ID   PIR_HUMAN               Reviewed;         290 AA.
AC   O00625; Q5U0G0; Q6FHD2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 183.
DE   RecName: Full=Pirin;
DE            EC=1.13.11.24 {ECO:0000269|PubMed:15951572};
DE   AltName: Full=Probable quercetin 2,3-dioxygenase PIR;
DE            Short=Probable quercetinase;
GN   Name=PIR;
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], PROPOSED FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=9079676; DOI=10.1074/jbc.272.13.8482;
RA   Wendler W.M.F., Kremmer E., Foerster R., Winnacker E.-L.;
RT   "Identification of pirin, a novel highly conserved nuclear protein.";
RL   J. Biol. Chem. 272:8482-8489(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   INTERACTION WITH BCL3, AND IDENTIFICATION IN A COMPLEX WITH BLC3; NFKB1;
RP   PIR AND TARGET DNA.
RX   PubMed=10362352; DOI=10.1038/sj.onc.1202717;
RA   Dechend R., Hirano F., Lehmann K., Heissmeyer V., Ansieau S., Wulczyn F.G.,
RA   Scheidereit C., Leutz A.;
RT   "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and
RT   nuclear co-regulators.";
RL   Oncogene 18:3316-3323(1999).
RN   [6]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=15951572; DOI=10.1074/jbc.m501034200;
RA   Adams M., Jia Z.;
RT   "Structural and biochemical analysis reveal pirins to possess quercetinase
RT   activity.";
RL   J. Biol. Chem. 280:28675-28682(2005).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=17288615; DOI=10.1186/1465-9921-8-10;
RA   Gelbman B.D., Heguy A., O'Connor T.P., Zabner J., Crystal R.G.;
RT   "Upregulation of pirin expression by chronic cigarette smoking is
RT   associated with bronchial epithelial cell apoptosis.";
RL   Respir. Res. 8:10-10(2007).
RN   [8]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20089166; DOI=10.1186/1471-2121-11-5;
RA   Licciulli S., Luise C., Zanardi A., Giorgetti L., Viale G., Lanfrancone L.,
RA   Carbone R., Alcalay M.;
RT   "Pirin delocalization in melanoma progression identified by high content
RT   immuno-detection based approaches.";
RL   BMC Cell Biol. 11:5-5(2010).
RN   [9]
RP   POSSIBLE INFLUENCE OF PIR POLYMORPHISMS ON BONE MINERAL DENSITY.
RX   PubMed=19766747; DOI=10.1016/j.bone.2009.09.012;
RA   Tang N.L., Liao C.D., Ching J.K., Suen E.W., Chan I.H., Orwoll E., Ho S.C.,
RA   Chan F.W., Kwok A.W., Kwok T., Woo J., Leung P.C.;
RT   "Sex-specific effect of Pirin gene on bone mineral density in a cohort of
RT   4000 Chinese.";
RL   Bone 46:543-550(2010).
RN   [10]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=20010624; DOI=10.1038/leu.2009.247;
RA   Licciulli S., Cambiaghi V., Scafetta G., Gruszka A.M., Alcalay M.;
RT   "Pirin downregulation is a feature of AML and leads to impairment of
RT   terminal myeloid differentiation.";
RL   Leukemia 24:429-437(2010).
RN   [11]
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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS, AND
RP   COFACTOR.
RX   PubMed=14573596; DOI=10.1074/jbc.m310022200;
RA   Pang H., Bartlam M., Zeng Q., Miyatake H., Hisano T., Miki K., Wong L.L.,
RA   Gao G.F., Rao Z.;
RT   "Crystal structure of human pirin: an iron-binding nuclear protein and
RT   transcription cofactor.";
RL   J. Biol. Chem. 279:1491-1498(2004).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH A SYNTHETIC
RP   INHIBITOR AND IRON IONS, INTERACTION WITH BCL3, COFACTOR, AND FUNCTION.
RX   PubMed=20711196; DOI=10.1038/nchembio.423;
RA   Miyazaki I., Simizu S., Okumura H., Takagi S., Osada H.;
RT   "A small-molecule inhibitor shows that pirin regulates migration of
RT   melanoma cells.";
RL   Nat. Chem. Biol. 6:667-673(2010).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS), AND FUNCTION.
