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   27-MAR-2024, entry version 169.
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 BMAL1 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 BMAL1 and CLOCK by
CC       inhibiting GSK3B-mediated phosphorylation and ubiquitination-dependent
CC       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 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; 13.
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; 9606-ENSP00000349208; -.
DR   PeptideAtlas; Q8TC59; -.
DR   ProteomicsDB; 74093; -. [Q8TC59-1]
DR   ProteomicsDB; 74094; -. [Q8TC59-2]
DR   Antibodypedia; 22585; 320 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   AGR; HGNC:17644; -.
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; CILNTAN; -.
DR   OrthoDB; 3060088at2759; -.
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; 16 hits in 1149 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 male germ line stem cell (sensu Vertebrata) in testis and 136 other cell types or tissues.
DR   ExpressionAtlas; Q8TC59; baseline and differential.
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: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:0004521; F:RNA endonuclease activity; 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:0048477; P:oogenesis; ISS:UniProtKB.
DR   GO; GO:0141006; P:piRNA-mediated retrotransposon silencing by heterochromatin formation; 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:0031047; P:regulatory ncRNA-mediated gene silencing; ISS:UniProtKB.
DR   GO; GO:0141005; P:retrotransposon silencing by heterochromatin formation; ISS:UniProtKB.
DR   GO; GO:0141008; P:retrotransposon silencing by mRNA destabilization; IEA:Ensembl.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0140965; P:secondary piRNA processing; IEA:Ensembl.
DR   GO; GO:0141007; P:siRNA-mediated retrotransposon silencing by heterochromatin formation; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   CDD; cd02845; PAZ_piwi_like; 1.
DR   CDD; cd04658; Piwi_piwi-like_Euk; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 2.170.260.10; paz domain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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   PANTHER; PTHR22891; EUKARYOTIC TRANSLATION INITIATION FACTOR 2C; 1.
DR   PANTHER; PTHR22891:SF187; PIWI-LIKE PROTEIN 2; 1.
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; PAZ domain; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS50822; PIWI; 1.
DR   Genevisible; Q8TC59; HS.
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          389..502
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
//