ID UBE2F_HUMAN Reviewed; 185 AA. AC Q969M7; A8K1Z8; B4DDT9; B4DFI1; B4DMK3; B4DZU2; B8ZZG2; C9J212; H9KVB9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 175. DE RecName: Full=NEDD8-conjugating enzyme UBE2F; DE EC=2.3.2.32 {ECO:0000269|PubMed:23201271}; DE AltName: Full=NEDD8 carrier protein UBE2F; DE AltName: Full=NEDD8 protein ligase UBE2F; DE AltName: Full=NEDD8-conjugating enzyme 2; DE AltName: Full=RING-type E3 NEDD8 transferase UBE2F; DE AltName: Full=Ubiquitin-conjugating enzyme E2 F; GN Name=UBE2F; Synonyms=NCE2; 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 [MRNA] (ISOFORM 1). RA Gladysheva T., Chau V.; RT "NEDD8-conjugating enzyme."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5). RC TISSUE=Brain, Brain cortex, Glial tumor, Substantia nigra, and Thymus; 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 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-185 IN COMPLEX WITH UBA3, RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH UBA3; NAE1 AND RBX2. RX PubMed=19250909; DOI=10.1016/j.molcel.2009.01.011; RA Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., RA Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.; RT "E2-RING expansion of the NEDD8 cascade confers specificity to cullin RT modification."; RL Mol. Cell 33:483-495(2009). RN [7] RP STRUCTURE BY NMR OF 23-185. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the UQ_CON domain from human NEDD8-conjugating RT enzyme NCE2."; RL Submitted (AUG-2007) to the PDB data bank. RN [8] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-25 IN COMPLEX WITH DCUN1D3, RP ACETYLATION AT MET-1, FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH RP DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5. 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). CC -!- FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 CC E1 complex and catalyzes its covalent attachment to other proteins. The CC specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, CC suggests that the RBX2-UBE2F complex neddylates specific target CC proteins, such as CUL5. {ECO:0000269|PubMed:19250909}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine CC + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + CC N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.; EC=2.3.2.32; CC Evidence={ECO:0000269|PubMed:23201271}; CC -!- PATHWAY: Protein modification; protein neddylation. CC -!- SUBUNIT: Interacts with UBA3 and RBX2 (PubMed:19250909). Interacts (N- CC terminally acetylated form) with (via DCUN1 domain) DCUN1D1, DCUN1D2, CC DCUN1D3, DCUN1D4 and DCUN1D5 (PubMed:23201271). CC {ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:23201271}. CC -!- INTERACTION: CC Q969M7; P62879: GNB2; NbExp=3; IntAct=EBI-1056876, EBI-356942; CC Q969M7; P80188: LCN2; NbExp=3; IntAct=EBI-1056876, EBI-11911016; CC Q969M7; P26367: PAX6; NbExp=3; IntAct=EBI-1056876, EBI-747278; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=Q969M7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q969M7-2; Sequence=VSP_037274; CC Name=3; CC IsoId=Q969M7-3; Sequence=VSP_037270; CC Name=4; CC IsoId=Q969M7-4; Sequence=VSP_037272, VSP_037273; CC Name=5; CC IsoId=Q969M7-5; Sequence=VSP_037271; CC Name=6; CC IsoId=Q969M7-6; Sequence=VSP_055750; CC Name=7; CC IsoId=Q969M7-7; Sequence=VSP_055749; CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). CC {ECO:0000269|PubMed:19250909}. CC -!