PUM2_MOUSE
ID PUM2_MOUSE Reviewed; 1066 AA.
AC Q80U58; Q80UZ9; Q91YW4; Q925A0; Q9ERC7;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Pumilio homolog 2;
GN Name=Pum2; Synonyms=Kiaa0235;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11780640;
RA White E.K., Moore-Jarrett T., Ruley H.E.;
RT "PUM2, a novel murine puf protein, and its consensus RNA-binding site.";
RL RNA 7:1855-1866(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12667987; DOI=10.1016/s1079-9796(03)00003-2;
RA Spassov D.S., Jurecic R.;
RT "Mouse Pum1 and Pum2 genes, members of the Pumilio family of RNA-binding
RT proteins, show differential expression in fetal and adult hematopoietic
RT stem cells and progenitors.";
RL Blood Cells Mol. Dis. 30:55-69(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary tumor;
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 NANOS3, AND TISSUE SPECIFICITY.
RX PubMed=18089289; DOI=10.1016/j.ydbio.2007.11.011;
RA Lolicato F., Marino R., Paronetto M.P., Pellegrini M., Dolci S.,
RA Geremia R., Grimaldi P.;
RT "Potential role of Nanos3 in maintaining the undifferentiated spermatogonia
RT population.";
RL Dev. Biol. 313:725-738(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-136 AND SER-587, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19861488; DOI=10.1530/rep-09-0373;
RA Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.;
RT "Functional reconstruction of NANOS3 expression in the germ cell lineage by
RT a novel transgenic reporter reveals distinct subcellular localizations of
RT NANOS3.";
RL Reproduction 139:381-393(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 706-1056.
RX PubMed=19540345; DOI=10.1016/j.jsb.2009.06.007;
RA Jenkins H.T., Baker-Wilding R., Edwards T.A.;
RT "Structure and RNA binding of the mouse Pumilio-2 Puf domain.";
RL J. Struct. Biol. 167:271-276(2009).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that acts as a post-
CC transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds
CC to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-
CC UGUANAUA-3', that is related to the Nanos Response Element (NRE).
CC Mediates post-transcriptional repression of transcripts via different
CC mechanisms: acts via direct recruitment of the CCR4-POP2-NOT
CC deadenylase leading to translational inhibition and mRNA degradation.
CC Also mediates deadenylation-independent repression by promoting
CC accessibility of miRNAs. Acts as a post-transcriptional repressor of
CC E2F3 mRNAs by binding to its 3'-UTR and facilitating miRNA regulation.
CC Plays a role in cytoplasmic sensing of viral infection. Represses a
CC program of genes necessary to maintain genomic stability such as key
CC mitotic, DNA repair and DNA replication factors. Its ability to repress
CC those target mRNAs is regulated by the lncRNA NORAD (non-coding RNA
CC activated by DNA damage) which, due to its high abundance and multitude
CC of PUMILIO binding sites, is able to sequester a significant fraction
CC of PUM1 and PUM2 in the cytoplasm. May regulate DCUN1D3 mRNA levels.
CC May support proliferation and self-renewal of stem cells. Binds
CC specifically to miRNA MIR199A precursor, with PUM1, regulates miRNA
CC MIR199A expression at a postranscriptional level (By similarity).
CC {ECO:0000250|UniProtKB:Q8TB72}.
CC -!- SUBUNIT: Homodimer; homodimerizes in vitro. Interacts with DAZ1, DAZL
CC and NANOS1 via its pumilio repeats. Interacts with NANOS3 (By
CC similarity). Interacts with SNAPIN. Recruits the CCR4-POP2-NOT
CC deadenylase leading to translational inhibition and mRNA degradation.
CC Interacts with DDX20. In case of viral infection, interacts with DHX58
CC (By similarity). {ECO:0000250|UniProtKB:Q8TB72}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19861488}.
CC Cytoplasmic granule {ECO:0000269|PubMed:19861488}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Note=The cytoplasmic granules are
CC stress granules which are a dense aggregation in the cytosol composed
CC of proteins and RNAs that appear when the cell is under stress.
CC Colocalizes with NANOS1 and SNAPIN in the perinuclear region of germ
CC cells (By similarity). Colocalizes with NANOS3 in the stress granules
CC (PubMed:19861488). {ECO:0000250|UniProtKB:Q8TB72,
CC ECO:0000269|PubMed:19861488}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80U58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U58-2; Sequence=VSP_009322, VSP_009323;
CC Name=3;
CC IsoId=Q80U58-3; Sequence=VSP_009321, VSP_009322, VSP_009323;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in embryonic stem
CC cells, heart, kidney, lung, skin, intestine, spleen and thymus.
CC Expressed at intermediate level in brain and liver. Weakly or not
CC expressed in muscles and stomach. Expressed at various stages of
CC myeloid and lymphoid cell development. In the testis expressed in the
CC spermatogoni, spermatocytes, spermatids and Sertoli cells.
