GenomeNet

Database: UniProt
Entry: Q9QYP1
LinkDB: Q9QYP1
Original site: Q9QYP1 
ID   LRP4_RAT                Reviewed;        1905 AA.
AC   Q9QYP1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   13-FEB-2019, entry version 144.
DE   RecName: Full=Low-density lipoprotein receptor-related protein 4;
DE            Short=LRP-4;
DE   AltName: Full=Multiple epidermal growth factor-like domains 7;
DE   Flags: Precursor;
GN   Name=Lrp4; Synonyms=Megf7;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 608-1905, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA   Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT   "Identification of high-molecular-weight proteins with multiple EGF-
RT   like motifs by motif-trap screening.";
RL   Genomics 51:27-34(1998).
RN   [3]
RP   INTERACTION WITH MUSK.
RX   PubMed=18848351; DOI=10.1016/j.cell.2008.10.002;
RA   Kim N., Stiegler A.L., Cameron T.O., Hallock P.T., Gomez A.M.,
RA   Huang J.H., Hubbard S.R., Dustin M.L., Burden S.J.;
RT   "Lrp4 is a receptor for Agrin and forms a complex with MuSK.";
RL   Cell 135:334-342(2008).
CC   -!- FUNCTION: Mediates SOST-dependent inhibition of bone formation (By
CC       similarity). Functions as a specific facilitator of SOST-mediated
CC       inhibition of Wnt signaling (By similarity). Plays a key role in
CC       the formation and the maintenance of the neuromuscular junction
CC       (NMJ), the synapse between motor neuron and skeletal muscle.
CC       Directly binds AGRIN and recruits it to the MUSK signaling
CC       complex. Mediates the AGRIN-induced phosphorylation of MUSK, the
CC       kinase of the complex. The activation of MUSK in myotubes induces
CC       the formation of NMJ by regulating different processes including
CC       the transcription of specific genes and the clustering of AChR in
CC       the postsynaptic membrane. Alternatively, may be involved in the
CC       negative regulation of the canonical Wnt signaling pathway, being
CC       able to antagonize the LRP6-mediated activation of this pathway.
CC       More generally, has been proposed to function as a cell surface
CC       endocytic receptor binding and internalizing extracellular ligands
CC       for degradation by lysosomes. Plays an essential role in the
CC       process of digit differentiation. {ECO:0000250|UniProtKB:Q8VI56}.
CC   -!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms
CC       an AGRIN receptor complex that binds AGRIN resulting in activation
CC       of MUSK (PubMed:18848351). Interacts (via the extracellular
CC       domain) with SOST; the interaction facilitates the inhibition of
CC       Wnt signaling (By similarity). Interacts with MESD; the
CC       interaction promotes glycosylation of LRP4 and its cell-surface
CC       expression (By similarity). {ECO:0000250|UniProtKB:Q8VI56,
CC       ECO:0000269|PubMed:18848351}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q8VI56}; Single-pass type I membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in different regions of the brain,
CC       mainly in the olfactory bulb, at lower level in the cerebral
CC       cortex and hippocampus. {ECO:0000269|PubMed:9693030}.
CC   -!- PTM: N-glycosylation is required for cell surface location.
CC       {ECO:0000250|UniProtKB:Q8VI56}.
CC   -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
DR   EMBL; AABR03025549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03027097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03027512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03029369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB011533; BAA88688.1; -; mRNA.
DR   UniGene; Rn.21381; -.
DR   PDB; 3V64; X-ray; 2.85 A; C/D=396-737.
DR   PDB; 3V65; X-ray; 3.30 A; B/D=353-737.
DR   PDBsum; 3V64; -.
DR   PDBsum; 3V65; -.
DR   ProteinModelPortal; Q9QYP1; -.
DR   SMR; Q9QYP1; -.
DR   CORUM; Q9QYP1; -.
DR   STRING; 10116.ENSRNOP00000021353; -.
DR   iPTMnet; Q9QYP1; -.
DR   PhosphoSitePlus; Q9QYP1; -.
DR   PaxDb; Q9QYP1; -.
