ID   UBE2H_HUMAN             Reviewed;         183 AA.
AC   P62256; A4D1L6; C9JY93; P37286; Q7Z6F4;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 H;
DE            EC=2.3.2.23 {ECO:0000269|PubMed:17588522, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:22496338, ECO:0000269|PubMed:29911972, ECO:0000269|PubMed:8132613};
DE   AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme H;
DE            EC=2.3.2.24 {ECO:0000269|PubMed:17588522, ECO:0000269|PubMed:8132613};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme H;
DE   AltName: Full=UbcH2;
DE   AltName: Full=Ubiquitin carrier protein H;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-20K;
DE   AltName: Full=Ubiquitin-protein ligase H;
GN   Name=UBE2H;
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), FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=8132613; DOI=10.1016/s0021-9258(17)37039-4;
RA   Kaiser P., Seufert W., Hoefferer L., Kofler B., Sachsenmaier C., Herzog H.,
RA   Jentsch S., Schweiger M., Schneider R.;
RT   "A human ubiquitin-conjugating enzyme homologous to yeast UBC8.";
RL   J. Biol. Chem. 269:8797-8802(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Lin L., Li S., Li H., Zhou G., Shen C., Zheng G., Ke R., Zhong G., Yu R.,
RA   Yang S.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING
RP   ENZYME, AND PATHWAY.
RX   PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014;
RA   Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.;
RT   "E3-independent monoubiquitination of ubiquitin-binding proteins.";
RL   Mol. Cell 26:891-898(2007).
RN   [9]
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   [10]
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   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, IDENTIFICATION IN THE CTLH COMPLEX,
RP   AND INTERACTION WITH WDR26 AND ARMC8.
RX   PubMed=29911972; DOI=10.7554/elife.35528;
RA   Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA   Picotti P., Stoffel M., Peter M.;
RT   "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT   the transcription factor Hbp1 for degradation.";
RL   Elife 7:0-0(2018).
RN   [12] {ECO:0007744|PDB:2Z5D}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-160, CATALYTIC ACTIVITY, AND
RP   AUTOUBIQUITINATION.
RX   PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA   Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA   Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA   Raught B., Dhe-Paganon S.;
RT   "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT   function screen.";
RL   Mol. Cell. Proteomics 11:329-341(2012).
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins (PubMed:8132613, PubMed:17588522,
CC       PubMed:20061386). E2 ubiquitin conjugating enzyme that transfers
CC       ubiquitin to MAEA, a core component of the CTLH E3 ubiquitin-protein
CC       ligase complex (PubMed:29911972). In vitro catalyzes 'Lys-11'- and
CC       'Lys-48'-linked polyubiquitination (PubMed:20061386). Capable, in
CC       vitro, to ubiquitinate histone H2A (PubMed:8132613).
CC       {ECO:0000269|PubMed:17588522, ECO:0000269|PubMed:20061386,
CC       ECO:0000269|PubMed:29911972, ECO:0000269|PubMed:8132613}.
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:17588522,
CC         ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:22496338,
CC         ECO:0000269|PubMed:29911972, ECO:0000269|PubMed:8132613};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC         cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.24; Evidence={ECO:0000269|PubMed:17588522,
CC         ECO:0000269|PubMed:8132613};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:17588522,
CC       ECO:0000269|PubMed:29911972, ECO:0000269|PubMed:8132613}.
CC   -!- SUBUNIT: Interacts with MAEA and WDR26, components of the CTLH complex
CC       that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or
CC       alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5.
CC       {ECO:0000269|PubMed:29911972}.
CC   -!- INTERACTION:
CC       P62256; P62879: GNB2; NbExp=3; IntAct=EBI-2129909, EBI-356942;
CC       P62256; P42858: HTT; NbExp=3; IntAct=EBI-2129909, EBI-466029;
CC       P62256; P43356: MAGEA2B; NbExp=2; IntAct=EBI-2129909, EBI-5650739;
CC       P62256; Q9UBF1: MAGEC2; NbExp=3; IntAct=EBI-2129909, EBI-5651487;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P62256-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P62256-2; Sequence=VSP_044580;
CC   -!- PTM: Autoubiquitinated in vitro in the presence of NEDD4L.
CC       {ECO:0000269|PubMed:22496338}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; Z29328; CAA82525.1; -; mRNA.
DR   EMBL; Z29330; CAA82527.1; -; mRNA.
DR   EMBL; Z29331; CAA82528.1; -; mRNA.
DR   EMBL; AY302138; AAP57630.1; -; mRNA.
DR   EMBL; BT006756; AAP35402.1; -; mRNA.
DR   EMBL; AC073320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC084865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236950; EAL24099.1; -; Genomic_DNA.
DR   EMBL; CH471070; EAW83736.1; -; Genomic_DNA.
DR   EMBL; BC006277; AAH06277.1; -; mRNA.
DR   CCDS; CCDS47710.1; -. [P62256-2]
DR   CCDS; CCDS5814.1; -. [P62256-1]
DR   PIR; A53516; A53516.