RX   PubMed=23716661; DOI=10.1073/pnas.1221743110;
RA   Liu F., Rehmani I., Esaki S., Fu R., Chen L., de Serrano V., Liu A.;
RT   "Pirin is an iron-dependent redox regulator of NF-kappaB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:9722-9727(2013).
CC   -!- FUNCTION: Transcriptional coregulator of NF-kappa-B which facilitates
CC       binding of NF-kappa-B proteins to target kappa-B genes in a redox-
CC       state-dependent manner. May be required for efficient terminal myeloid
CC       maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase
CC       activity (in vitro). {ECO:0000269|PubMed:15951572,
CC       ECO:0000269|PubMed:17288615, ECO:0000269|PubMed:20010624,
CC       ECO:0000269|PubMed:20711196, ECO:0000269|PubMed:23716661}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-
CC         dihydroxybenzoate + CO; Xref=Rhea:RHEA:15381, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17245, ChEBI:CHEBI:57628, ChEBI:CHEBI:57694;
CC         EC=1.13.11.24; Evidence={ECO:0000269|PubMed:15951572};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:14573596, ECO:0000269|PubMed:20711196};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:14573596,
CC       ECO:0000269|PubMed:20711196};
CC   -!- ACTIVITY REGULATION: Inhibited by kojic acid, sodium
CC       diethyldithiocarbamate and 1,10-phenanthroline monohydrochloride.
CC       {ECO:0000269|PubMed:15951572}.
CC   -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC       {ECO:0000305|PubMed:15951572}.
CC   -!- SUBUNIT: May interact with NF1/CTF1. Interacts with BCL3. Identified in
CC       a complex comprised of PIR, BLC3, NFKB1 and target DNA.
CC       {ECO:0000269|PubMed:10362352, ECO:0000269|PubMed:14573596,
CC       ECO:0000269|PubMed:20711196, ECO:0000269|PubMed:9079676}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20089166,
CC       ECO:0000269|PubMed:9079676}. Cytoplasm {ECO:0000269|PubMed:20089166}.
CC       Note=Predominantly localized in dot-like subnuclear structures.
CC       Cytoplasmic localization of PIR seems to positively correlate with
CC       melanoma progression. {ECO:0000269|PubMed:20089166,
CC       ECO:0000269|PubMed:9079676}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in a subset of melanomas. Detected
CC       at very low levels in most tissues (at protein level). Expressed in all
CC       tissues, with highest level of expression in heart and liver.
CC       {ECO:0000269|PubMed:20089166, ECO:0000269|PubMed:9079676}.
CC   -!- INDUCTION: Up-regulated in CD34(+) cells upon myelomonocytic
CC       differentiation. Down-regulated in many acute myeloid leukemias. Up-
CC       regulated in primary bronchial epithelial cells exposed to cigarette
CC       smoke extract. {ECO:0000269|PubMed:17288615,
CC       ECO:0000269|PubMed:20010624}.
CC   -!- POLYMORPHISM: Genetic variations in PIR might have a sex-specific
CC       influence on bone mineral density differences in some populations, as
CC       reported by PubMed:19766747. In a cohort of 4000 Chinese, a significant
CC       statistical association has been identified, in women but not in men,
CC       between the intronic SNP rs5935970 and lumbar spine bone mineral
CC       density, and between a haplotype composed of three SNPs with bone
CC       mineral density at other sites. {ECO:0000305|PubMed:19766747}.
CC   -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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; Y07868; CAA69195.1; -; mRNA.
DR   EMBL; Y07867; CAA69194.1; -; mRNA.
DR   EMBL; CR541822; CAG46621.1; -; mRNA.
DR   EMBL; BT019583; AAV38390.1; -; mRNA.
DR   EMBL; BT019584; AAV38391.1; -; mRNA.
DR   EMBL; BC002517; AAH02517.1; -; mRNA.
DR   CCDS; CCDS14167.1; -.
