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Low-density lipoprotein receptor-related protein 4 (LRP-4) (Multiple epidermal growth factor-like domains 7)

 LRP4_RAT                Reviewed;        1905 AA.
Q9QYP1;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
22-NOV-2017, entry version 138.
RecName: Full=Low-density lipoprotein receptor-related protein 4;
Short=LRP-4;
AltName: Full=Multiple epidermal growth factor-like domains 7;
Flags: Precursor;
Name=Lrp4; Synonyms=Megf7;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE OF 608-1905, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[3]
INTERACTION WITH MUSK.
PubMed=18848351; DOI=10.1016/j.cell.2008.10.002;
Kim N., Stiegler A.L., Cameron T.O., Hallock P.T., Gomez A.M.,
Huang J.H., Hubbard S.R., Dustin M.L., Burden S.J.;
"Lrp4 is a receptor for Agrin and forms a complex with MuSK.";
Cell 135:334-342(2008).
-!- FUNCTION: Mediates SOST-dependent inhibition of bone formation (By
similarity). Functions as a specific facilitator of SOST-mediated
inhibition of Wnt signaling (By similarity). Plays a key role in
the formation and the maintenance of the neuromuscular junction
(NMJ), the synapse between motor neuron and skeletal muscle.
Directly binds AGRIN and recruits it to the MUSK signaling
complex. Mediates the AGRIN-induced phosphorylation of MUSK, the
kinase of the complex. The activation of MUSK in myotubes induces
the formation of NMJ by regulating different processes including
the transcription of specific genes and the clustering of AChR in
the postsynaptic membrane. Alternatively, may be involved in the
negative regulation of the canonical Wnt signaling pathway, being
able to antagonize the LRP6-mediated activation of this pathway.
More generally, has been proposed to function as a cell surface
endocytic receptor binding and internalizing extracellular ligands
for degradation by lysosomes. Plays an essential role in the
process of digit differentiation. {ECO:0000250|UniProtKB:Q8VI56}.
-!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms
an AGRIN receptor complex that binds AGRIN resulting in activation
of MUSK (PubMed:18848351). Interacts (via the extracellular
domain) with SOST; the interaction facilitates the inhibition of
Wnt signaling (By similarity). Interacts with MESD; the
interaction promotes glycosylation of LRP4 and its cell-surface
expression (By similarity). {ECO:0000250|UniProtKB:Q8VI56,
ECO:0000269|PubMed:18848351}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q8VI56}; Single-pass type I membrane
protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in different regions of the brain,
mainly in the olfactory bulb, at lower level in the cerebral
cortex and hippocampus. {ECO:0000269|PubMed:9693030}.
-!- PTM: N-glycosylation is required for cell surface location.
{ECO:0000250|UniProtKB:Q8VI56}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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EMBL; AABR03025549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03027097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03027512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03029369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB011533; BAA88688.1; -; mRNA.
UniGene; Rn.21381; -.
PDB; 3V64; X-ray; 2.85 A; C/D=396-737.
PDB; 3V65; X-ray; 3.30 A; B/D=353-737.
PDBsum; 3V64; -.
PDBsum; 3V65; -.
ProteinModelPortal; Q9QYP1; -.
SMR; Q9QYP1; -.
CORUM; Q9QYP1; -.
STRING; 10116.ENSRNOP00000021353; -.
iPTMnet; Q9QYP1; -.
PhosphoSitePlus; Q9QYP1; -.
PaxDb; Q9QYP1; -.
PRIDE; Q9QYP1; -.
Ensembl; ENSRNOT00000021353; ENSRNOP00000021353; ENSRNOG00000015285.
UCSC; RGD:619731; rat.
RGD; 619731; Lrp4.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XPR2; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000047507; -.
HOVERGEN; HBG049163; -.
InParanoid; Q9QYP1; -.
OMA; LNGSNME; -.
OrthoDB; EOG091G0178; -.
PhylomeDB; Q9QYP1; -.
TreeFam; TF315253; -.
PRO; PR:Q9QYP1; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000015285; -.
ExpressionAtlas; Q9QYP1; baseline and differential.
Genevisible; Q9QYP1; RN.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
GO; GO:0034185; F:apolipoprotein binding; IPI:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
GO; GO:0042813; F:Wnt-activated receptor activity; IBA:GO_Central.
GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
GO; GO:0048856; P:anatomical structure development; ISO:RGD.
GO; GO:0030509; P:BMP signaling pathway; IEA:InterPro.
GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0001942; P:hair follicle development; ISO:RGD.
GO; GO:0001822; P:kidney development; ISO:RGD.
GO; GO:0060173; P:limb development; ISO:RGD.
GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:1901631; P:positive regulation of presynaptic membrane organization; ISS:UniProtKB.
GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
GO; GO:0097104; P:postsynaptic membrane assembly; ISS:UniProtKB.
GO; GO:0097105; P:presynaptic membrane assembly; ISS:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
GO; GO:0008104; P:protein localization; ISO:RGD.
GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
GO; GO:0043113; P:receptor clustering; ISO:RGD.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; IMP:UniProtKB.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; ISS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IBA:GO_Central.
CDD; cd00112; LDLa; 7.
Gene3D; 2.120.10.30; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR030799; LRP4.
PANTHER; PTHR44017:SF4; PTHR44017:SF4; 1.
Pfam; PF12662; cEGF; 1.
Pfam; PF00057; Ldl_recept_a; 8.
Pfam; PF00058; Ldl_recept_b; 16.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 7.
SMART; SM00179; EGF_CA; 2.
SMART; SM00192; LDLa; 8.
SMART; SM00135; LY; 20.
SUPFAM; SSF57184; SSF57184; 2.
SUPFAM; SSF57424; SSF57424; 8.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01209; LDLRA_1; 8.
PROSITE; PS50068; LDLRA_2; 8.
PROSITE; PS51120; LDLRB; 20.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
EGF-like domain; Endocytosis; Glycoprotein; Membrane; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Wnt signaling pathway.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1905 Low-density lipoprotein receptor-related
protein 4.
/FTId=PRO_0000017327.
TOPO_DOM 21 1723 Extracellular. {ECO:0000255}.
TRANSMEM 1724 1746 Helical. {ECO:0000255}.
TOPO_DOM 1747 1905 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 67 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 70 106 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 109 144 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 147 183 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 190 226 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 230 266 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 269 305 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 311 350 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 354 394 EGF-like 1; atypical.
DOMAIN 395 434 EGF-like 2; calcium-binding.
REPEAT 480 522 LDL-receptor class B 1.
REPEAT 523 565 LDL-receptor class B 2.
REPEAT 566 609 LDL-receptor class B 3.
REPEAT 610 652 LDL-receptor class B 4.
REPEAT 653 693 LDL-receptor class B 5.
DOMAIN 698 737 EGF-like 3.
REPEAT 785 827 LDL-receptor class B 6.
REPEAT 828 870 LDL-receptor class B 7.
REPEAT 871 914 LDL-receptor class B 8.
REPEAT 915 956 LDL-receptor class B 9.
REPEAT 957 998 LDL-receptor class B 10.
REPEAT 1093 1135 LDL-receptor class B 11.
REPEAT 1136 1178 LDL-receptor class B 12.
REPEAT 1179 1222 LDL-receptor class B 13.
REPEAT 1223 1263 LDL-receptor class B 14.
REPEAT 1264 1306 LDL-receptor class B 15.
REPEAT 1397 1439 LDL-receptor class B 16.
REPEAT 1440 1482 LDL-receptor class B 17.
REPEAT 1483 1526 LDL-receptor class B 18.
REPEAT 1527 1568 LDL-receptor class B 19.
REPEAT 1569 1610 LDL-receptor class B 20.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 719 719 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 901 901 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1077 1077 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1415 1415 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1467 1467 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 44 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 34 57 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 51 66 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 71 83 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 78 96 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 90 105 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 110 122 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 117 135 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 129 143 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 148 160 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 155 173 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 167 182 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 191 203 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 198 216 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 210 225 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 231 243 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 238 256 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 250 265 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 270 282 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 277 295 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 289 304 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 312 324 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 319 337 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 331 349 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 358 369 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 365 378 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 380 393 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 399 409 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 405 418 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 420 433 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 702 713 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 709 722 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 724 736 {ECO:0000255|PROSITE-ProRule:PRU00124}.
STRAND 364 369 {ECO:0000244|PDB:3V65}.
STRAND 399 402 {ECO:0000244|PDB:3V65}.
STRAND 406 409 {ECO:0000244|PDB:3V64}.
STRAND 424 426 {ECO:0000244|PDB:3V64}.
STRAND 433 438 {ECO:0000244|PDB:3V64}.
STRAND 441 445 {ECO:0000244|PDB:3V64}.
STRAND 450 453 {ECO:0000244|PDB:3V64}.
STRAND 460 464 {ECO:0000244|PDB:3V64}.
STRAND 470 476 {ECO:0000244|PDB:3V64}.
TURN 477 480 {ECO:0000244|PDB:3V64}.
STRAND 481 486 {ECO:0000244|PDB:3V64}.
TURN 487 490 {ECO:0000244|PDB:3V64}.
STRAND 491 496 {ECO:0000244|PDB:3V64}.
STRAND 503 506 {ECO:0000244|PDB:3V64}.