DR   PRIDE; Q9QYP1; -.
DR   Ensembl; ENSRNOT00000021353; ENSRNOP00000021353; ENSRNOG00000015285.
DR   UCSC; RGD:619731; rat.
DR   RGD; 619731; Lrp4.
DR   eggNOG; KOG1215; Eukaryota.
DR   eggNOG; ENOG410XPR2; LUCA.
DR   GeneTree; ENSGT00940000158287; -.
DR   HOGENOM; HOG000047507; -.
DR   HOVERGEN; HBG049163; -.
DR   InParanoid; Q9QYP1; -.
DR   OMA; CGRNHFT; -.
DR   PhylomeDB; Q9QYP1; -.
DR   TreeFam; TF315253; -.
DR   PRO; PR:Q9QYP1; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000015285; Expressed in 10 organ(s), highest expression level in lung.
DR   ExpressionAtlas; Q9QYP1; baseline and differential.
DR   Genevisible; Q9QYP1; RN.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
DR   GO; GO:0034185; F:apolipoprotein binding; IPI:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
DR   GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:InterPro.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:1901631; P:positive regulation of presynaptic membrane organization; ISS:UniProtKB.
DR   GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR   GO; GO:0097104; P:postsynaptic membrane assembly; ISS:UniProtKB.
DR   GO; GO:0097105; P:presynaptic membrane assembly; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR   GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR   GO; GO:0050808; P:synapse organization; IMP:UniProtKB.
DR   GO; GO:0051124; P:synaptic growth at neuromuscular junction; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 7.
DR   Gene3D; 2.120.10.30; -; 4.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR030799; LRP4.
DR   PANTHER; PTHR44017:SF4; PTHR44017:SF4; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 16.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 20.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF57424; SSF57424; 8.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 8.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 20.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Endocytosis; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Wnt signaling pathway.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21   1905       Low-density lipoprotein receptor-related
FT                                protein 4.
FT                                /FTId=PRO_0000017327.
FT   TOPO_DOM     21   1723       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1724   1746       Helical. {ECO:0000255}.
FT   TOPO_DOM   1747   1905       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       26     67       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       70    106       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      109    144       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      147    183       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      190    226       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      230    266       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      269    305       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      311    350       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      354    394       EGF-like 1; atypical.
FT   DOMAIN      395    434       EGF-like 2; calcium-binding.
FT   REPEAT      480    522       LDL-receptor class B 1.
FT   REPEAT      523    565       LDL-receptor class B 2.
FT   REPEAT      566    609       LDL-receptor class B 3.
FT   REPEAT      610    652       LDL-receptor class B 4.
FT   REPEAT      653    693       LDL-receptor class B 5.
FT   DOMAIN      698    737       EGF-like 3.
FT   REPEAT      785    827       LDL-receptor class B 6.
FT   REPEAT      828    870       LDL-receptor class B 7.
FT   REPEAT      871    914       LDL-receptor class B 8.
FT   REPEAT      915    956       LDL-receptor class B 9.
FT   REPEAT      957    998       LDL-receptor class B 10.
FT   REPEAT     1093   1135       LDL-receptor class B 11.
FT   REPEAT     1136   1178       LDL-receptor class B 12.
FT   REPEAT     1179   1222       LDL-receptor class B 13.
FT   REPEAT     1223   1263       LDL-receptor class B 14.
FT   REPEAT     1264   1306       LDL-receptor class B 15.
FT   REPEAT     1397   1439       LDL-receptor class B 16.
FT   REPEAT     1440   1482       LDL-receptor class B 17.
FT   REPEAT     1483   1526       LDL-receptor class B 18.
FT   REPEAT     1527   1568       LDL-receptor class B 19.
FT   REPEAT     1569   1610       LDL-receptor class B 20.
