PLXB2_MOUSE
ID PLXB2_MOUSE Reviewed; 1842 AA.
AC B2RXS4; Q3UH76;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Plexin-B2;
DE Flags: Precursor;
GN Name=Plxnb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH SEMA4C AND SEMA4D, AND
RP TISSUE SPECIFICITY.
RX PubMed=17554007; DOI=10.1523/jneurosci.5381-06.2007;
RA Deng S., Hirschberg A., Worzfeld T., Penachioni J.Y., Korostylev A.,
RA Swiercz J.M., Vodrazka P., Mauti O., Stoeckli E.T., Tamagnone L.,
RA Offermanns S., Kuner R.;
RT "Plexin-B2, but not Plexin-B1, critically modulates neuronal migration and
RT patterning of the developing nervous system in vivo.";
RL J. Neurosci. 27:6333-6347(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1240 AND SER-1248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-393.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1574, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19948886; DOI=10.1128/mcb.01458-09;
RA Hirschberg A., Deng S., Korostylev A., Paldy E., Costa M.R., Worzfeld T.,
RA Vodrazka P., Wizenmann A., Gotz M., Offermanns S., Kuner R.;
RT "Gene deletion mutants reveal a role for semaphorin receptors of the
RT plexin-B family in mechanisms underlying corticogenesis.";
RL Mol. Cell. Biol. 30:764-780(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH SEMA4C AND SEMA4G.
RX PubMed=21122816; DOI=10.1016/j.mcn.2010.11.005;
RA Maier V., Jolicoeur C., Rayburn H., Takegahara N., Kumanogoh A.,
RA Kikutani H., Tessier-Lavigne M., Wurst W., Friedel R.H.;
RT "Semaphorin 4C and 4G are ligands of Plexin-B2 required in cerebellar
RT development.";
RL Mol. Cell. Neurosci. 46:419-431(2011).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21966369; DOI=10.1371/journal.pone.0024795;
RA Roney K.E., O'Connor B.P., Wen H., Holl E.K., Guthrie E.H., Davis B.K.,
RA Jones S.W., Jha S., Sharek L., Garcia-Mata R., Bear J.E., Ting J.P.;
RT "Plexin-B2 negatively regulates macrophage motility, Rac, and Cdc42
RT activation.";
RL PLoS ONE 6:E24795-E24795(2011).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=29981480; DOI=10.1016/j.mcn.2018.06.008;
RA McDermott J.E., Goldblatt D., Paradis S.;
RT "Class 4 Semaphorins and Plexin-B receptors regulate GABAergic and
RT glutamatergic synapse development in the mammalian hippocampus.";
RL Mol. Cell. Neurosci. 92:50-66(2018).
CC -!- FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that
CC plays an important role in cell-cell signaling (PubMed:17554007). Plays
CC a role in glutamatergic synapse development and is required for SEMA4A-
CC mediated excitatory synapse development (PubMed:29981480). Binding to
CC class 4 semaphorins promotes downstream activation of RHOA and
CC phosphorylation of ERBB2 at 'Tyr-1248' (PubMed:17554007). Required for
CC normal differentiation and migration of neuronal cells during brain
CC corticogenesis and for normal embryonic brain development
CC (PubMed:19948886). Regulates the migration of cerebellar granule cells
CC in the developing brain (PubMed:21122816). Plays a role in RHOA
CC activation and subsequent changes of the actin cytoskeleton (By
CC similarity). Plays a role in axon guidance, invasive growth and cell
CC migration (By similarity). May modulate the activity of RAC1 and CDC42
CC (PubMed:21966369). Down-regulates macrophage migration in wound-healing
CC assays (in vitro) (PubMed:21966369). {ECO:0000250|UniProtKB:O15031,
CC ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:19948886,
CC ECO:0000269|PubMed:21122816, ECO:0000269|PubMed:21966369,
CC ECO:0000269|PubMed:29981480}.
CC -!- SUBUNIT: Monomer, and heterodimer with PLXNB1 (By similarity).
CC Interacts with MET, ARHGEF11 and ARHGEF12 (By similarity). May also
CC interact with MST1R (By similarity). Interacts with SEMA4C
CC (PubMed:17554007, PubMed:21122816). Interacts with SEMA4D
CC (PubMed:17554007). Interacts with SEMA4G (PubMed:21122816).