CC {ECO:0000269|PubMed:11780640, ECO:0000269|PubMed:12667987,
CC ECO:0000269|PubMed:18089289}.
CC -!- DOMAIN: The pumilio repeats mediate the association with RNA by packing
CC together to form a right-handed superhelix that approximates a half
CC donut. RNA-binding occurs on the concave side of the surface
CC (PubMed:19540345). PUM2 is composed of 8 pumilio repeats of 36
CC residues; each repeat binds a single nucleotide in its RNA target.
CC Residues at positions 12 and 16 of the pumilio repeat bind each RNA
CC base via hydrogen bonding or van der Waals contacts with the Watson-
CC Crick edge, while the amino acid at position 13 makes a stacking
CC interaction. The recognition of RNA by pumilio repeats is base
CC specific: cysteine and glutamine at position 12 and 16, respectively,
CC bind adenine; asparagine and glutamine bind uracil; and serine and
CC glutamate bind guanine (By similarity). {ECO:0000250|UniProtKB:Q14671,
CC ECO:0000269|PubMed:19540345}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65507.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AY027917; AAK21966.1; -; mRNA.
DR EMBL; AF315590; AAG31805.1; -; mRNA.
DR EMBL; AK122225; BAC65507.1; ALT_INIT; mRNA.
DR EMBL; BC013765; AAH13765.1; -; mRNA.
DR EMBL; BC041773; AAH41773.1; -; mRNA.
DR CCDS; CCDS25802.1; -. [Q80U58-1]
DR CCDS; CCDS49026.1; -. [Q80U58-2]
DR RefSeq; NP_001153691.1; NM_001160219.1. [Q80U58-1]
DR RefSeq; NP_001153694.1; NM_001160222.1. [Q80U58-2]
DR RefSeq; NP_109648.2; NM_030723.2. [Q80U58-1]
DR RefSeq; XP_006515340.1; XM_006515277.2. [Q80U58-1]
DR RefSeq; XP_006515341.1; XM_006515278.3. [Q80U58-1]
DR RefSeq; XP_006515342.1; XM_006515279.2. [Q80U58-1]
DR RefSeq; XP_006515348.1; XM_006515285.3. [Q80U58-2]
DR PDB; 3GVO; X-ray; 1.60 A; A=706-1056.
DR PDB; 3GVT; X-ray; 2.80 A; A/B=706-1056.
DR PDBsum; 3GVO; -.
DR PDBsum; 3GVT; -.
DR AlphaFoldDB; Q80U58; -.
DR SMR; Q80U58; -.
DR BioGRID; 219850; 13.
DR IntAct; Q80U58; 4.
DR MINT; Q80U58; -.
DR STRING; 10090.ENSMUSP00000131074; -.
DR iPTMnet; Q80U58; -.
DR PhosphoSitePlus; Q80U58; -.
DR EPD; Q80U58; -.
DR jPOST; Q80U58; -.
DR MaxQB; Q80U58; -.
DR PaxDb; Q80U58; -.
DR PeptideAtlas; Q80U58; -.
DR PRIDE; Q80U58; -.
DR ProteomicsDB; 301830; -. [Q80U58-1]
DR ProteomicsDB; 301831; -. [Q80U58-2]
DR ProteomicsDB; 301832; -. [Q80U58-3]
DR Antibodypedia; 12999; 433 antibodies from 38 providers.
DR DNASU; 80913; -.
DR Ensembl; ENSMUST00000163569; ENSMUSP00000131074; ENSMUSG00000020594. [Q80U58-1]
DR Ensembl; ENSMUST00000168361; ENSMUSP00000128292; ENSMUSG00000020594. [Q80U58-1]
DR Ensembl; ENSMUST00000169089; ENSMUSP00000132122; ENSMUSG00000020594. [Q80U58-2]
DR Ensembl; ENSMUST00000178015; ENSMUSP00000137020; ENSMUSG00000020594. [Q80U58-2]
DR GeneID; 80913; -.
DR KEGG; mmu:80913; -.
DR UCSC; uc007mzw.2; mouse. [Q80U58-3]
DR UCSC; uc007mzy.2; mouse. [Q80U58-1]
DR UCSC; uc007naa.2; mouse. [Q80U58-2]
DR CTD; 23369; -.
DR MGI; MGI:1931751; Pum2.
DR VEuPathDB; HostDB:ENSMUSG00000020594; -.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00940000157575; -.
DR InParanoid; Q80U58; -.
DR OMA; TPGHCLT; -.
DR OrthoDB; 207351at2759; -.
DR PhylomeDB; Q80U58; -.
DR TreeFam; TF318160; -.
DR BioGRID-ORCS; 80913; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pum2; mouse.
DR EvolutionaryTrace; Q80U58; -.
DR PRO; PR:Q80U58; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80U58; protein.
DR Bgee; ENSMUSG00000020594; Expressed in embryonic brain and 260 other tissues.
DR ExpressionAtlas; Q80U58; baseline and differential.
