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Myelin regulatory factor (EC 3.4.-.-) (Myelin gene regulatory factor) [Cleaved into: Myelin regulatory factor, N-terminal; Myelin regulatory factor, C-terminal]

 MYRF_MOUSE              Reviewed;        1138 AA.
Q3UR85; B2RXQ7; F8WJJ9; Q3V3K4;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
22-NOV-2017, entry version 102.
RecName: Full=Myelin regulatory factor;
EC=3.4.-.-;
AltName: Full=Myelin gene regulatory factor;
Contains:
RecName: Full=Myelin regulatory factor, N-terminal;
Contains:
RecName: Full=Myelin regulatory factor, C-terminal;
Name=Myrf; Synonyms=Gm1804, Gm98, Mrf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 525-1138 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Spinal cord;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
PubMed=19596243; DOI=10.1016/j.cell.2009.04.031;
Emery B., Agalliu D., Cahoy J.D., Watkins T.A., Dugas J.C.,
Mulinyawe S.B., Ibrahim A., Ligon K.L., Rowitch D.H., Barres B.A.;
"Myelin gene regulatory factor is a critical transcriptional regulator
required for CNS myelination.";
Cell 138:172-185(2009).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22956843; DOI=10.1523/JNEUROSCI.1069-12.2012;
Koenning M., Jackson S., Hay C.M., Faux C., Kilpatrick T.J.,
Willingham M., Emery B.;
"Myelin gene regulatory factor is required for maintenance of myelin
and mature oligodendrocyte identity in the adult CNS.";
J. Neurosci. 32:12528-12542(2012).
[6]
SUBCELLULAR LOCATION, SUBUNIT, PROTEOLYTIC PROCESSING, DNA-BINDING,
AND MUTAGENESIS OF 254-LYS--ARG-257; LYS-399; ARG-454; ARG-478;
SER-587 AND LYS-592.
PubMed=23966833; DOI=10.1371/journal.pbio.1001625;
Bujalka H., Koenning M., Jackson S., Perreau V.M., Pope B., Hay C.M.,
Mitew S., Hill A.F., Lu Q.R., Wegner M., Srinivasan R., Svaren J.,
Willingham M., Barres B.A., Emery B.;
"MYRF is a membrane-associated transcription factor that
autoproteolytically cleaves to directly activate myelin genes.";
PLoS Biol. 11:E1001625-E1001625(2013).
[7]
FUNCTION, AND INDUCTION.
PubMed=24204311; DOI=10.1371/journal.pgen.1003907;
Hornig J., Froeb F., Vogl M.R., Hermans-Borgmeyer I., Tamm E.R.,
Wegner M.;
"The transcription factors Sox10 and Myrf define an essential
regulatory network module in differentiating oligodendrocytes.";
PLoS Genet. 9:E1003907-E1003907(2013).
[8]
FUNCTION.
PubMed=27532821; DOI=10.1002/glia.23044;
Muth K.N., Piefke S., Weider M., Sock E., Hermans-Borgmeyer I.,
Wegner M., Kuespert M.;
"The dual-specificity phosphatase Dusp15 is regulated by Sox10 and
Myrf in myelinating oligodendrocytes.";
Glia 64:2120-2132(2016).
[9]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-384.
PubMed=28441531; DOI=10.1016/j.devcel.2017.03.022;
Meng J., Ma X., Tao H., Jin X., Witvliet D., Mitchell J., Zhu M.,
Dong M.Q., Zhen M., Jin Y., Qi Y.B.;
"Myrf ER-bound transcription factors drive C. elegans synaptic
plasticity via cleavage-dependent nuclear translocation.";
Dev. Cell 41:180-194(2017).
-!- FUNCTION: Myelin regulatory factor: Constitutes a precursor of the
transcription factor. Mediates the autocatalytic cleavage that
releases the Myelin regulatory factor, N-terminal component that
specifically activates transcription of central nervous system
(CNS) myelin genes. {ECO:0000269|PubMed:23966833}.
