PPIL2_HUMAN
ID PPIL2_HUMAN Reviewed; 520 AA.
AC Q13356; Q13357; Q8TAH2; Q9BWR8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=RING-type E3 ubiquitin-protein ligase PPIL2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:11435423};
DE AltName: Full=CYC4 {ECO:0000303|PubMed:11435423};
DE AltName: Full=Cyclophilin-60 {ECO:0000303|PubMed:8660300};
DE Short=Cyclophilin-like protein Cyp-60 {ECO:0000303|PubMed:8660300};
DE Short=Cyp60 {ECO:0000303|PubMed:8660300};
DE Short=hCyP-60 {ECO:0000303|PubMed:8660300};
DE AltName: Full=Probable inactive peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000305|PubMed:20676357};
DE Short=PPIase {ECO:0000305|PubMed:20676357};
DE AltName: Full=Rotamase PPIL2 {ECO:0000305};
GN Name=PPIL2 {ECO:0000312|HGNC:HGNC:9261};
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lymphocyte;
RX PubMed=8660300; DOI=10.1042/bj3140313;
RA Wang B.B., Hayenga K.J., Payan D.G., Fisher J.M.;
RT "Identification of a nuclear-specific cyclophilin which interacts with the
RT proteinase inhibitor eglin c.";
RL Biochem. J. 314:313-319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, and Kidney;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11435423; DOI=10.1074/jbc.m102755200;
RA Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.;
RT "U box proteins as a new family of ubiquitin-protein ligases.";
RL J. Biol. Chem. 276:33111-33120(2001).
RN [5]
RP INTERACTION WITH CRNKL1 AND HSP90.
RX PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
RA Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
RT "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular
RT chaperones.";
RL Genes Cells 9:533-548(2004).
RN [6]
RP FUNCTION, INTERACTION WITH BSG, AND SUBCELLULAR LOCATION.
RX PubMed=15946952; DOI=10.1074/jbc.m503770200;
RA Pushkarsky T., Yurchenko V., Vanpouille C., Brichacek B., Vaisman I.,
RA Hatakeyama S., Nakayama K.I., Sherry B., Bukrinsky M.I.;
RT "Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60.";
RL J. Biol. Chem. 280:27866-27871(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-482, 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-216, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 280-457.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human peptidylprolyl isomerase-like 2 isoform
RT B.";
RL Submitted (JAN-2006) to the PDB data bank.
RN [12] {ECO:0007744|PDB:1ZKC}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 280-457, FUNCTION, CAUTION, AND
RP MUTAGENESIS OF TYR-389.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
CC -!- FUNCTION: Has a ubiquitin-protein ligase activity acting as an E3
CC ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting
CC elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-
CC linked polyubiquitination of proteins could target them for proteasomal
CC degradation (PubMed:11435423). May also function as a chaperone,
CC playing a role in transport to the cell membrane of BSG/Basigin for
CC instance (PubMed:15946952). Probable inactive PPIase with no peptidyl-
CC prolyl cis-trans isomerase activity (PubMed:20676357).
CC {ECO:0000269|PubMed:11435423, ECO:0000269|PubMed:15946952,
CC ECO:0000269|PubMed:20676357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11435423};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:11435423}.
CC -!- SUBUNIT: Interacts with isoform 2 of BSG (PubMed:15946952). Interacts
CC (via the PPIase cyclophilin-type domain) with CRNKL1; they may form a
CC trimeric complex with HSP90. {ECO:0000269|PubMed:15189447,
CC ECO:0000269|PubMed:15946952}.
CC -!- INTERACTION:
CC Q13356; P36406: TRIM23; NbExp=3; IntAct=EBI-7705988, EBI-740098;
CC Q13356; Q96NB3: ZNF830; NbExp=2; IntAct=EBI-7705988, EBI-3920997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11435423,
CC ECO:0000269|PubMed:8660300}. Note=May also localize to the cytoplasm
CC and the cell membrane. {ECO:0000269|PubMed:15946952}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13356-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13356-2; Sequence=VSP_005182;
CC -!- TISSUE SPECIFICITY: Highest expression in thymus, pancreas and testis.
