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Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Epidermal growth factor receptor-related protein) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (p185erbB2) (p185neu) (CD antigen CD340)

 ERBB2_RAT               Reviewed;        1257 AA.
P06494; Q6P732;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 3.
20-JUN-2018, entry version 186.
RecName: Full=Receptor tyrosine-protein kinase erbB-2;
EC=2.7.10.1;
AltName: Full=Epidermal growth factor receptor-related protein;
AltName: Full=Proto-oncogene Neu;
AltName: Full=Proto-oncogene c-ErbB-2;
AltName: Full=p185erbB2;
AltName: Full=p185neu;
AltName: CD_antigen=CD340;
Flags: Precursor;
Name=Erbb2; Synonyms=Neu;
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].
TISSUE=Neuroblastoma;
PubMed=3945311; DOI=10.1038/319226a0;
Bargmann C.I., Hung M.-C., Weinberg R.A.;
"The neu oncogene encodes an epidermal growth factor receptor-related
protein.";
Nature 319:226-230(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 634-699.
PubMed=1682063; DOI=10.1093/carcin/12.10.1975;
Masui T., Mann A.M., Macatee T.L., Garland E.M., Okamura T.,
Smith R.A., Cohen S.M.;
"Direct DNA sequencing of the rat neu oncogene transmembrane domain
reveals no mutation in urinary bladder carcinomas induced by N-butyl-
N-(4-hydroxybutyl)nitrosamine, N-[4-(5-nitro-2-furyl)-2-
thiazolyl]formamide or N-methyl-N-nitrosourea.";
Carcinogenesis 12:1975-1978(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 852-905.
TISSUE=Sciatic nerve;
PubMed=2025425; DOI=10.1016/0896-6273(91)90167-X;
Lai C., Lemke G.;
"An extended family of protein-tyrosine kinase genes differentially
expressed in the vertebrate nervous system.";
Neuron 6:691-704(1991).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=7945309; DOI=10.1006/bbrc.1994.2368;
Xie Y., Hung M.C.;
"Nuclear localization of p185neu tyrosine kinase and its association
with transcriptional transactivation.";
Biochem. Biophys. Res. Commun. 203:1589-1598(1994).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056; SER-1080 AND
SER-1085, 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).
[7]
STRUCTURE BY NMR OF 650-668.
PubMed=1346763;
Gullick W.J., Bottomley A.C., Lofts F.J., Doak D.G., Mulvey D.,
Newman R., Crumpton M.J., Sternberg M.J.E., Campbell I.D.;
"Three dimensional structure of the transmembrane region of the proto-
oncogenic and oncogenic forms of the neu protein.";
EMBO J. 11:43-48(1992).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-631 IN COMPLEX WITH THE
ANTIBODY HERCEPTIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-68;
ASN-188 AND ASN-260.
PubMed=12610629; DOI=10.1038/nature01392;
Cho H.-S., Mason K., Ramyar K.X., Stanley A.M., Gabelli S.B.,
Denney D.W. Jr., Leahy D.J.;
"Structure of the extracellular region of HER2 alone and in complex
with the Herceptin Fab.";
Nature 421:756-760(2003).
-!- FUNCTION: Protein tyrosine kinase that is part of several cell
surface receptor complexes, but that apparently needs a coreceptor
for ligand binding. Essential component of a neuregulin-receptor
complex, although neuregulins do not interact with it alone. GP30
is a potential ligand for this receptor. Regulates outgrowth and
stabilization of peripheral microtubules (MTs). Upon ERBB2
activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the
phosphorylation and thus the inhibition of GSK3B at cell membrane.
This prevents the phosphorylation of APC and CLASP2, allowing its
association with the cell membrane. In turn, membrane-bound APC
allows the localization of MACF1 to the cell membrane, which is
required for microtubule capture and stabilization (By
similarity). Interacts (preferentially with the tyrosine
phosphorylated form) with CPNE3; this interaction occurs at the
cell membrane and is increased in a growth factor heregulin-
dependent manner (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P04626}.
-!- FUNCTION: In the nucleus is involved in transcriptional
regulation. Associates with the 5'-TCAAATTC-3' sequence in the
PTGS2/COX-2 promoter and activates its transcription. Implicated
in transcriptional activation of CDKN1A; the function involves
STAT3 and SRC. Involved in the transcription of rRNA genes by RNA
Pol I and enhances protein synthesis and cell growth (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Homodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part
of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact
with PIK3C2B when phosphorylated on Tyr-1198. Interacts with
PRKCABP and PLXNB1. Interacts (when phosphorylated on Tyr-1250)
with MEMO1. Interacts with MUC1. Interacts (when phosphorylated on
Tyr-1141) with GRB7 (via SH2 domain). Interacts (when
phosphorylated on Tyr-1250) with ERBIN Interacts with SRC, KPNB1,
RANBP2, EEA1, CRM1, CLTC, PTK6, RPA194, MYOC and ACTB. Interacts
with HSP90AA1 and HSP90AB1; the interaction suppresses ERBB2
kinase activity (By similarity). {ECO:0000250|UniProtKB:P04626,
ECO:0000250|UniProtKB:P70424}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cytoplasm, perinuclear
region {ECO:0000250}. Nucleus {ECO:0000269|PubMed:7945309}.