STRAND 515 519 {ECO:0000244|PDB:3V64}.
TURN 520 523 {ECO:0000244|PDB:3V64}.
STRAND 524 529 {ECO:0000244|PDB:3V64}.
TURN 530 533 {ECO:0000244|PDB:3V64}.
STRAND 534 539 {ECO:0000244|PDB:3V64}.
STRAND 546 549 {ECO:0000244|PDB:3V64}.
STRAND 556 562 {ECO:0000244|PDB:3V64}.
TURN 563 566 {ECO:0000244|PDB:3V64}.
STRAND 567 572 {ECO:0000244|PDB:3V64}.
STRAND 574 576 {ECO:0000244|PDB:3V64}.
STRAND 578 583 {ECO:0000244|PDB:3V64}.
STRAND 590 592 {ECO:0000244|PDB:3V64}.
STRAND 600 606 {ECO:0000244|PDB:3V64}.
TURN 607 610 {ECO:0000244|PDB:3V64}.
STRAND 611 616 {ECO:0000244|PDB:3V64}.
TURN 617 620 {ECO:0000244|PDB:3V64}.
STRAND 621 626 {ECO:0000244|PDB:3V64}.
STRAND 633 636 {ECO:0000244|PDB:3V64}.
STRAND 641 649 {ECO:0000244|PDB:3V64}.
STRAND 652 657 {ECO:0000244|PDB:3V64}.
TURN 658 661 {ECO:0000244|PDB:3V64}.
STRAND 662 667 {ECO:0000244|PDB:3V64}.
TURN 668 670 {ECO:0000244|PDB:3V64}.
STRAND 675 678 {ECO:0000244|PDB:3V64}.
STRAND 687 690 {ECO:0000244|PDB:3V64}.
HELIX 692 694 {ECO:0000244|PDB:3V64}.
TURN 701 704 {ECO:0000244|PDB:3V64}.
HELIX 705 708 {ECO:0000244|PDB:3V64}.
STRAND 710 714 {ECO:0000244|PDB:3V64}.
STRAND 717 719 {ECO:0000244|PDB:3V65}.
STRAND 721 723 {ECO:0000244|PDB:3V64}.
STRAND 728 731 {ECO:0000244|PDB:3V64}.
TURN 732 734 {ECO:0000244|PDB:3V64}.
STRAND 735 737 {ECO:0000244|PDB:3V64}.
SEQUENCE 1905 AA; 211880 MW; 9562A5729D69E29A CRC64;
MRRWWGALLL GALLCAHGTA SNLECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH
SDEDGCTLPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG
YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE
SCPSAVPSPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS
GLCVNAGWRC DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD
EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGVNDCGDN SDESPQQNCR PRTGEENCNV
NNGGCAQKCQ MIRGAVQCTC HTGYRLTEDG RTCQDVNECA EEGYCSQGCT NSEGAFQCWC
EAGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE
LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL
DGAHRKVLLW QSLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP
NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT
KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY
TCACPTGFRK INSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW
DSRDDHVYWT DVSTDTISRA KWDGTGQKVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI
EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASNRQVIISS
NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGQRIYW
TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRQRP PVTTPCAVEN GGCSHLCLRS
PSPSGFSCTC PTGINLLLDG KTCSPGMNSF LIFARRIDVR MVSLDIPYFA DVVVPINMTM
KNTIAIGVDP LEGKVYWSDS TLHRISRASL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW
TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS
DRTVLINNNL GWPNGLTVDK TSSQLLWADA HTERIEVADL NGANRHTLVS PVQHPYGLTL
LDSYIYWTDW QTRSIHRADK STGSNVILVR SNLPGLMDIQ AVDRAQPLGF NKCGSRNGGC
SHLCLPRPSG FSCACPTGIQ LKGDGKTCDP SPETYLLFSS RGSIRRISLD TDDHTDVHVP
VPGLNNVISL DYDSVDGKVY YTDVFLDVIR RADLNGSNME TVIGHGLKTT DGLAVDWVAR
NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN
LDGSERKVLI NADLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF
ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN
NGGCSHLCFA RASDFVCACP DEPDSHPCSL VPGLMPPAPR ATSLNEKSPV LPNTLPTTLH
SSTTRTRTSP EGAEGRCSER DAQLGLCAHS NEAVPAAPGE GLHVSYAVGG LLSVLLILLV
TAALMLYRHR KSKFTDPGMG NLTYSNPSYR TSTQEVKIEA APKPAMYNQL CYKKEGGPDH
SYTKEKIKIV EGIHLLAGHD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT
ETEQLLQEEQ SECSSVHTAT TPERRGSLPD TGWKHERKLS SESQV


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