CRBN_MOUSE
ID CRBN_MOUSE Reviewed; 445 AA.
AC Q8C7D2; Q3TVC2; Q5RJV6; Q6IS49; Q80XJ1; Q8BP45; Q8C6B7; Q9JKR4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein cereblon;
DE Short=Protein PiL;
GN Name=Crbn;
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Head, and Pancreas;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 6-445 (ISOFORM 1).
RC TISSUE=Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-445.
RA Rose J.B., van Driel I.R., Tan S.;
RT "A novel gene mutated in R197 insertional mutant mice.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20131966; DOI=10.3109/01677060903567849;
RA Higgins J.J., Tal A.L., Sun X., Hauck S.C., Hao J., Kosofosky B.E.,
RA Rajadhyaksha A.M.;
RT "Temporal and spatial mouse brain expression of cereblon, an ionic channel
RT regulator involved in human intelligence.";
RL J. Neurogenet. 24:18-26(2010).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=21995942; DOI=10.1016/j.bbr.2011.09.039;
RA Rajadhyaksha A.M., Ra S., Kishinevsky S., Lee A.S., Romanienko P.,
RA DuBoff M., Yang C., Zupan B., Byrne M., Daruwalla Z.R., Mark W.,
RA Kosofsky B.E., Toth M., Higgins J.J.;
RT "Behavioral characterization of cereblon forebrain-specific conditional
RT null mice: a model for human non-syndromic intellectual disability.";
RL Behav. Brain Res. 226:428-434(2012).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29530986; DOI=10.1523/jneurosci.2081-17.2018;
RA Choi T.Y., Lee S.H., Kim Y.J., Bae J.R., Lee K.M., Jo Y., Kim S.J.,
RA Lee A.R., Choi S., Choi L.M., Bang S., Song M.R., Chung J., Lee K.J.,
RA Kim S.H., Park C.S., Choi S.Y.;
RT "Cereblon Maintains Synaptic and Cognitive Function by Regulating BK
RT Channel.";
RL J. Neurosci. 38:3571-3583(2018).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 322-430 IN COMPLEX WITH
RP S-THALIDOMIDE AND ZINC, AND DOMAIN.
RX PubMed=25108355; DOI=10.1038/nsmb.2874;
RA Chamberlain P.P., Lopez-Girona A., Miller K., Carmel G., Pagarigan B.,
RA Chie-Leon B., Rychak E., Corral L.G., Ren Y.J., Wang M., Riley M.,
RA Delker S.L., Ito T., Ando H., Mori T., Hirano Y., Handa H., Hakoshima T.,
RA Daniel T.O., Cathers B.E.;
RT "Structure of the human cereblon-DDB1-lenalidomide complex reveals basis
RT for responsiveness to thalidomide analogs.";
RL Nat. Struct. Mol. Biol. 21:803-809(2014).
CC -!- FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3
CC protein ligase complex that mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins, such as MEIS2 or ILF2.
CC Normal degradation of key regulatory proteins is required for normal
CC limb outgrowth and expression of the fibroblast growth factor FGF8 (By
CC similarity). Maintains presynaptic glutamate release and consequently,
CC cognitive functions such as memory and learning, by negatively
CC regulating large-conductance calcium-activated potassium (BK) channels
CC in excitatory neurons (PubMed:29530986). Likely to function by
CC regulating the assembly and neuronal surface expression of BK channels
CC via its interaction with KCNT1 (By similarity). May also be involved in
CC regulating anxiety-like behaviors via a BK channel-independent
CC mechanism (PubMed:29530986). {ECO:0000250|UniProtKB:Q96SW2,
CC ECO:0000269|PubMed:29530986, ECO:0000305}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96SW2}.
CC -!- SUBUNIT: Component of a DCX (DDB1-CUL4-X-box) protein ligase complex,
CC at least composed of CRBN, CUL4A, DDB1 and RBX1. Interacts directly
CC with DDB1 (By similarity). Interacts with KCNT1 (By similarity).
CC Interacts with ILF2 (By similarity). {ECO:0000250|UniProtKB:Q56AP7,
CC ECO:0000250|UniProtKB:Q96SW2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96SW2}. Nucleus
CC {ECO:0000250|UniProtKB:Q96SW2}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C7D2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C7D2-2; Sequence=VSP_015210;
CC Name=3;
CC IsoId=Q8C7D2-3; Sequence=VSP_039063;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {ECO:0000269|PubMed:20131966}.
