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Protein transport protein Sec24B (SEC24-related protein B)

 SC24B_HUMAN             Reviewed;        1268 AA.
O95487; B7ZKM8; B7ZKN4; Q0VG08;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
20-JUN-2018, entry version 161.
RecName: Full=Protein transport protein Sec24B {ECO:0000305};
AltName: Full=SEC24-related protein B;
Name=SEC24B {ECO:0000312|HGNC:HGNC:10704};
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), SUBUNIT, SUBCELLULAR LOCATION,
AND TOPOLOGY.
TISSUE=B-cell;
PubMed=10075675; DOI=10.1074/jbc.274.12.7833;
Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L.,
Orci L., Paccaud J.-P.;
"Sec24 proteins and sorting at the endoplasmic reticulum.";
J. Biol. Chem. 274:7833-7840(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, 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).
[5]
FUNCTION, SUBUNIT, INTERACTION WITH SEC22B, AND MUTAGENESIS OF
ARG-715.
PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
Mancias J.D., Goldberg J.;
"The transport signal on Sec22 for packaging into COPII-coated
vesicles is a conformational epitope.";
Mol. Cell 26:403-414(2007).
[6]
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).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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).
[8]
INTERACTION WITH RNF139.
PubMed=19706601; DOI=10.1074/jbc.M109.041376;
Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.;
"The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8
hampers ER to Golgi transport of sterol regulatory element-binding
protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces
SREBP-2 cleavage.";
J. Biol. Chem. 284:28995-29004(2009).
[9]
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).
[10]
FUNCTION, AND INTERACTION WITH TMED2 AND TMED10.
PubMed=20427317; DOI=10.1242/jcs.062950;
Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
"Selective export of human GPI-anchored proteins from the endoplasmic
reticulum.";
J. Cell Sci. 123:1705-1715(2010).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-329 AND SER-1224, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-55 (ISOFORM 3), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
INTERACTION WITH CNIH4.
PubMed=24405750; DOI=10.1111/tra.12148;
Sauvageau E., Rochdi M.D., Oueslati M., Hamdan F.F., Percherancier Y.,
Simpson J.C., Pepperkok R., Bouvier M.;
"CNIH4 interacts with newly synthesized GPCR and controls their export
from the endoplasmic reticulum.";
Traffic 15:383-400(2014).
[15] {ECO:0000244|PDB:3EH1}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 518-1268 IN COMPLEX WITH
ZINC, AND FUNCTION.
PubMed=18843296; DOI=10.1038/emboj.2008.208;
Mancias J.D., Goldberg J.;
"Structural basis of cargo membrane protein discrimination by the
human COPII coat machinery.";
EMBO J. 27:2918-2928(2008).
-!- FUNCTION: Component of the coat protein complex II (COPII) which
promotes the formation of transport vesicles from the endoplasmic
reticulum (ER). The coat has two main functions, the physical
deformation of the endoplasmic reticulum membrane into vesicles
and the selection of cargo molecules for their transport to the
Golgi complex (PubMed:17499046, PubMed:20427317, PubMed:18843296).
Plays a central role in cargo selection within the COPII complex
and together with SEC24A may have a different specificity compared
to SEC24C and SEC24D. May package preferentially cargos with
cytoplasmic DxE or LxxLE motifs and may also recognize
conformational epitopes (PubMed:17499046, PubMed:18843296).
{ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296,
ECO:0000269|PubMed:20427317}.
-!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
complex, the Sec13/31 complex and SAR1 (PubMed:10075675,
PubMed:17499046). Interacts with RNF139 (PubMed:19706601).
Interacts with TMED2 and TMED10 (PubMed:20427317). Interacts with
CNIH4 (PubMed:24405750). {ECO:0000269|PubMed:10075675,
ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:19706601,
ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:24405750}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000269|PubMed:10075675}; Peripheral membrane
protein {ECO:0000305|PubMed:10075675}; Cytoplasmic side
{ECO:0000305|PubMed:10075675}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10075675}; Peripheral membrane protein
{ECO:0000269|PubMed:10075675}; Cytoplasmic side
{ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol
{ECO:0000269|PubMed:10075675}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O95487-1; Sequence=Displayed;
Name=2;
IsoId=O95487-2; Sequence=VSP_035987;
Name=3;
IsoId=O95487-3; Sequence=VSP_054432, VSP_054433;
Note=No experimental confirmation available. Contains a
phosphoserine at position 55. {ECO:0000244|PubMed:24275569};
-!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA10335.1; Type=Frameshift; Positions=459, 483; Evidence={ECO:0000305};
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EMBL; AJ131245; CAA10335.1; ALT_FRAME; mRNA.
EMBL; AC105314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040137; AAH40137.1; -; mRNA.
EMBL; BC117135; AAI17136.1; -; mRNA.
