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Next to BRCA1 gene 1 protein (Cell migration-inducing gene 19 protein) (Membrane component chromosome 17 surface marker 2) (Neighbor of BRCA1 gene 1 protein) (Protein 1A1-3B)

 NBR1_HUMAN              Reviewed;         966 AA.
Q14596; Q13173; Q15026; Q5J7Q8; Q96GB6; Q9NRF7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
25-OCT-2017, entry version 177.
RecName: Full=Next to BRCA1 gene 1 protein;
AltName: Full=Cell migration-inducing gene 19 protein;
AltName: Full=Membrane component chromosome 17 surface marker 2;
AltName: Full=Neighbor of BRCA1 gene 1 protein;
AltName: Full=Protein 1A1-3B;
Name=NBR1; Synonyms=1A13B, KIAA0049, M17S2; ORFNames=MIG19;
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 1), AND VARIANT ARG-923.
TISSUE=Ovary;
PubMed=8069304; DOI=10.1093/hmg/3.4.589;
Campbell I.G., Nicolai H.M., Foulkes W.D., Senger G., Stamp G.W.,
Allan G., Boyer C., Jones K., Bast R.C. Jr., Solomon E., Trowsdale J.,
Black D.M.;
"A novel gene encoding a B-box protein within the BRCA1 region at
17q21.1.";
Hum. Mol. Genet. 3:589-594(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. II.
The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 1:223-229(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kim J.W.;
"Identification of a human migration inducing gene.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ARG-923.
TISSUE=Lymph;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-42, AND VARIANT ARG-923.
TISSUE=Testis;
PubMed=11179671; DOI=10.1016/S0378-1119(00)00549-7;
Dimitrov S., Brennerova M., Forejt J.;
"Expression profiles and intergenic structure of head-to-head oriented
Brca1 and Nbr1 genes.";
Gene 262:89-98(2001).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 412-508.
PubMed=7581362; DOI=10.1093/hmg/4.8.1259;
Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J.,
Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H.,
Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S.,
Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H.,
Shattuck-Eidens D., Kamb A.;
"Comparison of the positional cloning methods used to isolate the
BRCA1 gene.";
Hum. Mol. Genet. 4:1259-1266(1995).
[9]
INTERACTION WITH SQSTM1, OLIGOMERIZATION, DOMAIN, AND MUTAGENESIS OF
LYS-12 AND ASP-50.
PubMed=12813044; DOI=10.1074/jbc.M303221200;
Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
Michaelsen E., Bjoerkoey G., Johansen T.;
"Interaction codes within the family of mammalian Phox and Bem1p
domain-containing proteins.";
J. Biol. Chem. 278:34568-34581(2003).
[10]
INTERACTION WITH SQSTM1; TTN AND RNF29.
PubMed=15802564; DOI=10.1126/science.1110463;
Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E.,
Kristensen J., Brandmeier B., Franzen G., Hedberg B., Gunnarsson L.G.,
Hughes S.M., Marchand S., Sejersen T., Richard I., Edstroem L.,
Ehler E., Udd B., Gautel M.;
"The kinase domain of titin controls muscle gene expression and
protein turnover.";
Science 308:1599-1603(2005).
[11]
INTERACTION WITH USP8, UBIQUITIN-BINDING, AND SUBCELLULAR LOCATION.
PubMed=19427866; DOI=10.1016/j.febslet.2009.04.049;
Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M.;
"Interactions with LC3 and polyubiquitin chains link nbr1 to
autophagic protein turnover.";
FEBS Lett. 583:1846-1852(2009).
[12]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH SQSTM1;
MAP1LC3A; MAP1LC3B; MAP1LC3C; GABARAP; GABARAPL1 AND GABARAPL2, AND
MUTAGENESIS OF ASP-50 AND TYR-732.
PubMed=19250911; DOI=10.1016/j.molcel.2009.01.020;
Kirkin V., Lamark T., Sou Y.S., Bjorkoy G., Nunn J.L., Bruun J.A.,
Shvets E., McEwan D.G., Clausen T.H., Wild P., Bilusic I.,
Theurillat J.P., Overvatn A., Ishii T., Elazar Z., Komatsu M.,
Dikic I., Johansen T.;
"A role for NBR1 in autophagosomal degradation of ubiquitinated
substrates.";
Mol. Cell 33:505-516(2009).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-625, 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).
[15]
STRUCTURE BY NMR OF 1-85 AND 916-956.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-024, a PB1 domain, and of RSGI RUH-
046, a UBA domain from human next to BRCA1 gene 1 protein (KIAA0049
protein) R923H variant.";
Submitted (NOV-2005) to the PDB data bank.
[16]
X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 1-85.
