ID DCAF5_HUMAN Reviewed; 942 AA. AC Q96JK2; B2RN31; G3V4J7; O60559; Q8N3V3; Q8N3V5; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 2. DT 02-OCT-2024, entry version 184. DE RecName: Full=DDB1- and CUL4-associated factor 5; DE AltName: Full=Breakpoint cluster region protein 2; DE Short=BCRP2; DE AltName: Full=WD repeat-containing protein 22; GN Name=DCAF5; Synonyms=BCRG2, KIAA1824, WDR22; 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=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skeletal muscle; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 262-942, AND TISSUE SPECIFICITY. RC TISSUE=Uterine leiomyoma; RX PubMed=9740667; DOI=10.1006/geno.1998.5406; RA Lynch R.A., Piper M., Bankier A., Bhugra B., Surti U., Liu J., Buckler A., RA Dear P.H., Menon A.G.; RT "Genomic and functional map of the chromosome 14 t(12;14) breakpoint RT cluster region in uterine leiomyoma."; RL Genomics 52:17-26(1998). RN [6] RP FUNCTION, INTERACTION WITH DDB1 AND CUL4A, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010; RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.; RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is RT required for S phase destruction of the replication factor Cdt1."; RL Mol. Cell 23:709-721(2006). RN [7] RP FUNCTION. RX PubMed=16964240; DOI=10.1038/nature05175; RA Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.; RT "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase RT machinery."; RL Nature 443:590-593(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648 AND SER-651, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-648 AND SER-794, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP FUNCTION, AND INTERACTION WITH DDB1; CUL4B; DNMT1 AND L3MBTL3. RX PubMed=29691401; DOI=10.1038/s41467-018-04019-9; RA Leng F., Yu J., Zhang C., Alejo S., Hoang N., Sun H., Lu F., Zhang H.; RT "Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3 and RT CRL4-DCAF5 ubiquitin ligase."; RL Nat. Commun. 9:1641-1641(2018). RN [13] RP FUNCTION. RX PubMed=30442713; DOI=10.1074/jbc.ra118.005336; RA Zhang C., Leng F., Saxena L., Hoang N., Yu J., Alejo S., Lee L., Qi D., RA Lu F., Sun H., Zhang H.; RT "Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and CRL4- RT DCAF5 ubiquitin ligase."; RL J. Biol. Chem. 294:476-489(2019). CC -!- FUNCTION: Is a substrate receptor for the CUL4-DDB1 E3 ubiquitin- CC protein ligase complex (CRL4) (PubMed:29691401, PubMed:30442713). The CC complex CRL4-DCAF5 is involved in the ubiquitination of a set of CC methylated non-histone proteins, including SOX2, DNMT1 and E2F1 CC (PubMed:29691401, PubMed:30442713). {ECO:0000269|PubMed:16949367, CC ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:29691401, CC ECO:0000269|PubMed:30442713}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with DDB1, CUL4A or CUL4B (PubMed:29691401). CC Interacts with L3MBTL3 (PubMed:29691401). Interacts with DNMT1 CC (PubMed:29691401). Interacts with E2F1 (PubMed:29691401). Interacts CC with SOX2 (By similarity). {ECO:0000250|UniProtKB:Q80T85, CC ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:29691401}. CC -!- INTERACTION: CC Q96JK2; Q16531: DDB1; NbExp=2; IntAct=EBI-3253159, EBI-350322; CC Q96JK2; P26358: DNMT1; NbExp=5; IntAct=EBI-3253159, EBI-719459; CC Q96JK2; Q96JM7: L3MBTL3; NbExp=4; IntAct=EBI-3253159, EBI-2686809; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96JK2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96JK2-2; Sequence=VSP_010386; CC Name=3; CC IsoId=Q96JK2-3; Sequence=VSP_055647; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9740667}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC08965.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB47453.