-!- FUNCTION: Myelin regulatory factor, C-terminal: Membrane-bound
part that has no transcription factor activity and remains
attached to the endoplasmic reticulum membrane following cleavage.
{ECO:0000269|PubMed:23966833}.
-!- FUNCTION: Myelin regulatory factor, N-terminal: Transcription
factor that specifically activates expression of myelin genes such
as MBP, MOG, MAG, DUSP15 and PLP1 during oligodendrocyte (OL)
maturation, thereby playing a central role in oligodendrocyte
maturation and CNS myelination (PubMed:19596243, PubMed:22956843,
PubMed:23966833, PubMed:24204311, PubMed:27532821). Specifically
recognizes and binds DNA sequence 5'-CTGGYAC-3' in the regulatory
regions of myelin-specific genes and directly activates their
expression. Not only required during oligodendrocyte
differentiation but is also required on an ongoing basis for the
maintenance of expression of myelin genes and for the maintenance
of a mature, viable oligodendrocyte phenotype (PubMed:19596243,
PubMed:22956843, PubMed:23966833). {ECO:0000269|PubMed:19596243,
ECO:0000269|PubMed:22956843, ECO:0000269|PubMed:23966833,
ECO:0000269|PubMed:24204311, ECO:0000269|PubMed:27532821}.
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:23966833}.
-!- SUBCELLULAR LOCATION: Myelin regulatory factor: Endoplasmic
reticulum membrane {ECO:0000269|PubMed:23966833}; Single-pass
membrane protein.
-!- SUBCELLULAR LOCATION: Myelin regulatory factor, N-terminal:
Nucleus {ECO:0000269|PubMed:23966833,
ECO:0000269|PubMed:28441531}. Cytoplasm
{ECO:0000269|PubMed:23966833}. Note=Translocates from the
cytoplasm to the nucleus upon autocatalytic cleavage.
{ECO:0000269|PubMed:23966833}.
-!- SUBCELLULAR LOCATION: Myelin regulatory factor, C-terminal:
Endoplasmic reticulum membrane {ECO:0000269|PubMed:23966833};
Single-pass membrane protein {ECO:0000269|PubMed:23966833}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q3UR85-1; Sequence=Displayed;
Name=2;
IsoId=Q3UR85-2; Sequence=VSP_031303, VSP_031304;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay. Dubious isoform due to
intron retention.;
Name=3;
IsoId=Q3UR85-3; Sequence=VSP_053374;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q3UR85-5; Sequence=VSP_053992, VSP_053993;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Specifically expressed by postmitotic
oligodendrocytes in the CNS. Not detected in the peripheral
nervous system (PNS). {ECO:0000269|PubMed:19596243}.
-!- DEVELOPMENTAL STAGE: At postnatal day 3 (P3), the expression is
restricted to cells in the hindbrain and cerebellum, subsequently
spreading rostrally throughout the white matter tracks over the
first 2 weeks postnatal, mirroring the expression of Plp1.
{ECO:0000269|PubMed:19596243}.
-!- INDUCTION: Expression is directly regulated by SOX10.
{ECO:0000269|PubMed:24204311}.
-!- DOMAIN: Myelin regulatory factor, N-terminal: The nuclear
localization signals mediate translocation to the nucleus.
{ECO:0000269|PubMed:23966833}.
-!- DOMAIN: Myelin regulatory factor: The peptidase S74 domain, also
named Intramolecular Chaperone Auto-processed (ICA) domain or
Intramolecuar Chaperone Domain (ICD), has protease activity and
mediates autocatalytic processing of the protein to generate the
Myelin regulatory factor, N-terminal active transcription factor
and the Myelin regulatory factor, C-terminal components.
{ECO:0000269|PubMed:23966833}.
-!- PTM: Myelin regulatory factor, C-terminal: Glycosylated.