PubMed=16376336; DOI=10.1016/j.febslet.2005.12.021;
Mueller S., Kursula I., Zou P., Wilmanns M.;
"Crystal structure of the PB1 domain of NBR1.";
FEBS Lett. 580:341-344(2006).
-!- FUNCTION: Acts probably as a receptor for selective autophagosomal
degradation of ubiquitinated targets.
{ECO:0000269|PubMed:19250911}.
-!- SUBUNIT: Homooligomer and heterooligomer. Interacts with TRIM55
(By similarity). Interacts with SQSTM1, titin/TTN, RNF29, USP8,
SQSTM1, MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1 and
GABARAPL2. Binds to ubiquitin and ubiquitinated proteins.
{ECO:0000250, ECO:0000269|PubMed:12813044,
ECO:0000269|PubMed:15802564, ECO:0000269|PubMed:19250911,
ECO:0000269|PubMed:19427866}.
-!- INTERACTION:
P38182:ATG8 (xeno); NbExp=7; IntAct=EBI-742698, EBI-2684;
O95166:GABARAP; NbExp=5; IntAct=EBI-742698, EBI-712001;
Q9H0R8:GABARAPL1; NbExp=4; IntAct=EBI-742698, EBI-746969;
P60520:GABARAPL2; NbExp=11; IntAct=EBI-742698, EBI-720116;
P42858:HTT; NbExp=3; IntAct=EBI-742698, EBI-466029;
Q9H492:MAP1LC3A; NbExp=5; IntAct=EBI-742698, EBI-720768;
Q9GZQ8:MAP1LC3B; NbExp=8; IntAct=EBI-742698, EBI-373144;
Q9BXW4:MAP1LC3C; NbExp=3; IntAct=EBI-742698, EBI-2603996;
Q13501:SQSTM1; NbExp=6; IntAct=EBI-742698, EBI-307104;
Q9H2B2:SYT4; NbExp=3; IntAct=EBI-742698, EBI-751132;
P40818:USP8; NbExp=3; IntAct=EBI-742698, EBI-1050865;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19427866}.
Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:19250911}.
Lysosome {ECO:0000269|PubMed:19250911}. Cytoplasm, myofibril,
sarcomere, M line {ECO:0000250|UniProtKB:Q501R9}. Note=In cardiac
muscles localizes to the sarcomeric M line (By similarity). Is
targeted to lysosomes for degradation (PubMed:19250911).
{ECO:0000250|UniProtKB:Q501R9, ECO:0000269|PubMed:19250911}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14596-1; Sequence=Displayed;
Name=2;
IsoId=Q14596-2; Sequence=VSP_004314;
Note=No experimental confirmation available.;
-!- DOMAIN: The PB1 domain mediates interaction with SQSTM1.
{ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:19250911}.
-!- CAUTION: Was originally thought to be the ovarian carcinoma
antigen CA125. {ECO:0000305|PubMed:8069304}.
-!- SEQUENCE CAUTION:
Sequence=BAA06417.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X76952; CAA54274.1; -; mRNA.
EMBL; D30756; BAA06417.2; ALT_INIT; mRNA.
EMBL; AY450308; AAS15047.1; -; mRNA.
EMBL; AC060780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC109326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60946.1; -; Genomic_DNA.
EMBL; BC009808; AAH09808.1; -; mRNA.
EMBL; AF227189; AAF74119.1; -; mRNA.
EMBL; U25764; AAA93228.1; -; Genomic_DNA.
CCDS; CCDS45694.1; -. [Q14596-1]
CCDS; CCDS77037.1; -. [Q14596-2]
RefSeq; NP_001278500.1; NM_001291571.1. [Q14596-2]
RefSeq; NP_001278501.1; NM_001291572.1.
RefSeq; NP_005890.2; NM_005899.4. [Q14596-1]
RefSeq; NP_114068.1; NM_031862.3. [Q14596-1]
RefSeq; XP_011523115.1; XM_011524813.1. [Q14596-1]
RefSeq; XP_016880131.1; XM_017024642.1. [Q14596-1]
UniGene; Hs.277721; -.
UniGene; Hs.708158; -.
PDB; 1WJ6; NMR; -; A=1-85.
PDB; 2BKF; X-ray; 1.56 A; A=1-85.
PDB; 2CP8; NMR; -; A=916-956.
PDB; 2G4S; X-ray; 2.15 A; A=1-85.
PDB; 2L8J; NMR; -; B=726-738.
PDB; 2MGW; NMR; -; A=913-959.
PDB; 2MJ5; NMR; -; B=913-959.
PDB; 4OLE; X-ray; 2.52 A; A/B/C/D=365-485.
PDBsum; 1WJ6; -.
PDBsum; 2BKF; -.
PDBsum; 2CP8; -.
