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Lysine-specific demethylase 3B (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 2B) (Jumonji domain-containing protein 1B) (Nuclear protein 5qNCA)

 KDM3B_HUMAN             Reviewed;        1761 AA.
Q7LBC6; A6H8X7; Q9BVH6; Q9BW93; Q9BZ52; Q9NYF4; Q9UPS0;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
27-SEP-2017, entry version 120.
RecName: Full=Lysine-specific demethylase 3B;
EC=1.14.11.-;
AltName: Full=JmjC domain-containing histone demethylation protein 2B;
AltName: Full=Jumonji domain-containing protein 1B;
AltName: Full=Nuclear protein 5qNCA;
Name=KDM3B; Synonyms=C5orf7, JHDM2B, JMJD1B, KIAA1082;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Bone marrow;
PubMed=11087669; DOI=10.1006/geno.2000.6345;
Lai F., Godley L.A., Fernald A.A., Orelli B.J., Pamintuan L., Zhao N.,
Le Beau M.M.;
"cDNA cloning and genomic structure of three genes localized to human
chromosome band 5q31 encoding potential nuclear proteins.";
Genomics 70:123-130(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT THR-256.
PubMed=11687974; DOI=10.1038/sj.onc.1204850;
Hu Z., Gomes I., Horrigan S.K., Kravarusic J., Mar B., Arbieva Z.,
Chyna B., Fulton N., Edassery S., Raza A., Westbrook C.A.;
"A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the
myeloid leukemia tumor suppressor gene on chromosome 5 band q31.";
Oncogene 20:6946-6954(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-256.
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-256.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
THR-256.
TISSUE=Brain, and Eye;
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).
[8]
FUNCTION, AND ENZYME ACTIVITY.
PubMed=16603237; DOI=10.1016/j.cell.2006.03.027;
Yamane K., Toumazou C., Tsukada Y.I., Erdjument-Bromage H., Tempst P.,
Wong J., Zhang Y.;
"JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription
activation by androgen receptor.";
Cell 125:483-495(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-798, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773 AND SER-779, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-361, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773; SER-779 AND
SER-798, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; SER-560; THR-614;
SER-766; SER-773; SER-778; SER-779; SER-1253 AND SER-1259, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-788, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
9' of histone H3, thereby playing a central role in histone code.
Demethylation of Lys residue generates formaldehyde and succinate.
May have tumor suppressor activity. {ECO:0000269|PubMed:16603237}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q7LBC6-1; Sequence=Displayed;
Name=2;
IsoId=Q7LBC6-2; Sequence=VSP_018299, VSP_018300;
Name=3;
IsoId=Q7LBC6-3; Sequence=VSP_018298;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in placenta,
skeletal muscle, kidney, heart and liver.
{ECO:0000269|PubMed:11087669, ECO:0000269|PubMed:11687974}.
-!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate
the association with nuclear receptors. {ECO:0000250}.
-!- MISCELLANEOUS: Its gene is located in the 5q region of the genome
which is deleted in del(5q) interstitial deletion, a frequent
deletion found in myeloid leukemias and myelodysplasias,
suggesting that it may be a good candidate for the del(5q) tumor
suppressor gene.
-!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA83034.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF251039; AAF63765.1; -; mRNA.
EMBL; AF338242; AAK13499.1; -; mRNA.
EMBL; AB029005; BAA83034.2; ALT_INIT; mRNA.
EMBL; AC104116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC113403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW62141.1; -; Genomic_DNA.
EMBL; BC000539; AAH00539.2; -; mRNA.
EMBL; BC001202; AAH01202.1; -; mRNA.
EMBL; BC146788; AAI46789.1; -; mRNA.
CCDS; CCDS34242.1; -. [Q7LBC6-1]
RefSeq; NP_057688.2; NM_016604.3.
UniGene; Hs.483486; -.
PDB; 4C8D; X-ray; 2.18 A; A=1380-1720.
PDBsum; 4C8D; -.
ProteinModelPortal; Q7LBC6; -.
SMR; Q7LBC6; -.
BioGrid; 119727; 31.
IntAct; Q7LBC6; 11.
MINT; MINT-1195273; -.
STRING; 9606.ENSP00000326563; -.
BindingDB; Q7LBC6; -.
ChEMBL; CHEMBL3784906; -.
iPTMnet; Q7LBC6; -.
PhosphoSitePlus; Q7LBC6; -.
BioMuta; KDM3B; -.
DMDM; 308153456; -.
EPD; Q7LBC6; -.
MaxQB; Q7LBC6; -.
PaxDb; Q7LBC6; -.
PeptideAtlas; Q7LBC6; -.
PRIDE; Q7LBC6; -.
Ensembl; ENST00000314358; ENSP00000326563; ENSG00000120733. [Q7LBC6-1]
Ensembl; ENST00000542866; ENSP00000439462; ENSG00000120733. [Q7LBC6-3]
GeneID; 51780; -.
KEGG; hsa:51780; -.
