ID UBC12_HUMAN Reviewed; 183 AA. AC P61081; O76069; Q8VC50; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 1. DT 27-MAR-2024, entry version 186. DE RecName: Full=NEDD8-conjugating enzyme Ubc12; DE EC=2.3.2.34 {ECO:0000269|PubMed:15361859}; DE AltName: Full=NEDD8 carrier protein; DE AltName: Full=Ubiquitin-conjugating enzyme E2 M; GN Name=UBE2M; Synonyms=UBC12; 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]. RX PubMed=9694792; DOI=10.1101/gad.12.15.2263; RA Osaka F., Kawasaki H., Aida N., Saeki M., Chiba T., Kawashima S., RA Tanaka K., Kato S.; RT "A new NEDD8-ligating system for cullin-4A."; RL Genes Dev. 12:2263-2268(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Placenta; RX PubMed=10207026; DOI=10.1074/jbc.274.17.12036; RA Gong L., Yeh E.T.H.; RT "Identification of the activating and conjugating enzymes of the NEDD8 RT conjugation pathway."; RL J. Biol. Chem. 274:12036-12042(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 MUTAGENESIS OF CYS-111. RX PubMed=10828074; DOI=10.1074/jbc.275.22.17008; RA Wada H., Yeh E.T.H., Kamitani T.; RT "A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 RT conjugation in vivo."; RL J. Biol. Chem. 275:17008-17015(2000). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP INTERACTION WITH RBX1. 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(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 INTERACTION WITH DCUN1D5. RX PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252; RA Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M., RA Goenen M., Ghossein R., Ramanathan S.Y., Singh B.; RT "Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity RT and nuclear localization."; RL Clin. Cancer Res. 20:372-381(2014). RN [11] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-169, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP INTERACTION WITH DCUN1D1. 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). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-26 IN COMPLEX WITH UBA3 AND RP NAE1, MUTAGENESIS OF MET-1; LEU-4; PHE-5; SER-6; LEU-7; GLN-9; GLN-10; RP LYS-11 AND LYS-12, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15361859; DOI=10.1038/nsmb826; RA Huang D.T., Miller D.W., Mathew R., Cassell R., Holton J.M., Roussel M.F., RA Schulman B.A.; RT "A unique E1-E2 interaction required for optimal conjugation of the RT ubiquitin-like protein NEDD8."; RL Nat. Struct. Mol. Biol. 11:927-935(2004). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 27-183 IN COMPLEX WITH UBA3 AND RP NAE1, AND MUTAGENESIS OF LEU-32; GLN-35; LYS-36; ILE-38; ASN-39; LEU-41; RP PHE-51; ASP-55 AND LEU-57. RX PubMed=15694336; DOI=10.1016/j.molcel.2004.12.020; RA Huang D.T., Paydar A., Zhuang M., Waddell M.B., Holton J.M., Schulman B.A.; RT "Structural basis for recruitment of Ubc12 by an E2 binding domain in RT NEDD8's E1."; RL Mol. Cell 17:341-350(2005). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-15 IN COMPLEX WITH CUL1 AND RP DCUN1D1, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-12 IN COMPLEX WITH CUL1 RP AND DCUN1D1, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=21940857; DOI=10.1126/science.1209307; RA Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.; RT "N-terminal acetylation acts as an avidity enhancer within an RT interconnected multiprotein complex."; RL Science 334:674-678(2011). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.28 ANGSTROMS) OF 1-12 IN COMPLEX WITH DCUN1D2, RP ACETYLATION AT MET-1, AND INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; RP 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 RBX1, but not RBX2, CC suggests that the RBX1-UBE2M complex neddylates specific target CC proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell CC proliferation. {ECO:0000269|PubMed:10207026, CC ECO:0000269|PubMed:15361859}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine + CC [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating CC enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]- CC yl-L-cysteine.; EC=2.3.2.34; Evidence={ECO:0000269|PubMed:15361859}; CC -!