{ECO:0000250|UniProtKB:Q9Y2G1}.
-!- PTM: Myelin regulatory factor: Follows autocatalytic cleavage via
the peptidase S74 domain. Autoprocessing is apparently
constitutive and is essential for transcriptional activity.
{ECO:0000269|PubMed:23966833}.
-!- DISRUPTION PHENOTYPE: Embryos die around E12.5. Conditional
knockout mice in which Mrf is lacking within the oligodendrocyte
lineage display severe deficits in myelin gene expression and
premyelinating oligodendrocytes fail to myelinate. These mice
display severe neurological abnormalities and die because of
seizures during the third postnatal week.
{ECO:0000269|PubMed:19596243, ECO:0000269|PubMed:22956843}.
-!- SIMILARITY: Belongs to the MRF family. {ECO:0000305}.
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EMBL; AK039649; BAE20548.1; -; mRNA.
EMBL; AK141695; BAE24803.1; -; mRNA.
EMBL; AC132148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC157942; AAI57943.1; -; mRNA.
CCDS; CCDS50387.1; -. [Q3UR85-3]
RefSeq; NP_001028653.1; NM_001033481.1. [Q3UR85-3]
RefSeq; XP_006526992.1; XM_006526929.3. [Q3UR85-1]
UniGene; Mm.329716; -.
PDB; 5H5P; X-ray; 2.46 A; A=351-532.
PDBsum; 5H5P; -.
ProteinModelPortal; Q3UR85; -.
SMR; Q3UR85; -.
STRING; 10090.ENSMUSP00000085329; -.
iPTMnet; Q3UR85; -.
PhosphoSitePlus; Q3UR85; -.
MaxQB; Q3UR85; -.
PaxDb; Q3UR85; -.
PeptideAtlas; Q3UR85; -.
PRIDE; Q3UR85; -.
Ensembl; ENSMUST00000088013; ENSMUSP00000085329; ENSMUSG00000036098. [Q3UR85-1]
Ensembl; ENSMUST00000186056; ENSMUSP00000140871; ENSMUSG00000036098. [Q3UR85-5]
Ensembl; ENSMUST00000189897; ENSMUSP00000139601; ENSMUSG00000036098. [Q3UR85-3]
GeneID; 225908; -.
KEGG; mmu:225908; -.
UCSC; uc008gpk.2; mouse. [Q3UR85-1]
UCSC; uc012bil.1; mouse. [Q3UR85-3]
UCSC; uc012bim.1; mouse. [Q3UR85-5]
CTD; 745; -.
MGI; MGI:2684944; Myrf.
eggNOG; KOG3661; Eukaryota.
eggNOG; ENOG410XPRK; LUCA.
GeneTree; ENSGT00530000063626; -.
HOGENOM; HOG000111718; -.
InParanoid; Q3UR85; -.
OMA; NIRAKSW; -.
OrthoDB; EOG091G0213; -.
PhylomeDB; Q3UR85; -.
TreeFam; TF312888; -.
PRO; PR:Q3UR85; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000036098; -.
CleanEx; MM_GM98; -.
ExpressionAtlas; Q3UR85; baseline and differential.
Genevisible; Q3UR85; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; NAS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0032286; P:central nervous system myelin maintenance; IMP:UniProtKB.
GO; GO:0022010; P:central nervous system myelination; IMP:UniProtKB.
GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB.
GO; GO:0048709; P:oligodendrocyte differentiation; IMP:UniProtKB.
GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.40.1390; -; 2.
InterPro; IPR026933; MRF.
InterPro; IPR026932; MRF_C1.
InterPro; IPR025719; MRF_C2.
InterPro; IPR024061; NDT80_DNA-bd_dom.
InterPro; IPR037141; NDT80_DNA-bd_dom_sf.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030392; S74_ICA.
InterPro; IPR036388; WH-like_DNA-bd_sf.
PANTHER; PTHR13029:SF16; PTHR13029:SF16; 1.
