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Protein unc-13 homolog A (Munc13-1)

 UN13A_RAT               Reviewed;        1735 AA.
Q62768;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 144.
RecName: Full=Protein unc-13 homolog A;
AltName: Full=Munc13-1;
Name=Unc13a; Synonyms=Unc13h1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=7559667; DOI=10.1074/jbc.270.42.25273;
Brose N., Hofmann K., Hata Y., Suedhof T.C.;
"Mammalian homologues of Caenorhabditis elegans unc-13 gene define
novel family of C2-domain proteins.";
J. Biol. Chem. 270:25273-25280(1995).
[2]
INTERACTION WITH SYNTAXIN 1.
PubMed=8999968; DOI=10.1074/jbc.272.4.2520;
Betz A., Okamoto M., Benseler F., Brose N.;
"Direct interaction of the rat unc-13 homologue Munc13-1 with the N
terminus of syntaxin.";
J. Biol. Chem. 272:2520-2526(1997).
[3]
INTERACTION WITH DOC2A.
PubMed=9195900; DOI=10.1074/jbc.272.26.16081;
Orita S., Naito A., Sakaguchi G., Maeda M., Igarashi H., Sasaki T.,
Takai Y.;
"Physical and functional interactions of Doc2 and Munc13 in Ca2+-
dependent exocytotic machinery.";
J. Biol. Chem. 272:16081-16084(1997).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-567.
PubMed=9697857; DOI=10.1016/S0896-6273(00)80520-6;
Betz A., Ashery U., Rickmann M., Augustin I., Neher E., Suedhof T.C.,
Rettig J., Brose N.;
"Munc13-1 is a presynaptic phorbol ester receptor that enhances
neurotransmitter release.";
Neuron 21:123-136(1998).
[5]
INTERACTION WITH DOC2A.
PubMed=9736751; DOI=10.1073/pnas.95.19.11418;
Mochida S., Orita S., Sakaguchi G., Sasaki T., Takai Y.;
"Role of the Doc2 alpha-Munc13-1 interaction in the neurotransmitter
release process.";
Proc. Natl. Acad. Sci. U.S.A. 95:11418-11422(1998).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9895278; DOI=10.1042/bj3370363;
Augustin I., Betz A., Herrmann C., Jo T., Brose N.;
"Differential expression of two novel Munc13 proteins in rat brain.";
Biochem. J. 337:363-371(1999).
[7]
FUNCTION, AND INTERACTION WITH RIMS1.
PubMed=11343654; DOI=10.1016/S0896-6273(01)00272-0;
Betz A., Thakur P., Junge H.J., Ashery U., Rhee J.S., Scheuss V.,
Rosenmund C., Rettig J., Brose N.;
"Functional interaction of the active zone proteins Munc13-1 and RIM1
in synaptic vesicle priming.";
Neuron 30:183-196(2001).
[8]
FUNCTION.
PubMed=11792326; DOI=10.1016/S0092-8674(01)00635-3;
Rhee J.S., Betz A., Pyott S., Reim K., Varoqueaux F., Augustin I.,
Hesse D., Suedhof T.C., Takahashi M., Rosenmund C., Brose N.;
"Beta phorbol ester- and diacylglycerol-induced augmentation of
transmitter release is mediated by Munc13s and not by PKCs.";
Cell 108:121-133(2002).
[9]
INTERACTION WITH BSN, AND IDENTIFICATION IN A COMPLEX WITH ERC2 AND
RIMS1.
PubMed=12163476; DOI=10.1083/jcb.200202083;
Ohtsuka T., Takao-Rikitsu E., Inoue E., Inoue M., Takeuchi M.,
Matsubara K., Deguchi-Tawarada M., Satoh K., Morimoto K.,
Nakanishi H., Takai Y.;
"Cast: a novel protein of the cytomatrix at the active zone of
synapses that forms a ternary complex with RIM1 and Munc13-1.";
J. Cell Biol. 158:577-590(2002).
[10]
TISSUE SPECIFICITY.
PubMed=12871971; DOI=10.1074/jbc.M303203200;
Sheu L., Pasyk E.A., Ji J., Huang X., Gao X., Varoqueaux F., Brose N.,
Gaisano H.Y.;
"Regulation of insulin exocytosis by Munc13-1.";
J. Biol. Chem. 278:27556-27563(2003).
[11]
INTERACTION WITH BSN.