CC {ECO:0000250|UniProtKB:O15031, ECO:0000269|PubMed:17554007,
CC ECO:0000269|PubMed:21122816}.
CC -!- INTERACTION:
CC B2RXS4; Q68FM7: Arhgef11; NbExp=2; IntAct=EBI-8496724, EBI-2365869;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21966369};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in macrophages from spleen and bone marrow
CC (at protein level) (PubMed:21966369). Detected in granule cells in the
CC developing cerebellum, dentate gyrus and olfactory bulb
CC (PubMed:17554007). Expressed in neurons and glia in the developing
CC hippocampus (PubMed:29981480). {ECO:0000269|PubMed:17554007,
CC ECO:0000269|PubMed:21966369, ECO:0000269|PubMed:29981480}.
CC -!- DISRUPTION PHENOTYPE: Embryonic and perinatal lethality, due to defects
CC in brain and neural tube development. Mice exhibit abnormal cortical
CC layering and defective migration and differentiation of several
CC subtypes of cortical neurons. Cranial neural folds fail to converge in
CC most embryos, leading to an open neural tube and exencephaly. Likewise,
CC mice exhibit defects in the embryonic development of the cerebellum and
CC the olfactory bulb. {ECO:0000269|PubMed:17554007,
CC ECO:0000269|PubMed:19948886}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK147538; BAE27981.1; -; mRNA.
DR EMBL; AC113069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL04367.1; -; Genomic_DNA.
DR EMBL; BC157960; AAI57961.1; -; mRNA.
DR EMBL; BC157961; AAI57962.1; -; mRNA.
DR EMBL; BC158086; AAI58087.1; -; mRNA.
DR EMBL; BC172162; AAI72162.1; -; mRNA.
DR CCDS; CCDS49698.1; -.
DR RefSeq; NP_001152993.1; NM_001159521.2.
DR RefSeq; NP_001271435.1; NM_001284506.1.
DR RefSeq; NP_620088.2; NM_138749.3.
DR RefSeq; XP_006520475.1; XM_006520412.1.
DR RefSeq; XP_006520476.1; XM_006520413.1.
DR RefSeq; XP_011243751.1; XM_011245449.1.
DR RefSeq; XP_011243752.1; XM_011245450.2.
DR RefSeq; XP_011243753.1; XM_011245451.2.
DR PDB; 5E6P; X-ray; 3.21 A; A=1226-1842.
DR PDB; 7KDC; X-ray; 3.10 A; C/D=1463-1565.
DR PDBsum; 5E6P; -.
DR PDBsum; 7KDC; -.
DR AlphaFoldDB; B2RXS4; -.
DR SMR; B2RXS4; -.
DR BioGRID; 228283; 14.
DR IntAct; B2RXS4; 2.
DR MINT; B2RXS4; -.
DR STRING; 10090.ENSMUSP00000051731; -.
DR GlyConnect; 2594; 15 N-Linked glycans (7 sites).
DR GlyGen; B2RXS4; 12 sites, 15 N-linked glycans (7 sites).
DR iPTMnet; B2RXS4; -.
DR PhosphoSitePlus; B2RXS4; -.
DR SwissPalm; B2RXS4; -.
DR EPD; B2RXS4; -.
DR jPOST; B2RXS4; -.
DR MaxQB; B2RXS4; -.
DR PaxDb; B2RXS4; -.
DR PeptideAtlas; B2RXS4; -.
DR PRIDE; B2RXS4; -.
DR ProteomicsDB; 289942; -.
DR Antibodypedia; 322; 153 antibodies from 22 providers.
DR DNASU; 140570; -.
DR Ensembl; ENSMUST00000060808; ENSMUSP00000051731; ENSMUSG00000036606.
DR Ensembl; ENSMUST00000109331; ENSMUSP00000104955; ENSMUSG00000036606.
DR GeneID; 140570; -.
DR KEGG; mmu:140570; -.
DR UCSC; uc007xfr.2; mouse.
DR CTD; 23654; -.
DR MGI; MGI:2154239; Plxnb2.
