ZN451_MOUSE
ID ZN451_MOUSE Reviewed; 1056 AA.
AC Q8C0P7;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=E3 SUMO-protein ligase ZNF451 {ECO:0000305|PubMed:26524493};
DE EC=2.3.2.- {ECO:0000269|PubMed:26524493};
DE AltName: Full=E3 SUMO-protein transferase ZNF451 {ECO:0000305};
DE AltName: Full=Zinc finger protein 451;
GN Name=Znf451; Synonyms=Zfp451;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26524493; DOI=10.1038/nsmb.3114;
RA Eisenhardt N., Chaugule V.K., Koidl S., Droescher M., Dogan E., Rettich J.,
RA Sutinen P., Imanishi S.Y., Hofmann K., Palvimo J.J., Pichler A.;
RT "A new vertebrate SUMO enzyme family reveals insights into SUMO-chain
RT assembly.";
RL Nat. Struct. Mol. Biol. 22:959-967(2015).
CC -!- FUNCTION: E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3
CC and facilitates UBE2I/UBC9-mediated sumoylation of target proteins.
CC Plays a role in protein SUMO2 modification in response to stress caused
CC by DNA damage and by proteasome inhibitors (in vitro). Required for
CC MCM4 sumoylation. Has no activity with SUMO1 (PubMed:26524493).
CC Preferentially transfers an additional SUMO2 chain onto the SUMO2
CC consensus site 'Lys-11'. Negatively regulates transcriptional
CC activation mediated by the SMAD4 complex in response to TGF-beta
CC signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-
CC 9'. Plays a role in regulating the transcription of AR targets (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y4E5,
CC ECO:0000269|PubMed:26524493}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000269|PubMed:26524493}.
CC -!- SUBUNIT: Homooligomer. Interacts (via N-terminal region) with SUMO1.
CC Interacts (via N-terminal region) with SUMO2. Interacts simultaneously
CC with two SUMO2 chains. Identified in a complex with SUMO2 and
CC UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two
CC SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to
CC another region of the same UBE2I/UBC9 molecule. Interacts (via C-
CC terminus) with ubiquitin. Interacts (via N-terminal zinc-finger
CC domains) with SMAD4 (via MH2 domain). Interacts with SMAD2 and SMAD3.
CC Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and
CC SMAD4. Interacts with EP300. Inhibits interaction between EP300 and the
CC SMAD4 complex. {ECO:0000250|UniProtKB:Q9Y4E5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y4E5}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:Q9Y4E5}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y4E5}. Note=Colocalizes with UBE2I/UBC9, SUMO1
CC and SUMO2 in nuclear granules; this probably requires sumoylation.
CC Desumoylation leads to diffuse nucleoplasmic location.
CC {ECO:0000250|UniProtKB:Q9Y4E5}.
CC -!- DOMAIN: Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus.
CC The most N-terminal region interacts with the SUMO2 chain that is
CC covalently bound to the UBE2I/UBC9 active site, while the second region
CC interacts with another SUMO2 that is non-covalently associated with the
CC same UBE2I/UBC9 chain. {ECO:0000250|UniProtKB:Q9Y4E5}.
CC -!- PTM: Sumoylated. Predominantly sumoylated on the N-terminal region that
CC is important for interaction with SUMO1 and SUMO2. Sumoylation is
CC important for localization in nuclear granules; desumoylation leads to
CC diffuse nucleoplasmic location. Autosumoylated (in vitro). Sumoylation
CC enhances E3 SUMO-protein ligase activity.
CC {ECO:0000250|UniProtKB:Q9Y4E5}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK030088; BAC26778.1; -; mRNA.
DR CCDS; CCDS14865.1; -.
DR RefSeq; NP_001277628.1; NM_001290699.1.
DR RefSeq; NP_598578.1; NM_133817.3.
DR AlphaFoldDB; Q8C0P7; -.
DR BioGRID; 221052; 4.
DR STRING; 10090.ENSMUSP00000019861; -.
DR iPTMnet; Q8C0P7; -.
DR PhosphoSitePlus; Q8C0P7; -.
DR EPD; Q8C0P7; -.
DR MaxQB; Q8C0P7; -.
DR PaxDb; Q8C0P7; -.
DR PRIDE; Q8C0P7; -.
DR ProteomicsDB; 275078; -.
DR Antibodypedia; 2845; 88 antibodies from 21 providers.
DR Ensembl; ENSMUST00000019861; ENSMUSP00000019861; ENSMUSG00000042197.
DR GeneID; 98403; -.
DR KEGG; mmu:98403; -.
DR UCSC; uc007anz.2; mouse.