CC -!- DEVELOPMENTAL STAGE: In brain, expression is abundant in the
CC cerebellum, with less expression in the neocortical, hippocampus and
CC striatum in adult. Neocortical expression increases from embryonic
CC stages to adulthood. {ECO:0000269|PubMed:20131966}.
CC -!- DOMAIN: The CULT domain binds thalidomide and related drugs.
CC Thalidomide binding leads to a change in substrate specificity of the
CC human DCX (DDB1-CUL4-X-box) E3 protein ligase complex, while no such
CC change is observed in rodents. {ECO:0000269|PubMed:25108355}.
CC -!- PTM: Ubiquitinated, ubiquitination is mediated by its own DCX protein
CC ligase complex. {ECO:0000250|UniProtKB:Q96SW2}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype, however mice display
CC increased BK channel activity and a subsequent decrease in synaptic
CC transmission and presynaptic release probability in excitatory synapses
CC (PubMed:29530986). Mice also display cognitive behavioral defects such
CC as abnormal passive avoidance, hyperanxious behavior and decreased
CC preference for new objects (PubMed:29530986). Treatment with the BK
CC blocker paxilline rescues all synaptic and behavioral abnormalities
CC except for hyperanxiety (PubMed:29530986). Brain and synaptic
CC morphology is normal and long-term synaptic plasticity is not affected
CC (PubMed:29530986). Conditional knockout in the forebrain results in no
CC obvious phenotype, however mice display a deficit in contextual fear
CC learning whereas anxiety-like behavior is unaffected (PubMed:21995942).
CC {ECO:0000269|PubMed:21995942, ECO:0000269|PubMed:29530986}.
CC -!- SIMILARITY: Belongs to the CRBN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF35895.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK050557; BAC34322.1; -; mRNA.
DR EMBL; AK076144; BAC36214.1; -; mRNA.
DR EMBL; AK077707; BAC36970.1; -; mRNA.
DR EMBL; AK160219; BAE35697.1; -; mRNA.
DR EMBL; BC046967; AAH46967.1; -; mRNA.
DR EMBL; BC069905; AAH69905.1; -; mRNA.
DR EMBL; BC086488; AAH86488.1; -; mRNA.
DR EMBL; AF229032; AAF35895.1; ALT_FRAME; mRNA.
DR CCDS; CCDS39583.1; -. [Q8C7D2-1]
DR CCDS; CCDS39584.1; -. [Q8C7D2-3]
DR RefSeq; NP_067424.2; NM_021449.3. [Q8C7D2-3]
DR RefSeq; NP_780566.1; NM_175357.3. [Q8C7D2-1]
DR PDB; 3WX1; X-ray; 1.93 A; A/B=322-430.
DR PDB; 3WX2; X-ray; 2.00 A; A/B=322-430.
DR PDB; 4TZC; X-ray; 1.88 A; A/B/C/D=322-428.
DR PDB; 4TZU; X-ray; 2.00 A; A/B/C/D=322-429.
DR PDB; 5YIZ; X-ray; 2.00 A; A/D/G/J/M/P/S/V/Y/b/e/h/k/n/q/t=322-430.
DR PDB; 5YJ0; X-ray; 1.80 A; A/D/G/J/M/P/S/V/Y/b/e/h/k/n/q/t=322-430.
DR PDB; 5YJ1; X-ray; 2.00 A; A/D/G/J/M/P/S/V/Y/b/e/h/k/n/q/t=322-430.
DR PDBsum; 3WX1; -.
DR PDBsum; 3WX2; -.
DR PDBsum; 4TZC; -.
DR PDBsum; 4TZU; -.
DR PDBsum; 5YIZ; -.
DR PDBsum; 5YJ0; -.
DR PDBsum; 5YJ1; -.
DR AlphaFoldDB; Q8C7D2; -.
DR SMR; Q8C7D2; -.
DR BioGRID; 208437; 10.
DR STRING; 10090.ENSMUSP00000108865; -.
DR iPTMnet; Q8C7D2; -.
DR PhosphoSitePlus; Q8C7D2; -.
DR EPD; Q8C7D2; -.
DR MaxQB; Q8C7D2; -.
DR PaxDb; Q8C7D2; -.
DR PeptideAtlas; Q8C7D2; -.
DR PRIDE; Q8C7D2; -.
DR ProteomicsDB; 278031; -. [Q8C7D2-1]
DR ProteomicsDB; 278032; -. [Q8C7D2-2]
DR ProteomicsDB; 278033; -. [Q8C7D2-3]
DR Antibodypedia; 25089; 154 antibodies from 29 providers.
DR DNASU; 58799; -.
