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Database: UniProt
Entry: O43660
LinkDB: O43660
Original site: O43660 
ID   PLRG1_HUMAN             Reviewed;         514 AA.
AC   O43660; B3KMK4; Q3KQY5; Q8WUD8;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   29-SEP-2021, entry version 184.
DE   RecName: Full=Pleiotropic regulator 1;
GN   Name=PLRG1;
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=9765207; DOI=10.1101/gad.12.19.3059;
RA   Nemeth K., Salchert K., Putnoky P., Bhalerao R., Koncz-Kalman Z.,
RA   Stankovic-Stangeland B., Bako L., Mathur J., Oekresz L., Stabel S.,
RA   Geigenberger P., Stitt M., Redei G.P., Schell J., Koncz C.;
RT   "Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD
RT   protein, in Arabidopsis.";
RL   Genes Dev. 12:3059-3073(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [5]
RP   PROTEIN SEQUENCE OF 8-41; 48-62; 69-113; 117-135; 141-180; 199-226;
RP   238-250; 258-268; 283-308; 321-355; 377-396; 443-449 AND 488-510,
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH CDC5L AND THE SPLICEOSOME.
RX   PubMed=11101529; DOI=10.1093/emboj/19.23.6569;
RA   Ajuh P., Kuster B., Panov K., Zomerdijk J.C.B.M., Mann M., Lamond A.I.;
RT   "Functional analysis of the human CDC5L complex and identification of its
RT   components by mass spectrometry.";
RL   EMBO J. 19:6569-6581(2000).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDC5L AND THE
RP   SPLICEOSOME.
RX   PubMed=11544257; DOI=10.1074/jbc.m105453200;
RA   Ajuh P., Sleeman J., Chusainow J., Lamond A.I.;
RT   "A direct interaction between the carboxyl-terminal region of CDC5L and the
RT   WD40 domain of PLRG1 is essential for pre-mRNA splicing.";
RL   J. Biol. Chem. 276:42370-42381(2001).
RN   [7]
RP   PROTEIN SEQUENCE OF 81-113 AND 450-476, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND INTERACTION WITH THE SPLICEOSOME.
RX   PubMed=12176931; DOI=10.1101/gr.473902;
RA   Rappsilber J., Ryder U., Lamond A.I., Mann M.;
RT   "Large-scale proteomic analysis of the human spliceosome.";
RL   Genome Res. 12:1231-1245(2002).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX,
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH CDC5L; PRPF19 AND BCAS2.
RX   PubMed=20176811; DOI=10.1128/mcb.01505-09;
RA   Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A.,
RA   Fischle W., Urlaub H., Luhrmann R.;
RT   "Molecular architecture of the human Prp19/CDC5L complex.";
RL   Mol. Cell. Biol. 30:2105-2119(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-201 AND SER-391, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [11] {ECO:0007744|PDB:4YVD}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 141-514.
RA   Zeng H., Dong A., Xu C., Tempel W., Li Y., He H., Bountra C.,
RA   Arrowsmith C.H., Edwards A.M., Brown P.J., Min J., Wu H.;
RT   "Crystal structure of human Pleiotropic Regulator 1 (PRL1).";
RL   Submitted (MAR-2015) to the PDB data bank.
RN   [12] {ECO:0007744|PDB:5XJC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA   Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT   "An Atomic Structure of the Human Spliceosome.";
RL   Cell 169:918-929(2017).
RN   [13] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28076346; DOI=10.1038/nature21079;
RA   Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA   Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT   "Cryo-EM structure of a human spliceosome activated for step 2 of
RT   splicing.";
RL   Nature 542:318-323(2017).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC       (PubMed:28502770, PubMed:28076346). Component of the PRP19-CDC5L
CC       complex that forms an integral part of the spliceosome and is required
CC       for activating pre-mRNA splicing (PubMed:11101529, PubMed:11544257).
CC       {ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:11544257,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:12176931,
CC       PubMed:28502770, PubMed:28076346). Component of the PRP19-CDC5L
CC       splicing complex composed of a core complex comprising a homotetramer
CC       of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably
CC       associated proteins CTNNBL1, CWC15 and HSPA8 (PubMed:11101529,
CC       PubMed:20176811). Interacts (via its WD40 repeat domain) directly with
CC       CDC5L (via its C-terminal); the interaction is required for mRNA
CC       splicing but not for spliceosome assembly (PubMed:11544257). Also
CC       interacts directly in the complex with BCAS2 and PRPF19
CC       (PubMed:20176811). {ECO:0000269|PubMed:11101529,
CC       ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:12176931,
CC       ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770}.