DR Genevisible; Q80U58; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR GO; GO:0035198; F:miRNA binding; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0062104; F:pumilio-response element binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0060612; P:adipose tissue development; IDA:MGI.
DR GO; GO:0051276; P:chromosome organization; IDA:MGI.
DR GO; GO:0001942; P:hair follicle development; IDA:MGI.
DR GO; GO:0035196; P:miRNA processing; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IDA:MGI.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISO:MGI.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:MGI.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:MGI.
DR GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:MGI.
DR GO; GO:0001501; P:skeletal system development; IDA:MGI.
DR GO; GO:0034063; P:stress granule assembly; IDA:MGI.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..1066
FT /note="Pumilio homolog 2"
FT /id="PRO_0000075920"
FT DOMAIN 706..1048
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 726..761
FT /note="Pumilio 1"
FT REPEAT 762..797
FT /note="Pumilio 2"
FT REPEAT 798..835
FT /note="Pumilio 3"
FT REPEAT 836..871
FT /note="Pumilio 4"
FT REPEAT 872..907
FT /note="Pumilio 5"
FT REPEAT 908..943
FT /note="Pumilio 6"
FT REPEAT 944..979
FT /note="Pumilio 7"
FT REPEAT 980..1022
FT /note="Pumilio 8"
FT REGION 1..260
FT /note="Interaction with SNAPIN"
FT /evidence="ECO:0000250"
FT REGION 106..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..745
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 777..781
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 813..817
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 851..855
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 887..891
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 923..927
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 959..963
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT REGION 1002..1006
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT COMPBIAS 106..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 674
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14671"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_009321"
FT VAR_SEQ 574..652
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009322"
FT VAR_SEQ 829..830
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009323"
FT CONFLICT 461
FT /note="M -> I (in Ref. 3; BAC65507)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="G -> A (in Ref. 2; AAG31805)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="F -> C (in Ref. 2; AAG31805)"
FT /evidence="ECO:0000305"
FT CONFLICT 559..560
FT /note="LG -> VR (in Ref. 2; AAG31805)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="F -> C (in Ref. 2; AAG31805)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="S -> A (in Ref. 2; AAG31805)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="S -> G (in Ref. 2; AAG31805)"
FT /evidence="ECO:0000305"
FT HELIX 709..715
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:3GVO"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:3GVT"
FT HELIX 731..735
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 738..748
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 753..763
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 767..771
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 776..786
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 789..799
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 803..807
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 812..822
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 825..828
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 831..834
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 835..837
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 841..846
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 850..860
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 863..865
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 867..872
FT /evidence="ECO:0007829|PDB:3GVO"
FT TURN 873..876
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 877..881
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 886..896
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 899..910
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 913..917
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 922..932
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 935..943
FT /evidence="ECO:0007829|PDB:3GVO"
FT TURN 944..947
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 949..953
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 958..968
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 971..982
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 991..997
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 1001..1011
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 1014..1024
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 1025..1027
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 1028..1031
FT /evidence="ECO:0007829|PDB:3GVO"
FT TURN 1035..1037
FT /evidence="ECO:0007829|PDB:3GVO"
FT HELIX 1038..1047
FT /evidence="ECO:0007829|PDB:3GVO"
SQ SEQUENCE 1066 AA; 114314 MW; 027AC00FA91B055E CRC64;
MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GTSHHSMSQP
IMVQRRSGQS FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGTFGTRD
AETDGPEKGD QKGKASPFEE DQNRDLKQDD EDSKINGRGL PNGMDADCKD FNRTPGSRQA
SPTEVVERLG PSTNPPEGLG PLPNPTANKP LVEEFSNPET QNLDAMDQVG LDSLQFDYPG
NQVPMDSSGA TVGLFDYNSQ QQLFQRTSAL TVQQLTAAQQ QQYALAAAQQ PHIAGVFSAG
LAPAAFVPNP YIISAAPPGT DPYTAAGLAA AATLAGPAVV PPQYYGVPWG VYPANLFQQQ
AAAAASNTAN QQAASQAQPG QQQVLRPGAG QRPITPSQGQ QGQQAESLAA AANPTLAFGQ
SLAAGMPGYQ VLAPTAYYDQ TGALVVGPGA RTGLGAPVRL MAPTPVLISS TAAQAAAAAA
AAGGTANSLT GSTNGLFRPI GTQPPQQQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS
HGPGQPGSAS LGFGSGSSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS
SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL HLGGLTNGSG
RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS DIMPSGRSRL LEDFRNNRFP
NLQLRDLIGH IVEFSQDQHG SRFIQQKLER ATPAERQIVF NEILQAAYQL MTDVFGNYVI
QKFFEFGSLD QKLALATRIR GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH
VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE
QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL ALSQHKFASN
VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY ANYVVQKMID MAEPAQRKII
MHKIRPHITT LRKYTYGKHI LAKLEKYYLK NSPDLGPIGG PPNGML