Pfam; PF13887; MRF_C1; 1.
Pfam; PF13888; MRF_C2; 1.
Pfam; PF05224; NDT80_PhoG; 1.
Pfam; PF13884; Peptidase_S74; 1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS51688; ICA; 1.
PROSITE; PS51517; NDT80; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Autocatalytic cleavage; Coiled coil; Complete proteome; Cytoplasm;
Differentiation; DNA-binding; Endoplasmic reticulum; Glycoprotein;
Hydrolase; Membrane; Nucleus; Protease; Reference proteome;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix.
CHAIN 1 1138 Myelin regulatory factor.
/FTId=PRO_0000318920.
CHAIN 1 586 Myelin regulatory factor, N-terminal.
{ECO:0000305|PubMed:23966833}.
/FTId=PRO_0000424312.
CHAIN 587 1138 Myelin regulatory factor, C-terminal.
{ECO:0000305|PubMed:23966833}.
/FTId=PRO_0000424313.
TOPO_DOM 1 768 Cytoplasmic. {ECO:0000255}.
TRANSMEM 769 789 Helical. {ECO:0000255}.
TOPO_DOM 790 1138 Lumenal. {ECO:0000255}.
DOMAIN 587 696 Peptidase S74.
DNA_BIND 250 541 NDT80. {ECO:0000255|PROSITE-
ProRule:PRU00850}.
COILED 680 711 {ECO:0000255}.
MOTIF 254 257 Nuclear localization signal.
{ECO:0000269|PubMed:23966833}.
MOTIF 491 494 Nuclear localization signal.
{ECO:0000269|PubMed:23966833}.
COMPBIAS 60 330 Pro-rich.
SITE 586 587 Cleavage; by autolysis.
{ECO:0000269|PubMed:23966833}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y2G1}.
CARBOHYD 1030 1030 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1052 1052 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1116 1116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 46 247 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_053992.
VAR_SEQ 779 779 S -> R (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_031303.
VAR_SEQ 780 1138 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_031304.
VAR_SEQ 803 829 SLAVSTSCLLALLRPQDPGGSEAMCPW -> R (in
isoform 3). {ECO:0000305}.
/FTId=VSP_053374.
VAR_SEQ 829 829 W -> CR (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_053993.
MUTAGEN 254 256 KKR->AAA: Abolishes nuclear localization.
MUTAGEN 384 384 G->R: Does not affect subcellular
location. Impaired DNA-binding.
{ECO:0000269|PubMed:28441531}.
MUTAGEN 399 399 K->A: Abolishes DNA-binding.
{ECO:0000269|PubMed:23966833}.
MUTAGEN 454 454 R->A: Abolishes DNA-binding.
{ECO:0000269|PubMed:23966833}.
MUTAGEN 478 478 R->A: Abolishes DNA-binding.
{ECO:0000269|PubMed:23966833}.
MUTAGEN 587 587 S->A: Prevents autocatalytic cleavage and
generation of Myelin regulatory factor,
N-terminal part.
{ECO:0000269|PubMed:23966833}.
MUTAGEN 587 587 S->C: Does not affect autocatalytic
cleavage and generation of Myelin
regulatory factor, N-terminal part.
{ECO:0000269|PubMed:23966833}.
MUTAGEN 592 592 K->H,R,M: Prevents autocatalytic cleavage
and generation of Myelin regulatory
factor, N-terminal part.
{ECO:0000269|PubMed:23966833}.
CONFLICT 860 860 K -> N (in Ref. 3; AAI57943).
{ECO:0000305}.
STRAND 353 355 {ECO:0000244|PDB:5H5P}.
HELIX 358 360 {ECO:0000244|PDB:5H5P}.
STRAND 363 366 {ECO:0000244|PDB:5H5P}.
STRAND 376 380 {ECO:0000244|PDB:5H5P}.
STRAND 386 388 {ECO:0000244|PDB:5H5P}.