CC Also detected in heart, placenta, lung, liver, skeletal muscle, kidney,
CC spleen, prostate, ovary, small intestine and colon. Poorly detected in
CC brain and leukocytes. Strong protein expression in lymph node
CC (cortical, paracortical and medullar regions), thyroid (follicular
CC epithelial cells), testis (developing spermatozoa), stomach (cells
CC lining the gastric pit), pancreas, kidney (proximal and distal-tubule
CC cells and collecting duct cells but not in glomeruli), endometrium and
CC colon (goblet cells). Moderate protein expression in spleen, prostate
CC (epithelium and squamous cell carcinomas), placenta and adrenal gland.
CC Weak protein expression in liver, heart, breast, ovary, and lung. No
CC protein expression in brain and bladder. High protein expression in
CC most lymphomas and melanomas. {ECO:0000269|PubMed:11435423,
CC ECO:0000269|PubMed:8660300}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Despite the fact that it belongs to the cyclophilin-type
CC PPIase family, a report has shown that it has probably no peptidyl-
CC prolyl cis-trans isomerase activity due to the presence of a tyrosine
CC instead of a tryptophan at position 389. {ECO:0000269|PubMed:20676357}.
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DR EMBL; U37219; AAC50376.1; -; mRNA.
DR EMBL; U37220; AAC50377.1; -; mRNA.
DR EMBL; U37221; AAC50378.1; -; mRNA.
DR EMBL; CR456548; CAG30434.1; -; mRNA.
DR EMBL; BC028385; AAH28385.1; -; mRNA.
DR EMBL; BC000022; AAH00022.1; -; mRNA.
DR CCDS; CCDS13793.1; -. [Q13356-1]
DR CCDS; CCDS46670.1; -. [Q13356-2]
DR PIR; S64705; S64705.
DR RefSeq; NP_001304925.1; NM_001317996.1. [Q13356-1]
DR RefSeq; NP_055152.1; NM_014337.3. [Q13356-1]
DR RefSeq; NP_680480.1; NM_148175.2. [Q13356-1]
DR RefSeq; NP_680481.1; NM_148176.2. [Q13356-2]
DR RefSeq; XP_005261505.1; XM_005261448.3. [Q13356-1]
DR RefSeq; XP_011528348.1; XM_011530046.2. [Q13356-1]
DR RefSeq; XP_011528349.1; XM_011530047.2. [Q13356-1]
DR PDB; 1ZKC; X-ray; 1.65 A; A/B=280-457.
DR PDB; 7ABI; EM; 8.00 A; t=1-520.
DR PDB; 7DVQ; EM; 2.89 A; 9=1-520.
DR PDBsum; 1ZKC; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; Q13356; -.
DR SMR; Q13356; -.
DR BioGRID; 117260; 71.
DR CORUM; Q13356; -.
DR IntAct; Q13356; 27.
DR MINT; Q13356; -.
DR STRING; 9606.ENSP00000334553; -.
DR GlyGen; Q13356; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13356; -.
DR MetOSite; Q13356; -.
DR PhosphoSitePlus; Q13356; -.
DR BioMuta; PPIL2; -.
DR DMDM; 23813917; -.
DR EPD; Q13356; -.
DR jPOST; Q13356; -.
DR MassIVE; Q13356; -.
DR MaxQB; Q13356; -.
DR PaxDb; Q13356; -.
DR PeptideAtlas; Q13356; -.
DR PRIDE; Q13356; -.
DR ProteomicsDB; 59341; -. [Q13356-1]
DR ProteomicsDB; 59342; -. [Q13356-2]
DR Antibodypedia; 23562; 208 antibodies from 26 providers.
DR DNASU; 23759; -.
