UB2G2_HUMAN
ID UB2G2_HUMAN Reviewed; 165 AA.
AC P60604; A6NMQ7; A8K3L4; D3DSL7; P56554;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 G2;
DE EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
DE AltName: Full=E2 ubiquitin-conjugating enzyme G2;
DE AltName: Full=Ubiquitin carrier protein G2;
DE AltName: Full=Ubiquitin-protein ligase G2;
GN Name=UBE2G2 {ECO:0000312|HGNC:HGNC:12483};
GN Synonyms=UBC7 {ECO:0000303|PubMed:23223569};
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).
RX PubMed=9693041; DOI=10.1006/geno.1998.5263;
RA Katsanis N., Fisher E.M.C.;
RT "Identification, expression, and chromosomal localization of ubiquitin
RT conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces
RT cerevisiae UBC7 gene.";
RL Genomics 51:128-131(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
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 GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [8]
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 [9]
RP INTERACTION WITH AUP1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=21127063; DOI=10.1074/jbc.m110.190785;
RA Spandl J., Lohmann D., Kuerschner L., Moessinger C., Thiele C.;
RT "Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds
RT the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region.";
RL J. Biol. Chem. 286:5599-5606(2011).
RN [10]
RP INTERACTION WITH AUP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21857022; DOI=10.1074/jbc.m111.284794;
RA Klemm E.J., Spooner E., Ploegh H.L.;
RT "Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet
RT accumulation and endoplasmic reticulum (ER) protein quality control.";
RL J. Biol. Chem. 286:37602-37614(2011).
RN [11]
RP FUNCTION IN ERAD PATHWAY.
RX PubMed=22607976; DOI=10.1016/j.molcel.2012.04.015;
RA Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H.,
RA Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T.,
RA Morino-Koga S., Wada I., Kai H.;
RT "STT3B-dependent posttranslational N-glycosylation as a surveillance system
RT for secretory protein.";
RL Mol. Cell 47:99-110(2012).
RN [12]
RP FUNCTION, INTERACTION WITH AUP1; AMFR AND RNF139, AND SUBCELLULAR LOCATION.
RX PubMed=23223569; DOI=10.1091/mbc.e12-07-0564;
RA Jo Y., Hartman I.Z., DeBose-Boyd R.A.;
RT "Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-
RT hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated
RT endoplasmic reticulum membranes.";
RL Mol. Biol. Cell 24:169-183(2013).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS).
RX PubMed=16582478; DOI=10.1107/s1744309106009006;
RA Arai R., Yoshikawa S., Murayama K., Imai Y., Takahashi R., Shirouzu M.,
RA Yokoyama S.;
RT "Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7).";
RL Acta Crystallogr. F 62:330-334(2006).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins (PubMed:20061386). In vitro
CC catalyzes 'Lys-48'-linked polyubiquitination (PubMed:20061386).
CC Involved in endoplasmic reticulum-associated degradation (ERAD)
CC (PubMed:22607976). Required for sterol-induced ubiquitination of 3-
CC hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent
CC proteasomal degradation (PubMed:23223569).
CC {ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:22607976,
CC ECO:0000269|PubMed:23223569}.
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, ECO:0000269|PubMed:20061386};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with AUP1 (via C-terminus); the interaction recruits
CC UBE2G2 to lipid droplets (PubMed:21127063, PubMed:21857022,
CC PubMed:23223569). Interacts with ubiquitin ligases AMFR/gp78 and
CC RNF139/TRC8; recruitment to lipid droplets by AUP1 facilitates
CC interaction of UBE2G2 with AMFR and RNF139, leading to sterol-induced
CC ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase and
CC its subsequent proteasomal degradation (PubMed:23223569).
CC {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022,
CC ECO:0000269|PubMed:23223569}.
CC -!- INTERACTION:
CC P60604; Q9UKV5: AMFR; NbExp=21; IntAct=EBI-1051028, EBI-1046367;
CC P60604; Q9Y679: AUP1; NbExp=6; IntAct=EBI-1051028, EBI-1058701;
CC P60604; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-1051028, EBI-9090282;
CC P60604; P0CG48: UBC; NbExp=3; IntAct=EBI-1051028, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:23223569}. Lipid droplet
CC {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:23223569}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60604-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60604-2; Sequence=VSP_046260;
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {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; AF032456; AAC32312.1; -; mRNA.
DR EMBL; BT006914; AAP35560.1; -; mRNA.
DR EMBL; AK290629; BAF83318.1; -; mRNA.
DR EMBL; AL163300; CAB90551.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09395.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09397.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09398.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09399.1; -; Genomic_DNA.
DR EMBL; BC001738; AAH01738.1; -; mRNA.
DR EMBL; BC008351; AAH08351.1; -; mRNA.
DR EMBL; BC011569; AAH11569.1; -; mRNA.
DR CCDS; CCDS13714.1; -. [P60604-1]
DR CCDS; CCDS33586.1; -. [P60604-2]
DR RefSeq; NP_001189418.1; NM_001202489.1.
DR RefSeq; NP_003334.2; NM_003343.5. [P60604-1]
DR RefSeq; NP_872630.1; NM_182688.2. [P60604-2]
DR RefSeq; XP_016883958.1; XM_017028469.1.