PubMed=14734538; DOI=10.1083/jcb.200307101;
Takao-Rikitsu E., Mochida S., Inoue E., Deguchi-Tawarada M., Inoue M.,
Ohtsuka T., Takai Y.;
"Physical and functional interaction of the active zone proteins,
CAST, RIM1, and Bassoon, in neurotransmitter release.";
J. Cell Biol. 164:301-311(2004).
[12]
DOMAIN, AND MUTAGENESIS OF GLN-1190; LEU-1279; ILE-1364; VAL-1603 AND
ASP-1655.
PubMed=16271475; DOI=10.1016/j.cub.2005.10.055;
Stevens D.R., Wu Z.-X., Matti U., Junge H.J., Schirra C., Becherer U.,
Wojcik S.M., Brose N., Rettig J.;
"Identification of the minimal protein domain required for priming
activity of Munc13-1.";
Curr. Biol. 15:2243-2248(2005).
[13]
INTERACTION WITH RIMS2.
PubMed=16052212; DOI=10.1038/sj.emboj.7600753;
Dulubova I., Lou X., Lu J., Huryeva I., Alam A., Schneggenburger R.,
Suedhof T.C., Rizo J.;
"A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?";
EMBO J. 24:2839-2850(2005).
[14]
INTERACTION WITH RIMS1, AND MUTAGENESIS OF THR-22; TYR-23; VAL-64;
HIS-119 AND ILE-121.
PubMed=16704978; DOI=10.1074/jbc.M601421200;
Andrews-Zwilling Y.S., Kawabe H., Reim K., Varoqueaux F., Brose N.;
"Binding to Rab3A-interacting molecule RIM regulates the presynaptic
recruitment of Munc13-1 and ubMunc13-2.";
J. Biol. Chem. 281:19720-19731(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-241; SER-244
AND SER-255, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[16]
STRUCTURE BY NMR OF 567-616.
PubMed=15667202; DOI=10.1021/bi0476127;
Shen N., Guryev O., Rizo J.;
"Intramolecular occlusion of the diacylglycerol-binding site in the C1
domain of munc13-1.";
Biochemistry 44:1089-1096(2005).
[17]
X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 1-128, AND X-RAY
CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 2-150 IN COMPLEX WITH RIMS2.
PubMed=16732694; DOI=10.1371/journal.pbio.0040192;
Lu J., Machius M., Dulubova I., Dai H., Suedhof T.C., Tomchick D.R.,
Rizo J.;
"Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer
switch.";
PLoS Biol. 4:1159-1172(2006).
-!- FUNCTION: Plays a role in vesicle maturation during exocytosis as
a target of the diacylglycerol second messenger pathway. Involved
in neurotransmitter release by acting in synaptic vesicle priming
prior to vesicle fusion and participates in the activity-dependent
refilling of readily releasable vesicle pool (RRP). Essential for
synaptic vesicle maturation in most excitatory/glutamatergic but
not inhibitory/GABA-mediated synapses. Also involved in secretory
granule priming in insulin secretion. Plays a role in dendrite
formation by melanocytes (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q9UPW8, ECO:0000269|PubMed:11343654,
ECO:0000269|PubMed:11792326, ECO:0000269|PubMed:9697857}.
-!- SUBUNIT: Interacts with the N-termini of STX1A and/or STX1B1 and
DOC2A. Interacts with BSN. Interacts with RIMS1 which recruits
UNC13A to the active zone. Forms homodimers via its first C2
domain. Also interacts via this domain with the zinc finger domain
of RIMS2. Part of a complex consisting of ERC2, RIMS1 and UNC13A.
Also part of a complex consisting of UNC13A, RIMS2 and RAB3A.
Interacts with FBXO45 (via SRY domain); leading to the degradation
of UNC13A by the proteasome (By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-15584670, EBI-15584670;
Q9JIS1:Rims2; NbExp=4; IntAct=EBI-15584670, EBI-6972631;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein. Cell junction, synapse, presynaptic cell
membrane; Peripheral membrane protein. Note=Localized to the
active zone of presynaptic density. Translocated to the plasma
membrane in response to phorbol ester binding.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q62768-1; Sequence=Displayed;
Name=2;
IsoId=Q62768-2; Sequence=VSP_011382;
Name=3;
IsoId=Q62768-3; Sequence=VSP_011383;
-!- TISSUE SPECIFICITY: Expressed in brain, with highest levels in the
olfactory bulb, striatum, cerebral cortex, hippocampus and
cerebellum. Also expressed in pancreatic islet cells.