DR Ensembl; ENSMUST00000013882; ENSMUSP00000013882; ENSMUSG00000005362. [Q8C7D2-3]
DR Ensembl; ENSMUST00000113239; ENSMUSP00000108865; ENSMUSG00000005362. [Q8C7D2-1]
DR GeneID; 58799; -.
DR KEGG; mmu:58799; -.
DR UCSC; uc009dda.2; mouse. [Q8C7D2-3]
DR UCSC; uc009ddb.2; mouse. [Q8C7D2-1]
DR CTD; 51185; -.
DR MGI; MGI:1913277; Crbn.
DR VEuPathDB; HostDB:ENSMUSG00000005362; -.
DR eggNOG; KOG1400; Eukaryota.
DR GeneTree; ENSGT00390000016404; -.
DR HOGENOM; CLU_025648_1_1_1; -.
DR InParanoid; Q8C7D2; -.
DR OMA; DNMGNHL; -.
DR OrthoDB; 1069900at2759; -.
DR PhylomeDB; Q8C7D2; -.
DR TreeFam; TF106115; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 58799; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Crbn; mouse.
DR PRO; PR:Q8C7D2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8C7D2; protein.
DR Bgee; ENSMUSG00000005362; Expressed in pontine nuclear group and 252 other tissues.
DR ExpressionAtlas; Q8C7D2; baseline and differential.
DR Genevisible; Q8C7D2; MM.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:UniProtKB.
DR GO; GO:0034766; P:negative regulation of ion transmembrane transport; ISO:MGI.
DR GO; GO:1902607; P:negative regulation of large conductance calcium-activated potassium channel activity; IMP:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd15777; CRBN_C_like; 1.
DR Gene3D; 2.30.130.40; -; 1.
DR InterPro; IPR034750; CULT.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR004910; Yippee/Mis18/Cereblon.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR Pfam; PF03226; Yippee-Mis18; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS51788; CULT; 1.
DR PROSITE; PS51787; LON_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..445
FT /note="Protein cereblon"
FT /id="PRO_0000076161"
FT DOMAIN 84..320
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 321..429
FT /note="CULT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25108355"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25108355"
FT BINDING 381
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000269|PubMed:25108355"
FT BINDING 383
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000269|PubMed:25108355"
FT BINDING 389
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000269|PubMed:25108355"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25108355"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25108355"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT VAR_SEQ 1..23
FT /note="MAGEGDQQDAAHNMGNHLPLLPA -> MGNHLPLLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015210"
FT VAR_SEQ 23
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039063"
FT CONFLICT 10
FT /note="A -> R (in Ref. 3; AAF35895)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="N -> D (in Ref. 3; AAF35895)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="H -> P (in Ref. 1; BAC36214)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="Q -> R (in Ref. 3; AAF35895)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="A -> G (in Ref. 3; AAF35895)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="L -> V (in Ref. 2; AAH86488)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="R -> A (in Ref. 3; AAF35895)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="I -> V (in Ref. 1; BAC36970)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="D -> N (in Ref. 1; BAE35697)"
FT /evidence="ECO:0000305"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:5YJ0"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5YJ0"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:5YJ0"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:5YJ0"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:4TZC"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3WX1"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:5YJ0"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:5YJ0"
FT STRAND 387..394
FT /evidence="ECO:0007829|PDB:5YJ0"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:5YJ0"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:5YJ0"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:5YJ0"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:5YJ0"
SQ SEQUENCE 445 AA; 50880 MW; D66C2C3D50366E27 CRC64;
MAGEGDQQDA AHNMGNHLPL LPADSEDEDD EIEMEVEDQD SKEARKPNII NFDTSLPTSH
TYLGADMEEF HGRTLHDDDS CQVIPVLPEV LMILIPGQTL PLQLSHPQEV SMVRNLIQKD
RTFAVLAYSN VQEREAQFGT TAEIYAYREE QEFGIEVVKV KAIGRQRFKV LELRTQSDGI
QQAKVQILPE CVLPSTMSAV QLESLNKCQV FPSKPISWED QYSCKWWQKY QKRKFHCANL
TSWPRWLYSL YDAETLMDRI KKQLREWDEN LKDDSLPENP IDFSYRVAAC LPIDDVLRIQ
LLKIGSAIQR LRCELDIMNK CTSLCCKQCQ ETEITTKNEI FSLSLCGPMA AYVNPHGYVH
ETLTVYKASN LNLIGRPSTV HSWFPGYAWT IAQCKICASH IGWKFTATKK DMSPQKFWGL
TRSALLPTIP ETEDEISPDK VILCL
