UBE2F_HUMAN
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 03-AUG-2022, entry version 167.
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}.
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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; 22.
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; Q969M7; -.
DR PeptideAtlas; Q969M7; -.
DR PRIDE; 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 Antibodypedia; 34487; 222 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 CTD; 140739; -.
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; YNMAPPK; -.
DR OrthoDB; 1302735at2759; -.
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; 49 hits in 1092 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 187 other tissues.
DR ExpressionAtlas; Q969M7; baseline and differential.
DR Genevisible; Q969M7; HS.
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: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; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
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