{ECO:0000269|PubMed:12871971, ECO:0000269|PubMed:7559667,
ECO:0000269|PubMed:9895278}.
-!- DEVELOPMENTAL STAGE: First detected at birth, after which
expression level is steadily increasing until it reaches a plateau
at P15. {ECO:0000269|PubMed:9895278}.
-!- DOMAIN: The C2 domains are not involved in calcium-dependent
phospholipid binding. {ECO:0000269|PubMed:16271475}.
-!- DOMAIN: The C-terminal region containing both MHD domains and the
third C2 domain is required for synaptic vesicle priming activity.
{ECO:0000269|PubMed:16271475}.
-!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
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EMBL; U24070; AAC52266.1; -; mRNA.
PIR; A57607; A57607.
RefSeq; NP_074052.1; NM_022861.1. [Q62768-1]
UniGene; Rn.10126; -.
PDB; 1Y8F; NMR; -; A=567-616.
PDB; 2CJS; X-ray; 1.78 A; A/B=2-150.
PDB; 2CJT; X-ray; 1.44 A; A/B/C/D=1-128.
PDB; 2KDU; NMR; -; B=458-492.
PDB; 3KWT; X-ray; 1.89 A; A=675-820.
PDB; 3KWU; X-ray; 1.37 A; A=675-820.
PDB; 3SWH; X-ray; 2.65 A; A/B=1148-1407, A/B=1453-1531.
PDB; 4Y21; X-ray; 2.90 A; A=942-1407, A=1453-1523.
PDB; 5UE8; X-ray; 3.35 A; A/B=529-1407, A/B=1452-1531.
PDB; 5UF7; X-ray; 2.90 A; A=942-1407, A=1453-1531.
PDBsum; 1Y8F; -.
PDBsum; 2CJS; -.
PDBsum; 2CJT; -.
PDBsum; 2KDU; -.
PDBsum; 3KWT; -.
PDBsum; 3KWU; -.
PDBsum; 3SWH; -.
PDBsum; 4Y21; -.
PDBsum; 5UE8; -.
PDBsum; 5UF7; -.
ProteinModelPortal; Q62768; -.
SMR; Q62768; -.
BioGrid; 249207; 1.
CORUM; Q62768; -.
DIP; DIP-29191N; -.
IntAct; Q62768; 3.
STRING; 10116.ENSRNOP00000025162; -.
CarbonylDB; Q62768; -.
iPTMnet; Q62768; -.
PhosphoSitePlus; Q62768; -.
SwissPalm; Q62768; -.
PaxDb; Q62768; -.
PRIDE; Q62768; -.
GeneID; 64829; -.
KEGG; rno:64829; -.
CTD; 23025; -.
RGD; 619722; Unc13a.
eggNOG; KOG1011; Eukaryota.
eggNOG; ENOG410XS5D; LUCA.
HOVERGEN; HBG057340; -.
InParanoid; Q62768; -.
KO; K15293; -.
PhylomeDB; Q62768; -.
EvolutionaryTrace; Q62768; -.
PRO; PR:Q62768; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0097060; C:synaptic membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005516; F:calmodulin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
GO; GO:0000149; F:SNARE binding; IDA:RGD.
GO; GO:0030507; F:spectrin binding; IPI:RGD.
GO; GO:0019905; F:syntaxin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0017075; F:syntaxin-1 binding; IDA:ParkinsonsUK-UCL.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0061789; P:dense core granule priming; IGI:SynGO-UCL.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:RGD.
GO; GO:0007269; P:neurotransmitter secretion; IDA:RGD.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:InterPro.
GO; GO:0016188; P:synaptic vesicle maturation; IEA:InterPro.
GO; GO:0016082; P:synaptic vesicle priming; IDA:RGD.
CDD; cd00029; C1; 1.
CDD; cd04027; C2B_Munc13; 1.
Gene3D; 2.60.40.150; -; 3.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR010439; CAPS_dom.
InterPro; IPR014770; Munc13_1.
InterPro; IPR014772; Munc13_dom-2.
InterPro; IPR019558; Munc13_subgr_dom-2.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR027080; Unc-13.
InterPro; IPR037302; Unc-13_C2B.
InterPro; IPR027082; Unc13A.
PANTHER; PTHR10480; PTHR10480; 1.
PANTHER; PTHR10480:SF1; PTHR10480:SF1; 1.
Pfam; PF00130; C1_1; 1.