- PATHWAY: Protein modification; protein neddylation. CC -!- SUBUNIT: Interacts with UBA3 and RBX1. Interacts (N-terminally CC acetylated form) with (via DCUN1 domain) DCUN1D1, DCUN1D2, DCUN1D3, CC DCUN1D4 and DCUN1D5 (PubMed:23201271, PubMed:28581483). CC {ECO:0000269|PubMed:15361859, ECO:0000269|PubMed:15694336, CC ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:21940857, CC ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:28581483}. CC -!- INTERACTION: CC P61081; Q13616: CUL1; NbExp=5; IntAct=EBI-1041660, EBI-359390; CC P61081; Q96GG9: DCUN1D1; NbExp=4; IntAct=EBI-1041660, EBI-740086; CC P61081; P62879: GNB2; NbExp=3; IntAct=EBI-1041660, EBI-356942; CC P61081; Q15843: NEDD8; NbExp=8; IntAct=EBI-1041660, EBI-716247; CC P61081; O60260-5: PRKN; NbExp=3; IntAct=EBI-1041660, EBI-21251460; CC P61081; P62877: RBX1; NbExp=7; IntAct=EBI-1041660, EBI-398523; CC P61081; Q8TBC4: UBA3; NbExp=2; IntAct=EBI-1041660, EBI-717567; CC -!- DOMAIN: Both the N-terminal docking peptide and the catalytic core CC domain must bind the UBA3-NAE1 complex simultaneously for optimal CC transfer of NEDD8. CC -!- PTM: The acetylation of Met-1 increases affinity for DCUN1D1 by about 2 CC orders of magnitude and is crucial for NEDD8 transfer to cullins. CC {ECO:0000269|PubMed:21940857, ECO:0000269|PubMed:23201271}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBC12 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; AB012191; BAA33145.1; -; mRNA. DR EMBL; AF075599; AAC26141.1; -; mRNA. DR EMBL; BT006754; AAP35400.1; -; mRNA. DR EMBL; BC058924; AAH58924.1; -; mRNA. DR CCDS; CCDS12987.1; -. DR RefSeq; NP_003960.1; NM_003969.3. DR PDB; 1TT5; X-ray; 2.60 A; E/F=1-26. DR PDB; 1Y8X; X-ray; 2.40 A; A=27-183. DR PDB; 2NVU; X-ray; 2.80 A; C=1-178. DR PDB; 3TDU; X-ray; 1.50 A; E/F=1-15. DR PDB; 3TDZ; X-ray; 2.00 A; E/F=2-12. DR PDB; 4GAO; X-ray; 3.28 A; C/E/F/H=1-12. DR PDB; 4P5O; X-ray; 3.11 A; G/I=2-183. DR PDBsum; 1TT5; -. DR PDBsum; 1Y8X; -. DR PDBsum; 2NVU; -. DR PDBsum; 3TDU; -. DR PDBsum; 3TDZ; -. DR PDBsum; 4GAO; -. DR PDBsum; 4P5O; -. DR AlphaFoldDB; P61081; -. DR SMR; P61081; -. DR BioGRID; 114504; 637. DR DIP; DIP-35679N; -. DR IntAct; P61081; 68. DR MINT; P61081; -. DR STRING; 9606.ENSP00000253023; -. DR BindingDB; P61081; -. DR ChEMBL; CHEMBL4295787; -. DR GlyGen; P61081; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61081; -. DR PhosphoSitePlus; P61081; -. DR SwissPalm; P61081; -. DR BioMuta; UBE2M; -. DR DMDM; 46577655; -. DR REPRODUCTION-2DPAGE; IPI00022597; -. DR EPD; P61081; -. DR jPOST; P61081; -. DR MassIVE; P61081; -. DR MaxQB; P61081; -. DR PaxDb; 9606-ENSP00000253023; -. DR PeptideAtlas; P61081; -. DR ProteomicsDB; 57261; -. DR Pumba; P61081; -. DR Antibodypedia; 3333; 230 antibodies from 34 providers. DR DNASU; 9040; -. DR Ensembl; ENST00000253023.8; ENSP00000253023.2; ENSG00000130725.8. DR GeneID; 9040; -. DR KEGG; hsa:9040; -. DR MANE-Select; ENST00000253023.8; ENSP00000253023.2; NM_003969.4; NP_003960.1. DR UCSC; uc002qtl.5; human. DR AGR; HGNC:12491; -. DR CTD; 9040; -. DR DisGeNET; 9040; -. DR GeneCards; UBE2M; -. DR HGNC; HGNC:12491; UBE2M. DR HPA; ENSG00000130725; Low tissue specificity. DR MIM; 603173; gene. DR neXtProt; NX_P61081; -. DR OpenTargets; ENSG00000130725; -. DR PharmGKB; PA37140; -. DR VEuPathDB; HostDB:ENSG00000130725; -. DR eggNOG; KOG0420; Eukaryota. DR GeneTree; ENSGT00940000162814; -. DR HOGENOM; CLU_030988_6_0_1; -. DR InParanoid; P61081; -. DR OMA; GYPHDAP; -. DR OrthoDB; 46085at2759; -. DR PhylomeDB; P61081; -. DR TreeFam; TF101125; -. DR BioCyc; MetaCyc:HS05432-MONOMER; -. DR BRENDA; 2.3.2.34; 2681. DR PathwayCommons; P61081; -. DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; P61081; -. DR SIGNOR; P61081; -. DR UniPathway; UPA00885; -. DR BioGRID-ORCS; 9040; 764 hits in 1130 CRISPR screens. DR ChiTaRS; UBE2M; human. DR