DR   RefSeq; NP_001189427.1; NM_001202498.1.
DR   RefSeq; NP_003335.1; NM_003344.3. [P62256-1]
DR   RefSeq; NP_874356.1; NM_182697.2. [P62256-2]
DR   PDB; 2Z5D; X-ray; 2.10 A; A/B=1-160.
DR   PDBsum; 2Z5D; -.
DR   AlphaFoldDB; P62256; -.
DR   SMR; P62256; -.
DR   BioGRID; 113176; 116.
DR   IntAct; P62256; 53.
DR   STRING; 9606.ENSP00000347836; -.
DR   ChEMBL; CHEMBL4105951; -.
DR   MoonDB; P62256; Predicted.
DR   iPTMnet; P62256; -.
DR   MetOSite; P62256; -.
DR   PhosphoSitePlus; P62256; -.
DR   SwissPalm; P62256; -.
DR   BioMuta; UBE2H; -.
DR   DMDM; 51338683; -.
DR   EPD; P62256; -.
DR   jPOST; P62256; -.
DR   MassIVE; P62256; -.
DR   MaxQB; P62256; -.
DR   PaxDb; 9606-ENSP00000347836; -.
DR   PeptideAtlas; P62256; -.
DR   ProteomicsDB; 57376; -. [P62256-1]
DR   ProteomicsDB; 621; -.
DR   Pumba; P62256; -.
DR   Antibodypedia; 1149; 223 antibodies from 29 providers.
DR   DNASU; 7328; -.
DR   Ensembl; ENST00000355621.8; ENSP00000347836.3; ENSG00000186591.13. [P62256-1]
DR   Ensembl; ENST00000473814.6; ENSP00000419097.2; ENSG00000186591.13. [P62256-2]
DR   GeneID; 7328; -.
DR   KEGG; hsa:7328; -.
DR   MANE-Select; ENST00000355621.8; ENSP00000347836.3; NM_003344.4; NP_003335.1.
DR   UCSC; uc003vpf.3; human. [P62256-1]
DR   AGR; HGNC:12484; -.
DR   CTD; 7328; -.
DR   DisGeNET; 7328; -.
DR   GeneCards; UBE2H; -.
DR   HGNC; HGNC:12484; UBE2H.
DR   HPA; ENSG00000186591; Low tissue specificity.
DR   MIM; 601082; gene.
DR   neXtProt; NX_P62256; -.
DR   OpenTargets; ENSG00000186591; -.
DR   PharmGKB; PA37133; -.
DR   VEuPathDB; HostDB:ENSG00000186591; -.
DR   eggNOG; KOG0416; Eukaryota.
DR   GeneTree; ENSGT00390000004852; -.
DR   InParanoid; P62256; -.
DR   OMA; SPSIGFC; -.
DR   OrthoDB; 619890at2759; -.
DR   PhylomeDB; P62256; -.
DR   TreeFam; TF101121; -.
DR   BRENDA; 2.3.2.23; 2681.
DR   BRENDA; 2.3.2.24; 2681.
DR   PathwayCommons; P62256; -.
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; P62256; -.
DR   SIGNOR; P62256; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 7328; 351 hits in 1173 CRISPR screens.
DR   ChiTaRS; UBE2H; human.
DR   EvolutionaryTrace; P62256; -.
DR   GeneWiki; UBE2H; -.
DR   GenomeRNAi; 7328; -.
DR   Pharos; P62256; Tbio.
DR   PRO; PR:P62256; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P62256; Protein.
DR   Bgee; ENSG00000186591; Expressed in secondary oocyte and 199 other cell types or tissues.
DR   ExpressionAtlas; P62256; 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:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
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; Ubiquitin Conjugating Enzyme; 1.
DR   IDEAL; IID00637; -.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF128; UBIQUITIN-CONJUGATING ENZYME E2 H; 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; P62256; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..183
FT                   /note="Ubiquitin-conjugating enzyme E2 H"
FT                   /id="PRO_0000082486"
FT   DOMAIN          1..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          152..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        87
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62257"
FT   VAR_SEQ         69..99
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_044580"
FT   CONFLICT        165
FT                   /note="S -> P (in Ref. 2; AAP57630)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..20
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   TURN            45..48
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   STRAND          50..56
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   TURN            59..63
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   HELIX           88..94
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   HELIX           108..114
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   HELIX           124..132
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   HELIX           134..148
FT                   /evidence="ECO:0007829|PDB:2Z5D"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:2Z5D"
SQ   SEQUENCE   183 AA;  20655 MW;  3DD5D365945F708C CRC64;
     MSSPSPGKRR MDTDVVKLIE SKHEVTILGG LNEFVVKFYG PQGTPYEGGV WKVRVDLPDK
     YPFKSPSIGF MNKIFHPNID EASGTVCLDV INQTWTALYD LTNIFESFLP QLLAYPNPID
     PLNGDAAAMY LHRPEEYKQK IKEYIQKYAT EEALKEQEEG TGDSSSESSM SDFSEDEAQD
     MEL
//