- PTM: The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 CC orders of magnitude and is crucial for NEDD8 transfer to cullins. CC {ECO:0000269|PubMed:23201271}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBE2F CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}. 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; AF310723; AAL26792.1; -; mRNA. DR EMBL; AK290063; BAF82752.1; -; mRNA. DR EMBL; AK293334; BAG56850.1; -; mRNA. DR EMBL; AK294107; BAG57442.1; -; mRNA. DR EMBL; AK297502; BAG59915.1; -; mRNA. DR EMBL; AK303094; BAG64204.1; -; mRNA. DR EMBL; AC016776; AAY24220.1; -; Genomic_DNA. DR EMBL; CH471063; EAW71129.1; -; Genomic_DNA. DR EMBL; CH471063; EAW71132.1; -; Genomic_DNA. DR EMBL; BC010549; AAH10549.1; -; mRNA. DR CCDS; CCDS2523.1; -. [Q969M7-1] DR CCDS; CCDS63175.1; -. [Q969M7-7] DR CCDS; CCDS63176.1; -. [Q969M7-6] DR CCDS; CCDS63177.1; -. [Q969M7-3] DR RefSeq; NP_001265234.1; NM_001278305.1. [Q969M7-1] DR RefSeq; NP_001265235.1; NM_001278306.1. [Q969M7-7] DR RefSeq; NP_001265236.1; NM_001278307.1. [Q969M7-3] DR RefSeq; NP_001265237.1; NM_001278308.1. [Q969M7-6] DR RefSeq; NP_542409.1; NM_080678.2. [Q969M7-1] DR PDB; 2EDI; NMR; -; A=26-185. DR PDB; 3FN1; X-ray; 2.50 A; B=21-185. DR PDB; 4GBA; X-ray; 2.40 A; F/G=1-25. DR PDBsum; 2EDI; -. DR PDBsum; 3FN1; -. DR PDBsum; 4GBA; -. DR AlphaFoldDB; Q969M7; -. DR SMR; Q969M7; -. DR BioGRID; 126682; 25. DR ELM; Q969M7; -. DR IntAct; Q969M7; 9. DR STRING; 9606.ENSP00000478474; -. DR BindingDB; Q969M7; -. DR ChEMBL; CHEMBL4523422; -. DR iPTMnet; Q969M7; -. DR PhosphoSitePlus; Q969M7; -. DR BioMuta; UBE2F; -. DR DMDM; 74751725; -. DR EPD; Q969M7; -. DR jPOST; Q969M7; -. DR MassIVE; Q969M7; -. DR MaxQB; Q969M7; -. DR PaxDb; 9606-ENSP00000478474; -. DR PeptideAtlas; Q969M7; -. DR ProteomicsDB; 46263; -. DR ProteomicsDB; 75795; -. [Q969M7-1] DR ProteomicsDB; 75796; -. [Q969M7-2] DR ProteomicsDB; 75797; -. [Q969M7-3] DR ProteomicsDB; 75798; -. [Q969M7-4] DR ProteomicsDB; 75799; -. [Q969M7-5] DR ProteomicsDB; 8148; -. DR Pumba; Q969M7; -. DR Antibodypedia; 34487; 250 antibodies from 31 providers. DR DNASU; 140739; -. DR Ensembl; ENST00000272930.9; ENSP00000272930.4; ENSG00000184182.19. [Q969M7-1] DR Ensembl; ENST00000409633.5; ENSP00000387299.1; ENSG00000184182.19. [Q969M7-6] DR Ensembl; ENST00000409953.5; ENSP00000386680.1; ENSG00000184182.19. [Q969M7-7] DR Ensembl; ENST00000414443.5; ENSP00000399183.1; ENSG00000184182.19. [Q969M7-3] DR Ensembl; ENST00000433241.5; ENSP00000393515.1; ENSG00000184182.19. [Q969M7-4] DR Ensembl; ENST00000441728.6; ENSP00000409749.2; ENSG00000184182.19. [Q969M7-5] DR Ensembl; ENST00000612130.4; ENSP00000478474.1; ENSG00000184182.19. [Q969M7-1] DR GeneID; 140739; -. DR KEGG; hsa:140739; -. DR MANE-Select; ENST00000272930.9; ENSP00000272930.4; NM_080678.3; NP_542409.1. DR UCSC; uc002vxk.4; human. [Q969M7-1] DR AGR; HGNC:12480; -. DR DisGeNET; 140739; -. DR GeneCards; UBE2F; -. DR HGNC; HGNC:12480; UBE2F. DR HPA; ENSG00000184182; Low tissue specificity. DR MIM; 617700; gene. DR neXtProt; NX_Q969M7; -. DR OpenTargets; ENSG00000184182; -. DR PharmGKB; PA37130; -. DR VEuPathDB; HostDB:ENSG00000184182; -. DR eggNOG; KOG0420; Eukaryota. DR GeneTree; ENSGT00940000154349; -. DR InParanoid; Q969M7; -. DR OMA; GMGWAPT; -. DR OrthoDB; 46085at2759; -. DR PhylomeDB; Q969M7; -. DR TreeFam; TF101125; -. DR