UB2L6_HUMAN
ID UB2L6_HUMAN Reviewed; 153 AA.
AC O14933; A6NDM6; A8MY53; Q8N5D8; Q9UEZ0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Ubiquitin/ISG15-conjugating enzyme E2 L6;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme L6;
DE AltName: Full=Retinoic acid-induced gene B protein;
DE Short=RIG-B;
DE AltName: Full=UbcH8;
DE AltName: Full=Ubiquitin carrier protein L6;
DE AltName: Full=Ubiquitin-protein ligase L6;
GN Name=UBE2L6; Synonyms=UBCH8;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=10894956; DOI=10.1159/000015593;
RA Ardley H.C., Rose S.A., Tan N., Leek J.P., Markham A.F., Robinson P.A.;
RT "Genomic organization of the human ubiquitin-conjugating enzyme gene,
RT UBE2L6 on chromosome 11q12.";
RL Cytogenet. Cell Genet. 89:137-140(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu T., Mao M., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y.,
RA Wang Z., Chen S., Chen Z.;
RT "Human retinoic acid induced gene B (RIG-B) mRNA.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-153 (ISOFORM 1).
RX PubMed=9153201; DOI=10.1074/jbc.272.21.13548;
RA Kumar S., Kao W.H., Howley P.M.;
RT "Physical interaction between specific E2 and Hect E3 enzymes determines
RT functional cooperativity.";
RL J. Biol. Chem. 272:13548-13554(1997).
RN [10]
RP PROTEIN SEQUENCE OF 140-146, FUNCTION IN ISG15 ATTACHMENT, AND INDUCTION BY
RP IFNB1.
RX PubMed=15131269; DOI=10.1073/pnas.0402528101;
RA Zhao C., Beaudenon S.L., Kelley M.L., Waddell M.B., Yuan W., Schulman B.A.,
RA Huibregtse J.M., Krug R.M.;
RT "The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-
RT alpha/beta-induced ubiquitin-like protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7578-7582(2004).
RN [11]
RP INTERACTION WITH RNF19A.
RX PubMed=11237715; DOI=10.1006/bbrc.2001.4414;
RA Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.;
RT "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase
RT activity.";
RL Biochem. Biophys. Res. Commun. 281:706-713(2001).
RN [12]
RP FUNCTION, AND ISGYLATION.
RX PubMed=16428300; DOI=10.1093/jb/mvi172;
RA Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.;
RT "Link between the ubiquitin conjugation system and the ISG15 conjugation
RT system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme.";
RL J. Biochem. 138:711-719(2005).
RN [13]
RP INTERACTION WITH RNF144B.
RX PubMed=16427630; DOI=10.1016/j.febslet.2005.09.105;
RA Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.;
RT "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent
RT apoptosis.";
RL FEBS Lett. 580:940-947(2006).
RN [14]
RP INTERACTION WITH RNF19B, AND TISSUE SPECIFICITY.
RX PubMed=16709802; DOI=10.4049/jimmunol.176.11.6454;
RA Fortier J.M., Kornbluth J.;
RT "NK lytic-associated molecule, involved in NK cytotoxic function, is an E3
RT ligase.";
RL J. Immunol. 176:6454-6463(2006).
RN [15]
RP FUNCTION IN UBIQUITINATION OF FLT3, AND INTERACTION WITH FLT3.
RX PubMed=20508617; DOI=10.1038/leu.2010.114;
RA Buchwald M., Pietschmann K., Muller J.P., Bohmer F.D., Heinzel T.,
RA Kramer O.H.;
RT "Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for
RT proteasomal degradation.";
RL Leukemia 24:1412-1421(2010).
RN [16]
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 [17]
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 [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-153.
RA Mizushima T., Suzuki M., Teshima N., Yamane T., Murata S., Tanaka K.;
RT "Crystal structure of Ubch8.";
RL Submitted (MAR-2005) to the PDB data bank.
RN [19]
RP STRUCTURE BY NMR IN COMPLEX WITH UBIQUITIN.