Pfam; PF00168; C2; 3.
Pfam; PF06292; DUF1041; 1.
Pfam; PF10540; Membr_traf_MHD; 1.
SMART; SM00109; C1; 1.
SMART; SM00239; C2; 3.
SMART; SM01145; DUF1041; 1.
PROSITE; PS50004; C2; 2.
PROSITE; PS51258; MHD1; 1.
PROSITE; PS51259; MHD2; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Differentiation;
Exocytosis; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
CHAIN 1 1735 Protein unc-13 homolog A.
/FTId=PRO_0000188574.
DOMAIN 1 79 C2 1. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 676 782 C2 2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 1106 1249 MHD1. {ECO:0000255|PROSITE-
ProRule:PRU00587}.
DOMAIN 1358 1525 MHD2. {ECO:0000255|PROSITE-
ProRule:PRU00588}.
DOMAIN 1564 1691 C2 3. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
ZN_FING 566 616 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
COILED 319 370 {ECO:0000255}.
COMPBIAS 320 452 Glu-rich.
METAL 580 580 Zinc 1.
METAL 583 583 Zinc 1.
METAL 597 597 Zinc 2.
METAL 600 600 Zinc 2.
METAL 608 608 Zinc 1.
METAL 616 616 Zinc 2.
MOD_RES 239 239 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 1434 1456 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_011382.
VAR_SEQ 1541 1559 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_011383.
MUTAGEN 22 22 T->I: No effect on binding to RIMS1.
{ECO:0000269|PubMed:16704978}.
MUTAGEN 23 23 Y->N: No effect on binding to RIMS1.
{ECO:0000269|PubMed:16704978}.
MUTAGEN 64 64 V->M: No effect on binding to RIMS1.
{ECO:0000269|PubMed:16704978}.
MUTAGEN 119 119 H->R: No effect on binding to RIMS1.
{ECO:0000269|PubMed:16704978}.
MUTAGEN 121 121 I->N: Abolishes binding to RIMS1.
{ECO:0000269|PubMed:16704978}.
MUTAGEN 567 567 H->K: Loss of phorbol-ester binding.
{ECO:0000269|PubMed:9697857}.
MUTAGEN 1190 1190 Q->R: Loss of binding to STX1B and
priming activity; when associated with P-
1279 and E-1655.
{ECO:0000269|PubMed:16271475}.
MUTAGEN 1279 1279 L->P: Loss of binding to STX1B and
priming activity; when associated with R-
1190 and E-1655.
{ECO:0000269|PubMed:16271475}.
MUTAGEN 1364 1364 I->F: Loss of binding to STX1B and
priming activity.
{ECO:0000269|PubMed:16271475}.
MUTAGEN 1603 1603 V->D: Loss of binding to STX1B and
priming activity.
{ECO:0000269|PubMed:16271475}.
MUTAGEN 1655 1655 D->E: Loss of binding to STX1B and
priming activity; when associated with R-
1190 and P-1279.
{ECO:0000269|PubMed:16271475}.
STRAND 2 12 {ECO:0000244|PDB:2CJT}.
HELIX 17 19 {ECO:0000244|PDB:2CJT}.
STRAND 21 28 {ECO:0000244|PDB:2CJT}.
STRAND 31 34 {ECO:0000244|PDB:2CJT}.
STRAND 38 42 {ECO:0000244|PDB:2CJT}.
STRAND 44 53 {ECO:0000244|PDB:2CJT}.
STRAND 57 66 {ECO:0000244|PDB:2CJT}.
STRAND 72 81 {ECO:0000244|PDB:2CJT}.
HELIX 82 84 {ECO:0000244|PDB:2CJT}.
STRAND 95 98 {ECO:0000244|PDB:2CJT}.
STRAND 102 106 {ECO:0000244|PDB:2CJT}.
STRAND 109 111 {ECO:0000244|PDB:2CJT}.
STRAND 120 128 {ECO:0000244|PDB:2CJT}.
HELIX 135 150 {ECO:0000244|PDB:2CJS}.
HELIX 459 478 {ECO:0000244|PDB:2KDU}.
HELIX 487 490 {ECO:0000244|PDB:2KDU}.
HELIX 544 558 {ECO:0000244|PDB:5UE8}.
STRAND 569 572 {ECO:0000244|PDB:5UE8}.
STRAND 581 583 {ECO:0000244|PDB:5UE8}.
HELIX 590 592 {ECO:0000244|PDB:5UE8}.