DR PDB; 2CYX; X-ray; 2.56 A; A/B/C=1-165.
DR PDB; 2KLY; NMR; -; A=1-165.
DR PDB; 2LXP; NMR; -; A=2-165.
DR PDB; 3H8K; X-ray; 1.80 A; A=2-165.
DR PDB; 4LAD; X-ray; 2.30 A; A=1-165.
DR PDB; 7LEW; X-ray; 1.74 A; A=1-165.
DR PDBsum; 2CYX; -.
DR PDBsum; 2KLY; -.
DR PDBsum; 2LXP; -.
DR PDBsum; 3H8K; -.
DR PDBsum; 4LAD; -.
DR PDBsum; 7LEW; -.
DR AlphaFoldDB; P60604; -.
DR BMRB; P60604; -.
DR SMR; P60604; -.
DR BioGRID; 113175; 77.
DR DIP; DIP-50750N; -.
DR IntAct; P60604; 37.
DR MINT; P60604; -.
DR STRING; 9606.ENSP00000338348; -.
DR ChEMBL; CHEMBL4523256; -.
DR iPTMnet; P60604; -.
DR PhosphoSitePlus; P60604; -.
DR SwissPalm; P60604; -.
DR BioMuta; UBE2G2; -.
DR DMDM; 45593583; -.
DR EPD; P60604; -.
DR jPOST; P60604; -.
DR MassIVE; P60604; -.
DR MaxQB; P60604; -.
DR PaxDb; P60604; -.
DR PeptideAtlas; P60604; -.
DR PRIDE; P60604; -.
DR ProteomicsDB; 1554; -.
DR ProteomicsDB; 57218; -. [P60604-1]
DR TopDownProteomics; P60604-1; -. [P60604-1]
DR Antibodypedia; 1148; 422 antibodies from 32 providers.
DR DNASU; 7327; -.
DR Ensembl; ENST00000330942.9; ENSP00000331384.5; ENSG00000184787.19. [P60604-2]
DR Ensembl; ENST00000345496.7; ENSP00000338348.3; ENSG00000184787.19. [P60604-1]
DR GeneID; 7327; -.
DR KEGG; hsa:7327; -.
DR MANE-Select; ENST00000345496.7; ENSP00000338348.3; NM_003343.6; NP_003334.2.
DR UCSC; uc002zfx.4; human. [P60604-1]
DR CTD; 7327; -.
DR DisGeNET; 7327; -.
DR GeneCards; UBE2G2; -.
DR HGNC; HGNC:12483; UBE2G2.
DR HPA; ENSG00000184787; Low tissue specificity.
DR MIM; 603124; gene.
DR neXtProt; NX_P60604; -.
DR OpenTargets; ENSG00000184787; -.
DR PharmGKB; PA37132; -.
DR VEuPathDB; HostDB:ENSG00000184787; -.
DR eggNOG; KOG0426; Eukaryota.
DR GeneTree; ENSGT00940000158193; -.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; P60604; -.
DR OMA; KMWRENR; -.
DR OrthoDB; 1317014at2759; -.
DR PhylomeDB; P60604; -.
DR TreeFam; TF101118; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; P60604; -.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P60604; -.
DR SIGNOR; P60604; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7327; 176 hits in 1086 CRISPR screens.
DR ChiTaRS; UBE2G2; human.
DR EvolutionaryTrace; P60604; -.
DR GeneWiki; UBE2G2; -.
DR GenomeRNAi; 7327; -.
DR Pharos; P60604; Tbio.
DR PRO; PR:P60604; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P60604; protein.
DR Bgee; ENSG00000184787; Expressed in tendon of biceps brachii and 202 other tissues.
DR ExpressionAtlas; P60604; baseline and differential.
DR Genevisible; P60604; HS.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IMP:UniProtKB.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR DisProt; DP02100; -.
DR Gene3D; 3.10.110.10; -; 1.
DR IDEAL; IID00307; -.
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 Endoplasmic reticulum; Lipid droplet; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..165
FT /note="Ubiquitin-conjugating enzyme E2 G2"
FT /id="PRO_0000082483"
FT DOMAIN 4..164
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 89
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046260"
FT CONFLICT 12
FT /note="E -> V (in Ref. 1; AAC32312)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..107
FT /note="MGYESSA -> HGLREQP (in Ref. 1; AAC32312)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:7LEW"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:7LEW"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:7LEW"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7LEW"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:7LEW"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:7LEW"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:7LEW"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7LEW"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:7LEW"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2CYX"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:7LEW"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:2CYX"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:7LEW"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:7LEW"
SQ SEQUENCE 165 AA; 18566 MW; 74DEC732A79575E3 CRC64;
MAGTALKRLM AEYKQLTLNP PEGIVAGPMN EENFFEWEAL IMGPEDTCFE FGVFPAILSF
PLDYPLSPPK MRFTCEMFHP NIYPDGRVCI SILHAPGDDP MGYESSAERW SPVQSVEKIL
LSVVSMLAEP NDESGANVDA SKMWRDDREQ FYKIAKQIVQ KSLGL