DR Ensembl; ENST00000335025.12; ENSP00000334553.7; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000398831.8; ENSP00000381812.3; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000406385.1; ENSP00000384299.1; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000626352.2; ENSP00000486725.1; ENSG00000100023.20. [Q13356-2]
DR Ensembl; ENST00000679534.1; ENSP00000504893.1; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000679540.1; ENSP00000506328.1; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000679795.1; ENSP00000506144.1; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000680061.1; ENSP00000505910.1; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000680393.1; ENSP00000506542.1; ENSG00000100023.20. [Q13356-1]
DR Ensembl; ENST00000681956.1; ENSP00000506158.1; ENSG00000100023.20. [Q13356-1]
DR GeneID; 23759; -.
DR KEGG; hsa:23759; -.
DR MANE-Select; ENST00000398831.8; ENSP00000381812.3; NM_014337.4; NP_055152.1.
DR UCSC; uc002zvg.5; human. [Q13356-1]
DR CTD; 23759; -.
DR DisGeNET; 23759; -.
DR GeneCards; PPIL2; -.
DR HGNC; HGNC:9261; PPIL2.
DR HPA; ENSG00000100023; Low tissue specificity.
DR MIM; 607588; gene.
DR neXtProt; NX_Q13356; -.
DR OpenTargets; ENSG00000100023; -.
DR PharmGKB; PA33588; -.
DR VEuPathDB; HostDB:ENSG00000100023; -.
DR eggNOG; KOG0883; Eukaryota.
DR GeneTree; ENSGT00940000153189; -.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; Q13356; -.
DR OMA; NFIKHCA; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q13356; -.
DR TreeFam; TF300854; -.
DR PathwayCommons; Q13356; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR SignaLink; Q13356; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23759; 759 hits in 1126 CRISPR screens.
DR ChiTaRS; PPIL2; human.
DR EvolutionaryTrace; Q13356; -.
DR GeneWiki; PPIL2; -.
DR GenomeRNAi; 23759; -.
DR Pharos; Q13356; Tbio.
DR PRO; PR:Q13356; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q13356; protein.
DR Bgee; ENSG00000100023; Expressed in right lobe of thyroid gland and 187 other tissues.
DR ExpressionAtlas; Q13356; baseline and differential.
DR Genevisible; Q13356; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR CDD; cd16663; RING-Ubox_PPIL2; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR026951; PPIL2_U-box_dom.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..520
FT /note="RING-type E3 ubiquitin-protein ligase PPIL2"
FT /id="PRO_0000064171"
FT DOMAIN 35..108
FT /note="U-box"
FT DOMAIN 278..433
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 456..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..217
FT /evidence="ECO:0000255"
FT COMPBIAS 457..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 482
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 490..520
FT /note="KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW -> EQQRKSPQPVPLSPCPR
FT RSPVGVLGTSAPGSSRLPDDH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005182"
FT MUTAGEN 389
FT /note="Y->H: No peptidyl-prolyl cis-trans isomerase
FT activity; enables interaction with cyclosporin A."
FT /evidence="ECO:0000269|PubMed:20676357"
FT MUTAGEN 389
FT /note="Y->W: Gain of a peptidyl-prolyl cis-trans isomerase
FT activity; enables interaction with cyclosporin A."
FT /evidence="ECO:0000269|PubMed:20676357"
FT CONFLICT 455
FT /note="V -> I (in Ref. 3; AAH28385)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:1ZKC"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1ZKC"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:1ZKC"
FT TURN 313..318
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1ZKC"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:1ZKC"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1ZKC"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:1ZKC"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:1ZKC"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:1ZKC"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:1ZKC"
FT HELIX 439..455
FT /evidence="ECO:0007829|PDB:1ZKC"
SQ SEQUENCE 520 AA; 58823 MW; 3FFA51C3D82F0957 CRC64;
MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV
FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR
TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK
IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH
YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT
PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH
TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD
RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV
GKYINPAATK RAAEEEPSTS ATVPMSKKKP SRGFGDFSSW