EMBL; BC143268; AAI43269.1; -; mRNA.
EMBL; BC143276; AAI43277.1; -; mRNA.
CCDS; CCDS43260.1; -. [O95487-2]
CCDS; CCDS47124.1; -. [O95487-1]
CCDS; CCDS75179.1; -. [O95487-3]
RefSeq; NP_001036199.1; NM_001042734.3. [O95487-2]
RefSeq; NP_001287742.1; NM_001300813.2. [O95487-3]
RefSeq; NP_001305014.1; NM_001318085.1.
RefSeq; NP_001305015.1; NM_001318086.1.
RefSeq; NP_006314.2; NM_006323.4. [O95487-1]
UniGene; Hs.292472; -.
PDB; 3EH1; X-ray; 1.80 A; A=518-1268.
PDBsum; 3EH1; -.
ProteinModelPortal; O95487; -.
SMR; O95487; -.
BioGrid; 115696; 56.
IntAct; O95487; 33.
MINT; O95487; -.
STRING; 9606.ENSP00000265175; -.
iPTMnet; O95487; -.
PhosphoSitePlus; O95487; -.
BioMuta; SEC24B; -.
EPD; O95487; -.
MaxQB; O95487; -.
PaxDb; O95487; -.
PeptideAtlas; O95487; -.
PRIDE; O95487; -.
ProteomicsDB; 50915; -.
ProteomicsDB; 50916; -. [O95487-2]
Ensembl; ENST00000265175; ENSP00000265175; ENSG00000138802. [O95487-1]
Ensembl; ENST00000399100; ENSP00000382051; ENSG00000138802. [O95487-2]
Ensembl; ENST00000504968; ENSP00000428564; ENSG00000138802. [O95487-3]
GeneID; 10427; -.
KEGG; hsa:10427; -.
UCSC; uc003hzk.4; human. [O95487-1]
CTD; 10427; -.
DisGeNET; 10427; -.
EuPathDB; HostDB:ENSG00000138802.11; -.
GeneCards; SEC24B; -.
HGNC; HGNC:10704; SEC24B.
HPA; HPA038181; -.
MIM; 607184; gene.
neXtProt; NX_O95487; -.
OpenTargets; ENSG00000138802; -.
PharmGKB; PA35627; -.
eggNOG; KOG1985; Eukaryota.
eggNOG; COG5028; LUCA.
GeneTree; ENSGT00590000082962; -.
HOGENOM; HOG000196365; -.
HOVERGEN; HBG054850; -.
InParanoid; O95487; -.
KO; K14007; -.
OMA; NILPMTP; -.
OrthoDB; EOG091G011M; -.
PhylomeDB; O95487; -.
TreeFam; TF354244; -.
Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
ChiTaRS; SEC24B; human.
EvolutionaryTrace; O95487; -.
GeneWiki; SEC24B; -.
GenomeRNAi; 10427; -.
PRO; PR:O95487; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138802; -.
CleanEx; HS_SEC24B; -.
Genevisible; O95487; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
GO; GO:0090110; P:cargo loading into COPII-coated vesicle; IDA:UniProtKB.
GO; GO:0021747; P:cochlear nucleus development; IEA:Ensembl.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0061156; P:pulmonary artery morphogenesis; IEA:Ensembl.
GO; GO:1901301; P:regulation of cargo loading into COPII-coated vesicle; IEA:Ensembl.
GO; GO:0090178; P:regulation of establishment of planar polarity involved in neural tube closure; IEA:Ensembl.
Gene3D; 3.40.20.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
InterPro; IPR007123; Gelsolin-like_dom.
InterPro; IPR036180; Gelsolin-like_dom_sf.
InterPro; IPR006900; Sec23/24_helical_dom.
InterPro; IPR036175; Sec23/24_helical_dom_sf.
InterPro; IPR006896; Sec23/24_trunk_dom.
InterPro; IPR012990; Sec23_24_beta_S.
InterPro; IPR036465; vWFA_dom_sf.
InterPro; IPR006895; Znf_Sec23_Sec24.
InterPro; IPR036174; Znf_Sec23_Sec24_sf.
Pfam; PF00626; Gelsolin; 1.
Pfam; PF08033; Sec23_BS; 1.
Pfam; PF04815; Sec23_helical; 1.
Pfam; PF04811; Sec23_trunk; 1.
Pfam; PF04810; zf-Sec23_Sec24; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF81811; SSF81811; 1.
SUPFAM; SSF82754; SSF82754; 1.
SUPFAM; SSF82919; SSF82919; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
ER-Golgi transport; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 1268 Protein transport protein Sec24B.
/FTId=PRO_0000205155.
REPEAT 1141 1213 Gelsolin-like. {ECO:0000255}.
REGION 605 629 Zinc finger-like.