STRAND 594 597 {ECO:0000244|PDB:5UE8}.
TURN 598 600 {ECO:0000244|PDB:5UE8}.
TURN 606 608 {ECO:0000244|PDB:5UE8}.
HELIX 609 611 {ECO:0000244|PDB:5UE8}.
HELIX 616 627 {ECO:0000244|PDB:5UE8}.
HELIX 630 650 {ECO:0000244|PDB:5UE8}.
HELIX 653 661 {ECO:0000244|PDB:5UE8}.
HELIX 666 680 {ECO:0000244|PDB:5UE8}.
STRAND 689 700 {ECO:0000244|PDB:3KWU}.
STRAND 712 718 {ECO:0000244|PDB:3KWU}.
STRAND 721 724 {ECO:0000244|PDB:3KWU}.
STRAND 735 744 {ECO:0000244|PDB:3KWU}.
STRAND 746 748 {ECO:0000244|PDB:5UE8}.
STRAND 750 757 {ECO:0000244|PDB:3KWU}.
HELIX 762 767 {ECO:0000244|PDB:3KWU}.
TURN 768 770 {ECO:0000244|PDB:3KWU}.
STRAND 774 784 {ECO:0000244|PDB:3KWU}.
HELIX 785 787 {ECO:0000244|PDB:3KWU}.
STRAND 790 797 {ECO:0000244|PDB:3KWU}.
STRAND 810 818 {ECO:0000244|PDB:3KWU}.
HELIX 828 843 {ECO:0000244|PDB:5UE8}.
TURN 844 850 {ECO:0000244|PDB:5UE8}.
TURN 869 871 {ECO:0000244|PDB:5UE8}.
HELIX 872 880 {ECO:0000244|PDB:5UE8}.
TURN 881 883 {ECO:0000244|PDB:5UE8}.
HELIX 886 897 {ECO:0000244|PDB:5UE8}.
HELIX 898 900 {ECO:0000244|PDB:5UE8}.
STRAND 901 903 {ECO:0000244|PDB:5UE8}.
HELIX 906 920 {ECO:0000244|PDB:5UE8}.
HELIX 932 936 {ECO:0000244|PDB:5UE8}.
HELIX 944 961 {ECO:0000244|PDB:5UF7}.
HELIX 964 967 {ECO:0000244|PDB:5UF7}.
HELIX 973 995 {ECO:0000244|PDB:5UF7}.
HELIX 1005 1026 {ECO:0000244|PDB:5UF7}.
HELIX 1028 1035 {ECO:0000244|PDB:5UF7}.
STRAND 1039 1041 {ECO:0000244|PDB:4Y21}.
STRAND 1051 1053 {ECO:0000244|PDB:4Y21}.
HELIX 1059 1077 {ECO:0000244|PDB:5UF7}.
HELIX 1079 1082 {ECO:0000244|PDB:5UF7}.
TURN 1087 1089 {ECO:0000244|PDB:5UF7}.
HELIX 1092 1116 {ECO:0000244|PDB:5UF7}.
HELIX 1123 1140 {ECO:0000244|PDB:5UF7}.
TURN 1141 1143 {ECO:0000244|PDB:5UF7}.
TURN 1145 1147 {ECO:0000244|PDB:5UF7}.
STRAND 1148 1150 {ECO:0000244|PDB:5UF7}.
HELIX 1159 1187 {ECO:0000244|PDB:3SWH}.
STRAND 1192 1195 {ECO:0000244|PDB:3SWH}.
HELIX 1201 1218 {ECO:0000244|PDB:3SWH}.
HELIX 1224 1256 {ECO:0000244|PDB:3SWH}.
STRAND 1258 1261 {ECO:0000244|PDB:5UF7}.
HELIX 1263 1285 {ECO:0000244|PDB:3SWH}.
TURN 1286 1290 {ECO:0000244|PDB:3SWH}.
HELIX 1293 1320 {ECO:0000244|PDB:3SWH}.
HELIX 1322 1337 {ECO:0000244|PDB:3SWH}.
HELIX 1353 1378 {ECO:0000244|PDB:3SWH}.
HELIX 1381 1402 {ECO:0000244|PDB:3SWH}.
STRAND 1454 1456 {ECO:0000244|PDB:3SWH}.
STRAND 1458 1461 {ECO:0000244|PDB:4Y21}.
HELIX 1472 1487 {ECO:0000244|PDB:3SWH}.
