ID PIAS3_HUMAN Reviewed; 628 AA.
AC Q9Y6X2; Q9UFI3;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 27-MAR-2024, entry version 201.
DE RecName: Full=E3 SUMO-protein ligase PIAS3;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase PIAS3 {ECO:0000305};
DE AltName: Full=Protein inhibitor of activated STAT protein 3;
GN Name=PIAS3;
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] OF 2-628.
RX PubMed=10319586; DOI=10.1007/s100380050141;
RA Ueki N., Seki N., Yano K., Saito T., Masuho Y., Muramatsu M.-A.;
RT "Isolation and chromosomal assignment of a human gene encoding protein
RT inhibitor of activated STAT3 (PIAS3).";
RL J. Hum. Genet. 44:193-196(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 310-628.
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP FUNCTION, INTERACTION WITH STAT3, AND TISSUE SPECIFICITY.
RX PubMed=9388184; DOI=10.1126/science.278.5344.1803;
RA Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K.;
RT "Specific inhibition of Stat3 signal transduction by PIAS3.";
RL Science 278:1803-1805(1997).
RN [5]
RP INTERACTION WITH AR, AND INDUCTION.
RX PubMed=11071847; DOI=10.1006/bbrc.2000.3753;
RA Junicho A., Matsuda T., Yamamoto T., Kishi H., Korkmaz K., Saatcioglu F.,
RA Fuse H., Muraguchi A.;
RT "Protein inhibitor of activated STAT3 regulates androgen receptor signaling
RT in prostate carcinoma cells.";
RL Biochem. Biophys. Res. Commun. 278:9-13(2000).
RN [6]
RP INTERACTION WITH GFI1.
RX PubMed=11060035; DOI=10.1093/emboj/19.21.5845;
RA Roedel B., Tavassoli K., Karsunky H., Schmidt T., Bachmann M., Schaper F.,
RA Heinrich P., Shuai K., Elsaesser H.-P., Moeroey T.;
RT "The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting
RT with the STAT3 inhibitor PIAS3.";
RL EMBO J. 19:5845-5855(2000).
RN [7]
RP INTERACTION WITH ZFHX3.
RX PubMed=14715251; DOI=10.1016/j.bbrc.2003.12.054;
RA Nojiri S., Joh T., Miura Y., Sakata N., Nomura T., Nakao H., Sobue S.,
RA Ohara H., Asai K., Ito M.;
RT "ATBF1 enhances the suppression of STAT3 signaling by interaction with
RT PIAS3.";
RL Biochem. Biophys. Res. Commun. 314:97-103(2004).
RN [8]
RP INTERACTION WITH PLAG1.
RX PubMed=15208321; DOI=10.1074/jbc.m401753200;
RA Van Dyck F., Delvaux E.L.D., Van de Ven W.J.M., Chavez M.V.;
RT "Repression of the transactivating capacity of the oncoprotein PLAG1 by
RT SUMOylation.";
RL J. Biol. Chem. 279:36121-36131(2004).
RN [9]
RP INTERACTION WITH TRIM8.
RX PubMed=20516148; DOI=10.1242/jcs.068981;
RA Okumura F., Matsunaga Y., Katayama Y., Nakayama K.I., Hatakeyama S.;
RT "TRIM8 modulates STAT3 activity through negative regulation of PIAS3.";
RL J. Cell Sci. 123:2238-2245(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH MTA1.
RX PubMed=21965678; DOI=10.1074/jbc.m111.267237;
RA Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1
RT (MTA1) synergistically regulate its transcriptional repressor function.";
RL J. Biol. Chem. 286:43793-43808(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH CCAR2.
RX PubMed=25406032; DOI=10.1038/ncomms6483;
RA Park J.H., Lee S.W., Yang S.W., Yoo H.M., Park J.M., Seong M.W., Ka S.H.,
RA Oh K.H., Jeon Y.J., Chung C.H.;
RT "Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis in
RT response to DNA damage.";
RL Nat. Commun. 5:5483-5483(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-230 AND LYS-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [13]
RP FUNCTION.
RX PubMed=24651376; DOI=10.1371/journal.pone.0092746;
RA Sun X., Li J., Dong F.N., Dong J.T.;
RT "Characterization of nuclear localization and SUMOylation of the ATBF1
RT transcription factor in epithelial cells.";
RL PLoS ONE 9:E92746-E92746(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [15]
RP INTERACTION WITH PRDM1.
