TR30A_MOUSE
ID TR30A_MOUSE Reviewed; 496 AA.
AC P15533; Q3UV85; Q3UZ29; Q99K55; Q99PQ7; Q99PQ8; Q99PQ9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Tripartite motif-containing protein 30A;
DE AltName: Full=Down regulatory protein of interleukin-2 receptor;
DE AltName: Full=Tripartite motif-containing protein 30;
GN Name=Trim30a; Synonyms=Rpt-1, Rpt1, Trim30;
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 ALPHA).
RX PubMed=2965815; DOI=10.1073/pnas.85.8.2733;
RA Patarca R., Schwartz J., Singh R.P., Kong Q.-T., Murphy E., Anderson Y.,
RA Sheng F.-Y.W., Singh P., Johnson K.A., Guarnagia S.M., Durfee T.,
RA Blattner F., Cantor H.;
RT "rpt-1, an intracellular protein from helper/inducer T cells that regulates
RT gene expression of interleukin 2 receptor and human immunodeficiency virus
RT type 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2733-2737(1988).
RN [2]
RP ERRATUM OF PUBMED:2965815.
RA Patarca R., Schwartz J., Singh R.P., Kong Q.-T., Murphy E., Anderson Y.,
RA Sheng F.-Y.W., Singh P., Johnson K.A., Guarnagia S.M., Durfee T.,
RA Blattner F., Cantor H.;
RL Proc. Natl. Acad. Sci. U.S.A. 85:5224-5224(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ALPHA AND BETA),
RP HOMOMULTIMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC STRAIN=C57BL/6J; TISSUE=Bone, 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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC STRAIN=Czech II; TISSUE=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 [8]
RP FUNCTION, INTERACTION WITH NR2C2; TAB2 AND TAB3, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF CYS-35.
RX PubMed=18345001; DOI=10.1038/ni1577;
RA Shi M., Deng W., Bi E., Mao K., Ji Y., Lin G., Wu X., Tao Z., Li Z.,
RA Cai X., Sun S., Xiang C., Sun B.;
RT "TRIM30 alpha negatively regulates TLR-mediated NF-kappa B activation by
RT targeting TAB2 and TAB3 for degradation.";
RL Nat. Immunol. 9:369-377(2008).
RN [9]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=19147168; DOI=10.1016/j.virol.2008.12.018;
RA Tareen S.U., Sawyer S.L., Malik H.S., Emerman M.;
RT "An expanded clade of rodent Trim5 genes.";
RL Virology 385:473-483(2009).
RN [10]
RP FUNCTION, INTERACTION WITH NR2C2, AND MUTAGENESIS OF CYS-35.
RX PubMed=21048113; DOI=10.4049/jimmunol.1001099;
RA Hu Y., Mao K., Zeng Y., Chen S., Tao Z., Yang C., Sun S., Wu X., Meng G.,
RA Sun B.;
RT "Tripartite-motif protein 30 negatively regulates NLRP3 inflammasome
RT activation by modulating reactive oxygen species production.";
RL J. Immunol. 185:7699-7705(2010).
RN [11]
RP STRUCTURE BY NMR OF 1-78.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the zinc finger, C3HC4 type (RING finger) domain
RT tripartite motif protein 30.";
RL Submitted (FEB-2008) to the PDB data bank.
CC -!- FUNCTION: Trans-acting factor that regulates gene expression of
CC interleukin 2 receptor alpha chain. May affect IL2R-alpha expression
CC through cis-acting negative regulatory elements or through competition
CC with proteins that bind to enhancer or activator sequences. Negatively
CC regulates Toll-like receptor (TLR)-mediated activation of NFKB by
CC promoting degradation of TAB2 and TAB3 and preventing TRAF6
CC autoubiquitination. Negatively regulates production of reactive oxygen
CC species (ROS) which inhibits activation of the NLRP3 inflammasome
CC complex. This, in turn, regulates activation of CASP1 and subsequent
CC cleavage of IL1B and IL18. No activity detected against a range of
CC retroviruses including a number of lentiviruses, gammaretroviruses and
CC betaretroviruses. {ECO:0000269|PubMed:18345001,
CC ECO:0000269|PubMed:19147168, ECO:0000269|PubMed:21048113}.
CC -!- SUBUNIT: Homomultimer. Interacts with NR2C2/TAK1, TAB2 and TAB3. Does
CC not interact with NLRP3, NLRC4 or TAB1. {ECO:0000269|PubMed:18345001,
CC ECO:0000269|PubMed:21048113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=P15533-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P15533-2; Sequence=VSP_005762, VSP_005763;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and lymph nodes (at
CC protein level). {ECO:0000269|PubMed:18345001}.
CC -!- INDUCTION: By the TLR ligands lipopolysaccharide, CpG dinucleotide and
CC polyinosinic-polycytidylic acid. {ECO:0000269|PubMed:18345001}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40073.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG53470.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J03776; AAA40073.1; ALT_FRAME; mRNA.
DR EMBL; AF220014; AAG53468.1; -; mRNA.
DR EMBL; AF220015; AAG53469.1; -; mRNA.