-!- PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e.
one subunit of the dimeric receptor phosphorylates tyrosine
residues on the other subunit. Ligand-binding increases
phosphorylation on tyrosine residues. Signaling via SEMA4C
promotes phosphorylation at Tyr-1250. Dephosphorylated by PTPN12.
{ECO:0000250|UniProtKB:P04626}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAH61863.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA27059.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X03362; CAA27059.1; ALT_INIT; mRNA.
EMBL; BC061863; AAH61863.1; ALT_INIT; mRNA.
PIR; A24562; TVRTNU.
UniGene; Rn.93966; -.
PDB; 1IIJ; NMR; -; A=647-681.
PDB; 1N8Y; X-ray; 2.40 A; C=23-631.
PDB; 2J1H; Model; -; A/B=649-681.
PDBsum; 1IIJ; -.
PDBsum; 1N8Y; -.
PDBsum; 2J1H; -.
ProteinModelPortal; P06494; -.
SMR; P06494; -.
STRING; 10116.ENSRNOP00000040591; -.
BindingDB; P06494; -.
ChEMBL; CHEMBL3848; -.
iPTMnet; P06494; -.
PhosphoSitePlus; P06494; -.
PaxDb; P06494; -.
PRIDE; P06494; -.
UCSC; RGD:2561; rat.
RGD; 2561; Erbb2.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
HOGENOM; HOG000230982; -.
HOVERGEN; HBG000490; -.
InParanoid; P06494; -.
PhylomeDB; P06494; -.
BRENDA; 2.7.10.1; 5301.
EvolutionaryTrace; P06494; -.
PRO; PR:P06494; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043219; C:lateral loop; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005902; C:microvillus; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0051879; F:Hsp90 protein binding; IPI:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
GO; GO:0007417; P:central nervous system development; TAS:RGD.
GO; GO:0044849; P:estrous cycle; IMP:RGD.
GO; GO:0010001; P:glial cell differentiation; IGI:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0060056; P:mammary gland involution; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0007422; P:peripheral nervous system development; IMP:RGD.
GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:RGD.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:RGD.
GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0045595; P:regulation of cell differentiation; TAS:RGD.
GO; GO:0042127; P:regulation of cell proliferation; TAS:RGD.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
GO; GO:0048678; P:response to axon injury; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
GO; GO:0048485; P:sympathetic nervous system development; IMP:RGD.
GO; GO:0043586; P:tongue development; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
Pfam; PF00757; Furin-like; 1.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00261; FU; 4.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Activator; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Disulfide bond; DNA-binding;
Glycoprotein; Kinase; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Proto-oncogene; Receptor;
Reference proteome; Signal; Transcription; Transcription regulation;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1257 Receptor tyrosine-protein kinase erbB-2.
/FTId=PRO_0000016671.
TOPO_DOM 23 654 Extracellular. {ECO:0000255}.
TRANSMEM 655 677 Helical. {ECO:0000255}.
TOPO_DOM 678 1257 Cytoplasmic. {ECO:0000255}.
DOMAIN 722 989 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 728 736 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 678 691 Required for interaction with KPNB1 and
EEA1. {ECO:0000250}.
REGION 1197 1199 Interaction with PIK3C2B. {ECO:0000250}.
MOTIF 678 691 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 159 369 Cys-rich.
COMPBIAS 473 646 Cys-rich.
ACT_SITE 847 847 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 755 755 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1056 1056 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1080 1080 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1085 1085 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1109 1109 Phosphoserine.
{ECO:0000250|UniProtKB:P04626}.
MOD_RES 1114 1114 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04626}.
MOD_RES 1141 1141 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04626}.
MOD_RES 1168 1168 Phosphothreonine.
{ECO:0000250|UniProtKB:P04626}.
MOD_RES 1198 1198 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04626}.
MOD_RES 1250 1250 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P04626}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1N8Y}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1N8Y}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1N8Y,
ECO:0000269|PubMed:12610629}.
CARBOHYD 532 532 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 631 631 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 53 {ECO:0000244|PDB:1N8Y}.
DISULFID 163 193 {ECO:0000244|PDB:1N8Y}.
DISULFID 196 205 {ECO:0000244|PDB:1N8Y}.
DISULFID 200 213 {ECO:0000244|PDB:1N8Y}.