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB058727; BAB47453.1; ALT_INIT; mRNA. DR EMBL; AL391262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL831932; CAD38589.1; -; mRNA. DR EMBL; AL831823; CAD38537.2; -; mRNA. DR EMBL; CH471061; EAW80981.1; -; Genomic_DNA. DR EMBL; CH471061; EAW80983.1; -; Genomic_DNA. DR EMBL; BC136632; AAI36633.1; -; mRNA. DR EMBL; AF044774; AAC08965.1; ALT_FRAME; mRNA. DR CCDS; CCDS32106.1; -. [Q96JK2-1] DR CCDS; CCDS61480.1; -. [Q96JK2-2] DR CCDS; CCDS61481.1; -. [Q96JK2-3] DR RefSeq; NP_001271135.1; NM_001284206.1. [Q96JK2-3] DR RefSeq; NP_001271136.1; NM_001284207.1. [Q96JK2-2] DR RefSeq; NP_003852.1; NM_003861.2. [Q96JK2-1] DR RefSeq; XP_016877223.1; XM_017021734.1. DR RefSeq; XP_016877224.1; XM_017021735.1. DR PDB; 3I89; X-ray; 3.00 A; B=13-25. DR PDB; 8TL6; EM; 2.63 A; B=1-942. DR PDBsum; 3I89; -. DR PDBsum; 8TL6; -. DR AlphaFoldDB; Q96JK2; -. DR EMDB; EMD-41363; -. DR SMR; Q96JK2; -. DR BioGRID; 114343; 98. DR ComplexPortal; CPX-2782; CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2783; CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4B variant. DR DIP; DIP-48763N; -. DR IntAct; Q96JK2; 74. DR MINT; Q96JK2; -. DR STRING; 9606.ENSP00000341351; -. DR iPTMnet; Q96JK2; -. DR PhosphoSitePlus; Q96JK2; -. DR BioMuta; DCAF5; -. DR DMDM; 47606200; -. DR jPOST; Q96JK2; -. DR MassIVE; Q96JK2; -. DR PaxDb; 9606-ENSP00000341351; -. DR PeptideAtlas; Q96JK2; -. DR ProteomicsDB; 33252; -. DR ProteomicsDB; 76975; -. [Q96JK2-1] DR ProteomicsDB; 76976; -. [Q96JK2-2] DR Pumba; Q96JK2; -. DR Antibodypedia; 54896; 20 antibodies from 10 providers. DR DNASU; 8816; -. DR Ensembl; ENST00000341516.10; ENSP00000341351.5; ENSG00000139990.18. [Q96JK2-1] DR Ensembl; ENST00000554215.5; ENSP00000451551.1; ENSG00000139990.18. [Q96JK2-2] DR Ensembl; ENST00000556847.5; ENSP00000452052.1; ENSG00000139990.18. [Q96JK2-2] DR Ensembl; ENST00000557386.5; ENSP00000451845.1; ENSG00000139990.18. [Q96JK2-3] DR GeneID; 8816; -. DR KEGG; hsa:8816; -. DR MANE-Select; ENST00000341516.10; ENSP00000341351.5; NM_003861.3; NP_003852.1. DR UCSC; uc001xkp.4; human. [Q96JK2-1] DR AGR; HGNC:20224; -. DR CTD; 8816; -. DR DisGeNET; 8816; -. DR GeneCards; DCAF5; -. DR HGNC; HGNC:20224; DCAF5. DR HPA; ENSG00000139990; Low tissue specificity. DR MIM; 603812; gene. DR neXtProt; NX_Q96JK2; -. DR OpenTargets; ENSG00000139990; -. DR PharmGKB; PA165478844; -. DR VEuPathDB; HostDB:ENSG00000139990; -. DR eggNOG; KOG4227; Eukaryota. DR GeneTree; ENSGT00950000182900; -. DR HOGENOM; CLU_018663_0_0_1; -. DR InParanoid; Q96JK2; -. DR OMA; DENTCET; -. DR OrthoDB; 2968013at2759; -. DR PhylomeDB; Q96JK2; -. DR TreeFam; TF320710; -. DR PathwayCommons; Q96JK2; -. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; Q96JK2; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 8816; 24 hits in 1196 CRISPR screens. DR ChiTaRS; DCAF5; human. DR EvolutionaryTrace; Q96JK2; -. DR GenomeRNAi; 8816; -. DR Pharos; Q96JK2; Tdark. DR PRO; PR:Q96JK2; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q96JK2; protein. DR Bgee; ENSG00000139990; Expressed in secondary oocyte and 184 other cell types or tissues. DR ExpressionAtlas; Q96JK2; baseline and differential. DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IBA:GO_Central. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3. DR InterPro; IPR045151; DCAF8. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR15574:SF43; DDB1- AND CUL4-ASSOCIATED FACTOR 5; 1. DR PANTHER; PTHR15574; WD REPEAT DOMAIN-CONTAINING FAMILY; 1. DR Pfam; PF00400; WD40; 4. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; KW Ubl conjugation pathway; WD repeat. FT CHAIN 1..942 FT /note="DDB1- and CUL4-associated factor 5" FT /id="PRO_0000051369" FT REPEAT 51..91 FT /note="WD 1" FT REPEAT 99..139 FT /note="WD 2" FT REPEAT 140..180 FT /note="WD 3" FT REPEAT 185..225 FT /note="WD 4" FT REPEAT 277..317 FT /note="WD 5" FT REPEAT 331..370 FT /note="WD 6" FT REGION 449..478 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 490..509 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 544..655 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 676..824 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 