RX PubMed=28842558; DOI=10.1038/s41467-017-00476-w;
RA Wang W.F., Yan L., Liu Z., Liu L.X., Lin J., Liu Z.Y., Chen X.P., Zhang W.,
RA Xu Z.Z., Shi T., Li J.M., Zhao Y.L., Meng G., Xia Y., Li J.Y., Zhu J.;
RT "HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal
RT misfolded Blimp-1s in lymphoma cells.";
RL Nat. Commun. 8:363-363(2017).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-56; LYS-230; LYS-307;
RP LYS-466 AND LYS-482, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO)
CC ligase, stabilizing the interaction between UBE2I and the substrate,
CC and as a SUMO-tethering factor. Plays a crucial role as a
CC transcriptional coregulation in various cellular pathways, including
CC the STAT pathway and the steroid hormone signaling pathway. Involved in
CC regulating STAT3 signaling via inhibiting STAT3 DNA-binding and
CC suppressing cell growth. Enhances the sumoylation of MTA1 and may
CC participate in its paralog-selective sumoylation (PubMed:21965678,
CC PubMed:9388184). Sumoylates CCAR2 which promotes its interaction with
CC SIRT1 (PubMed:25406032). Diminishes the sumoylation of ZFHX3 by
CC preventing the colocalization of ZFHX3 with SUMO1 in the nucleus
CC (PubMed:24651376). {ECO:0000269|PubMed:21965678,
CC ECO:0000269|PubMed:24651376, ECO:0000269|PubMed:25406032,
CC ECO:0000269|PubMed:9388184}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Monomer (By similarity). Binds SUMO1 and UBE2I. Interacts with
CC BCL11A, HMGA2, IRF1, MITF and NCOA2. Interacts with STAT5; the
CC interaction occurs on stimulation by PRL. Interacts with GFI1; the
CC interaction relieves the inhibitory effect of PIAS3 on STAT3-mediated
CC transcriptional activity (By similarity). Interacts with AR, PLAG1 and
CC ZFHX3. Interacts with STAT3; the interaction occurs on stimulation by
CC IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3.
CC Interacts with MTA1. Interacts with CCAR2 (via N-terminus). Interacts
CC with TRIM8 (PubMed:20516148). Interacts with PRDM1/Blimp-1
CC (PubMed:28842558). {ECO:0000250|UniProtKB:O54714,
CC ECO:0000269|PubMed:11060035, ECO:0000269|PubMed:11071847,
CC ECO:0000269|PubMed:14715251, ECO:0000269|PubMed:15208321,
CC ECO:0000269|PubMed:20516148, ECO:0000269|PubMed:21965678,
CC ECO:0000269|PubMed:25406032, ECO:0000269|PubMed:28842558,
CC ECO:0000269|PubMed:9388184}.
CC -!- INTERACTION:
CC Q9Y6X2; Q92993: KAT5; NbExp=3; IntAct=EBI-2803703, EBI-399080;
CC Q9Y6X2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2803703, EBI-11742507;
CC Q9Y6X2; Q9UIS9: MBD1; NbExp=3; IntAct=EBI-2803703, EBI-867196;
CC Q9Y6X2; O60664: PLIN3; NbExp=3; IntAct=EBI-2803703, EBI-725795;
CC Q9Y6X2; P17252: PRKCA; NbExp=3; IntAct=EBI-2803703, EBI-1383528;
CC Q9Y6X2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2803703, EBI-9090795;
CC Q9Y6X2; P61981: YWHAG; NbExp=3; IntAct=EBI-2803703, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54714}. Nucleus
CC {ECO:0000250|UniProtKB:O54714}. Nucleus speckle
CC {ECO:0000250|UniProtKB:O54714}. Note=Colocalizes with MITF in the
CC nucleus. Colocalizes with GFI1 in nuclear dots. Colocalizes with SUMO1
CC in nuclear granules. {ECO:0000250|UniProtKB:O54714}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9388184}.
CC -!- INDUCTION: By dihydrotestosterone (DHT) in prostate cancer cells.
CC {ECO:0000269|PubMed:11071847}.
CC -!- DOMAIN: The PINIT domain of PIAS3 is required for STAT3-PIAS3
CC interaction and for translocation to the nucleus.
CC -!- DOMAIN: The LXXLL motif is a transcriptional coregulator signature.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA78533.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/41709/PIAS3";
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DR EMBL; AB021868; BAA78533.1; ALT_INIT; mRNA.
DR EMBL; BC001154; AAH01154.2; -; mRNA.
DR EMBL; BC030556; AAH30556.2; -; mRNA.
DR CCDS; CCDS72866.1; -.
DR PIR; T34525; T34525.
DR RefSeq; NP_006090.2; NM_006099.3.
DR PDB; 4MVT; X-ray; 2.30 A; A/B/C/D=112-467.
DR PDBsum; 4MVT; -.
DR AlphaFoldDB; Q9Y6X2; -.
DR SMR; Q9Y6X2; -.
DR BioGRID; 115673; 75.
DR CORUM; Q9Y6X2; -.
DR DIP; DIP-5969N; -.
DR ELM; Q9Y6X2; -.
DR IntAct; Q9Y6X2; 54.
DR MINT; Q9Y6X2; -.
DR STRING; 9606.ENSP00000376765; -.
DR iPTMnet; Q9Y6X2; -.
DR PhosphoSitePlus; Q9Y6X2; -.
DR BioMuta; PIAS3; -.
DR DMDM; 56405390; -.
DR EPD; Q9Y6X2; -.
DR jPOST; Q9Y6X2; -.