UCSC; uc003lcy.1; human. [Q7LBC6-1]
CTD; 51780; -.
DisGeNET; 51780; -.
EuPathDB; HostDB:ENSG00000120733.13; -.
GeneCards; KDM3B; -.
HGNC; HGNC:1337; KDM3B.
HPA; HPA016610; -.
HPA; HPA057202; -.
MIM; 609373; gene.
neXtProt; NX_Q7LBC6; -.
OpenTargets; ENSG00000120733; -.
PharmGKB; PA25918; -.
eggNOG; KOG1356; Eukaryota.
eggNOG; ENOG410XTAA; LUCA.
GeneTree; ENSGT00530000063039; -.
InParanoid; Q7LBC6; -.
KO; K15601; -.
OMA; IICKRLR; -.
OrthoDB; EOG091G00RB; -.
PhylomeDB; Q7LBC6; -.
TreeFam; TF324723; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
ChiTaRS; KDM3B; human.
GeneWiki; JMJD1B; -.
GenomeRNAi; 51780; -.
PRO; PR:Q7LBC6; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000120733; -.
CleanEx; HS_JMJD1B; -.
ExpressionAtlas; Q7LBC6; baseline and differential.
Genevisible; Q7LBC6; HS.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0016209; F:antioxidant activity; IEA:Ensembl.
GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0072718; P:response to cisplatin; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR003347; JmjC_dom.
Pfam; PF02373; JmjC; 1.
SMART; SM00558; JmjC; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; Dioxygenase; Iron; Isopeptide bond; Metal-binding;
Nucleus; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 1761 Lysine-specific demethylase 3B.
/FTId=PRO_0000234373.
DOMAIN 1498 1721 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 1031 1056 C6-type. {ECO:0000255}.
MOTIF 1293 1297 LXXLL motif.
COMPBIAS 647 744 Ser-rich.
METAL 1560 1560 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 1562 1562 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 1689 1689 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 361 361 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 546 546 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZPY7}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZPY7}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 614 614 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 773 773 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 778 778 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 779 779 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 798 798 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231}.
MOD_RES 1253 1253 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 788 788 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1002 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018298.
VAR_SEQ 1 344 Missing (in isoform 2).
{ECO:0000303|PubMed:11087669}.
/FTId=VSP_018299.
VAR_SEQ 345 349 TFVPQ -> MGAME (in isoform 2).
{ECO:0000303|PubMed:11087669}.
/FTId=VSP_018300.
VARIANT 256 256 A -> T (in dbSNP:rs6865472).
{ECO:0000269|PubMed:10470851,
ECO:0000269|PubMed:11687974,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_026221.
VARIANT 1201 1201 S -> N (in dbSNP:rs7706614).
/FTId=VAR_026222.
CONFLICT 569 569 C -> R (in Ref. 1; AAF63765).
{ECO:0000305}.
STRAND 1382 1385 {ECO:0000244|PDB:4C8D}.
TURN 1386 1389 {ECO:0000244|PDB:4C8D}.
STRAND 1390 1394 {ECO:0000244|PDB:4C8D}.
HELIX 1401 1410 {ECO:0000244|PDB:4C8D}.
STRAND 1415 1417 {ECO:0000244|PDB:4C8D}.
HELIX 1420 1423 {ECO:0000244|PDB:4C8D}.
HELIX 1426 1429 {ECO:0000244|PDB:4C8D}.
HELIX 1431 1438 {ECO:0000244|PDB:4C8D}.
STRAND 1441 1447 {ECO:0000244|PDB:4C8D}.
TURN 1448 1450 {ECO:0000244|PDB:4C8D}.
STRAND 1453 1458 {ECO:0000244|PDB:4C8D}.
HELIX 1459 1464 {ECO:0000244|PDB:4C8D}.
TURN 1465 1467 {ECO:0000244|PDB:4C8D}.
HELIX 1469 1471 {ECO:0000244|PDB:4C8D}.
STRAND 1483 1485 {ECO:0000244|PDB:4C8D}.
HELIX 1493 1497 {ECO:0000244|PDB:4C8D}.
HELIX 1499 1508 {ECO:0000244|PDB:4C8D}.
HELIX 1512 1515 {ECO:0000244|PDB:4C8D}.
TURN 1524 1526 {ECO:0000244|PDB:4C8D}.
STRAND 1539 1543 {ECO:0000244|PDB:4C8D}.
HELIX 1550 1553 {ECO:0000244|PDB:4C8D}.
STRAND 1556 1560 {ECO:0000244|PDB:4C8D}.
STRAND 1563 1574 {ECO:0000244|PDB:4C8D}.
STRAND 1577 1579 {ECO:0000244|PDB:4C8D}.
HELIX 1583 1592 {ECO:0000244|PDB:4C8D}.
HELIX 1597 1604 {ECO:0000244|PDB:4C8D}.
STRAND 1610 1616 {ECO:0000244|PDB:4C8D}.
HELIX 1619 1621 {ECO:0000244|PDB:4C8D}.