DR   RefSeq; NP_001018119.1; NM_001018109.2.
DR   RefSeq; NP_003653.1; NM_003662.3.
DR   PDB; 1J1L; X-ray; 2.10 A; A=1-290.
DR   PDB; 3ACL; X-ray; 2.35 A; A=2-290.
DR   PDB; 4ERO; X-ray; 2.65 A; A=1-290.
DR   PDB; 4EWA; X-ray; 2.47 A; A=1-290.
DR   PDB; 4EWD; X-ray; 2.15 A; A=1-290.
DR   PDB; 4EWE; X-ray; 1.56 A; A=1-290.
DR   PDB; 4GUL; X-ray; 1.80 A; A=3-290.
DR   PDB; 4HLT; X-ray; 1.70 A; A=3-290.
DR   PDB; 5JCT; X-ray; 1.73 A; A=1-290.
DR   PDB; 6H1H; X-ray; 1.54 A; A=1-290.
DR   PDB; 6H1I; X-ray; 1.69 A; A=1-290.
DR   PDB; 6N0J; X-ray; 1.79 A; A=2-290.
DR   PDB; 6N0K; X-ray; 1.46 A; A=2-290.
DR   PDBsum; 1J1L; -.
DR   PDBsum; 3ACL; -.
DR   PDBsum; 4ERO; -.
DR   PDBsum; 4EWA; -.
DR   PDBsum; 4EWD; -.
DR   PDBsum; 4EWE; -.
DR   PDBsum; 4GUL; -.
DR   PDBsum; 4HLT; -.
DR   PDBsum; 5JCT; -.
DR   PDBsum; 6H1H; -.
DR   PDBsum; 6H1I; -.
DR   PDBsum; 6N0J; -.
DR   PDBsum; 6N0K; -.
DR   AlphaFoldDB; O00625; -.
DR   SMR; O00625; -.
DR   BioGRID; 114114; 82.
DR   IntAct; O00625; 6.
DR   MINT; O00625; -.
DR   STRING; 9606.ENSP00000369786; -.
DR   BindingDB; O00625; -.
DR   ChEMBL; CHEMBL2010627; -.
DR   iPTMnet; O00625; -.
DR   PhosphoSitePlus; O00625; -.
DR   BioMuta; PIR; -.
DR   EPD; O00625; -.
DR   jPOST; O00625; -.
DR   MassIVE; O00625; -.
DR   MaxQB; O00625; -.
DR   PaxDb; 9606-ENSP00000369786; -.
DR   PeptideAtlas; O00625; -.
DR   ProteomicsDB; 47999; -.
DR   Pumba; O00625; -.
DR   TopDownProteomics; O00625; -.
DR   Antibodypedia; 358; 225 antibodies from 31 providers.
DR   DNASU; 8544; -.
DR   Ensembl; ENST00000380420.10; ENSP00000369785.5; ENSG00000087842.11.
DR   Ensembl; ENST00000380421.3; ENSP00000369786.3; ENSG00000087842.11.
DR   GeneID; 8544; -.
DR   KEGG; hsa:8544; -.
DR   MANE-Select; ENST00000380420.10; ENSP00000369785.5; NM_001018109.3; NP_001018119.1.
DR   UCSC; uc004cwu.5; human.
DR   AGR; HGNC:30048; -.
DR   CTD; 8544; -.
DR   DisGeNET; 8544; -.
DR   GeneCards; PIR; -.
DR   HGNC; HGNC:30048; PIR.
DR   HPA; ENSG00000087842; Low tissue specificity.
DR   MIM; 300931; gene.
DR   neXtProt; NX_O00625; -.
DR   OpenTargets; ENSG00000087842; -.
DR   PharmGKB; PA134870022; -.
DR   VEuPathDB; HostDB:ENSG00000087842; -.
DR   eggNOG; ENOG502QQ5A; Eukaryota.
DR   GeneTree; ENSGT00390000008044; -.
DR   HOGENOM; CLU_045717_0_1_1; -.
DR   InParanoid; O00625; -.
DR   OMA; TPWHPHR; -.
DR   OrthoDB; 47035at2759; -.