COMPBIAS 379 387 Poly-Glu.
METAL 605 605 Zinc. {ECO:0000244|PDB:3EH1}.
METAL 608 608 Zinc. {ECO:0000244|PDB:3EH1}.
METAL 626 626 Zinc. {ECO:0000244|PDB:3EH1}.
METAL 629 629 Zinc. {ECO:0000244|PDB:3EH1}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 329 329 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1224 1224 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 44 44 N -> NETGFHHVAQASLELLDPSNLPASASQIAGST (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054432.
VAR_SEQ 354 388 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035987.
VAR_SEQ 496 496 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054433.
VARIANT 456 456 A -> G (in dbSNP:rs35705351).
/FTId=VAR_047934.
MUTAGEN 715 715 R->A: Decreased ability to package the
SNARE SEC22B cargo into COPII vesicles.
Has no effect on other cargos packaging.
{ECO:0000269|PubMed:17499046}.
CONFLICT 23 23 A -> S (in Ref. 1; CAA10335).
{ECO:0000305}.
HELIX 520 522 {ECO:0000244|PDB:3EH1}.
STRAND 524 526 {ECO:0000244|PDB:3EH1}.
TURN 527 529 {ECO:0000244|PDB:3EH1}.
HELIX 548 553 {ECO:0000244|PDB:3EH1}.
TURN 557 559 {ECO:0000244|PDB:3EH1}.
STRAND 560 570 {ECO:0000244|PDB:3EH1}.
HELIX 571 577 {ECO:0000244|PDB:3EH1}.
STRAND 582 585 {ECO:0000244|PDB:3EH1}.
TURN 606 608 {ECO:0000244|PDB:3EH1}.
STRAND 617 625 {ECO:0000244|PDB:3EH1}.
TURN 627 629 {ECO:0000244|PDB:3EH1}.
STRAND 632 634 {ECO:0000244|PDB:3EH1}.
HELIX 637 639 {ECO:0000244|PDB:3EH1}.
HELIX 651 653 {ECO:0000244|PDB:3EH1}.
HELIX 655 658 {ECO:0000244|PDB:3EH1}.
STRAND 660 666 {ECO:0000244|PDB:3EH1}.
HELIX 668 670 {ECO:0000244|PDB:3EH1}.
STRAND 672 674 {ECO:0000244|PDB:3EH1}.
STRAND 679 685 {ECO:0000244|PDB:3EH1}.
HELIX 688 693 {ECO:0000244|PDB:3EH1}.
HELIX 695 706 {ECO:0000244|PDB:3EH1}.
TURN 707 709 {ECO:0000244|PDB:3EH1}.
STRAND 717 731 {ECO:0000244|PDB:3EH1}.
STRAND 740 745 {ECO:0000244|PDB:3EH1}.
HELIX 755 757 {ECO:0000244|PDB:3EH1}.
STRAND 759 761 {ECO:0000244|PDB:3EH1}.
TURN 762 765 {ECO:0000244|PDB:3EH1}.
HELIX 766 775 {ECO:0000244|PDB:3EH1}.
HELIX 776 778 {ECO:0000244|PDB:3EH1}.
HELIX 790 801 {ECO:0000244|PDB:3EH1}.
TURN 802 804 {ECO:0000244|PDB:3EH1}.
STRAND 806 812 {ECO:0000244|PDB:3EH1}.
HELIX 831 834 {ECO:0000244|PDB:3EH1}.
STRAND 835 837 {ECO:0000244|PDB:3EH1}.
HELIX 847 857 {ECO:0000244|PDB:3EH1}.
STRAND 860 866 {ECO:0000244|PDB:3EH1}.
HELIX 874 877 {ECO:0000244|PDB:3EH1}.
HELIX 879 882 {ECO:0000244|PDB:3EH1}.
TURN 883 885 {ECO:0000244|PDB:3EH1}.
STRAND 888 890 {ECO:0000244|PDB:3EH1}.
TURN 896 898 {ECO:0000244|PDB:3EH1}.
HELIX 900 915 {ECO:0000244|PDB:3EH1}.
STRAND 919 928 {ECO:0000244|PDB:3EH1}.
STRAND 932 943 {ECO:0000244|PDB:3EH1}.
STRAND 945 954 {ECO:0000244|PDB:3EH1}.
STRAND 960 968 {ECO:0000244|PDB:3EH1}.
STRAND 974 985 {ECO:0000244|PDB:3EH1}.
STRAND 991 1003 {ECO:0000244|PDB:3EH1}.
HELIX 1006 1011 {ECO:0000244|PDB:3EH1}.
HELIX 1015 1032 {ECO:0000244|PDB:3EH1}.
HELIX 1035 1054 {ECO:0000244|PDB:3EH1}.