PDBsum; 2G4S; -.
PDBsum; 2L8J; -.
PDBsum; 2MGW; -.
PDBsum; 2MJ5; -.
PDBsum; 4OLE; -.
ProteinModelPortal; Q14596; -.
SMR; Q14596; -.
BioGrid; 110253; 51.
IntAct; Q14596; 27.
MINT; MINT-2806845; -.
STRING; 9606.ENSP00000343479; -.
iPTMnet; Q14596; -.
PhosphoSitePlus; Q14596; -.
UniCarbKB; Q14596; -.
BioMuta; NBR1; -.
DMDM; 296439290; -.
EPD; Q14596; -.
MaxQB; Q14596; -.
PaxDb; Q14596; -.
PeptideAtlas; Q14596; -.
PRIDE; Q14596; -.
DNASU; 4077; -.
Ensembl; ENST00000341165; ENSP00000343479; ENSG00000188554. [Q14596-1]
Ensembl; ENST00000589872; ENSP00000467816; ENSG00000188554. [Q14596-2]
Ensembl; ENST00000590996; ENSP00000466667; ENSG00000188554. [Q14596-1]
GeneID; 4077; -.
KEGG; hsa:4077; -.
UCSC; uc010czd.4; human. [Q14596-1]
CTD; 4077; -.
DisGeNET; 4077; -.
EuPathDB; HostDB:ENSG00000188554.13; -.
GeneCards; NBR1; -.
HGNC; HGNC:6746; NBR1.
HPA; HPA022944; -.
HPA; HPA022999; -.
HPA; HPA023999; -.
MIM; 166945; gene.
neXtProt; NX_Q14596; -.
OpenTargets; ENSG00000188554; -.
PharmGKB; PA30510; -.
eggNOG; KOG4351; Eukaryota.
eggNOG; KOG4582; Eukaryota.
eggNOG; ENOG4111TKN; LUCA.
GeneTree; ENSGT00390000016335; -.
HOGENOM; HOG000220861; -.
HOVERGEN; HBG052578; -.
InParanoid; Q14596; -.
KO; K17987; -.
OMA; AYKALFA; -.
OrthoDB; EOG091G0RGJ; -.
PhylomeDB; Q14596; -.
TreeFam; TF328428; -.
SIGNOR; Q14596; -.
EvolutionaryTrace; Q14596; -.
GeneWiki; NBR1; -.
GenomeRNAi; 4077; -.
PRO; PR:Q14596; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000188554; -.
CleanEx; HS_NBR1; -.
ExpressionAtlas; Q14596; baseline and differential.
Genevisible; Q14596; HS.
GO; GO:0005776; C:autophagosome; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005770; C:late endosome; ISS:UniProtKB.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000407; C:pre-autophagosomal structure; IBA:GO_Central.
GO; GO:0051019; F:mitogen-activated protein kinase binding; ISS:BHF-UCL.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0016236; P:macroautophagy; IDA:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0030500; P:regulation of bone mineralization; ISS:BHF-UCL.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
CDD; cd14947; NBR1_like; 1.
CDD; cd06396; PB1_NBR1; 1.
InterPro; IPR032350; N_BRCA1_central.
InterPro; IPR033513; NBR1.
InterPro; IPR000270; PB1_dom.
InterPro; IPR034852; PB1_NBR1.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like.
InterPro; IPR000433; Znf_ZZ.
PANTHER; PTHR20930:SF2; PTHR20930:SF2; 1.
Pfam; PF16158; N_BRCA1_IG; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00569; ZZ; 1.
SMART; SM00666; PB1; 1.
SMART; SM00291; ZnF_ZZ; 1.
SUPFAM; SSF46934; SSF46934; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS50030; UBA; 1.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Lysosome; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Zinc; Zinc-finger.
CHAIN 1 966 Next to BRCA1 gene 1 protein.
/FTId=PRO_0000096746.
DOMAIN 4 85 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 913 957 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
ZN_FING 211 257 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
REGION 542 636 ATG8 family protein-binding.
REGION 727 738 ATG8 family protein-binding.
COMPBIAS 703 714 Poly-Glu.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000250|UniProtKB:Q501R9}.
MOD_RES 596 596 Phosphoserine.
{ECO:0000250|UniProtKB:Q501R9}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 910 966 PIISEDQTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVV
TELLQLNNNDWYSQRY -> GLWGLLSFLHLAKKCFFLKAP
SEAFSWF (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004314.
VARIANT 923 923 H -> R (in dbSNP:rs8482).
{ECO:0000269|PubMed:11179671,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8069304}.
/FTId=VAR_016106.
MUTAGEN 12 12 K->A: No effect on interaction with
SQSTM1. {ECO:0000269|PubMed:12813044}.
