DCNL4_HUMAN
ID DCNL4_HUMAN Reviewed; 292 AA.
AC Q92564; B4DH25; Q7Z3F3; Q7Z6B8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DCN1-like protein 4 {ECO:0000305};
DE Short=DCNL4 {ECO:0000303|PubMed:23201271};
DE AltName: Full=DCUN1 domain-containing protein 4;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 4;
GN Name=DCUN1D4 {ECO:0000312|HGNC:HGNC:28998}; Synonyms=KIAA0276;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP DOMAIN, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B; CUL5; UBE2F AND
RP UBE2M, AND FUNCTION.
RX PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
RA Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
RA Bennett E.J., Schulman B.A.;
RT "Structural conservation of distinctive N-terminal acetylation-dependent
RT interactions across a family of mammalian NEDD8 ligation enzymes.";
RL Structure 21:42-53(2013).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP INTERACTION WITH CUL1; CUL2; CUL3; CUL5; CAND; RNF7 AND RBX1, SUBCELLULAR
RP LOCATION, FUNCTION, AND MUTAGENESIS OF ASP-250; ALA-274 AND ASP-280.
RX PubMed=26906416; DOI=10.1242/jcs.181784;
RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
RL J. Cell Sci. 129:1441-1454(2016).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [11] {ECO:0007744|PDB:5V89}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 102-292 IN COMPLEX WITH CUL1.
RX PubMed=28581483; DOI=10.1038/nchembio.2386;
RA Scott D.C., Hammill J.T., Min J., Rhee D.Y., Connelly M., Sviderskiy V.O.,
RA Bhasin D., Chen Y., Ong S.S., Chai S.C., Goktug A.N., Huang G., Monda J.K.,
RA Low J., Kim H.S., Paulo J.A., Cannon J.R., Shelat A.A., Chen T.,
RA Kelsall I.R., Alpi A.F., Pagala V., Wang X., Peng J., Singh B.,
RA Harper J.W., Schulman B.A., Guy R.K.;
RT "Blocking an N-terminal acetylation-dependent protein interaction inhibits
RT an E3 ligase.";
RL Nat. Chem. Biol. 13:850-857(2017).
CC -!- FUNCTION: Contributes to the neddylation of all cullins by transferring
CC NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to
CC different cullin C-terminal domain-RBX complexes which are necessary
CC for the activation of cullin-RING E3 ubiquitin ligases (CRLs).
CC {ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:26906416}.
CC -!- SUBUNIT: Interacts (via the DCUN1 domain) with the unneddylated
CC cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these
CC interactions promote the cullin neddylation and the identity of the
CC cullin dictates the affinity of the interaction (PubMed:26906416,
CC PubMed:23201271). Interacts with RBX1 and RNF7 (PubMed:26906416).
CC Interacts with CAND1; this interaction is bridged by cullins such as
CC CUL3 and strongly inhibits the neddylation of CUL3. These CAND-cullin-
CC DCNL complexes can only be neddylated in the presence of a substrate
CC adapter (PubMed:26906416). Interacts (via DCUN1 domain) with UBE2M (N-
CC terminally acetylated form) and probably with UBE2F (N-terminally
CC acetylated form) (PubMed:23201271). {ECO:0000269|PubMed:23201271,
CC ECO:0000269|PubMed:26906416}.
CC -!- INTERACTION:
CC Q92564; PRO_0000037946 [P29991]; Xeno; NbExp=3; IntAct=EBI-2654610, EBI-8826488;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26906416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92564-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92564-2; Sequence=VSP_016016;
CC Name=3;
CC IsoId=Q92564-3; Sequence=VSP_054381;
CC -!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates the
CC interaction with different cullins (PubMed:23201271). The DCUN1 domain
CC mediates the interaction with the N-terminally acetylated NEDD8-
CC conjugating E2s enzyme leading to the NEDD8 transfer from N-terminally
CC acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal
CC domain-RBX complexes; the neddylation efficiency correlates with the
CC DCUN1D5-cullin and DCUN1D5-E2 interaction affinities (PubMed:23201271).
CC {ECO:0000269|PubMed:23201271}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD97912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D87466; BAA13405.1; ALT_INIT; mRNA.
DR EMBL; AK294894; BAG57986.1; -; mRNA.
DR EMBL; BX537944; CAD97912.1; ALT_INIT; mRNA.
DR EMBL; AC027271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053897; AAH53897.2; -; mRNA.
DR CCDS; CCDS33982.1; -. [Q92564-1]
DR CCDS; CCDS3487.2; -. [Q92564-2]
DR CCDS; CCDS75123.1; -. [Q92564-3]
DR RefSeq; NP_001035492.1; NM_001040402.2. [Q92564-1]
DR RefSeq; NP_001274684.1; NM_001287755.1. [Q92564-3]
DR RefSeq; NP_001274686.1; NM_001287757.1.
DR RefSeq; NP_055930.2; NM_015115.3. [Q92564-2]
DR PDB; 5V89; X-ray; 1.55 A; A=102-292.
DR PDBsum; 5V89; -.
DR AlphaFoldDB; Q92564; -.
DR SMR; Q92564; -.
