MIB1_MOUSE
ID MIB1_MOUSE Reviewed; 1006 AA.
AC Q80SY4; Q5XK51; Q6IS57; Q6YI52; Q6ZPT8; Q8BNR1; Q8C6W2; Q921Q1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase MIB1;
DE EC=2.3.2.27;
DE AltName: Full=DAPK-interacting protein 1;
DE Short=DIP-1;
DE AltName: Full=Mind bomb homolog 1;
DE AltName: Full=RING-type E3 ubiquitin transferase MIB1 {ECO:0000305};
GN Name=Mib1; Synonyms=Dip1, Kiaa1323, Mib;
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], FUNCTION, TISSUE SPECIFICITY, AND
RP UBIQUITINATION.
RC TISSUE=Urinary bladder;
RX PubMed=12351649; DOI=10.1074/jbc.m208585200;
RA Jin Y., Blue E.K., Dixon S., Shao Z., Gallagher P.J.;
RT "A death-associated protein kinase (DAPK)-interacting protein, DIP-1, is an
RT E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis
RT and regulates the cellular levels of DAPK.";
RL J. Biol. Chem. 277:46980-46986(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RX PubMed=12530964; DOI=10.1016/s1534-5807(02)00409-4;
RA Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D., Yeo S.-Y.,
RA Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M., Lewis J.,
RA Chandrasekharappa S.C., Chitnis A.B.;
RT "Mind bomb is a ubiquitin ligase that is essential for efficient activation
RT of Notch signaling by Delta.";
RL Dev. Cell 4:67-82(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP UBIQUITINATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1006.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Head;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 547-1006.
RC STRAIN=129, and FVB/N; TISSUE=Embryo, and Mammary tumor;
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 864-1006.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
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).
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. Involved in ubiquitination of centriolar satellite CEP131,
CC CEP290 and PCM1 proteins and hence inhibits primary cilium formation in
CC proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of
CC TBK1, which probably participates in kinase activation (By similarity).
CC Probably mediates ubiquitination and subsequent proteasomal degradation
CC of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to
CC promote TNF-induced apoptosis. {ECO:0000250,
CC ECO:0000269|PubMed:12351649}.
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 CEP131 and PCM1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q80SY4; Q8IY22: CMIP; Xeno; NbExp=2; IntAct=EBI-645227, EBI-7689652;
CC Q80SY4; Q6DI32: snx5; Xeno; NbExp=4; IntAct=EBI-645227, EBI-8574974;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriolar satellite {ECO:0000250}. Cytoplasm. Cell
CC membrane. Note=Displaced from centriolar satellites in response to
CC cellular stress, such as ultraviolet light (UV) radiation or heat shock
CC (By similarity). Localizes to the plasma membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues tested. Present in embryo,
CC embryonic stem cells, bladder, skeletal muscle, bladder, uterus,
CC testis, stomach, colon, ileum, trachea, lung, aorta, kidney, spleen,
CC liver and vas deferens (at protein level). Highly expressed in testis.
CC {ECO:0000269|PubMed:12351649, ECO:0000269|PubMed:15824097}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed both in embryos and adult
CC tissues. In 9.5 dpc and 10.5 dpc embryos, it is expressed in the tail
CC bud, limb buds and somites. Expressed in the same pattern than MIB2 in
CC the skin and intestine at postnatal day 1 (P1) and in the hair follicle
CC in the skin in the adult. {ECO:0000269|PubMed:15824097}.
CC -!- PTM: Ubiquitinated; this modification is inhibited in response to
CC cellular stress, such as ultraviolet light (UV) radiation or heat shock
CC (By similarity). Ubiquitinated; possibly via autoubiquitination.
CC {ECO:0000250, ECO:0000269|PubMed:12351649,
CC ECO:0000269|PubMed:15824097}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11287.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH69870.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC Sequence=AAN18022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38042.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AY245539; AAO91933.1; -; mRNA.
DR EMBL; AY149907; AAN75492.1; -; mRNA.
DR EMBL; AY147848; AAN18022.1; ALT_INIT; mRNA.
DR EMBL; AY974091; AAX84653.1; -; mRNA.
DR EMBL; AK053035; BAC35245.1; -; mRNA.
DR EMBL; AK080847; BAC38042.1; ALT_SEQ; mRNA.
DR EMBL; BC011287; AAH11287.1; ALT_INIT; mRNA.
DR EMBL; BC069870; AAH69870.1; ALT_SEQ; mRNA.
