PIWL2_HUMAN
ID PIWL2_HUMAN Reviewed; 973 AA.
AC Q8TC59; A8K4S3; A8K8S5; B0AZN9; B0AZP2; B4DR22; E7ECA4; Q96SW6; Q9NW28;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Piwi-like protein 2;
DE EC=3.1.26.- {ECO:0000250|UniProtKB:Q8CDG1};
DE AltName: Full=Cancer/testis antigen 80;
DE Short=CT80;
GN Name=PIWIL2; Synonyms=HILI;
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=12906857; DOI=10.1016/s0888-7543(03)00129-0;
RA Sasaki T., Shiohama A., Minoshima S., Shimizu N.;
RT "Identification of eight members of the Argonaute family in the human
RT genome.";
RL Genomics 82:323-330(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Zhang K., Lu Y., Li C.;
RT "Identification of piwil2-like (PL2L106) protein in HeLa cells.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16377660; DOI=10.1093/hmg/ddi430;
RA Lee J.H., Schutte D., Wulf G., Fuzesi L., Radzun H.-J., Schweyer S.,
RA Engel W., Nayernia K.;
RT "Stem-cell protein Piwil2 is widely expressed in tumors and inhibits
RT apoptosis through activation of Stat3/Bcl-XL pathway.";
RL Hum. Mol. Genet. 15:201-211(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH ARNTL AND CLOCK.
RX PubMed=28903391; DOI=10.18632/oncotarget.18973;
RA Lu Y., Zheng X., Hu W., Bian S., Zhang Z., Tao D., Liu Y., Ma Y.;
RT "Cancer/testis antigen PIWIL2 suppresses circadian rhythms by regulating
RT the stability and activity of BMAL1 and CLOCK.";
RL Oncotarget 8:54913-54924(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 387-525, AND RNA-BINDING.
RX PubMed=21193640; DOI=10.1073/pnas.1017762108;
RA Tian Y., Simanshu D.K., Ma J.B., Patel D.J.;
RT "Structural basis for piRNA 2'-O-methylated 3'-end recognition by Piwi PAZ
RT (Piwi/Argonaute/Zwille) domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:903-910(2011).
CC -!- FUNCTION: Endoribonuclease that plays a central role during
CC spermatogenesis by repressing transposable elements and preventing
CC their mobilization, which is essential for the germline integrity (By
CC similarity). Plays an essential role in meiotic differentiation of
CC spermatocytes, germ cell differentiation and in self-renewal of
CC spermatogonial stem cells (By similarity). Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC govern the methylation and subsequent repression of transposons (By
CC similarity). During piRNA biosynthesis, plays a key role in the piRNA
CC amplification loop, also named ping-pong amplification cycle, by acting
CC as a 'slicer-competent' piRNA endoribonuclease that cleaves primary
CC piRNAs, which are then loaded onto 'slicer-incompetent' PIWIL4 (By
CC similarity). PIWIL2 slicing produces a pre-miRNA intermediate, which is
CC then processed in mature piRNAs, and as well as a 16 nucleotide by-
CC product that is degraded (By similarity). Required for PIWIL4/MIWI2
CC nuclear localization and association with secondary piRNAs antisense
CC (By similarity). Besides their function in transposable elements
CC repression, piRNAs are probably involved in other processes during
CC meiosis such as translation regulation (By similarity). Indirectly
CC modulates expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7,
CC THY1, CD9 and STRA8 (By similarity). When overexpressed, acts as an
CC oncogene by inhibition of apoptosis and promotion of proliferation in
CC tumors (PubMed:16377660). Represses circadian rhythms by promoting the
CC stability and activity of core clock components ARNTL/BMAL1 and CLOCK
CC by inhibiting GSK3B-mediated phosphorylation and ubiquitination-
CC dependent degradation of these proteins (PubMed:28903391).
CC {ECO:0000250|UniProtKB:Q8CDG1, ECO:0000269|PubMed:16377660,
CC ECO:0000269|PubMed:28903391}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9JMB7};
CC -!- SUBUNIT: Interacts with DDX4, MAEL, EIF3A, EIF4E, EIF4G, PRMT5 and
CC WDR77 (By similarity). Associates with EIF4E- and EIF4G-containing m7G
CC cap-binding complexes (By similarity). Interacts (when methylated on
CC arginine residues) with TDRD1 and TDRKH/TDRD2 (By similarity).
CC Interacts with TDRD12 (By similarity). Component of the PET complex, at
CC least composed of EXD1, PIWIL2, TDRD12 and piRNAs (By similarity).
CC Interacts with MOV10L1 (By similarity). Interacts with GPAT2 (By
CC similarity). Interacts with TEX19 (By similarity). Interacts with GSK3B
CC (By similarity). Interacts (via PIWI domain) with ARNTL/BMAL1 and CLOCK
CC (PubMed:28903391). Interacts with TEX15 (By similarity).
CC {ECO:0000250|UniProtKB:Q8CDG1, ECO:0000269|PubMed:28903391}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8CDG1}.