DR VEuPathDB; HostDB:ENSMUSG00000036606; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; B2RXS4; -.
DR OMA; CTPPIDE; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; B2RXS4; -.
DR TreeFam; TF312962; -.
DR BioGRID-ORCS; 140570; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Plxnb2; mouse.
DR PRO; PR:B2RXS4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; B2RXS4; protein.
DR Bgee; ENSMUSG00000036606; Expressed in pyloric antrum and 293 other tissues.
DR Genevisible; B2RXS4; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:1904861; P:excitatory synapse assembly; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IGI:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Developmental protein; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1842
FT /note="Plexin-B2"
FT /id="PRO_0000415710"
FT TOPO_DOM 20..1201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1202..1222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1223..1842
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..468
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 806..895
FT /note="IPT/TIG 1"
FT DOMAIN 898..982
FT /note="IPT/TIG 2"
FT DOMAIN 986..1095
FT /note="IPT/TIG 3"
FT SITE 1168..1169
FT /note="Cleavage; by proprotein convertases"
FT /evidence="ECO:0000250"
FT MOD_RES 1240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 112..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 250..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 266..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 331..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 471..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 477..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 480..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 491..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 557..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 1382
FT /note="E -> G (in Ref. 1; BAE27981)"
FT /evidence="ECO:0000305"
FT HELIX 1281..1290
FT /evidence="ECO:0007829|PDB:5E6P"
FT STRAND 1296..1300
FT /evidence="ECO:0007829|PDB:5E6P"
FT TURN 1301..1304
FT /evidence="ECO:0007829|PDB:5E6P"
FT TURN 1310..1312
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1313..1327
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1330..1342
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1348..1361
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1366..1385
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1400..1412
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1414..1417
FT /evidence="ECO:0007829|PDB:5E6P"
FT TURN 1418..1421
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1422..1437
FT /evidence="ECO:0007829|PDB:5E6P"
FT TURN 1443..1445
FT /evidence="ECO:0007829|PDB:5E6P"
FT STRAND 1448..1450
FT /evidence="ECO:0007829|PDB:5E6P"
FT STRAND 1466..1473
FT /evidence="ECO:0007829|PDB:7KDC"
FT TURN 1474..1476
FT /evidence="ECO:0007829|PDB:7KDC"
FT STRAND 1481..1486
FT /evidence="ECO:0007829|PDB:7KDC"
FT HELIX 1491..1502
FT /evidence="ECO:0007829|PDB:7KDC"
FT TURN 1503..1505
FT /evidence="ECO:0007829|PDB:7KDC"
FT HELIX 1508..1510
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1514..1516
FT /evidence="ECO:0007829|PDB:7KDC"
FT STRAND 1517..1521
FT /evidence="ECO:0007829|PDB:7KDC"
FT STRAND 1523..1526
FT /evidence="ECO:0007829|PDB:7KDC"