EvolutionaryTrace; P61081; -. DR GeneWiki; UBE2M; -. DR GenomeRNAi; 9040; -. DR Pharos; P61081; Tchem. DR PRO; PR:P61081; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P61081; Protein. DR Bgee; ENSG00000130725; Expressed in right frontal lobe and 186 other cell types or tissues. DR ExpressionAtlas; P61081; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; 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; IEA:UniProtKB-EC. DR GO; GO:0019788; F:NEDD8 transferase activity; IDA:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0036211; P:protein modification process; IMP:UniProtKB. 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 UCD-2DPAGE; P61081; -. DR Genevisible; P61081; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Methylation; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway. FT CHAIN 1..183 FT /note="NEDD8-conjugating enzyme Ubc12" FT /id="PRO_0000082488" FT DOMAIN 29..173 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT REGION 1..57 FT /note="Interaction with UBA3" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 111 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:21940857, FT ECO:0000269|PubMed:23201271" FT MOD_RES 3 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 169 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P61082" FT MOD_RES 169 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MUTAGEN 1 FT /note="M->A: No effect on thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 4 FT /note="L->A: Impairs thioester intermediate formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 5 FT /note="F->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 6 FT /note="S->A: Slightly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 7 FT /note="L->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 9 FT /note="Q->A: Impairs thioester intermediate formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 10 FT /note="Q->A: No effect on thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 11 FT /note="K->A: No effect on thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 12 FT /note="K->A: Impairs thioester intermediate formation." FT /evidence="ECO:0000269|PubMed:15361859" FT MUTAGEN 32 FT /note="L->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 35 FT /note="Q->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 36 FT /note="K->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 38 FT /note="I->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 39 FT /note="N->A: No effect on thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 41 FT /note="L->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 51 FT /note="F->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 55 FT /note="D->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 57 FT /note="L->A: Strongly impairs thioester intermediate FT formation." FT /evidence="ECO:0000269|PubMed:15694336" FT MUTAGEN 111 FT /note="C->S: Forms a stable complex with NEDD8, which FT prevents subsequent NEDD8 conjugation to cullins." FT /evidence="ECO:0000269|PubMed:10828074" FT HELIX 4..14 FT /evidence="ECO:0007829|PDB:3TDU" FT HELIX 29..39 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:1Y8X" FT TURN 70..73 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:1Y8X" FT TURN 84..88 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:2NVU" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:1Y8X" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:1Y8X" FT HELIX 125..137 FT /evidence="ECO:0007829|PDB:1Y8X" FT HELIX 147..154 FT /evidence="ECO:0007829|PDB:1Y8X" FT HELIX 157..169 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:1Y8X" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:1Y8X" SQ SEQUENCE 183 AA; 20900 MW; E3C288CA6A98BC5C CRC64; MIKLFSLKQQ KKEEESAGGT KGSSKKASAA QLRIQKDINE LNLPKTCDIS FSDPDDLLNF KLVICPDEGF YKSGKFVFSF KVGQGYPHDP PKVKCETMVY HPNIDLEGNV CLNILREDWK PVLTINSIIY GLQYLFLEPN PEDPLNKEAA EVLQNNRRLF EQNVQRSMRG GYIGSTYFER CLK //