PLXD1_MOUSE
ID PLXD1_MOUSE Reviewed; 1925 AA.
AC Q3UH93; Q68HV1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Plexin-D1;
DE Flags: Precursor;
GN Name=Plxnd1;
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 [MRNA].
RC STRAIN=BALB/cJ;
RA Duke-Cohan J.S., Ahmed W., Reinherz E.L.;
RT "Identification of mouse plexin D1.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
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 [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH SEMA3A; SEMA3C AND
RP NRP1.
RX PubMed=15239958; DOI=10.1016/j.devcel.2004.06.002;
RA Gitler A.D., Lu M.M., Epstein J.A.;
RT "PlexinD1 and semaphorin signaling are required in endothelial cells for
RT cardiovascular development.";
RL Dev. Cell 7:107-116(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEMA3E AND SEMA4A.
RX PubMed=17318185; DOI=10.1038/sj.emboj.7601589;
RA Toyofuku T., Yabuki M., Kamei J., Kamei M., Makino N., Kumanogoh A.,
RA Hori M.;
RT "Semaphorin-4A, an activator for T-cell-mediated immunity, suppresses
RT angiogenesis via plexin-D1.";
RL EMBO J. 26:1373-1384(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19027330; DOI=10.1016/j.immuni.2008.10.008;
RA Choi Y.I., Duke-Cohan J.S., Ahmed W.B., Handley M.A., Mann F.,
RA Epstein J.A., Clayton L.K., Reinherz E.L.;
RT "PlexinD1 glycoprotein controls migration of positively selected thymocytes
RT into the medulla.";
RL Immunity 29:888-898(2008).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18992737; DOI=10.1016/j.ydbio.2008.09.031;
RA Zhang Y., Singh M.K., Degenhardt K.R., Lu M.M., Bennett J., Yoshida Y.,
RA Epstein J.A.;
RT "Tie2Cre-mediated inactivation of plexinD1 results in congenital heart,
RT vascular and skeletal defects.";
RL Dev. Biol. 325:82-93(2009).
RN [8]
RP FUNCTION.
RX PubMed=19421194; DOI=10.1038/nature08000;
RA Pecho-Vrieseling E., Sigrist M., Yoshida Y., Jessell T.M., Arber S.;
RT "Specificity of sensory-motor connections encoded by Sema3e-Plxnd1
RT recognition.";
RL Nature 459:842-846(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 [10]
RP FUNCTION.
RX PubMed=22179111; DOI=10.1038/nn.3003;
RA Ding J.B., Oh W.J., Sabatini B.L., Gu C.;
RT "Semaphorin 3E-Plexin-D1 signaling controls pathway-specific synapse
RT formation in the striatum.";
RL Nat. Neurosci. 15:215-223(2012).
CC -!- FUNCTION: Cell surface receptor for SEMA4A and for class 3 semaphorins,
CC such as SEMA3A, SEMA3C and SEMA3E. Plays an important role in cell-cell
CC signaling, and in regulating the migration of a wide spectrum of cell
CC types. Regulates the migration of thymocytes in the medulla. Regulates
CC endothelial cell migration. Plays an important role in ensuring the
CC specificity of synapse formation. Mediates anti-angiogenic signaling in
CC response to SEMA3E. Required for normal development of the heart and
CC vasculature. {ECO:0000269|PubMed:15239958, ECO:0000269|PubMed:17318185,
CC ECO:0000269|PubMed:18992737, ECO:0000269|PubMed:19027330,
CC ECO:0000269|PubMed:19421194, ECO:0000269|PubMed:22179111}.
CC -!- SUBUNIT: Interacts with NRP1 and SEMA4A (PubMed:15239958,
CC PubMed:17318185). Interacts with SH3BP1; they dissociate upon SEMA3E
CC binding to PLXND1 allowing SH3BP1 to transduce downstream signal
CC through RAC1 inactivation (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y4D7, ECO:0000269|PubMed:15239958,
CC ECO:0000269|PubMed:17318185}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17318185,
CC ECO:0000269|PubMed:19027330}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17318185, ECO:0000269|PubMed:19027330}. Cell
CC projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q9Y4D7}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic heart and vascular
CC endothelium, brain, dorsal root ganglia, adrenal gland, lung
CC mesenchyme, small intestine and in the ossification centers of
CC vertebral bodies. {ECO:0000269|PubMed:18992737}.
CC -!- DISRUPTION PHENOTYPE: Neonate lethality, due to defects in the
CC development of the heart outflow tract and in aortic arch patterning,
CC plus defects in peripheral vasculature. Mice also display skeletal
CC defects, but these may be caused by defects in the embryonic
CC vasculature. {ECO:0000269|PubMed:15239958,
CC ECO:0000269|PubMed:18992737}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AY688678; AAT99561.1; -; mRNA.
DR EMBL; AK147513; BAE27964.1; -; mRNA.
DR EMBL; AC139761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS20448.1; -.