RX PubMed=19928833; DOI=10.1021/bi901686j;
RA Serniwka S.A., Shaw G.S.;
RT "The structure of the UbcH8-ubiquitin complex shows a unique ubiquitin
RT interaction site.";
RL Biochemistry 48:12169-12179(2009).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15 to
CC other proteins. Functions in the E6/E6-AP-induced ubiquitination of
CC p53/TP53. Promotes ubiquitination and subsequent proteasomal
CC degradation of FLT3. {ECO:0000269|PubMed:15131269,
CC ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20508617}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with RNF19A, RNF19B and RNF144B. Interacts with FLT3
CC (tyrosine phosphorylated). {ECO:0000269|PubMed:11237715,
CC ECO:0000269|PubMed:16427630, ECO:0000269|PubMed:16709802,
CC ECO:0000269|PubMed:19928833, ECO:0000269|PubMed:20508617}.
CC -!- INTERACTION:
CC O14933; O95376: ARIH2; NbExp=13; IntAct=EBI-2129974, EBI-711158;
CC O14933; Q8N9I9: DTX3; NbExp=6; IntAct=EBI-2129974, EBI-2340258;
CC O14933; P62879: GNB2; NbExp=3; IntAct=EBI-2129974, EBI-356942;
CC O14933; Q99732: LITAF; NbExp=3; IntAct=EBI-2129974, EBI-725647;
CC O14933; Q17RB8: LONRF1; NbExp=7; IntAct=EBI-2129974, EBI-2341787;
CC O14933; O15344: MID1; NbExp=3; IntAct=EBI-2129974, EBI-2340316;
CC O14933; Q9BYM8: RBCK1; NbExp=7; IntAct=EBI-2129974, EBI-2340624;
CC O14933; Q7Z419: RNF144B; NbExp=4; IntAct=EBI-2129974, EBI-2129982;
CC O14933; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-2129974, EBI-2466594;
CC O14933; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-2129974, EBI-723313;
CC O14933; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-2129974, EBI-6929619;
CC O14933; Q9BZR9: TRIM8; NbExp=4; IntAct=EBI-2129974, EBI-2340370;
CC O14933; Q99PZ6: ospG; Xeno; NbExp=2; IntAct=EBI-2129974, EBI-9316527;
CC O14933; Q8CJB9: Rnf40; Xeno; NbExp=2; IntAct=EBI-2129974, EBI-6110162;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14933-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14933-2; Sequence=VSP_037344;
CC -!- TISSUE SPECIFICITY: Present in natural killer cells (at protein level).
CC {ECO:0000269|PubMed:16709802}.
CC -!- INDUCTION: By IFNB1/IFN-beta. {ECO:0000269|PubMed:15131269}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16428300}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB64566.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ243268; CAB64566.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ243269; CAB64566.1; JOINED; Genomic_DNA.
DR EMBL; AJ243270; CAB64566.1; JOINED; Genomic_DNA.
DR EMBL; AJ243271; CAB64566.1; JOINED; Genomic_DNA.
DR EMBL; AF061736; AAD17525.1; -; mRNA.
DR EMBL; AK315755; BAG38109.1; -; mRNA.
DR EMBL; CR457126; CAG33407.1; -; mRNA.
DR EMBL; AK226165; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AP002893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73757.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW73759.1; -; Genomic_DNA.
DR EMBL; BC032491; AAH32491.1; -; mRNA.
DR EMBL; AF031141; AAB86433.1; -; mRNA.
DR CCDS; CCDS7960.1; -. [O14933-1]
DR CCDS; CCDS7961.1; -. [O14933-2]
DR RefSeq; NP_004214.1; NM_004223.4. [O14933-1]
DR RefSeq; NP_937826.1; NM_198183.2. [O14933-2]
DR PDB; 1WZV; X-ray; 2.10 A; A/B=2-153.
DR PDB; 1WZW; X-ray; 2.40 A; A=2-153.
DR PDB; 2KJH; NMR; -; A=2-153.
DR PDBsum; 1WZV; -.
DR PDBsum; 1WZW; -.
DR PDBsum; 2KJH; -.
DR AlphaFoldDB; O14933; -.
