ligase MIB2"
FT /id="PRO_0000055948"
FT DOMAIN 1..80
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 149..227
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 480..509
FT /note="ANK 1"
FT REPEAT 513..542
FT /note="ANK 2"
FT REPEAT 546..575
FT /note="ANK 3"
FT REPEAT 579..611
FT /note="ANK 4"
FT REPEAT 615..644
FT /note="ANK 5"
FT REPEAT 649..679
FT /note="ANK 6"
FT REPEAT 683..712
FT /note="ANK 7"
FT REPEAT 716..744
FT /note="ANK 8"
FT REPEAT 785..814
FT /note="ANK 9"
FT ZN_FING 86..138
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 850..885
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 929..962
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AX9"
FT VAR_SEQ 289..324
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014397"
FT VAR_SEQ 289..294
FT /note="FIGQMG -> VSHLFC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014398"
FT VAR_SEQ 295..973
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014399"
FT VAR_SEQ 415..422
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014400"
FT VAR_SEQ 467..474
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014401"
FT MUTAGEN 874
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:15824097"
FT MUTAGEN 951
FT /note="C->S: Abolishes ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:15824097"
FT CONFLICT 89
FT /note="I -> T (in Ref. 2; BAB79447/BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="E -> G (in Ref. 2; BAB79447/BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> L (in Ref. 2; BAB79447/BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="V -> S (in Ref. 2; BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="E -> D (in Ref. 2; BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="E -> D (in Ref. 2; BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="V -> L (in Ref. 2; BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="G -> R (in Ref. 2; BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="K -> R (in Ref. 2; BAB86856)"
FT /evidence="ECO:0000305"
FT CONFLICT 745..750
FT /note="LQLLSR -> CSCCQG (in Ref. 6; BAC25227)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="Q -> R (in Ref. 2; BAB86856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 973 AA; 105961 MW; 3E9406DEB30541D7 CRC64;
MDLDPHAGVQ VGMRVVRGMD WKWGQQDGGE GGVGTVVELG RHGSPSTPDR TVVVQWDQGT
RTNYRAGYQG AHDLLLYDNA QIGIRHPNII CDCCKKHGLR GMRWKCRVCF DYDLCTQCYM
HNKHDLTHAF ERYETSHSRP VTLSPRQGLP RIPLRGIFQG AKVVRGPDWE WGSQDGGEGK
TGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LRCVGEAAGG FYYKEHLPKL
GKPAELQRRV SADGQPFQRG DKVKCLLDTD VLRDMQEGHG GWNPRMAEFI GQMGTVHRIT
DRGDVRVQFN HETRWTFHPG ALTKHNSFWV GDVVRVIGDL DTVKRLQAGH GEWTDDMAPA
LGRVGKVVKV FGDGNLRVAV GGQRWTFSPS CLVAYRPEED ANLDVAERAR ENKSAASVSV
AGSLSVALDK LRTQKSDPEH PGRLVVEAAL GNVARALDLL RRHPEQASYH PALVVDTKNQ
GRTALQVAAY LGQVELVRLL LQARASMDLP DDEGNTVLHY TAMGNQPEAT RVLLSAGCAV
DARNGTRSTA LHVAVQRGFL EVVKILCERG CDVNLPDAHA DTPLHSAISA GAGASSIVEV
LTEVPGIDVT ATNSQGFTLL HHASLKGHVL AVRKILARAR QLVDAKKEDG FTALHLAALN
NHREVAQVLI REGRCDVNVR NRKLQSPLHL AVQQAHLGLV PLLVDAGCSV NTEDEEGDTA
LHVALQRHQL LPLVADRAGG DPGPLQLLSR LQASGLPGCT ELTVGAAVAC FLALEGADVS
YANHRGRSPL DLATEGRVLK ALQGCAQRFR ERQAGGGGGV PPGPRHVLST PNTVTNLHVS
GTAGPEAAEC LVCSELALLI LFSPCQHRTV CEECARRMKK CIRCQVVISK KLRPDGSEVV
NAIQVPGPPR QLVEELQSRY RQMEERITCP ICIDSHIRLV FQCGHGACAP CGAALNACPI
CRQPIRDRIQ IFV