CC Note=Present in chromatoid body. Probable component of the meiotic
CC nuage, also named P granule, a germ-cell-specific organelle required to
CC repress transposon activity during meiosis.
CC {ECO:0000250|UniProtKB:Q8CDG1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TC59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TC59-2; Sequence=VSP_036664;
CC -!- TISSUE SPECIFICITY: Expressed in adult testis and in most tumors.
CC {ECO:0000269|PubMed:16377660}.
CC -!- PTM: Arginine methylation by PRMT5 is required for the interaction with
CC Tudor domain-containing protein TDRD1 and subsequent localization to
CC the meiotic nuage, also named P granule.
CC {ECO:0000250|UniProtKB:Q8CDG1}.
CC -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91558.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55155.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB079367; BAC81342.1; -; mRNA.
DR EMBL; HQ651229; ADV17663.1; -; mRNA.
DR EMBL; AK001213; BAA91558.1; ALT_INIT; mRNA.
DR EMBL; AK027497; BAB55155.1; ALT_SEQ; mRNA.
DR EMBL; AK291038; BAF83727.1; -; mRNA.
DR EMBL; AK292440; BAF85129.1; -; mRNA.
DR EMBL; AK299068; BAG61134.1; -; mRNA.
DR EMBL; AK315830; BAF98721.1; -; mRNA.
DR EMBL; AK315833; BAF98724.1; -; mRNA.
DR EMBL; BC025995; AAH25995.1; -; mRNA.
DR EMBL; BC111751; AAI11752.1; -; mRNA.
DR CCDS; CCDS6029.1; -. [Q8TC59-1]
DR CCDS; CCDS83261.1; -. [Q8TC59-2]
DR RefSeq; NP_001129193.1; NM_001135721.1. [Q8TC59-1]
DR RefSeq; NP_001317409.1; NM_001330480.1. [Q8TC59-2]
DR RefSeq; NP_060538.2; NM_018068.3. [Q8TC59-1]
DR PDB; 3O7X; X-ray; 2.92 A; A/B/C/D=387-525.
DR PDB; 3QIR; X-ray; 2.45 A; A/B/C/D=386-533.
DR PDBsum; 3O7X; -.
DR PDBsum; 3QIR; -.
DR AlphaFoldDB; Q8TC59; -.
DR SMR; Q8TC59; -.
DR BioGRID; 120431; 10.
DR IntAct; Q8TC59; 9.
DR STRING; 9606.ENSP00000349208; -.
DR iPTMnet; Q8TC59; -.
DR PhosphoSitePlus; Q8TC59; -.
DR BioMuta; PIWIL2; -.
DR DMDM; 74730558; -.
DR EPD; Q8TC59; -.
DR jPOST; Q8TC59; -.
DR MassIVE; Q8TC59; -.
DR MaxQB; Q8TC59; -.
DR PaxDb; Q8TC59; -.
DR PeptideAtlas; Q8TC59; -.
DR PRIDE; Q8TC59; -.
DR ProteomicsDB; 74093; -. [Q8TC59-1]
DR ProteomicsDB; 74094; -. [Q8TC59-2]
DR Antibodypedia; 22585; 257 antibodies from 34 providers.
DR DNASU; 55124; -.
DR Ensembl; ENST00000356766.11; ENSP00000349208.6; ENSG00000197181.12. [Q8TC59-1]
DR Ensembl; ENST00000454009.6; ENSP00000406956.2; ENSG00000197181.12. [Q8TC59-1]
DR Ensembl; ENST00000521356.5; ENSP00000428267.1; ENSG00000197181.12. [Q8TC59-2]
DR Ensembl; ENST00000611073.1; ENSP00000478103.1; ENSG00000197181.12. [Q8TC59-2]
DR GeneID; 55124; -.
DR KEGG; hsa:55124; -.
DR MANE-Select; ENST00000356766.11; ENSP00000349208.6; NM_018068.5; NP_060538.2.
DR UCSC; uc011kzf.2; human. [Q8TC59-1]
DR CTD; 55124; -.
DR DisGeNET; 55124; -.
DR GeneCards; PIWIL2; -.
DR HGNC; HGNC:17644; PIWIL2.
DR HPA; ENSG00000197181; Tissue enriched (testis).
DR MIM; 610312; gene.
DR neXtProt; NX_Q8TC59; -.
DR OpenTargets; ENSG00000197181; -.
DR PharmGKB; PA38461; -.
DR VEuPathDB; HostDB:ENSG00000197181; -.
DR eggNOG; KOG1042; Eukaryota.
DR GeneTree; ENSGT00950000183200; -.
DR HOGENOM; CLU_008813_0_0_1; -.
DR InParanoid; Q8TC59; -.
DR OMA; CLPFYNV; -.
DR PhylomeDB; Q8TC59; -.
DR TreeFam; TF354206; -.
DR PathwayCommons; Q8TC59; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q8TC59; -.
DR BioGRID-ORCS; 55124; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; PIWIL2; human.
DR GenomeRNAi; 55124; -.
