RUBIC_MOUSE
ID RUBIC_MOUSE Reviewed; 956 AA.
AC Q80U62; Q3TAX3; Q3TD96; Q3TDF7; Q3TDU2; Q6NWW8; Q6P9T7; Q6PG18; Q8BMP7;
AC Q8BY22;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Run domain Beclin-1-interacting and cysteine-rich domain-containing protein {ECO:0000250|UniProtKB:Q92622};
DE Short=Rubicon;
GN Name=Rubcn {ECO:0000250|UniProtKB:Q92622}; Synonyms=Kiaa0226;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Pituitary, 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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BECN1; PIK3C3 AND
RP UVRAG.
RX PubMed=19270693; DOI=10.1038/ncb1854;
RA Zhong Y., Wang Q.J., Li X., Yan Y., Backer J.M., Chait B.T., Heintz N.,
RA Yue Z.;
RT "Distinct regulation of autophagic activity by Atg14L and Rubicon
RT associated with Beclin 1-phosphatidylinositol-3-kinase complex.";
RL Nat. Cell Biol. 11:468-476(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and 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: Inhibits PIK3C3 activity; under basal conditions negatively
CC regulates PI3K complex II (PI3KC3-C2) function in autophagy. Negatively
CC regulates endosome maturation and degradative endocytic trafficking and
CC impairs autophagosome maturation process (PubMed:19270693). Can
CC sequester UVRAG from association with a class C Vps complex (possibly
CC the HOPS complex) and negatively regulates Rab7 activation (By
CC similarity). {ECO:0000250|UniProtKB:Q92622,
CC ECO:0000269|PubMed:19270693}.
CC -!- FUNCTION: Involved in regulation of pathogen-specific host defense of
CC activated macrophages. Following bacterial infection promotes NADH
CC oxidase activity by association with CYBA thereby affecting TLR2
CC signaling and probably other TLR-NOX pathways. Stabilizes the CYBA:CYBB
CC NADPH oxidase heterodimer, increases its association with TLR2 and its
CC phagosome trafficking to induce antimicrobial burst of ROS and
CC production of inflammatory cytokines. Following fungal or viral
CC infection (implicating CLEC7A (dectin-1)-mediated myeloid cell
CC activation or DDX58/RIG-I-dependent sensing of RNA viruses) negatively
CC regulates pro-inflammatory cytokine production by association with
CC CARD9 and sequestering it from signaling complexes (By similarity).
CC {ECO:0000250|UniProtKB:Q92622}.
CC -!- SUBUNIT: Associates with PI3K (PI3KC3/PI3K-III/class III
CC phosphatidylinositol 3-kinase) complex II (PI3KC3-C2) in which the core
CC composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4
CC and BECN1 is associated with UVRAG; in the complex interacts directly
CC with PI3KC3 and UVRAG (PubMed:19270693). Interacts with Rab7 (RAB7A or
CC RAB7B) (GTP-bound form); Rab7 and UVRAG compete for RUBCN binding; can
CC interact simultaneously with Rab7 and the PI3K complex. Interacts with
CC CYBA and CYBB; indicative for the association with the CYBA:CYBB NADPH
CC oxidase heterodimer. Interacts with NOX4 and probably associates with
CC the CYBA:NOX4 complex. Interacts with YWHAB and CARD9 in a competitive
CC and stimulation-dependent manner; RUBCN exchanges interaction from
CC YWHAB to CARD9 upon stimulation with beta-1,3-glucan (By similarity).
CC {ECO:0000250|UniProtKB:Q92622, ECO:0000269|PubMed:19270693}.
CC -!- INTERACTION:
CC Q80U62; P00533: EGFR; Xeno; NbExp=2; IntAct=EBI-3506572, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:19270693}.
CC Lysosome {ECO:0000269|PubMed:19270693}. Early endosome
CC {ECO:0000269|PubMed:19270693}. Note=Predominantly located in late
CC endosomes/lysosomes, only partially detected in early endosome and not
CC at all in the Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80U62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U62-2; Sequence=VSP_017111;
CC Name=3;
CC IsoId=Q80U62-3; Sequence=VSP_017110, VSP_017111;
CC Name=4;
CC IsoId=Q80U62-4; Sequence=VSP_039474, VSP_017110, VSP_017111;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57307.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65503.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122221; BAC65503.1; ALT_INIT; mRNA.