STRAND 1066 1068 {ECO:0000244|PDB:3EH1}.
HELIX 1069 1071 {ECO:0000244|PDB:3EH1}.
HELIX 1074 1082 {ECO:0000244|PDB:3EH1}.
TURN 1085 1087 {ECO:0000244|PDB:3EH1}.
HELIX 1095 1107 {ECO:0000244|PDB:3EH1}.
HELIX 1110 1117 {ECO:0000244|PDB:3EH1}.
STRAND 1120 1123 {ECO:0000244|PDB:3EH1}.
STRAND 1133 1135 {ECO:0000244|PDB:3EH1}.
STRAND 1138 1140 {ECO:0000244|PDB:3EH1}.
HELIX 1150 1152 {ECO:0000244|PDB:3EH1}.
STRAND 1157 1162 {ECO:0000244|PDB:3EH1}.
STRAND 1164 1171 {ECO:0000244|PDB:3EH1}.
HELIX 1177 1182 {ECO:0000244|PDB:3EH1}.
HELIX 1189 1191 {ECO:0000244|PDB:3EH1}.
STRAND 1194 1196 {ECO:0000244|PDB:3EH1}.
HELIX 1205 1219 {ECO:0000244|PDB:3EH1}.
STRAND 1221 1223 {ECO:0000244|PDB:3EH1}.
STRAND 1226 1236 {ECO:0000244|PDB:3EH1}.
HELIX 1237 1241 {ECO:0000244|PDB:3EH1}.
HELIX 1255 1267 {ECO:0000244|PDB:3EH1}.
SEQUENCE 1268 AA; 137418 MW; 0E08B982D0982F84 CRC64;
MSAPAGSSHP AASARIPPKF GGAAVSGAAA PAGPGAGPAP HQQNGPAQNQ MQVPSGYGLH
HQNYIAPSGH YSQGPGKMTS LPLDTQCGDY YSALYTVPTQ NVTPNTVNQQ PGAQQLYSRG
PPAPHIVGST LGSFQGAASS ASHLHTSASQ PYSSFVNHYN SPAMYSASSS VASQGFPSTC
GHYAMSTVSN AAYPSVSYPS LPAGDTYGQM FTSQNAPTVR PVKDNSFSGQ NTAISHPSPL
PPLPSQQHHQ QQSLSGYSTL TWSSPGLPST QDNLIRNHTG SLAVANNNPT ITVADSLSCP
VMQNVQPPKS SPVVSTVLSG SSGSSSTRTP PTANHPVEPV TSVTQPSELL QQKGVQYGEY
VNNQASSAPT PLSSTSDDEE EEEEDEEAGV DSSSTTSSAS PMPNSYDALE GGSYPDMLSS
SASSPAPDPA PEPDPASAPA PASAPAPVVP QPSKMAKPFG YGYPTLQPGY QNATAPLISG
VQPSNPVYSG FQQYPQQYPG VNQLSSSIGG LSLQSSPQPE SLRPVNLTQE RNILPMTPVW
APVPNLNADL KKLNCSPDSF RCTLTNIPQT QALLNKAKLP LGLLLHPFRD LTQLPVITSN
TIVRCRSCRT YINPFVSFID QRRWKCNLCY RVNDVPEEFM YNPLTRSYGE PHKRPEVQNS
TVEFIASSDY MLRPPQPAVY LFVLDVSHNA VEAGYLTILC QSLLENLDKL PGDSRTRIGF
MTFDSTIHFY NLQEGLSQPQ MLIVSDIDDV FLPTPDSLLV NLYESKELIK DLLNALPNMF
TNTRETHSAL GPALQAAFKL MSPTGGRVSV FQTQLPSLGA GLLQSREDPN QRSSTKVVQH
LGPATDFYKK LALDCSGQQT AVDLFLLSSQ YSDLASLACM SKYSAGCIYY YPSFHYTHNP
SQAEKLQKDL KRYLTRKIGF EAVMRIRCTK GLSMHTFHGN FFVRSTDLLS LANINPDAGF
AVQLSIEESL TDTSLVCFQT ALLYTSSKGE RRIRVHTLCL PVVSSLADVY AGVDVQAAIC
LLANMAVDRS VSSSLSDARD ALVNAVVDSL SAYGSTVSNL QHSALMAPSS LKLFPLYVLA
LLKQKAFRTG TSTRLDDRVY AMCQIKSQPL VHLMKMIHPN LYRIDRLTDE GAVHVNDRIV
PQPPLQKLSA EKLTREGAFL MDCGSVFYIW VGKGCDNNFI EDVLGYTNFA SIPQKMTHLP
ELDTLSSERA RSFITWLRDS RPLSPILHIV KDESPAKAEF FQHLIEDRTE AAFSYYEFLL
HVQQQICK


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