HELIX 1488 1490 {ECO:0000244|PDB:3SWH}.
HELIX 1495 1499 {ECO:0000244|PDB:3SWH}.
HELIX 1502 1513 {ECO:0000244|PDB:3SWH}.
TURN 1516 1518 {ECO:0000244|PDB:5UF7}.
SEQUENCE 1735 AA; 196356 MW; BFE7D0467D258900 CRC64;
MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM FEINRLDLGL
TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQAIMADSEI CGTKDPTFHR
ILLDAHFELP LDIPEEEARY WAKKLEQLNA MRDQDEYSFQ DQQDKPLPVP SSQCCNWNYF
GWGEQNDDPD SAVDDRDSDY RSETSNSIPP PYYTTSQPNA SVHQYSVRPP PLGSRESYSD
SMHSYEEFSE PRALSPTGSS RYASSGELSQ GSSQLSEDFD PDEHSLQGSE LDDERDRDSY
HSCHSSVSYH KDSPRWDQDE EDLEDLEDLE DEELPEEEEL EEEELEEEEE LEEEELELEE
EEEVPDDLAS YTQQEDTTVA EPKEFKRISF PTAAPQKEDK VSAVPIEAPD VSKGIPKAAT
PEEKAAAECA QEAEPPKSEE SFRSREAEEG QEGQDAMSRA KANWLRAFNK VRMQLQEARG
EGEMSKSLWF KGGPGGGLII IDSMPDIRKR KPIPLVSDLA MSLVQSRKAG ITSALASSTL
NNEELKNHVY KKTLQALIYP ISCTTPHNFE VWTATTPTYC YECEGLLWGI ARQGMRCTEC
GVKCHEKCQD LLNADCLQRA AEKSSKHGAE DRTQNIIMVL KDRMKIRERN KPEIFELIQE
VFAVTKSAHT QQMKAVKQSV LDGTSKWSAK ISITVVCAQG LQAKDKTGSS DPYVTVQVGK
TKKRTKTIYG NLNPVWEENF HFECHNSSDR IKVRVLDEDD DIKSRVKQRF KRESDDFLGQ
TIIEVRTLSG EMDVWYNLDK RTDKSAVSGA IRLHISVEIK GEEKVAPYHV QYTCLHENLF
HFVTDVQNNG VVKIPDAKGD DAWKVYYDET AQEIVDEFAM RYGVESIYQA MTHFACLSSK
YMCPGVPAVM STLLANINAY YAHTTASTNV SASDRFAASN FGKERFVKLL DQLHNSLRID
LSMYRNNFPA SSPERLQDLK STVDLLTSIT FFRMKVQELQ SPPRASQVVK DCVKACLNST
YEYIFNNCHE LYGREYQTDP AKKGEVPPEE QGPSIKNLDF WSKLITLIVS IIEEDKNSYT
PCLNQFPQEL NVGKISAEVM WSLFAQDMKY AMEEHDKHRL CKSADYMNLH FKVKWLYNEY
VAELPTFKDR VPEYPAWFEP FVIQWLDENE EVSRDFLHGA LERDKKDGFQ QTSEHALFSC
SVVDVFSQLN QSFEIIKKLE CPDPQIVGHY MRRFAKTISN VLLQYADIVS KDFASYCSKE
KEKVPCILMN NTQQLRVQLE KMFEAMGGKE LDAEASGTLK ELQVKLNNVL DELSHVFATS
FQPHIEECVR QMGDILSQVK GTGNVPASAC SSVAQDADNV LQPIMDLLDS NLTLFAKICE
KTVLKRVLKE LWKLVMNTME RTIVLPPLTD QTMIGTLLRK HGKGLEKGRV KLPSHSDGTQ
MIFNAAKELG QLSKLKDHMV REEAKSLTPK QCAVVELALD TIKQYFHAGG VGLKKTFLEK
SPDLQSLRYA LSLYTQATDL LIKTFVQTQS AQVHGGKGTR FTLSEDVCPE MGSGVEDPVG
EVSVHVELFT HPGTGEQKVT VKVVAANDLK WQTSGIFRPF IEVNIVGPQL SDKKRKFATK
SKNNSWAPKY NESFQFSLSA DAGPECYELQ VCVKDYCFAR EDRTVELAVL QLRELAQRGS
AACWLPLGRR IHMDDTGLTV LRILSQRSND EVAKEFVKLK SDTRSAEEGG AAPAP


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