TURN 389 392 {ECO:0000244|PDB:5H5P}.
STRAND 393 397 {ECO:0000244|PDB:5H5P}.
STRAND 402 409 {ECO:0000244|PDB:5H5P}.
STRAND 414 419 {ECO:0000244|PDB:5H5P}.
STRAND 422 425 {ECO:0000244|PDB:5H5P}.
STRAND 428 437 {ECO:0000244|PDB:5H5P}.
STRAND 440 445 {ECO:0000244|PDB:5H5P}.
STRAND 447 450 {ECO:0000244|PDB:5H5P}.
STRAND 456 458 {ECO:0000244|PDB:5H5P}.
STRAND 462 464 {ECO:0000244|PDB:5H5P}.
STRAND 470 483 {ECO:0000244|PDB:5H5P}.
STRAND 502 512 {ECO:0000244|PDB:5H5P}.
STRAND 515 524 {ECO:0000244|PDB:5H5P}.
STRAND 527 530 {ECO:0000244|PDB:5H5P}.
SEQUENCE 1138 AA; 123288 MW; A59CDDA18CDE7054 CRC64;
MEVVDETEAL QRFFEGHDIS GALEPSNIDT SILEEYIGKE DASDLCFPEI SAPASTASFP
HGPPAIPGSS GLHHLSPPGS GPSPGRHGPL PPPTYGTPLN CNNNNGMGTA PKPFLGGSGP
PIKAEPKAPY APGTLPDSPP DSGSEAYSPQ QVNDPHLLRT ITPETLCHVG VSSRLEHPPP
PPAHLPGPPP PPPPPPHYPV LQRDLYMKAE PPVPPYAAMG PGLVPPELHH TQQTQVLHQL
LQQHGAELPP HPSKKRKHSE SPPNTLNAQM LNGMIKQEPG TVTALPPHPA RAPSPPWPPQ
GPLSPGTGSL PLSIARAQTP PWHPPGAPSP GLLQDSDSLS GSYLDPNYQS IKWQPHQQNK
WATLYDANYK ELPMLTYRVD ADKGFNFSVG DDAFVCQKKN HFQVTVYIGM LGEPKYVKTP
EGLKPLDCFY LKLHGVKLEA LNQSINIEQS QSDRSKRPFN PVTVNLPPEQ VTKVTVGRLH
FSETTANNMR KKGKPNPDQR YFMLVVALQA HAQNQNYTLA AQISERIIVR ASNPGQFESD
SDVLWQRAQL PDTVFHHGRV GINTDRPDEA LVVHGNVKVM GSLMHPSDLR AKEHVQEVDT
TEQLKRISRM RLVHYRYKPE FAASAGIEAT APETGVIAQE VKEILPEAVK DTGDVVFANG
KTIENFLVVN KERIFMENVG AVKELCKLTD NLETRIDELE RWSHKLAKLR RLDSLKSTGS
SGAFSHAGSQ FSRAGSVPHK KRPPKLANKS SPAVPDQACI SQRFLQGTII ALVVVMAFSV
VSMSTLYVLS LRSEEDLVDA DGSLAVSTSC LLALLRPQDP GGSEAMCPWS SQSFGTTQLR
QSSMTTGLPG TQPSLLLVTK SASGPALRAL DLCSSQPCPI VCCSPPVSSP ATDPALGPTL
TPTPSPSSNP KHSGPGQMAP LPVTNIRAKS WGISANGISY SKHSKSLEPL ASPVVPFPGG
QSKTKNSPSF NLQSRARRGA PQPSPSPAQF TQTQGQLDPA PSLTSIQLLE NSMPITSQYC
VPEGACRLGN FTYHIPVSSS TPLHLSLTLQ MNSSTPVSVV LCSLTSEEEP CEEGGFLQRF
HPHQDTQGTS HQWPVTILSF REFTYHFRVT LLGQANCSSE AIVQPATDYY FHFYRLCD


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