FT   CARBOHYD    264    264       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    498    498       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    719    719       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    901    901       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1077   1077       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1415   1415       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1467   1467       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     44       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     34     57       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     51     66       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     71     83       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     78     96       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     90    105       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    110    122       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    117    135       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    129    143       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    148    160       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    155    173       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    167    182       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    191    203       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    198    216       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    210    225       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    231    243       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    238    256       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    250    265       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    270    282       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    277    295       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    289    304       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    312    324       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    319    337       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    331    349       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    358    369       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    365    378       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    380    393       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    399    409       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    405    418       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    420    433       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    702    713       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    709    722       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    724    736       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   STRAND      364    369       {ECO:0000244|PDB:3V65}.
FT   STRAND      399    402       {ECO:0000244|PDB:3V65}.
FT   STRAND      406    409       {ECO:0000244|PDB:3V64}.
FT   STRAND      424    426       {ECO:0000244|PDB:3V64}.
FT   STRAND      433    438       {ECO:0000244|PDB:3V64}.
FT   STRAND      441    445       {ECO:0000244|PDB:3V64}.
FT   STRAND      450    453       {ECO:0000244|PDB:3V64}.
FT   STRAND      460    464       {ECO:0000244|PDB:3V64}.
FT   STRAND      470    476       {ECO:0000244|PDB:3V64}.
FT   TURN        477    480       {ECO:0000244|PDB:3V64}.
FT   STRAND      481    486       {ECO:0000244|PDB:3V64}.
FT   TURN        487    490       {ECO:0000244|PDB:3V64}.
FT   STRAND      491    496       {ECO:0000244|PDB:3V64}.
FT   STRAND      503    506       {ECO:0000244|PDB:3V64}.
FT   STRAND      515    519       {ECO:0000244|PDB:3V64}.
FT   TURN        520    523       {ECO:0000244|PDB:3V64}.
FT   STRAND      524    529       {ECO:0000244|PDB:3V64}.
FT   TURN        530    533       {ECO:0000244|PDB:3V64}.
FT   STRAND      534    539       {ECO:0000244|PDB:3V64}.
FT   STRAND      546    549       {ECO:0000244|PDB:3V64}.
FT   STRAND      556    562       {ECO:0000244|PDB:3V64}.
FT   TURN        563    566       {ECO:0000244|PDB:3V64}.
FT   STRAND      567    572       {ECO:0000244|PDB:3V64}.
FT   STRAND      574    576       {ECO:0000244|PDB:3V64}.
FT   STRAND      578    583       {ECO:0000244|PDB:3V64}.
FT   STRAND      590    592       {ECO:0000244|PDB:3V64}.
FT   STRAND      600    606       {ECO:0000244|PDB:3V64}.
FT   TURN        607    610       {ECO:0000244|PDB:3V64}.
FT   STRAND      611    616       {ECO:0000244|PDB:3V64}.
FT   TURN        617    620       {ECO:0000244|PDB:3V64}.
FT   STRAND      621    626       {ECO:0000244|PDB:3V64}.
FT   STRAND      633    636       {ECO:0000244|PDB:3V64}.
FT   STRAND      641    649       {ECO:0000244|PDB:3V64}.
FT   STRAND      652    657       {ECO:0000244|PDB:3V64}.
FT   TURN        658    661       {ECO:0000244|PDB:3V64}.
FT   STRAND      662    667       {ECO:0000244|PDB:3V64}.
FT   TURN        668    670       {ECO:0000244|PDB:3V64}.
FT   STRAND      675    678       {ECO:0000244|PDB:3V64}.
FT   STRAND      687    690       {ECO:0000244|PDB:3V64}.
FT   HELIX       692    694       {ECO:0000244|PDB:3V64}.
FT   TURN        701    704       {ECO:0000244|PDB:3V64}.
FT   HELIX       705    708       {ECO:0000244|PDB:3V64}.
FT   STRAND      710    714       {ECO:0000244|PDB:3V64}.
FT   STRAND      717    719       {ECO:0000244|PDB:3V65}.
FT   STRAND      721    723       {ECO:0000244|PDB:3V64}.
FT   STRAND      728    731       {ECO:0000244|PDB:3V64}.
FT   TURN        732    734       {ECO:0000244|PDB:3V64}.
FT   STRAND      735    737       {ECO:0000244|PDB:3V64}.
SQ   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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