DR   PhylomeDB; O00625; -.
DR   TreeFam; TF300002; -.
DR   PathwayCommons; O00625; -.
DR   Reactome; R-HSA-8935690; Digestion.
DR   SignaLink; O00625; -.
DR   UniPathway; UPA00724; -.
DR   BioGRID-ORCS; 8544; 4 hits in 783 CRISPR screens.
DR   ChiTaRS; PIR; human.
DR   EvolutionaryTrace; O00625; -.
DR   GeneWiki; PIR_(gene); -.
DR   GenomeRNAi; 8544; -.
DR   Pharos; O00625; Tchem.
DR   PRO; PR:O00625; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; O00625; Protein.
DR   Bgee; ENSG00000087842; Expressed in C1 segment of cervical spinal cord and 186 other cell types or tissues.
DR   ExpressionAtlas; O00625; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR   GO; GO:0008127; F:quercetin 2,3-dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB.
DR   GO; GO:0007586; P:digestion; TAS:Reactome.
DR   GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR   CDD; cd20288; cupin_pirin-like_C; 1.
DR   CDD; cd02909; cupin_pirin_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012093; Pirin.
DR   InterPro; IPR008778; Pirin_C_dom.
DR   InterPro; IPR003829; Pirin_N_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR13903:SF8; PIRIN; 1.
DR   PANTHER; PTHR13903; PIRIN-RELATED; 1.
DR   Pfam; PF02678; Pirin; 1.
DR   Pfam; PF05726; Pirin_C; 1.
DR   PIRSF; PIRSF006232; Pirin; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   UCD-2DPAGE; O00625; -.
DR   Genevisible; O00625; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..290
FT                   /note="Pirin"
FT                   /id="PRO_0000214051"
FT   BINDING         56
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:14573596,
FT                   ECO:0000269|PubMed:20711196, ECO:0007744|PDB:1J1L,
FT                   ECO:0007744|PDB:3ACL"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:14573596,
FT                   ECO:0000269|PubMed:20711196, ECO:0007744|PDB:1J1L,
FT                   ECO:0007744|PDB:3ACL"
FT   BINDING         101
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:14573596,
FT                   ECO:0000269|PubMed:20711196, ECO:0007744|PDB:1J1L,
FT                   ECO:0007744|PDB:3ACL"
FT   BINDING         103
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000269|PubMed:14573596,
FT                   ECO:0000269|PubMed:20711196, ECO:0007744|PDB:1J1L,
FT                   ECO:0007744|PDB:3ACL"
FT   VARIANT         228
FT                   /note="V -> A (in dbSNP:rs34104000)"
FT                   /id="VAR_050543"
FT   CONFLICT        24
FT                   /note="V -> D (in Ref. 2; CAG46621)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="K -> R (in Ref. 2; CAG46621)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..12
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:5JCT"
FT   STRAND          39..47
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          52..67
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:6N0J"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          111..119
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          130..134
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          147..156
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          169..176
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          191..199
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          201..204
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:6H1I"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          216..220
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          222..229
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          236..243
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          251..253
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   HELIX           261..273
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   HELIX           279..281
FT                   /evidence="ECO:0007829|PDB:6N0K"
FT   TURN            287..289
FT                   /evidence="ECO:0007829|PDB:4EWA"
SQ   SEQUENCE   290 AA;  32113 MW;  D06AC100F356496D CRC64;
     MGSSKKVTLS VLSREQSEGV GARVRRSIGR PELKNLDPFL LFDEFKGGRP GGFPDHPHRG
     FETVSYLLEG GSMAHEDFCG HTGKMNPGDL QWMTAGRGIL HAEMPCSEEP AHGLQLWVNL
     RSSEKMVEPQ YQELKSEEIP KPSKDGVTVA VISGEALGIK SKVYTRTPTL YLDFKLDPGA
     KHSQPIPKGW TSFIYTISGD VYIGPDDAQQ KIEPHHTAVL GEGDSVQVEN KDPKRSHFVL
     IAGEPLREPV IQHGPFVMNT NEEISQAILD FRNAKNGFER AKTWKSKIGN
//