FT STRAND 1532..1534
FT /evidence="ECO:0007829|PDB:7KDC"
FT TURN 1549..1553
FT /evidence="ECO:0007829|PDB:7KDC"
FT STRAND 1559..1564
FT /evidence="ECO:0007829|PDB:7KDC"
FT STRAND 1592..1595
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1623..1647
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1656..1671
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1677..1687
FT /evidence="ECO:0007829|PDB:5E6P"
FT TURN 1688..1692
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1693..1698
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1700..1702
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1710..1725
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1740..1744
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1747..1764
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1771..1785
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1786..1788
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1791..1804
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1806..1815
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1817..1821
FT /evidence="ECO:0007829|PDB:5E6P"
FT HELIX 1824..1834
FT /evidence="ECO:0007829|PDB:5E6P"
FT STRAND 1837..1841
FT /evidence="ECO:0007829|PDB:5E6P"
SQ SEQUENCE 1842 AA; 206230 MW; 0D445E7354C107FF CRC64;
MALPLWALTF LGLTGLGLSL RSRKPESFRS ETELNHLAVD EVTGVVYVGA VNALYQLSAD
LHVQQHVVTG PFMDNKKCTP PIEASQCHEA VLTDNFNQLL LLDPPGKRLV ECGSLFKGIC
ALRAMSNISV RLFYEDGSGE KSFVASNDER VATVGLVTST RPDGERVLFV GKGNGPHDNG
IIVSTRLLDR AEGREAFEAY SDHTTFKAGY LSTNTQQFVA AFEDDFYVFF VFNHQDKHPA
KNRTLLARMC KDDPSYYSYV EMDLQCQDPS DPQDSAFGTC LAASVATSGA GRALYAVFSR
DGRSTGGPGA GLCVFPLDKV REKIEANRNA CYTGAREAGR TIFYKPFHGE IQCGGHLIGA
SESFPCGSEH LPYPLGSRDG LVATAVLHRG GLNLTAVTVT AENDHTVAFL GTSDGRILKV
YLAPDGTSAE YGSIPVDINK KIKQDLALSG NLSSLYAMTQ DKVFRLPVQE CLSYVTCAQC
RDSQDPYCGW CVIEGRCTRK SECSRAEETG HWLWSREKSC VAITDAFPQN MSRRAQGEVR
LSVSPLPTLT EDDELLCLFG DSPPHPARVE DDTVICNSPS SIPSTPPGQD HVDVSIQLLL
KSGSVFLTSH QYPFYDCREA MSLVENLPCI SCASNRWTCQ WDLQYYECRE ASPNPEEGII
RAHMEDNCPQ FLAPDPLVIP MNHETEVTFQ GKNLETVKVS SLYVGSELLN FEETVTMHES
DTFSFRTPKL SHDGNETLPL HLYVKSFGKN IDSKLQVTLY NCSFGRSDCS LCLAADPAYR
CVWCRGQNRC VYEALCSNVT SECPPPVITR IQPETGPLGG GILVTIHGSN LGVKADDVKK
ITVAGQNCAF EPRGYSVSTR IVCAIEASEM PFTGGIEVDV NGKLGHSPPH VQFTYQQPQP
LSVEPRQGPQ AGGTTLTING THLDTGSKED VRVTLNDVPC EVTKFGAQLQ CVTGQQLAPG
QVTLEIYYGG SRVPSPGISF TYCENPMIRA FEPLRSFVSG GRSINVTGQG FSLIQKFAMV
VIAEPLRSWR RRRREAGALE RVTVEGMEYV FYNDTKVVFL SPAVPEEPEA YNLTVLIRMD
GHCAPLRTEA GVFEYVADPT FENFTGGVKK QVNKLIHARG TNLNKAMTLE EAEAFVGAER
CIMKTLTETD LYCEPPEVQP PPKRRQKRDT AHNLPEFIVK FGSREWVLGR VEYDTRASDV
PLSLILPLVM VPMVFIIVVS IYCYWRKSQQ AEREYEKIKS QLEGLEESVR DRCKKEFTDL
MIEMEDQTND VHEAGIPTLD YKTYTDRVFF LPSKDGDKDV MITGKLDIPE SRRPIVEQAL
YQFSNLLNSK SFLINFIHTL ENQREFSARA KVYFASLLTV ALHGKLEYYT DIMRTLFLEL
MEQYVVAKNP KLMLRRSETV VERMLSNWMS ICLYQYLKDS AGEPLYKLFK AIKHQVEKGP
VDAVQKKAKY TLNDTGLLGD DVEYAPLTVS VIVQDEGIDA IPVKVLNCDT ISQVKEKIID
QVYRTQPCSC WPKPDSVVLE WRPGSTAQIL SDLDLTSQRE GRWKRINTLM HYNVRDGATL
ILSKVGVSQQ PEDSQQDLPG ERHALLEEEN RVWHLVRPTD EVDEGKSKRG SMKEKERTKA
ITEIYLTRLL SVKGTLQQFV DNFFQSVLAP GHAVPPAVKY FFDFLDEQAE KHDIRDEDTI
HIWKTNSLPL RFWVNILKNP HFIFDVHVHE VVDASLSVIA QTFMDACTRT EHKLSRDSPS
NKLLYAKEIS TYKKMVEDYY KGIRQMVQVS DQDMNTHLAE ISRAHTDSLN TLVALHQLYQ
YTQKYYDEII NALEEDPAAQ KMQLAFRLQQ IAAALENKVT DL