DR EMBL; AF220016; AAG53470.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK134144; BAE22032.1; -; mRNA.
DR EMBL; AK137506; BAE23387.1; -; mRNA.
DR EMBL; AC122400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC142110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL16725.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL16726.1; -; Genomic_DNA.
DR EMBL; BC005447; AAH05447.1; -; mRNA.
DR CCDS; CCDS40068.1; -. [P15533-1]
DR PIR; A30891; A30891.
DR RefSeq; NP_033125.2; NM_009099.2. [P15533-1]
DR RefSeq; XP_006507534.1; XM_006507471.2.
DR PDB; 2ECW; NMR; -; A=1-78.
DR PDBsum; 2ECW; -.
DR AlphaFoldDB; P15533; -.
DR BMRB; P15533; -.
DR SMR; P15533; -.
DR BioGRID; 203018; 7.
DR IntAct; P15533; 2.
DR STRING; 10090.ENSMUSP00000076189; -.
DR iPTMnet; P15533; -.
DR PhosphoSitePlus; P15533; -.
DR EPD; P15533; -.
DR jPOST; P15533; -.
DR MaxQB; P15533; -.
DR PaxDb; P15533; -.
DR PRIDE; P15533; -.
DR ProteomicsDB; 297517; -. [P15533-1]
DR ProteomicsDB; 297518; -. [P15533-2]
DR DNASU; 20128; -.
DR Ensembl; ENSMUST00000076922; ENSMUSP00000076189; ENSMUSG00000030921. [P15533-1]
DR GeneID; 20128; -.
DR KEGG; mmu:20128; -.
DR UCSC; uc009iwh.1; mouse. [P15533-1]
DR UCSC; uc009iwi.1; mouse. [P15533-2]
DR CTD; 20128; -.
DR MGI; MGI:98178; Trim30a.
DR VEuPathDB; HostDB:ENSMUSG00000030921; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154647; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; P15533; -.
DR OMA; KVNICAQ; -.
DR OrthoDB; 1110108at2759; -.
DR PhylomeDB; P15533; -.
DR TreeFam; TF342569; -.
DR BioGRID-ORCS; 20128; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Trim30a; mouse.
DR EvolutionaryTrace; P15533; -.
DR PRO; PR:P15533; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P15533; protein.
DR Bgee; ENSMUSG00000030921; Expressed in peripheral lymph node and 174 other tissues.
DR Genevisible; P15533; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:1990462; C:omegasome; ISO:MGI.
DR GO; GO:0000932; C:P-body; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IMP:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IMP:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..496
FT /note="Tripartite motif-containing protein 30A"
FT /id="PRO_0000056244"
FT DOMAIN 281..496
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..59
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 91..132
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 205..210
FT /note="Highly hydrophilic"
FT COILED 173..239
FT /evidence="ECO:0000255"
FT MOTIF 268..276
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 145..151
FT /note="GALWKLM -> SLHHTEL (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005762"
FT VAR_SEQ 152..496
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005763"
FT MUTAGEN 35
FT /note="C->S: Reduced interaction with NR2C2 and enhanced
FT interaction with TAB2 and TAB3. Does not decrease TAB2 or
FT TAB3 expression. No effect on inhibition of ROS or negative
FT regulation of NLRP3 inflammasome activation."
FT /evidence="ECO:0000269|PubMed:18345001,
FT ECO:0000269|PubMed:21048113"
FT CONFLICT 68
FT /note="R -> K (in Ref. 7; AAH05447)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="W -> R (in Ref. 7; AAH05447)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="E -> Q (in Ref. 7; AAH05447)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="T -> S (in Ref. 7; AAH05447)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="K -> N (in Ref. 7; AAH05447)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="R -> C (in Ref. 7; AAH05447)"
FT /evidence="ECO:0000305"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:2ECW"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2ECW"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2ECW"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2ECW"
SQ SEQUENCE 496 AA; 57330 MW; 66502B93BDC3A1D2 CRC64;
MASSVLEMIK EEVTCPICLE LLKEPVSADC NHSFCRACIT LNYESNRNTD GKGNCPVCRV
PYPFGNLRPN LHVANIVERL KGFKSIPEEE QKVNICAQHG EKLRLFCRKD MMVICWLCER
SQEHRGHQTA LIEEVDQEYK EKLQGALWKL MKKAKICDEW QDDLQLQRVD WENQIQINVE
NVQRQFKGLR DLLDSKENEE LQKLKKEKKE VMEKLEESEN ELEDQTELVR DLISDVEHHL
ELSTLEMLQG ANCVLRRSQS LSLQQPQTVP QKRKRTFQAP DLKGMLQVYQ GLMDIQQYWV
HMTLHARNNA VIAINKEKRQ IQYRSYNTVP VSEIYHLGVL GYPALSSGKH YWEVDISRSD
AWLLGLNDGK CAQPQLHSKE EMGIKKNLHS QIKQNVLFQP KCGYWVIGMK NPSVYKAFDE
CSITHNSSIL VISLPDRPSR VGVFLDRKAG TLSFYDVSNC GALIYRFYDP AFPVEVYPYF
NPMKCSEPMT ICGPPS