DR RefSeq; NP_080652.2; NM_026376.3.
DR PDB; 5V6R; X-ray; 2.70 A; A/B=1339-1925.
DR PDB; 5V6T; X-ray; 3.19 A; A=1339-1925.
DR PDBsum; 5V6R; -.
DR PDBsum; 5V6T; -.
DR AlphaFoldDB; Q3UH93; -.
DR SMR; Q3UH93; -.
DR BioGRID; 212439; 8.
DR CORUM; Q3UH93; -.
DR IntAct; Q3UH93; 1.
DR MINT; Q3UH93; -.
DR STRING; 10090.ENSMUSP00000015511; -.
DR GlyConnect; 2597; 2 N-Linked glycans (4 sites).
DR GlyGen; Q3UH93; 9 sites, 2 N-linked glycans (4 sites).
DR iPTMnet; Q3UH93; -.
DR PhosphoSitePlus; Q3UH93; -.
DR MaxQB; Q3UH93; -.
DR PaxDb; Q3UH93; -.
DR PeptideAtlas; Q3UH93; -.
DR PRIDE; Q3UH93; -.
DR ProteomicsDB; 289944; -.
DR Antibodypedia; 33285; 256 antibodies from 34 providers.
DR DNASU; 67784; -.
DR Ensembl; ENSMUST00000015511; ENSMUSP00000015511; ENSMUSG00000030123.
DR GeneID; 67784; -.
DR KEGG; mmu:67784; -.
DR UCSC; uc009djn.1; mouse.
DR CTD; 23129; -.
DR MGI; MGI:2154244; Plxnd1.
DR VEuPathDB; HostDB:ENSMUSG00000030123; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; Q3UH93; -.
DR OMA; NESVVRC; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q3UH93; -.
DR TreeFam; TF312962; -.
DR Reactome; R-MMU-416700; Other semaphorin interactions.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 67784; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Plxnd1; mouse.
DR PRO; PR:Q3UH93; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UH93; protein.
DR Bgee; ENSMUSG00000030123; Expressed in cortical plate and 218 other tissues.
DR ExpressionAtlas; Q3UH93; baseline and differential.
DR Genevisible; Q3UH93; MM.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IC:MGI.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0017154; F:semaphorin receptor activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IDA:MGI.
DR GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:ARUK-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
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 GO; GO:0007416; P:synapse assembly; IMP:UniProtKB.
DR CDD; cd11247; Sema_plexin_D1; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR042719; Plexin-D1_Sema.
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; 1.
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; Angiogenesis; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..48
FT /evidence="ECO:0000255"
FT CHAIN 49..1925
FT /note="Plexin-D1"
FT /id="PRO_0000415890"
FT TOPO_DOM 49..1271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1272..1292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1293..1925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..548
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 893..977
FT /note="IPT/TIG 1"
FT DOMAIN 983..1065
FT /note="IPT/TIG 2"
FT DOMAIN 1071..1145
FT /note="IPT/TIG 3"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 142..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 324..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 347..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 551..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 557..602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 560..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 571..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 639..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 14
FT /note="R -> W (in Ref. 1; AAT99561)"
FT /evidence="ECO:0000305"
FT HELIX 1351..1359
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1390..1392
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1400..1402
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1403..1417
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1420..1431
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1438..1451
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1452..1454
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1456..1473
FT /evidence="ECO:0007829|PDB:5V6R"
FT TURN 1474..1476
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1479..1481
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1489..1508
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1511..1525
FT /evidence="ECO:0007829|PDB:5V6R"
FT TURN 1532..1534
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1537..1539
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1543..1545
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1555..1562