DR BioGRID; 116759; 23.
DR IntAct; Q92564; 4.
DR STRING; 9606.ENSP00000389900; -.
DR BindingDB; Q92564; -.
DR ChEMBL; CHEMBL4295914; -.
DR iPTMnet; Q92564; -.
DR PhosphoSitePlus; Q92564; -.
DR BioMuta; DCUN1D4; -.
DR DMDM; 78099237; -.
DR EPD; Q92564; -.
DR jPOST; Q92564; -.
DR MassIVE; Q92564; -.
DR MaxQB; Q92564; -.
DR PaxDb; Q92564; -.
DR PeptideAtlas; Q92564; -.
DR PRIDE; Q92564; -.
DR ProteomicsDB; 4184; -.
DR ProteomicsDB; 75320; -. [Q92564-1]
DR ProteomicsDB; 75321; -. [Q92564-2]
DR Antibodypedia; 23882; 110 antibodies from 17 providers.
DR DNASU; 23142; -.
DR Ensembl; ENST00000334635.10; ENSP00000334625.5; ENSG00000109184.15. [Q92564-1]
DR Ensembl; ENST00000381441.7; ENSP00000370850.3; ENSG00000109184.15. [Q92564-2]
DR Ensembl; ENST00000451288.6; ENSP00000389900.2; ENSG00000109184.15. [Q92564-3]
DR GeneID; 23142; -.
DR KEGG; hsa:23142; -.
DR MANE-Select; ENST00000334635.10; ENSP00000334625.5; NM_001040402.3; NP_001035492.1.
DR UCSC; uc003gze.5; human. [Q92564-1]
DR CTD; 23142; -.
DR DisGeNET; 23142; -.
DR GeneCards; DCUN1D4; -.
DR HGNC; HGNC:28998; DCUN1D4.
DR HPA; ENSG00000109184; Low tissue specificity.
DR MIM; 612977; gene.
DR neXtProt; NX_Q92564; -.
DR OpenTargets; ENSG00000109184; -.
DR PharmGKB; PA142672010; -.
DR VEuPathDB; HostDB:ENSG00000109184; -.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000156935; -.
DR HOGENOM; CLU_047042_3_1_1; -.
DR InParanoid; Q92564; -.
DR OMA; DEELAWP; -.
DR OrthoDB; 1418097at2759; -.
DR PhylomeDB; Q92564; -.
DR TreeFam; TF354270; -.
DR PathwayCommons; Q92564; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q92564; -.
DR BioGRID-ORCS; 23142; 16 hits in 1078 CRISPR screens.
DR ChiTaRS; DCUN1D4; human.
DR GeneWiki; DCUN1D4; -.
DR GenomeRNAi; 23142; -.
DR Pharos; Q92564; Tchem.
DR PRO; PR:Q92564; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q92564; protein.
DR Bgee; ENSG00000109184; Expressed in calcaneal tendon and 198 other tissues.
DR ExpressionAtlas; Q92564; baseline and differential.
DR Genevisible; Q92564; HS.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IMP:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR GO; GO:2000436; P:positive regulation of protein neddylation; IMP:UniProtKB.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR Gene3D; 1.10.238.200; -; 1.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR042460; DCN1-like_PONY.
DR InterPro; IPR005176; PONY_dom.
DR PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..292
FT /note="DCN1-like protein 4"
FT /id="PRO_0000129503"
FT DOMAIN 101..287
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT REGION 43..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..9
FT /note="MHSDAAAVN -> MEVEAALGCSGQGRGCGGVAPAGRGRERASERGTRVRIS
FT KGLSGAGGSVRKAD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054381"
FT VAR_SEQ 206..240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016016"
FT MUTAGEN 250
FT /note="D->A: Does not affect localization at nucleus; when
FT associated with R-274 and A-280."
FT /evidence="ECO:0000269|PubMed:26906416"
FT MUTAGEN 274
FT /note="A->R: Does not affect localization at nucleus; when
FT associated with A-250 and A-280."
FT /evidence="ECO:0000269|PubMed:26906416"
FT MUTAGEN 280
FT /note="D->A: Does not affect localization at nucleus; when
FT associated with A-250 and R-274."
FT /evidence="ECO:0000269|PubMed:26906416"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:5V89"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:5V89"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:5V89"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:5V89"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:5V89"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5V89"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:5V89"
SQ SEQUENCE 292 AA; 34068 MW; 1927AA612E075E9C CRC64;
MHSDAAAVNF QLNSHLSTLA NIHKIYHTLN KLNLTEDIGQ DDHQTGSLRS CSSSDCFNKV
MPPRKKRRPA SGDDLSAKKS RHDSMYRKYD STRIKTEEEA FSSKRCLEWF YEYAGTDDVV
GPEGMEKFCE DIGVEPENVV MLVLAWKLDA QNMGYFTLQE WLKGMTSLQC DTTEKLRNTL
DYLRSFLNDS TNFKLIYRYA FDFAREKDQR SLDINTAKCM LGLLLGKIWP LFPVFHQFLE
QSKYKVINKD QWCNVLEFSR TINLDLSNYD EDGAWPVLLD EFVEWYKDKQ MS