DR Pharos; Q8TC59; Tbio.
DR PRO; PR:Q8TC59; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8TC59; protein.
DR Bgee; ENSG00000197181; Expressed in secondary oocyte and 135 other tissues.
DR ExpressionAtlas; Q8TC59; baseline and differential.
DR Genevisible; Q8TC59; HS.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0097433; C:dense body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0010370; C:perinucleolar chromocenter; IEA:Ensembl.
DR GO; GO:1990923; C:PET complex; ISS:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0034584; F:piRNA binding; IDA:UniProtKB.
DR GO; GO:1905538; F:polysome binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0071442; P:positive regulation of histone H3-K14 acetylation; IEA:Ensembl.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IEA:Ensembl.
DR GO; GO:0060903; P:positive regulation of meiosis I; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0000966; P:RNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Cytoplasm;
KW Developmental protein; Differentiation; Endonuclease; Hydrolase; Meiosis;
KW Metal-binding; Methylation; Nuclease; Oogenesis; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing; Spermatogenesis;
KW Translation regulation.
FT CHAIN 1..973
FT /note="Piwi-like protein 2"
FT /id="PRO_0000234569"
FT DOMAIN 384..496
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 668..959
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 28..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 745
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 783
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 815
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT ACT_SITE 948
FT /evidence="ECO:0000250|UniProtKB:A8D8P8"
FT MOD_RES 47
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 76
FT /note="Omega-N-methylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 76
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 97
FT /note="Omega-N-methylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 97
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 102
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 102
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 146
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 158
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 165
FT /note="Symmetric dimethylarginine; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT MOD_RES 551
FT /note="Symmetric dimethylarginine; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:Q8CDG1"
FT VAR_SEQ 887..922
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_036664"
FT CONFLICT 18
FT /note="Q -> R (in Ref. 3; BAG61134)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="I -> T (in Ref. 3; BAF98721)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="K -> N (in Ref. 3; BAA91558)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="Q -> R (in Ref. 3; BAF98724)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="V -> G (in Ref. 3; BAF83727)"
FT /evidence="ECO:0000305"
FT CONFLICT 961
FT /note="E -> G (in Ref. 3; BAB55155)"
FT /evidence="ECO:0000305"
FT HELIX 390..413
FT /evidence="ECO:0007829|PDB:3QIR"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:3QIR"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:3QIR"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:3QIR"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3QIR"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:3QIR"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:3QIR"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:3QIR"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:3QIR"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:3O7X"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:3O7X"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3QIR"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:3QIR"
SQ SEQUENCE 973 AA; 109849 MW; C44398136B144CA0 CRC64;
MDPFRPSFRG QSPIHPSQCQ AVRMPGCWPQ ASKPLDPALG RGAPAGRGHV FGKPEEPSTQ
RGPAQRESVG LVSMFRGLGI ETVSKTPLKR EMLPSGRGIL GRGLSANLVR KDREELSPTF
WDPKVLAAGD SKMAETSVGW SRTLGRGSSD ASLLPLGRAA GGISREVDKP PCTFSTPSRG
PPQLSSPPAL PQSPLHSPDR PLVLTVEHKE KELIVKQGSK GTPQSLGLNL VKIQCHNEAV
YQYHVTFSPN VECKSMRFGM LKDHQAVTGN VTAFDGSILY LPVKLQQVLE LKSQRKTDSA
EISIKIQMTK ILEPCSDLCI PFYNVVFRRV MKLLDMKLVG RNFYDPTSAM VLQQHRLQIW
PGYAASIRRT DGGLFLLADV SHKVIRNDCV LDVMHAIYQQ NKEHFQDECT KLLVGNIVIT
RYNNRTYRID DVDWNKTPKD SFTMSDGKEI TFLEYYSKNY GITVKEEDQP LLIHRPSERQ
DNHGMLLKGE ILLLPELSFM TGIPEKMKKD FRAMKDLAQQ INLSPKQHHS ALECLLQRIA
KNEAATNELM RWGLRLQKDV HKIEGRVLPM ERINLKNTSF ITSQELNWVK EVTRDPSILT
IPMHFWALFY PKRAMDQARE LVNMLEKIAG PIGMRMSPPA WVELKDDRIE TYVRTIQSTL
GAEGKIQMVV CIIMGPRDDL YGAIKKLCCV QSPVPSQVVN VRTIGQPTRL RSVAQKILLQ
INCKLGGELW GVDIPLKQLM VIGMDVYHDP SRGMRSVVGF VASINLTLTK WYSRVVFQMP
HQEIVDSLKL CLVGSLKKFY EVNHCLPEKI VVYRDGVSDG QLKTVANYEI PQLQKCFEAF
ENYQPKMVVF VVQKKISTNL YLAAPQNFVT PTPGTVVDHT ITSCEWVDFY LLAHHVRQGC
GIPTHYVCVL NTANLSPDHM QRLTFKLCHM YWNWPGTIRV PAPCKYAHKL AFLSGHILHH
EPAIQLCENL FFL
