LRP4_RAT
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 03-AUG-2022, entry version 159.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., 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., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., 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., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT 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-like
RT 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., Huang J.H.,
RA 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 the
CC formation and the maintenance of the neuromuscular junction (NMJ), the
CC synapse between motor neuron and skeletal muscle. Directly binds AGRIN
CC and recruits it to the MUSK signaling complex. Mediates the AGRIN-
CC induced phosphorylation of MUSK, the kinase of the complex. The
CC activation of MUSK in myotubes induces the formation of NMJ by
CC regulating different processes including the transcription of specific
CC genes and the clustering of AChR in the postsynaptic membrane.
CC Alternatively, may be involved in the negative regulation of the
CC canonical Wnt signaling pathway, being able to antagonize the LRP6-
CC mediated activation of this pathway. More generally, has been proposed
CC to function as a cell surface endocytic receptor binding and
CC internalizing extracellular ligands for degradation by lysosomes. Plays
CC an essential role in the process of digit differentiation.
CC {ECO:0000250|UniProtKB:Q8VI56}.
CC -!- SUBUNIT: Homooligomer. Interacts with MUSK; the heterodimer forms an
CC AGRIN receptor complex that binds AGRIN resulting in activation of MUSK
CC (PubMed:18848351). Interacts (via the extracellular domain) with SOST;
CC the interaction facilitates the inhibition of Wnt signaling (By
CC similarity). Interacts with MESD; the interaction promotes
CC glycosylation of LRP4 and its cell-surface expression (By similarity).
CC {ECO:0000250|UniProtKB:Q8VI56, ECO:0000269|PubMed:18848351}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VI56};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in different regions of the brain, mainly
CC in the olfactory bulb, at lower level in the cerebral cortex and
CC 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}.
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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 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 AlphaFoldDB; Q9QYP1; -.
DR SMR; Q9QYP1; -.
DR CORUM; Q9QYP1; -.
DR STRING; 10116.ENSRNOP00000021353; -.
DR GlyGen; Q9QYP1; 8 sites.
DR iPTMnet; Q9QYP1; -.
DR PhosphoSitePlus; Q9QYP1; -.
DR PaxDb; Q9QYP1; -.
DR PRIDE; Q9QYP1; -.
DR ABCD; Q9QYP1; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000021353; ENSRNOP00000021353; ENSRNOG00000015285.
DR UCSC; RGD:619731; rat.
DR RGD; 619731; Lrp4.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000158287; -.
DR HOGENOM; CLU_000085_4_1_1; -.
DR InParanoid; Q9QYP1; -.
DR OMA; NNRYTAI; -.
DR PhylomeDB; Q9QYP1; -.
DR TreeFam; TF315253; -.
DR PRO; PR:Q9QYP1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000015285; Expressed in lung and 19 other tissues.
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; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0048856; P:anatomical structure development; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0048699; P:generation of neurons; IBA:GO_Central.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0060173; P:limb development; ISO:RGD.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:UniProtKB.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
DR GO; GO:0043113; P:receptor clustering; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
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 assembly at neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.120.10.30; -; 4.
DR Gene3D; 4.10.400.10; -; 8.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
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 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; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Endocytosis;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1905
FT /note="Low-density lipoprotein receptor-related protein 4"
FT /id="PRO_0000017327"
FT TOPO_DOM 21..1723
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1724..1746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1747..1905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..67
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 70..106
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 109..144
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 147..183
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 190..226
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 230..266
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 269..305
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 311..350
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 354..394
FT /note="EGF-like 1; atypical"
FT DOMAIN 395..434
FT /note="EGF-like 2; calcium-binding"
FT REPEAT 480..522
FT /note="LDL-receptor class B 1"
FT REPEAT 523..565
FT /note="LDL-receptor class B 2"
FT REPEAT 566..609
FT /note="LDL-receptor class B 3"
FT REPEAT 610..652
FT /note="LDL-receptor class B 4"
FT REPEAT 653..693
FT /note="LDL-receptor class B 5"
FT DOMAIN 698..737
FT /note="EGF-like 3"
FT REPEAT 785..827
FT /note="LDL-receptor class B 6"
FT REPEAT 828..870
FT /note="LDL-receptor class B 7"
FT REPEAT 871..914
FT /note="LDL-receptor class B 8"
FT REPEAT 915..956
FT /note="LDL-receptor class B 9"
FT REPEAT 957..998
FT /note="LDL-receptor class B 10"
FT REPEAT 1093..1135
FT /note="LDL-receptor class B 11"
FT REPEAT 1136..1178
FT /note="LDL-receptor class B 12"
FT REPEAT 1179..1222
FT /note="LDL-receptor class B 13"
FT REPEAT 1223..1263
FT /note="LDL-receptor class B 14"
FT REPEAT 1264..1306
FT /note="LDL-receptor class B 15"
FT REPEAT 1397..1439
FT /note="LDL-receptor class B 16"
FT REPEAT 1440..1482
FT /note="LDL-receptor class B 17"
FT REPEAT 1483..1526
FT /note="LDL-receptor class B 18"
FT REPEAT 1527..1568
FT /note="LDL-receptor class B 19"
FT REPEAT 1569..1610
FT /note="LDL-receptor class B 20"
FT REGION 1659..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1853..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 901
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 34..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 51..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 71..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 78..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 90..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 110..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 117..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 129..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 148..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 155..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 167..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 191..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 198..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 210..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 231..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 238..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 250..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 270..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 277..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 289..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 312..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 319..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 331..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 358..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 365..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 380..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 399..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 405..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 420..433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 702..713
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 709..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 724..736
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:3V65"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:3V65"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 477..480
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 487..490
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 520..523
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 556..562
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 600..606
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 607..610
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 617..620
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 641..649
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 652..657
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 658..661
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 662..667
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:3V64"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 701..704
FT /evidence="ECO:0007829|PDB:3V64"
FT HELIX 705..708
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 710..714
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:3V65"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 728..731
FT /evidence="ECO:0007829|PDB:3V64"
FT TURN 732..734
FT /evidence="ECO:0007829|PDB:3V64"
FT STRAND 735..737
FT /evidence="ECO:0007829|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