DR MassIVE; Q9Y6X2; -.
DR MaxQB; Q9Y6X2; -.
DR PaxDb; 9606-ENSP00000376765; -.
DR PeptideAtlas; Q9Y6X2; -.
DR ProteomicsDB; 86810; -.
DR Pumba; Q9Y6X2; -.
DR Antibodypedia; 20233; 294 antibodies from 39 providers.
DR DNASU; 10401; -.
DR Ensembl; ENST00000393045.7; ENSP00000376765.2; ENSG00000131788.16.
DR GeneID; 10401; -.
DR KEGG; hsa:10401; -.
DR MANE-Select; ENST00000393045.7; ENSP00000376765.2; NM_006099.3; NP_006090.2.
DR UCSC; uc001eoc.2; human.
DR AGR; HGNC:16861; -.
DR CTD; 10401; -.
DR DisGeNET; 10401; -.
DR GeneCards; PIAS3; -.
DR HGNC; HGNC:16861; PIAS3.
DR HPA; ENSG00000131788; Low tissue specificity.
DR MIM; 605987; gene.
DR neXtProt; NX_Q9Y6X2; -.
DR OpenTargets; ENSG00000131788; -.
DR PharmGKB; PA134989011; -.
DR VEuPathDB; HostDB:ENSG00000131788; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR InParanoid; Q9Y6X2; -.
DR OMA; QFMANIQ; -.
DR OrthoDB; 20246at2759; -.
DR PhylomeDB; Q9Y6X2; -.
DR TreeFam; TF323787; -.
DR PathwayCommons; Q9Y6X2; -.
DR Reactome; R-HSA-3232118; SUMOylation of transcription factors.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-4755510; SUMOylation of immune response proteins.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR SignaLink; Q9Y6X2; -.
DR SIGNOR; Q9Y6X2; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 10401; 28 hits in 1194 CRISPR screens.
DR ChiTaRS; PIAS3; human.
DR GeneWiki; PIAS3; -.
DR GenomeRNAi; 10401; -.
DR Pharos; Q9Y6X2; Tbio.
DR PRO; PR:Q9Y6X2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y6X2; Protein.
DR Bgee; ENSG00000131788; Expressed in right uterine tube and 173 other cell types or tissues.
DR ExpressionAtlas; Q9Y6X2; baseline and differential.
DR Genevisible; Q9Y6X2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IEA:Ensembl.
DR CDD; cd16820; SP-RING_PIAS3; 1.
DR Gene3D; 2.60.120.780; PINIT domain; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR IDEAL; IID00506; -.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF10; E3 SUMO-PROTEIN LIGASE PIAS3; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..628
FT /note="E3 SUMO-protein ligase PIAS3"
FT /id="PRO_0000218979"
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 115..280
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT ZN_FING 312..393
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 1..200
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000269|PubMed:25406032"
FT REGION 450..460
FT /note="SUMO1-binding"
FT /evidence="ECO:0000250"
FT REGION 597..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..23
FT /note="LXXLL motif"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 466
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 390
FT /note="S -> C (in dbSNP:rs17354559)"
FT /id="VAR_050535"
FT STRAND 135..147
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:4MVT"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4MVT"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 268..279
FT /evidence="ECO:0007829|PDB:4MVT"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:4MVT"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:4MVT"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:4MVT"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:4MVT"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:4MVT"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:4MVT"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:4MVT"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4MVT"
SQ SEQUENCE 628 AA; 68017 MW; 7C06EF599D48F87D CRC64;
MAELGELKHM VMSFRVSELQ VLLGFAGRNK SGRKHELLAK ALHLLKSSCA PSVQMKIKEL
YRRRFPRKTL GPSDLSLLSL PPGTSPVGSP GPLAPIPPTL LAPGTLLGPK REVDMHPPLP
QPVHPDVTMK PLPFYEVYGE LIRPTTLAST SSQRFEEAHF TFALTPQQVQ QILTSREVLP
GAKCDYTIQV QLRFCLCETS CPQEDYFPPN LFVKVNGKLC PLPGYLPPTK NGAEPKRPSR
PINITPLARL SATVPNTIVV NWSSEFGRNY SLSVYLVRQL TAGTLLQKLR AKGIRNPDHS
RALIKEKLTA DPDSEVATTS LRVSLMCPLG KMRLTVPCRA LTCAHLQSFD AALYLQMNEK
KPTWTCPVCD KKAPYESLII DGLFMEILSS CSDCDEIQFM EDGSWCPMKP KKEASEVCPP
PGYGLDGLQY SPVQGGDPSE NKKKVEVIDL TIESSSDEED LPPTKKHCSV TSAAIPALPG
SKGVLTSGHQ PSSVLRSPAM GTLGGDFLSS LPLHEYPPAF PLGADIQGLD LFSFLQTESQ
HYGPSVITSL DEQDALGHFF QYRGTPSHFL GPLAPTLGSS HCSATPAPPP GRVSSIVAPG
GALREGHGGP LPSGPSLTGC RSDIISLD
//