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1566..1568
FT /evidence="ECO:0007829|PDB:5V6T"
FT STRAND 1570..1575
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1580..1591
FT /evidence="ECO:0007829|PDB:5V6R"
FT TURN 1592..1594
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1597..1599
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1603..1605
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1606..1610
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1613..1615
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1617..1619
FT /evidence="ECO:0007829|PDB:5V6T"
FT STRAND 1622..1624
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1628..1630
FT /evidence="ECO:0007829|PDB:5V6T"
FT STRAND 1633..1635
FT /evidence="ECO:0007829|PDB:5V6R"
FT TURN 1639..1643
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1648..1654
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1672..1675
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1701..1725
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1730..1732
FT /evidence="ECO:0007829|PDB:5V6T"
FT HELIX 1735..1749
FT /evidence="ECO:0007829|PDB:5V6R"
FT TURN 1750..1752
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1756..1764
FT /evidence="ECO:0007829|PDB:5V6R"
FT TURN 1765..1771
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1772..1777
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1779..1781
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1789..1806
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1820..1822
FT /evidence="ECO:0007829|PDB:5V6T"
FT TURN 1823..1827
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1828..1844
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1850..1863
FT /evidence="ECO:0007829|PDB:5V6R"
FT STRAND 1865..1868
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1870..1883
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1885..1893
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1896..1900
FT /evidence="ECO:0007829|PDB:5V6R"
FT HELIX 1903..1921
FT /evidence="ECO:0007829|PDB:5V6R"
SQ SEQUENCE 1925 AA; 211608 MW; 7385B372DC53AF2E CRC64;
MARRAAGGAP PSARAAAAVP LRPRPHSRGP GLLPLPLLLL LGAARAGALE IQRRFPSPTP
TNNFALDGTA GTVYLAAVNR LYQLSSANLS LEAEATVGPV PDSPLCHAPQ LPQASCEHPR
RLTDNYNKIL QLDPGQGLVV ACGSIYQGLC QLRRRGNISA LAVSFPPAAP TAEPVTVFPS
MLNVAANHPN ASTVGLVLPP TSGTGGSRLL VGATYTGFGS AFFPRNRSLE DHRFENTPEI
AIRSLDARGD LAKLFTFDLN PSDDNILKIK QGAKEQHKLG FVRAFLHPAV PPHSAQPYAY
LALNSEARAG DKDSQARSLL ARICLPRGAG GDAKKLTESY IQLGLQCAGG AGRGDLYSRL
VSVFPAREQF FAVFERPQGA PGARNAPAAL CAFRFDDVQA AIRAARTACF VEPAPDVVAV
LDSVVQGTGP ACESKRNIQL QPEQLDCGAA HLQHPLTILQ PLRASPVFRA PGLTAVAVAS
ANNYTAVFLG TATGRLLKIS LNESMQVVSR RVLTVAYGEP VHHVMQFDPM DPGYLYLMTS
HQMARVKVAA CEVHSTCGDC VGAADAYCGW CTLETRCTLQ QDCTNSSQPH FWTSASEGPS
RCPAMTVLPS EIDVHRDYTG MILQISGSLP SLSGMEMACD YGNGVRTVAR VPGPAYDHQI
AYCNLLPRAQ FPSFPAGQDH VTVEMSVRVK GHNIVSANFT IYDCSRIGQV YPHTACTSCL
STQWPCSWCI QLHSCVSNQS QCQDSPNPTS PQDCPQILPS PLAPVPTGGS QDILVPLTKA
TFFHGSSLEC SFGLEESFEA VWANNSLVRC NQVVLHTTQK SQVFPLSLKL KGPPDRFLDS
PNPMTVVVYN CAMGSPDCSQ CLGREDLGHL CVWNDGCRLR GPLQPLPGTC PAPEIRAIEP
LSGPLDGGTL LTIRGRNLGR RLSDVAHGVW IGSVACEPLA DRYTVSEEIV CATGPAAGAF
SDVVTVNVSK EGRSREQFSY VLPTVHSLEP SMGPKAGGTR ITIHGSDLNV GSMLQVLVND
TDPCTDLTRT ATSITCTVPG GTLPSPVPVC VRFESRGCVH GNLTFWYMQN PVITAISPGR
SPVSGGRTIT VAGERFHMVQ NVSMAVHHIG REPTFCKVLN STLITCPSPG ALSNASAPVD
FFINGRAYAD EAAEELLDPA EAQRGSRFRL DYLPNPQFST AKREKWIKHH PGEPLTLVIH
KEQDSLGLES HEYHIKIGQV SCDIQIISDR VIHCSVNESL GTAEGQLPIT IQVGNFNQTI
ATLQLGGSET AIVVSIVICS VLLLLSVVAL FVFCTKSRRA ERYWQKTLLQ MEEMESQIRE
EIRKGFAELQ TDMTDLTKEL NRSQGIPFLE YKHFVTRTFF PKCSSLYEER YVLPSKTLNS
QGGSPPQETH PLLGEWNIPE HCRPSMEEGI SLFSSLLNNK HFLIVFVHAL EQQKDFAVRD
RCSLASLLTI ALHGKLEYYT SIMKELLVDL IDASAAKNPK LMLRRTESVV EKMLTNWMSI
CMYGCLRETV GEPFFLLLCA IKQQINKGSI DAITGKARYT LNEEWLLREN IEAKPRNLNV
SFQGCGMDSL SVRAMDTDTL TQVKEKILEA FCKNVPYSQW PRAEDVDLEW FASSTQSYVL
RDLDDTSVVE DGRKKLNTLA HYKIPEGASL AMSLTDKKDS TLGRVKDLDT EKYFHLVLPT
DELVEPKKSH RQSHRKKVLP EIYLTRLLST KGTLQKFLDD LFKAILSIRE DKPPLAVKYF
FDFLEEQAEK RGISDPDTLH IWKTNSLPLR FWVNILKNPQ FVFDIEKTDH IDACLSVIAQ
AFIDACSISD LQLGKDSPTN KLLYAKEIPE YRKTVQRYYK QIQDMTPLSE QEMNAHLAEE
SRKYQNEFNT NVAMAEIYKY AKRYRPQIMA ALEANPTARR TQLQHKFEQV VALMENNIYE
CYSEA