BRENDA; 2.3.2.34; 2681. DR PathwayCommons; Q969M7; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q969M7; -. DR SIGNOR; Q969M7; -. DR UniPathway; UPA00885; -. DR BioGRID-ORCS; 140739; 61 hits in 1170 CRISPR screens. DR EvolutionaryTrace; Q969M7; -. DR GenomeRNAi; 140739; -. DR Pharos; Q969M7; Tbio. DR PRO; PR:Q969M7; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q969M7; Protein. DR Bgee; ENSG00000184182; Expressed in body of pancreas and 189 other cell types or tissues. DR ExpressionAtlas; Q969M7; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061654; F:NEDD8 conjugating enzyme activity; IDA:UniProtKB. DR GO; GO:0061663; F:NEDD8 ligase activity; IEA:UniProtKB-EC. DR GO; GO:0019788; F:NEDD8 transferase activity; IBA:GO_Central. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0045116; P:protein neddylation; IDA:UniProtKB. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24067:SF261; NEDD8-CONJUGATING ENZYME UBC-12; 1. DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS00183; UBC_1; 1. DR PROSITE; PS50127; UBC_2; 1. DR Genevisible; Q969M7; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Nucleotide-binding; Reference proteome; Transferase; KW Ubl conjugation pathway. FT CHAIN 1..185 FT /note="NEDD8-conjugating enzyme UBE2F" FT /id="PRO_0000263077" FT DOMAIN 32..185 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT REGION 1..29 FT /note="Interaction with UBA3" FT /evidence="ECO:0000269|PubMed:19250909" FT ACT_SITE 116 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:23201271" FT VAR_SEQ 1..39 FT /note="MLTLASKLKRDDGLKGSRTAATASDSTRRVSVRDKLLVK -> MVLGAGPAS FT PVSGSP (in isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_055749" FT VAR_SEQ 40..71 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037270" FT VAR_SEQ 72..185 FT /note="DEGYYQGGKFQFETEVPDAYNMVPPKVKCLTKIWHPNITETGEICLSLLREH FT SIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKEDFRNKVDDYIKR FT YAR -> ASQSEMPDQDLAPQHHRDRGNMSEFIERTFN (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037271" FT VAR_SEQ 118..120 FT /note="SLL -> RIF (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037272" FT VAR_SEQ 121..185 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037273" FT VAR_SEQ 149..169 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_055750" FT VAR_SEQ 170..185 FT /note="EDFRNKVDDYIKRYAR -> SPMLLLHRRTSGIKWMTTSNVMPDNKRGRLQA FT HGLCYSLSLT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037274" FT CONFLICT 181 FT /note="K -> E (in Ref. 2; BAF82752)" FT /evidence="ECO:0000305" FT HELIX 4..8 FT /evidence="ECO:0007829|PDB:4GBA" FT HELIX 32..44 FT /evidence="ECO:0007829|PDB:3FN1" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:3FN1" FT TURN 75..78 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:2EDI" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:3FN1" FT HELIX 136..145 FT /evidence="ECO:0007829|PDB:3FN1" FT TURN 146..150 FT /evidence="ECO:0007829|PDB:3FN1" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:3FN1" FT HELIX 159..167 FT /evidence="ECO:0007829|PDB:3FN1" FT HELIX 169..183 FT /evidence="ECO:0007829|PDB:3FN1" SQ SEQUENCE 185 AA; 21077 MW; B22C86238D13216E CRC64; MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC TCKVHFPDPN KLHCFQLTVT PDEGYYQGGK FQFETEVPDA YNMVPPKVKC LTKIWHPNIT ETGEICLSLL REHSIDGTGW APTRTLKDVV WGLNSLFTDL LNFDDPLNIE AAEHHLRDKE DFRNKVDDYI KRYAR //