DR EMBL; AK030368; BAC26925.1; -; mRNA.
DR EMBL; AK042428; BAC31257.1; -; mRNA.
DR EMBL; AK170002; BAE41507.1; -; mRNA.
DR EMBL; AK170223; BAE41645.1; -; mRNA.
DR EMBL; AK170312; BAE41708.1; -; mRNA.
DR EMBL; AK171583; BAE42541.1; -; mRNA.
DR EMBL; AC139244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057307; AAH57307.1; ALT_INIT; mRNA.
DR EMBL; BC060601; AAH60601.1; -; mRNA.
DR EMBL; BC067390; AAH67390.1; -; mRNA.
DR CCDS; CCDS28124.1; -. [Q80U62-2]
DR CCDS; CCDS49832.1; -. [Q80U62-1]
DR RefSeq; NP_001186967.1; NM_001200038.1. [Q80U62-1]
DR RefSeq; NP_766203.1; NM_172615.4. [Q80U62-2]
DR AlphaFoldDB; Q80U62; -.
DR SMR; Q80U62; -.
DR BioGRID; 426598; 5.
DR IntAct; Q80U62; 21.
DR MINT; Q80U62; -.
DR STRING; 10090.ENSMUSP00000087114; -.
DR iPTMnet; Q80U62; -.
DR PhosphoSitePlus; Q80U62; -.
DR EPD; Q80U62; -.
DR jPOST; Q80U62; -.
DR MaxQB; Q80U62; -.
DR PaxDb; Q80U62; -.
DR PRIDE; Q80U62; -.
DR ProteomicsDB; 260747; -. [Q80U62-1]
DR ProteomicsDB; 260748; -. [Q80U62-2]
DR ProteomicsDB; 260749; -. [Q80U62-3]
DR ProteomicsDB; 260750; -. [Q80U62-4]
DR Antibodypedia; 54002; 217 antibodies from 27 providers.
DR Ensembl; ENSMUST00000040986; ENSMUSP00000048811; ENSMUSG00000035629. [Q80U62-2]
DR Ensembl; ENSMUST00000089684; ENSMUSP00000087114; ENSMUSG00000035629. [Q80U62-1]
DR Ensembl; ENSMUST00000115105; ENSMUSP00000110757; ENSMUSG00000035629. [Q80U62-3]
DR GeneID; 100502698; -.
DR KEGG; mmu:100502698; -.
DR UCSC; uc007yzk.2; mouse. [Q80U62-1]
DR UCSC; uc007yzl.2; mouse. [Q80U62-2]
DR CTD; 9711; -.
DR MGI; MGI:1915160; Rubcn.
DR VEuPathDB; HostDB:ENSMUSG00000035629; -.
DR eggNOG; KOG1829; Eukaryota.
DR eggNOG; KOG4381; Eukaryota.
DR GeneTree; ENSGT00940000160658; -.
DR HOGENOM; CLU_013778_0_0_1; -.
DR InParanoid; Q80U62; -.
DR OMA; EQVKCNR; -.
DR OrthoDB; 177737at2759; -.
DR PhylomeDB; Q80U62; -.
DR TreeFam; TF317067; -.
DR BioGRID-ORCS; 100502698; 2 hits in 39 CRISPR screens.
DR ChiTaRS; Rubcn; mouse.
DR PRO; PR:Q80U62; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q80U62; protein.
DR Bgee; ENSMUSG00000035629; Expressed in secondary oocyte and 215 other tissues.
DR ExpressionAtlas; Q80U62; baseline and differential.
DR Genevisible; Q80U62; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; ISO:MGI.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; ISO:MGI.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR025258; Zf-RING_9.
DR Pfam; PF02759; RUN; 1.
DR Pfam; PF13901; zf-RING_9; 1.