HELIX 1622 1634 {ECO:0000244|PDB:4C8D}.
HELIX 1646 1649 {ECO:0000244|PDB:4C8D}.
HELIX 1656 1666 {ECO:0000244|PDB:4C8D}.
STRAND 1671 1676 {ECO:0000244|PDB:4C8D}.
STRAND 1680 1683 {ECO:0000244|PDB:4C8D}.
STRAND 1689 1704 {ECO:0000244|PDB:4C8D}.
HELIX 1707 1709 {ECO:0000244|PDB:4C8D}.
HELIX 1710 1719 {ECO:0000244|PDB:4C8D}.
SEQUENCE 1761 AA; 191581 MW; FB900FCBF0675CD8 CRC64;
MADAAASPVG KRLLLLFADT AASASASAPA AAAASGDPGP ALRTRAWRAG TVRAMSGAVP
QDLAIFVEFD GCNWKQHSWV KVHAEEVIVL LLEGSLVWAP REDPVLLQGI RVSIAQWPAL
TFTPLVDKLG LGSVVPVEYL LDRELRFLSD ANGLHLFQMG TDSQNQILLE HAALRETVNA
LISDQKLQEI FSRGPYSVQG HRVKIYQPEG EEGWLYGVVS HQDSITRLME VSVTESGEIK
SVDPRLIHVM LMDNSAPQSE GGTLKAVKSS KGKKKRESIE GKDGRRRKSA SDSGCDPASK
KLKGDRGEVD SNGSDGGEAS RGPWKGGNAS GEPGLDQRAK QPPSTFVPQI NRNIRFATYT
KENGRTLVVQ DEPVGGDTPA SFTPYSTATG QTPLAPEVGG AENKEAGKTL EQVGQGIVAS
AAVVTTASST PNTVRISDTG LAAGTVPEKQ KGSRSQASGE NSRNSILASS GFGAPLPSSS
QPLTFGSGRS QSNGVLATEN KPLGFSFGCS SAQEAQKDTD LSKNLFFQCM SQTLPTSNYF
TTVSESLADD SSSRDSFKQS LESLSSGLCK GRSVLGTDTK PGSKAGSSVD RKVPAESMPT
LTPAFPRSLL NARTPENHEN LFLQPPKLSR EEPSNPFLAF VEKVEHSPFS SFASQASGSS
SSATTVTSKV APSWPESHSS ADSASLAKKK PLFITTDSSK LVSGVLGSAL TSGGPSLSAM
GNGRSSSPTS SLTQPIEMPT LSSSPTEERP TVGPGQQDNP LLKTFSNVFG RHSGGFLSSP
ADFSQENKAP FEAVKRFSLD ERSLACRQDS DSSTNSDLSD LSDSEEQLQA KTGLKGIPEH
LMGKLGPNGE RSAELLLGKS KGKQAPKGRP RTAPLKVGQS VLKDVSKVKK LKQSGEPFLQ
DGSCINVAPH LHKCRECRLE RYRKFKEQEQ DDSTVACRFF HFRRLIFTRK GVLRVEGFLS
PQQSDPDAMN LWIPSSSLAE GIDLETSKYI LANVGDQFCQ LVMSEKEAMM MVEPHQKVAW
KRAVRGVREM CDVCETTLFN IHWVCRKCGF GVCLDCYRLR KSRPRSETEE MGDEEVFSWL
KCAKGQSHEP ENLMPTQIIP GTALYNIGDM VHAARGKWGI KANCPCISRQ NKSVLRPAVT
NGMSQLPSIN PSASSGNETT FSGGGGPAPV TTPEPDHVPK ADSTDIRSEE PLKTDSSASN
SNSELKAIRP PCPDTAPPSS ALHWLADLAT QKAKEETKEA GSLRSVLNKE SHSPFGLDSF
NSTAKVSPLT PKLFNSLLLG PTASNNKTEG SSLRDLLHSG PGKLPQTPLD TGIPFPPVFS
TSSAGVKSKA SLPNFLDHII ASVVENKKTS DASKRACNLT DTQKEVKEMV MGLNVLDPHT
SHSWLCDGRL LCLHDPSNKN NWKIFRECWK QGQPVLVSGV HKKLKSELWK PEAFSQEFGD
QDVDLVNCRN CAIISDVKVR DFWDGFEIIC KRLRSEDGQP MVLKLKDWPP GEDFRDMMPT
RFEDLMENLP LPEYTKRDGR LNLASRLPSY FVRPDLGPKM YNAYGLITAE DRRVGTTNLH
LDVSDAVNVM VYVGIPIGEG AHDEEVLKTI DEGDADEVTK QRIHDGKEKP GALWHIYAAK
DAEKIRELLR KVGEEQGQEN PPDHDPIHDQ SWYLDQTLRK RLYEEYGVQG WAIVQFLGDA
VFIPAGAPHQ VHNLYSCIKV AEDFVSPEHV KHCFRLTQEF RHLSNTHTNH EDKLQVKNII
YHAVKDAVGT LKAHESKLAR S


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