DR BMRB; O14933; -.
DR SMR; O14933; -.
DR BioGRID; 114672; 110.
DR DIP; DIP-41477N; -.
DR IntAct; O14933; 35.
DR MINT; O14933; -.
DR STRING; 9606.ENSP00000287156; -.
DR iPTMnet; O14933; -.
DR MetOSite; O14933; -.
DR PhosphoSitePlus; O14933; -.
DR SwissPalm; O14933; -.
DR BioMuta; UBE2L6; -.
DR EPD; O14933; -.
DR jPOST; O14933; -.
DR MassIVE; O14933; -.
DR MaxQB; O14933; -.
DR PaxDb; O14933; -.
DR PeptideAtlas; O14933; -.
DR PRIDE; O14933; -.
DR ProteomicsDB; 48316; -. [O14933-1]
DR ProteomicsDB; 48317; -. [O14933-2]
DR Antibodypedia; 1142; 361 antibodies from 34 providers.
DR CPTC; O14933; 3 antibodies.
DR DNASU; 9246; -.
DR Ensembl; ENST00000287156.9; ENSP00000287156.4; ENSG00000156587.16. [O14933-1]
DR Ensembl; ENST00000340573.8; ENSP00000341980.4; ENSG00000156587.16. [O14933-2]
DR GeneID; 9246; -.
DR KEGG; hsa:9246; -.
DR MANE-Select; ENST00000287156.9; ENSP00000287156.4; NM_004223.5; NP_004214.1.
DR UCSC; uc001nkn.3; human. [O14933-1]
DR CTD; 9246; -.
DR DisGeNET; 9246; -.
DR GeneCards; UBE2L6; -.
DR HGNC; HGNC:12490; UBE2L6.
DR HPA; ENSG00000156587; Low tissue specificity.
DR MIM; 603890; gene.
DR neXtProt; NX_O14933; -.
DR OpenTargets; ENSG00000156587; -.
DR PharmGKB; PA37139; -.
DR VEuPathDB; HostDB:ENSG00000156587; -.
DR eggNOG; KOG0422; Eukaryota.
DR GeneTree; ENSGT00940000161981; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; O14933; -.
DR OMA; RPNLEEP; -.
DR OrthoDB; 1420213at2759; -.
DR PhylomeDB; O14933; -.
DR TreeFam; TF313043; -.
DR BRENDA; 2.3.2.23; 2681.
DR PathwayCommons; O14933; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O14933; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9246; 18 hits in 1089 CRISPR screens.
DR ChiTaRS; UBE2L6; human.
DR EvolutionaryTrace; O14933; -.
DR GeneWiki; UBE2L6; -.
DR GenomeRNAi; 9246; -.
DR Pharos; O14933; Tbio.
DR PRO; PR:O14933; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O14933; protein.
DR Bgee; ENSG00000156587; Expressed in granulocyte and 200 other tissues.
DR ExpressionAtlas; O14933; baseline and differential.
DR Genevisible; O14933; HS.
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:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0042296; F:ISG15 transferase activity; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; EXP:Reactome.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:ProtInc.
DR GO; GO:0032020; P:ISG15-protein conjugation; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; Alternative splicing; Direct protein sequencing;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..153
FT /note="Ubiquitin/ISG15-conjugating enzyme E2 L6"
FT /id="PRO_0000082478"
FT DOMAIN 2..149
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 86
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_037344"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:1WZV"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1WZV"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1WZV"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1WZV"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1WZV"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:1WZV"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1WZV"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2KJH"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1WZV"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1WZV"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:1WZV"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1WZV"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1WZV"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:1WZV"
SQ SEQUENCE 153 AA; 17769 MW; D79768775344EFAE CRC64;
MMASMRVVKE LEDLQKKPPP YLRNLSSDDA NVLVWHALLL PDQPPYHLKA FNLRISFPPE
YPFKPPMIKF TTKIYHPNVD ENGQICLPII SSENWKPCTK TCQVLEALNV LVNRPNIREP
LRMDLADLLT QNPELFRKNA EEFTLRFGVD RPS