CC   -!- INTERACTION:
CC       O43660; P52272: HNRNPM; NbExp=5; IntAct=EBI-1051504, EBI-486809;
CC       O43660-2; P54253: ATXN1; NbExp=3; IntAct=EBI-11743883, EBI-930964;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11101529,
CC       ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770}. Nucleus speckle
CC       {ECO:0000269|PubMed:11544257}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O43660-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43660-2; Sequence=VSP_008804;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the WD repeat PRL1/PRL2 family. {ECO:0000305}.
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DR   EMBL; AF044333; AAD09407.1; -; mRNA.
DR   EMBL; AK002108; BAG51016.1; -; mRNA.
DR   EMBL; CH471056; EAX04941.1; -; Genomic_DNA.
DR   EMBL; BC020786; AAH20786.1; -; mRNA.
DR   EMBL; BC106004; AAI06005.1; -; mRNA.
DR   CCDS; CCDS34083.1; -. [O43660-1]
DR   CCDS; CCDS56341.1; -. [O43660-2]
DR   RefSeq; NP_001188493.1; NM_001201564.1. [O43660-2]
DR   RefSeq; NP_002660.1; NM_002669.3. [O43660-1]
DR   PDB; 4YVD; X-ray; 1.70 A; A=141-514.
DR   PDB; 5MQF; EM; 5.90 A; D=1-514.
DR   PDB; 5XJC; EM; 3.60 A; T=1-514.
DR   PDB; 5YZG; EM; 4.10 A; T=1-514.
DR   PDB; 5Z56; EM; 5.10 A; T=1-514.
DR   PDB; 5Z57; EM; 6.50 A; T=1-514.
DR   PDB; 5Z58; EM; 4.90 A; T=1-514.
DR   PDB; 6FF4; EM; 16.00 A; D=1-514.
DR   PDB; 6FF7; EM; 4.50 A; D=1-514.
DR   PDB; 6ICZ; EM; 3.00 A; T=1-514.
DR   PDB; 6ID0; EM; 2.90 A; T=1-514.
DR   PDB; 6ID1; EM; 2.86 A; T=1-514.
DR   PDB; 6QDV; EM; 3.30 A; J=185-504.
DR   PDB; 6ZYM; EM; 3.40 A; D=1-514.
DR   PDB; 7AAV; EM; 4.20 A; G=1-514.
DR   PDB; 7ABF; EM; 3.90 A; G=1-514.
DR   PDB; 7ABG; EM; 7.80 A; G=1-514.
DR   PDB; 7ABI; EM; 8.00 A; G=1-514.
DR   PDB; 7DH6; X-ray; 2.58 A; A/B/C/D=140-514.
DR   PDB; 7DVQ; EM; 2.89 A; T=1-514.
DR   PDBsum; 4YVD; -.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5XJC; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 5Z58; -.
DR   PDBsum; 6FF4; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 6QDV; -.
DR   PDBsum; 6ZYM; -.
DR   PDBsum; 7AAV; -.
DR   PDBsum; 7ABF; -.
DR   PDBsum; 7ABG; -.
DR   PDBsum; 7ABI; -.
DR   PDBsum; 7DH6; -.
DR   PDBsum; 7DVQ; -.
DR   SMR; O43660; -.
DR   BioGRID; 111370; 135.
DR   ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR   CORUM; O43660; -.
DR   IntAct; O43660; 58.
DR   MINT; O43660; -.
DR   STRING; 9606.ENSP00000424417; -.
DR   GlyGen; O43660; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O43660; -.
DR   MetOSite; O43660; -.
DR   PhosphoSitePlus; O43660; -.
DR   SwissPalm; O43660; -.
DR   BioMuta; PLRG1; -.
DR   EPD; O43660; -.
DR   jPOST; O43660; -.
DR   MassIVE; O43660; -.
DR   MaxQB; O43660; -.
DR   PaxDb; O43660; -.
DR   PeptideAtlas; O43660; -.
DR   PRIDE; O43660; -.
DR   ProteomicsDB; 49091; -. [O43660-1]
DR   ProteomicsDB; 49092; -. [O43660-2]
DR   Antibodypedia; 16702; 249 antibodies.
DR   DNASU; 5356; -.
DR   Ensembl; ENST00000302078; ENSP00000303191; ENSG00000171566. [O43660-2]
DR   Ensembl; ENST00000499023; ENSP00000424417; ENSG00000171566. [O43660-1]
DR   GeneID; 5356; -.
DR   KEGG; hsa:5356; -.
DR   UCSC; uc003iny.4; human. [O43660-1]
DR   CTD; 5356; -.
DR   DisGeNET; 5356; -.