889..942 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 449..469 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 554..568 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 570..599 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 621..651 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 699..714 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 756..774 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..815 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 897..911 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 914..942 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 500 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q80T85" FT MOD_RES 531 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80T85" FT MOD_RES 533 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80T85" FT MOD_RES 626 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80T85" FT MOD_RES 628 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80T85" FT MOD_RES 645 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 648 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 794 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..82 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_010386" FT VAR_SEQ 132 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_055647" FT CONFLICT 149 FT /note="S -> F (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 404 FT /note="Y -> H (in Ref. 5; AAC08965)" FT /evidence="ECO:0000305" FT CONFLICT 607 FT /note="N -> D (in Ref. 5; AAC08965)" FT /evidence="ECO:0000305" FT CONFLICT 836..841 FT /note="RLHPRP -> TLHLS (in Ref. 5; AAC08965)" FT /evidence="ECO:0000305" FT HELIX 14..24 FT /evidence="ECO:0007829|PDB:8TL6" FT HELIX 29..39 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:8TL6" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 78..82 FT /evidence="ECO:0007829|PDB:8TL6" FT HELIX 83..87 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 106..109 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 121..129 FT /evidence="ECO:0007829|PDB:8TL6" FT TURN 130..133 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:8TL6" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 202..207 FT /evidence="ECO:0007829|PDB:8TL6" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 247..251 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:8TL6" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 266..272 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:8TL6" FT TURN 289..292 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 294..298 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 304..308 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 336..342 FT /evidence="ECO:0007829|PDB:8TL6" FT TURN 343..346 FT /evidence="ECO:0007829|PDB:8TL6" FT STRAND 347..363 FT /evidence="ECO:0007829|PDB:8TL6" SQ SEQUENCE 942 AA; 103963 MW; 3C627BA3FB2DC522 CRC64; MKRRAGLGGS MRSVVGFLSQ RGLHGDPLLT QDFQRRRLRG CRNLYKKDLL GHFGCVNAIE FSNNGGQWLV SGGDDRRVLL WHMEQAIHSR VKPIQLKGEH HSNIFCLAFN SGNTKVFSGG NDEQVILHDV ESSETLDVFA HEDAVYGLSV SPVNDNIFAS SSDDGRVLIW DIRESPHGEP FCLANYPSAF HSVMFNPVEP RLLATANSKE GVGLWDIRKP QSSLLRYGGN LSLQSAMSVR FNSNGTQLLA LRRRLPPVLY DIHSRLPVFQ FDNQGYFNSC TMKSCCFAGD RDQYILSGSD DFNLYMWRIP ADPEAGGIGR VVNGAFMVLK GHRSIVNQVR FNPHTYMICS SGVEKIIKIW SPYKQPGCTG DLDGRIEDDS RCLYTHEEYI SLVLNSGSGL SHDYANQSVQ EDPRMMAFFD SLVRREIEGW SSDSDSDLSE STILQLHAGV SERSGYTDSE SSASLPRSPP PTVDESADNA FHLGPLRVTT TNTVASTPPT PTCEDAASRQ QRLSALRRYQ DKRLLALSNE SDSEENVCEV ELDTDLFPRP RSPSPEDESS SSSSSSSSED EEELNERRAS TWQRNAMRRR QKTTREDKPS APIKPTNTYI GEDNYDYPQI KVDDLSSSPT SSPERSTSTL EIQPSRASPT SDIESVERKI YKAYKWLRYS YISYSNNKDG ETSLVTGEAD EGRAGTSHKD NPAPSSSKEA CLNIAMAQRN QDLPPEGCSK DTFKEETPRT PSNGPGHEHS SHAWAEVPEG TSQDTGNSGS VEHPFETKKL NGKALSSRAE EPPSPPVPKA SGSTLNSGSG NCPRTQSDDS EERSLETICA NHNNGRLHPR PPHPHNNGQN LGELEVVAYS SPGHSDTDRD NSSLTGTLLH KDCCGSEMAC ETPNAGTRED PTDTPATDSS RAVHGHSGLK RQRIELEDTD SENSSSEKKL KT //