MUTAGEN 50 50 D->R: Loss of interaction with SQSTM1.
{ECO:0000269|PubMed:12813044,
ECO:0000269|PubMed:19250911}.
MUTAGEN 732 732 Y->A: Loss of interaction ATG8 family
proteins. {ECO:0000269|PubMed:19250911}.
CONFLICT 746 770 LGDSMYSSALSQPGLERGAEGKPGV -> WGILCTALRSHS
QAWSEVLKASLGF (in Ref. 1; CAA54274).
{ECO:0000305}.
STRAND 5 11 {ECO:0000244|PDB:2BKF}.
STRAND 14 21 {ECO:0000244|PDB:2BKF}.
HELIX 23 25 {ECO:0000244|PDB:2BKF}.
HELIX 28 39 {ECO:0000244|PDB:2BKF}.
STRAND 42 49 {ECO:0000244|PDB:2BKF}.
STRAND 55 58 {ECO:0000244|PDB:2BKF}.
HELIX 61 73 {ECO:0000244|PDB:2BKF}.
TURN 74 76 {ECO:0000244|PDB:2BKF}.
STRAND 77 84 {ECO:0000244|PDB:2BKF}.
STRAND 373 380 {ECO:0000244|PDB:4OLE}.
STRAND 384 386 {ECO:0000244|PDB:4OLE}.
STRAND 391 400 {ECO:0000244|PDB:4OLE}.
STRAND 402 404 {ECO:0000244|PDB:4OLE}.
STRAND 410 418 {ECO:0000244|PDB:4OLE}.
STRAND 420 423 {ECO:0000244|PDB:4OLE}.
HELIX 425 428 {ECO:0000244|PDB:4OLE}.
STRAND 439 447 {ECO:0000244|PDB:4OLE}.
STRAND 453 463 {ECO:0000244|PDB:4OLE}.
STRAND 466 478 {ECO:0000244|PDB:4OLE}.
HELIX 917 927 {ECO:0000244|PDB:2CP8}.
HELIX 932 939 {ECO:0000244|PDB:2CP8}.
TURN 940 944 {ECO:0000244|PDB:2CP8}.
HELIX 946 956 {ECO:0000244|PDB:2CP8}.
SEQUENCE 966 AA; 107413 MW; 6A057E67947838EF CRC64;
MEPQVTLNVT FKNEIQSFLV SDPENTTWAD IEAMVKVSFD LNTIQIKYLD EENEEVSINS
QGEYEEALKM AVKQGNQLQM QVHEGHHVVD EAPPPVVGAK RLAARAGKKP LAHYSSLVRV
LGSDMKTPED PAVQSFPLVP CDTDQPQDKP PDWFTSYLET FREQVVNETV EKLEQKLHEK
LVLQNPSLGS CPSEVSMPTS EETLFLPENQ FSWHIACNNC QRRIVGVRYQ CSLCPSYNIC
EDCEAGPYGH DTNHVLLKLR RPVVGSSEPF CHSKYSTPRL PAALEQVRLQ KQVDKNFLKA
EKQRLRAEKK QRKAEVKELK KQLKLHRKIH LWNSIHGLQS PKSPLGRPES LLQSNTLMLP
LQPCTSVMPM LSAAFVDENL PDGTHLQPGT KFIKHWRMKN TGNVKWSADT KLKFMWGNLT
LASTEKKDVL VPCLKAGHVG VVSVEFIAPA LEGTYTSHWR LSHKGQQFGP RVWCSIIVDP
FPSEESPDNI EKGMISSSKT DDLTCQQEET FLLAKEERQL GEVTEQTEGT AACIPQKAKN
VASERELYIP SVDLLTAQDL LSFELLDINI VQELERVPHN TPVDVTPCMS PLPHDSPLIE
KPGLGQIEEE NEGAGFKALP DSMVSVKRKA ENIASVEEAE EDLSGTQFVC ETVIRSLTLD
AAPDHNPPCR QKSLQMTFAL PEGPLGNEKE EIIHIAEEEA VMEEEEDEED EEEEDELKDE
VQSQSSASSE DYIIILPECF DTSRPLGDSM YSSALSQPGL ERGAEGKPGV EAGQEPAEAG
ERLPGGENQP QEHSISDILT TSQTLETVPL IPEVVELPPS LPRSSPCVHH HGSPGVDLPV
TIPEVSSVPD QIRGEPRGSS GLVNSRQKSY DHSRHHHGSS IAGGLVKGAL SVAASAYKAL
FAGPPVTAQP IISEDQTAAL MAHLFEMGFC DRQLNLRLLK KHNYNILQVV TELLQLNNND
WYSQRY


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