DR SMART; SM01175; DUF4206; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR PROSITE; PS50826; RUN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Endocytosis; Endosome; Immunity; Lysosome;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..956
FT /note="Run domain Beclin-1-interacting and cysteine-rich
FT domain-containing protein"
FT /id="PRO_0000050737"
FT DOMAIN 49..190
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT REGION 50..181
FT /note="Interaction with PIK3C3"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT REGION 205..437
FT /note="Interaction with YWHAB"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT REGION 233..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..585
FT /note="Interaction with UVRAG"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT REGION 490..542
FT /note="Interaction with BECN1"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT REGION 547..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..609
FT /note="Interaction with CYBA"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT REGION 656..744
FT /note="Interaction with CARD9"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT REGION 705..956
FT /note="Interaction with Rab7"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT COMPBIAS 233..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92622"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039474"
FT VAR_SEQ 347..360
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017110"
FT VAR_SEQ 423..437
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017111"
FT CONFLICT 5
FT /note="G -> S (in Ref. 2; BAE41507/BAE41645)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="D -> G (in Ref. 3; AAH67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="T -> N (in Ref. 2; BAE41507/BAE41645/BAE41708)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="S -> P (in Ref. 2; BAE41645)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="D -> G (in Ref. 2; BAE41708)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="P -> S (in Ref. 3; AAH67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="Q -> L (in Ref. 3; AAH67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="S -> G (in Ref. 2; BAE42541)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="A -> T (in Ref. 3; AAH67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="H -> Q (in Ref. 2; BAE42541)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="C -> R (in Ref. 3; AAH67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="A -> T (in Ref. 2; BAE41708)"
FT /evidence="ECO:0000305"
FT CONFLICT 951
FT /note="T -> P (in Ref. 2; BAC31257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 106860 MW; E5D8CD691C0D5184 CRC64;
MRPEGAGMDL GGGDGERLLE KSRREHWQLL GNLKTTVEGL VSANCPNVWS KYGGLERLCR
DMQNILYHGL IHDQVCCRQA DYWQFVKDIR WLSPHSALHV EKFISLHESD QSDTDSVSER
AVAELWLQHS LQCHCLSAQL RPLLGDRQYI RKFYTETAFL LSDAHVTAML QCLEAVEQNN
PRLLAQIDAS MFARKQESPL LVTKSQSLTA LPGSTYTPPA SYAQHSYFGS SSSLQSMPQS
SHSSERRSTS FSLSGPSWQP QEDRECLSPA ETQTTPAPLP SDSTLAQDSP LTAQEMSDST
LTSPLEASWV SSQNDSPSDV SEGPEYLAIG NPAPHGRTAS CESHSSNGES SSSHLFSSSS
SQKLESAASS LGDQEEGRQS QAGSVLRRSS FSEGQTAPVA SGTKKSHIRS HSDTNIASRG
AAGGPRNITI IVEDPIAEGG QYLCSGEGMF RRPSEGQSLI SYLSEQDFGS CADLEKENAH
FSISESLIAA IELMKCNMMS QCLEEEEVEE EDSDREIQEL KQKIRLRRQQ IRTKNLLPAY
RETENGSFRV TSSSSQFSSR DSTQLSESGS AEDADDLEIQ DADIRRSAVS NGKSSFSQNL
SHCFLHSTSA EAVAMGLLKQ FEGMQLPAAS ELEWLVPEHD APQKLLPIPD SLPISPDDGQ
HADIYKLRIR VRGNLEWAPP RPQIIFNVHP APTRKIAVAK QNYRCAGCGI RTDPDYIKRL
RYCEYLGKYF CQCCHENAQM VVPSRILRKW DFSKYYVSNF SKDLLLKIWN DPLFNVQDIN
SALYRKVKLL NQVRLLRVQL YHMKNMFKTC RLAKELLDSF DVVPGHLTED LHLYSLSDLT
ATKKGELGPR LAELTRAGAA HVERCMLCQA KGFICEFCQN EEDVIFPFEL HKCRTCEECK
ACYHKTCFKS GRCPRCERLQ ARRELLAKQS LESYLSDYEE EPTEALALEA TVLETT