DISULFID 221 228 {ECO:0000244|PDB:1N8Y}.
DISULFID 225 236 {ECO:0000244|PDB:1N8Y}.
DISULFID 237 245 {ECO:0000244|PDB:1N8Y}.
DISULFID 241 253 {ECO:0000244|PDB:1N8Y}.
DISULFID 256 265 {ECO:0000244|PDB:1N8Y}.
DISULFID 269 296 {ECO:0000244|PDB:1N8Y}.
DISULFID 300 312 {ECO:0000244|PDB:1N8Y}.
DISULFID 316 332 {ECO:0000244|PDB:1N8Y}.
DISULFID 335 339 {ECO:0000244|PDB:1N8Y}.
DISULFID 343 368 {ECO:0000244|PDB:1N8Y}.
DISULFID 476 506 {ECO:0000244|PDB:1N8Y}.
DISULFID 513 522 {ECO:0000244|PDB:1N8Y}.
DISULFID 517 530 {ECO:0000244|PDB:1N8Y}.
DISULFID 533 542 {ECO:0000244|PDB:1N8Y}.
DISULFID 546 562 {ECO:0000244|PDB:1N8Y}.
DISULFID 565 578 {ECO:0000244|PDB:1N8Y}.
DISULFID 569 586 {ECO:0000244|PDB:1N8Y}.
DISULFID 589 598 {ECO:0000244|PDB:1N8Y}.
DISULFID 602 625 {ECO:0000244|PDB:1N8Y}.
DISULFID 628 636 {ECO:0000250|UniProtKB:P04626}.
DISULFID 632 644 {ECO:0000250|UniProtKB:P04626}.
VARIANT 661 661 V -> E (in oncogenic NEU).
CONFLICT 145 145 S -> G (in Ref. 2; AAH61863).
{ECO:0000305}.
CONFLICT 505 509 LCVSS -> CGLE (in Ref. 2; AAH61863).
{ECO:0000305}.
STRAND 25 27 {ECO:0000244|PDB:1N8Y}.
HELIX 39 50 {ECO:0000244|PDB:1N8Y}.
STRAND 54 63 {ECO:0000244|PDB:1N8Y}.
HELIX 72 74 {ECO:0000244|PDB:1N8Y}.
STRAND 79 82 {ECO:0000244|PDB:1N8Y}.
STRAND 84 88 {ECO:0000244|PDB:1N8Y}.
TURN 109 111 {ECO:0000244|PDB:1N8Y}.
STRAND 112 117 {ECO:0000244|PDB:1N8Y}.
STRAND 153 158 {ECO:0000244|PDB:1N8Y}.
HELIX 170 173 {ECO:0000244|PDB:1N8Y}.
HELIX 176 178 {ECO:0000244|PDB:1N8Y}.
STRAND 183 185 {ECO:0000244|PDB:1N8Y}.
STRAND 201 203 {ECO:0000244|PDB:1N8Y}.
STRAND 205 209 {ECO:0000244|PDB:1N8Y}.
STRAND 228 232 {ECO:0000244|PDB:1N8Y}.
HELIX 233 235 {ECO:0000244|PDB:1N8Y}.
STRAND 241 243 {ECO:0000244|PDB:1N8Y}.
STRAND 245 249 {ECO:0000244|PDB:1N8Y}.
STRAND 252 261 {ECO:0000244|PDB:1N8Y}.
STRAND 264 268 {ECO:0000244|PDB:1N8Y}.
STRAND 272 274 {ECO:0000244|PDB:1N8Y}.
STRAND 290 292 {ECO:0000244|PDB:1N8Y}.
STRAND 295 299 {ECO:0000244|PDB:1N8Y}.
STRAND 310 315 {ECO:0000244|PDB:1N8Y}.
STRAND 320 324 {ECO:0000244|PDB:1N8Y}.
STRAND 330 334 {ECO:0000244|PDB:1N8Y}.
HELIX 349 351 {ECO:0000244|PDB:1N8Y}.
TURN 359 361 {ECO:0000244|PDB:1N8Y}.
HELIX 362 365 {ECO:0000244|PDB:1N8Y}.
STRAND 369 377 {ECO:0000244|PDB:1N8Y}.
HELIX 379 383 {ECO:0000244|PDB:1N8Y}.
TURN 386 389 {ECO:0000244|PDB:1N8Y}.
HELIX 395 401 {ECO:0000244|PDB:1N8Y}.
STRAND 406 409 {ECO:0000244|PDB:1N8Y}.
STRAND 411 414 {ECO:0000244|PDB:1N8Y}.
HELIX 424 426 {ECO:0000244|PDB:1N8Y}.
TURN 439 441 {ECO:0000244|PDB:1N8Y}.
STRAND 442 448 {ECO:0000244|PDB:1N8Y}.