DR   GeneCards; PLRG1; -.
DR   HGNC; HGNC:9089; PLRG1.
DR   HPA; ENSG00000171566; Low tissue specificity.
DR   MIM; 605961; gene.
DR   neXtProt; NX_O43660; -.
DR   OpenTargets; ENSG00000171566; -.
DR   PharmGKB; PA33416; -.
DR   VEuPathDB; HostDB:ENSG00000171566; -.
DR   eggNOG; KOG0285; Eukaryota.
DR   GeneTree; ENSGT00940000155316; -.
DR   HOGENOM; CLU_000288_72_2_1; -.
DR   InParanoid; O43660; -.
DR   OMA; FAMCFDQ; -.
DR   OrthoDB; 1157847at2759; -.
DR   PhylomeDB; O43660; -.
DR   TreeFam; TF105684; -.
DR   PathwayCommons; O43660; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; O43660; -.
DR   SIGNOR; O43660; -.
DR   BioGRID-ORCS; 5356; 708 hits in 1019 CRISPR screens.
DR   ChiTaRS; PLRG1; human.
DR   GeneWiki; PLRG1; -.
DR   GenomeRNAi; 5356; -.
DR   Pharos; O43660; Tbio.
DR   PRO; PR:O43660; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; O43660; protein.
DR   Bgee; ENSG00000171566; Expressed in secondary oocyte and 216 other tissues.
DR   ExpressionAtlas; O43660; baseline and differential.
DR   Genevisible; O43660; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Spliceosome; WD repeat.
FT   CHAIN           1..514
FT                   /note="Pleiotropic regulator 1"
FT                   /id="PRO_0000051133"
FT   REPEAT          202..241
FT                   /note="WD 1"
FT   REPEAT          244..283
FT                   /note="WD 2"
FT   REPEAT          286..325
FT                   /note="WD 3"
FT   REPEAT          328..367
FT                   /note="WD 4"
FT   REPEAT          370..410
FT                   /note="WD 5"
FT   REPEAT          411..449
FT                   /note="WD 6"
FT   REPEAT          460..499
FT                   /note="WD 7"
FT   REGION          135..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         96..104
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_008804"
FT   STRAND          194..200
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          207..212
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          216..223
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          238..242
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          249..254
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          256..265
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          270..274
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            275..278
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          279..283
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          291..296
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          298..307
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          310..316
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            317..319
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          322..327
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          333..338
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          340..343
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          345..349
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          354..358
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            359..362
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          363..368
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          377..380
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          384..390
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          395..399
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            400..403
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          404..409
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          416..421
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            423..425
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   STRAND          426..431
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          436..440
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            441..443
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          446..450
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          456..458
FT                   /evidence="ECO:0007829|PDB:6ID0"
FT   HELIX           460..462
FT                   /evidence="ECO:0007829|PDB:6ID1"
FT   STRAND          465..470
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   STRAND          472..475
FT                   /evidence="ECO:0007829|PDB:6FF4"
FT   STRAND          476..481
FT                   /evidence="ECO:0007829|PDB:4YVD"
FT   TURN            482..484
FT                   /evidence="ECO:0007829|PDB:6ICZ"
FT   STRAND          486..491
FT                   /evidence="ECO:0007829|PDB:4YVD"
SQ   SEQUENCE   514 AA;  57194 MW;  8C914CAF5F7887BD CRC64;
     MVEEVQKHSV HTLVFRSLKR THDMFVADNG KPVPLDEESH KRKMAIKLRN EYGPVLHMPT
     SKENLKEKGP QNATDSYVHK QYPANQGQEV EYFVAGTHPY PPGPGVALTA DTKIQRMPSE
     SAAQSLAVAL PLQTKADANR TAPSGSEYRH PGASDRPQPT AMNSIVMETG NTKNSALMAK
     KAPTMPKPQW HPPWKLYRVI SGHLGWVRCI AVEPGNQWFV TGSADRTIKI WDLASGKLKL
     SLTGHISTVR GVIVSTRSPY LFSCGEDKQV KCWDLEYNKV IRHYHGHLSA VYGLDLHPTI
     DVLVTCSRDS TARIWDVRTK ASVHTLSGHT NAVATVRCQA AEPQIITGSH DTTIRLWDLV
     AGKTRVTLTN HKKSVRAVVL HPRHYTFASG SPDNIKQWKF PDGSFIQNLS GHNAIINTLT
     VNSDGVLVSG ADNGTMHLWD WRTGYNFQRV HAAVQPGSLD SESGIFACAF DQSESRLLTA
     EADKTIKVYR EDDTATEETH PVSWKPEIIK RKRF
//
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