DR CTD; 98403; -.
DR MGI; MGI:2137896; Zfp451.
DR VEuPathDB; HostDB:ENSMUSG00000042197; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00390000011354; -.
DR HOGENOM; CLU_010658_0_0_1; -.
DR InParanoid; Q8C0P7; -.
DR OMA; FACPACF; -.
DR OrthoDB; 148216at2759; -.
DR PhylomeDB; Q8C0P7; -.
DR TreeFam; TF331947; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 98403; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp451; mouse.
DR PRO; PR:Q8C0P7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C0P7; protein.
DR Bgee; ENSMUSG00000042197; Expressed in spermatid and 246 other tissues.
DR ExpressionAtlas; Q8C0P7; baseline and differential.
DR Genevisible; Q8C0P7; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061665; F:SUMO ligase activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; ISS:UniProtKB.
DR GO; GO:0060633; P:negative regulation of transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR041192; PIN_11.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF18479; PIN_11; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1056
FT /note="E3 SUMO-protein ligase ZNF451"
FT /id="PRO_0000047599"
FT ZN_FING 169..195
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..277
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 315..338
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..385
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..517
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 527..550
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 604..629
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..657
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 665..688
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 751..774
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 787..810
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..344
FT /note="Important for interaction with SUMO1 and SUMO2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT REGION 1..246
FT /note="Sufficient for E3 SUMO-protein ligase activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..37
FT /note="Interaction with SUMO2 1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT REGION 42..50
FT /note="Interaction with SUMO2 2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT REGION 168..521
FT /note="Important for interaction with SMAD4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT REGION 806..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1056
FT /note="Important for ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT MOTIF 38..41
FT /note="PLRP"
FT /evidence="ECO:0000305"
FT COMPBIAS 843..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT MOD_RES 158
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 431
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 729
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 746
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 788
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 815
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 843
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 849
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 947
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 988
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
FT CROSSLNK 989
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E5"
SQ SEQUENCE 1056 AA; 120070 MW; 7D8FBC0B50ECA622 CRC64;
MGDPGPEIIE SVPPAGPEAS ESTTDENEDD IQFVSEGPLR PVLEYIDLVS SDDEEPSTSH
SDENFKCKDY IDHQKDKVAL TLARLARHVE VEKQQKEEKN RAFREKIDFQ HAHGLQELEF
IQGHSETEAA RQCVDQWLKM PGLRTNAANS GTKRSFQRGG RMWRSEKPIL CPIMHCNKEF
DNGHLLLGHL KRFDHSPCDP TITLHGPLAN SFACAVCYEH FVTQQQYKDH LLSRTAAADG
HSNSLLPQII QCYACPQCFL LFSTKDECLK HMSTKNHFHQ SFKLSDNKGT ARPISFPSFA
KKRLVSLCKD VPFQVKCVAC HQTLRSHMEL TAHFRVRCQN AGPVAIAEKS ITQVAKEFIV
RGYCSDCNQV FMDVASTQSH KNSGHKITLA NSVEESVLLY CHISEGSRPP CDLHLFSQPK
ISSLKRILSV KESSAEDCIV PTKKVNLGVE SLGGATRVQR QSPAVTAWFC ECRRQFPSEE
AVEKHVFSAN TMCYKCVVCG KVCEDSGVMR LHMSRFHGGA HLNNFLFWCR TCKKELVKKD
AIMAHITEFH SGHRYFYEMD EVEEEEEEAM PSSSVESHLN TDKPPSPIAV VDHCPANSPP
RGRWQCRICE DMFESQECVK QHCMSLTSHR FHRYSCAHCR KTFHKVETLY RHCQDEHDSE
IMMKYFCGLC DLIFNKEEEF LSHYKEHHSI DYVFVSEKTK TSIKTEGDFK IVETSSLLSC
GCHESYMCKI NRKEDYDRCL PVLLEKGRLW FRCSSCSATA QNVTDINTHV CQVHRKEKSE
EEQQYVIKCG ICTKAFQNTE SAQQHFHRKH AALQKPTATP GGANRSSTCQ LAASASHAEK
NLKQPSSQKH SDVEKGAEHD VRCQNIEEEV ELPDVDYLRT MTHIVFVDFD NWSNFFGHLP
GHLNQGTFIW GFQGGNTNWK PPLSCKVYNY LSRIGCFFLH PRCSKRKDAA DFAICMHAGR
LDEQLPKQIP FTILSGDQGF LELENQFKKT QRPAHILNPH HLEGDMMCAL LNSISDTTKE
CDSDDSSGMK GSPAEELRAT EDVELEEAIR RSLEEM