DR EMBL; BC083072; AAH83072.1; -; mRNA.
DR EMBL; AK129331; BAC98141.1; -; mRNA.
DR CCDS; CCDS29058.1; -.
DR RefSeq; NP_659109.2; NM_144860.2.
DR RefSeq; XP_006525873.1; XM_006525810.2.
DR RefSeq; XP_006525874.1; XM_006525811.3.
DR AlphaFoldDB; Q80SY4; -.
DR SMR; Q80SY4; -.
DR BioGRID; 230365; 45.
DR IntAct; Q80SY4; 30.
DR MINT; Q80SY4; -.
DR STRING; 10090.ENSMUSP00000054428; -.
DR iPTMnet; Q80SY4; -.
DR PhosphoSitePlus; Q80SY4; -.
DR EPD; Q80SY4; -.
DR MaxQB; Q80SY4; -.
DR PaxDb; Q80SY4; -.
DR PRIDE; Q80SY4; -.
DR ProteomicsDB; 293477; -.
DR Antibodypedia; 7263; 345 antibodies from 37 providers.
DR DNASU; 225164; -.
DR Ensembl; ENSMUST00000052838; ENSMUSP00000054428; ENSMUSG00000024294.
DR Ensembl; ENSMUST00000165555; ENSMUSP00000131712; ENSMUSG00000024294.
DR GeneID; 225164; -.
DR KEGG; mmu:225164; -.
DR UCSC; uc008ebc.1; mouse.
DR CTD; 57534; -.
DR MGI; MGI:2443157; Mib1.
DR VEuPathDB; HostDB:ENSMUSG00000024294; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00940000156781; -.
DR HOGENOM; CLU_007287_1_0_1; -.
DR InParanoid; Q80SY4; -.
DR OMA; CCGGIGR; -.
DR OrthoDB; 220300at2759; -.
DR PhylomeDB; Q80SY4; -.
DR TreeFam; TF324147; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 225164; 9 hits in 75 CRISPR screens.
DR ChiTaRS; Mib1; mouse.
DR PRO; PR:Q80SY4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q80SY4; protein.
DR Bgee; ENSMUSG00000024294; Expressed in metanephric cortical collecting duct and 241 other tissues.
DR ExpressionAtlas; Q80SY4; baseline and differential.
DR Genevisible; Q80SY4; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
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:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 3.
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; 9.
DR SMART; SM00184; RING; 3.
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; 6.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 3.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW Metal-binding; Notch signaling pathway; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1006
FT /note="E3 ubiquitin-protein ligase MIB1"
FT /id="PRO_0000055944"
FT DOMAIN 6..74
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 143..221
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 430..460
FT /note="ANK 1"
FT REPEAT 463..492
FT /note="ANK 2"
FT REPEAT 496..525
FT /note="ANK 3"
FT REPEAT 529..558
FT /note="ANK 4"
FT REPEAT 562..591
FT /note="ANK 5"
FT REPEAT 595..627
FT /note="ANK 6"
FT REPEAT 631..661
FT /note="ANK 7"
FT REPEAT 665..694
FT /note="ANK 8"
FT REPEAT 698..729
FT /note="ANK 9"
FT ZN_FING 80..132
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 819..854
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 866..901
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 963..996
FT /note="RING-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 935..962
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 103
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="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 112
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YT6"
FT CONFLICT 742
FT /note="L -> F (in Ref. 4; BAC38042)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="R -> K (in Ref. 3; AAN18022/AAX84653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1006 AA; 110088 MW; 5A8FE2A1BEE638DE CRC64;
MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT VCYHGDKHHL
RHRFYRITTP GSERVLLESR RKSKKITARG IFAGARVVRG VDWQWEDQDG GNGRRGKVTE
IQDWSASSPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN
RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL LQRGHGEWAE
AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV APAGSAISNA SGERLSQLLK
KLFETQESGD LNEELVKAAA NGDVAKVEDL LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL
KLLLKQNVDV EAEDKDGDRA VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK
GHLQVVKTLL DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGNANLD
IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD TPLHEALRHH TLSQLRQLQD
MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK SAASIACFLA ANGADLSIRN KKGQSPLDLC
PDPSLCKALA KCHKEKVSGQ VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC
SLCSPRVKKC LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ASLMKKCVQC
RAVVERRVPF ITCCGGKSSE DPSDEISSGN IPVLQKDKDN TNVNADVQKL QQQLQDIKEQ
TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE RRILLY