STRAND 464 470 {ECO:0000244|PDB:1N8Y}.
HELIX 483 486 {ECO:0000244|PDB:1N8Y}.
STRAND 494 499 {ECO:0000244|PDB:1N8Y}.
TURN 507 510 {ECO:0000244|PDB:1N8Y}.
HELIX 518 520 {ECO:0000244|PDB:1N8Y}.
STRAND 522 526 {ECO:0000244|PDB:1N8Y}.
STRAND 530 538 {ECO:0000244|PDB:1N8Y}.
STRAND 541 544 {ECO:0000244|PDB:1N8Y}.
STRAND 547 553 {ECO:0000244|PDB:1N8Y}.
STRAND 558 561 {ECO:0000244|PDB:1N8Y}.
STRAND 573 575 {ECO:0000244|PDB:1N8Y}.
STRAND 577 582 {ECO:0000244|PDB:1N8Y}.
HELIX 583 585 {ECO:0000244|PDB:1N8Y}.
STRAND 586 594 {ECO:0000244|PDB:1N8Y}.
STRAND 597 601 {ECO:0000244|PDB:1N8Y}.
STRAND 604 606 {ECO:0000244|PDB:1N8Y}.
STRAND 615 619 {ECO:0000244|PDB:1N8Y}.
STRAND 623 627 {ECO:0000244|PDB:1N8Y}.
HELIX 650 669 {ECO:0000244|PDB:1IIJ}.
HELIX 670 674 {ECO:0000244|PDB:1IIJ}.
HELIX 675 679 {ECO:0000244|PDB:1IIJ}.
SEQUENCE 1257 AA; 138832 MW; 6129264583011402 CRC64;
MELAAWCRWG FLLALLPPGI AGTQVCTGTD MKLRLPASPE THLDMLRHLY QGCQVVQGNL
ELTYVPANAS LSFLQDIQEV QGYMLIAHNQ VKRVPLQRLR IVRGTQLFED KYALAVLDNR
DPQDNVAAST PGRTPEGLRE LQLRSLTEIL KGGVLIRGNP QLCYQDMVLW KDVFRKNNQL
APVDIDTNRS RACPPCAPAC KDNHCWGESP EDCQILTGTI CTSGCARCKG RLPTDCCHEQ
CAAGCTGPKH SDCLACLHFN HSGICELHCP ALVTYNTDTF ESMHNPEGRY TFGASCVTTC
PYNYLSTEVG SCTLVCPPNN QEVTAEDGTQ RCEKCSKPCA RVCYGLGMEH LRGARAITSD
NVQEFDGCKK IFGSLAFLPE SFDGDPSSGI APLRPEQLQV FETLEEITGY LYISAWPDSL
RDLSVFQNLR IIRGRILHDG AYSLTLQGLG IHSLGLRSLR ELGSGLALIH RNAHLCFVHT
VPWDQLFRNP HQALLHSGNR PEEDLCVSSG LVCNSLCAHG HCWGPGPTQC VNCSHFLRGQ
ECVEECRVWK GLPREYVSDK RCLPCHPECQ PQNSSETCFG SEADQCAACA HYKDSSSCVA
RCPSGVKPDL SYMPIWKYPD EEGICQPCPI NCTHSCVDLD ERGCPAEQRA SPVTFIIATV
VGVLLFLILV VVVGILIKRR RQKIRKYTMR RLLQETELVE PLTPSGAMPN QAQMRILKET
ELRKVKVLGS GAFGTVYKGI WIPDGENVKI PVAIKVLREN TSPKANKEIL DEAYVMAGVG
SPYVSRLLGI CLTSTVQLVT QLMPYGCLLD HVREHRGRLG SQDLLNWCVQ IAKGMSYLED
VRLVHRDLAA RNVLVKSPNH VKITDFGLAR LLDIDETEYH ADGGKVPIKW MALESILRRR
FTHQSDVWSY GVTVWELMTF GAKPYDGIPA REIPDLLEKG ERLPQPPICT IDVYMIMVKC
WMIDSECRPR FRELVSEFSR MARDPQRFVV IQNEDLGPSS PMDSTFYRSL LEDDDMGDLV
DAEEYLVPQQ GFFSPDPTPG TGSTAHRRHR SSSTRSGGGE LTLGLEPSEE GPPRSPLAPS
EGAGSDVFDG DLAMGVTKGL QSLSPHDLSP LQRYSEDPTL PLPPETDGYV APLACSPQPE
YVNQSEVQPQ PPLTPEGPLP PVRPAGATLE RPKTLSPGKN GVVKDVFAFG GAVENPEYLV
PREGTASPPH PSPAFSPAFD NLYYWDQNSS EQGPPPSNFE GTPTAENPEY LGLDVPV


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