PLXA3_MOUSE
ID PLXA3_MOUSE Reviewed; 1872 AA.
AC P70208; A5D6Q5; Q684J0; Q8BWZ5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Plexin-A3;
DE Flags: Precursor;
GN Name=Plxna3;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=8806646; DOI=10.1006/bbrc.1996.1367;
RA Kameyama T., Murakami Y., Suto F., Kawakami A., Takagi S., Hirata T.,
RA Fujisawa H.;
RT "Identification of plexin family molecules in mice.";
RL Biochem. Biophys. Res. Commun. 226:396-402(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1116-1560.
RC STRAIN=NMRI; TISSUE=Embryo;
RA Kolb-Kokocinski A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J.,
RA Pepperkok R., Wiemann S., Poustka A.;
RT "Towards functional annotation of all Xq28 genes: expression and
RT intracellular localization analyses reveal novel candidates for disease
RT genes.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1138-1872.
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=11683995; DOI=10.1016/s0896-6273(01)00478-0;
RA Cheng H.J., Bagri A., Yaron A., Stein E., Pleasure S.J.,
RA Tessier-Lavigne M.;
RT "Plexin-A3 mediates semaphorin signaling and regulates the development of
RT hippocampal axonal projections.";
RL Neuron 32:249-263(2001).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18262512; DOI=10.1016/j.ydbio.2008.01.002;
RA Waimey K.E., Huang P.H., Chen M., Cheng H.J.;
RT "Plexin-A3 and plexin-A4 restrict the migration of sympathetic neurons but
RT not their neural crest precursors.";
RL Dev. Biol. 315:448-458(2008).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18804103; DOI=10.1016/j.ydbio.2008.08.020;
RA Schwarz Q., Waimey K.E., Golding M., Takamatsu H., Kumanogoh A.,
RA Fujisawa H., Cheng H.J., Ruhrberg C.;
RT "Plexin A3 and plexin A4 convey semaphorin signals during facial nerve
RT development.";
RL Dev. Biol. 324:1-9(2008).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19020035; DOI=10.1523/jneurosci.3573-08.2008;
RA Ben-Zvi A., Manor O., Schachner M., Yaron A., Tessier-Lavigne M., Behar O.;
RT "The Semaphorin receptor PlexinA3 mediates neuronal apoptosis during dorsal
RT root ganglia development.";
RL J. Neurosci. 28:12427-12432(2008).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20010807; DOI=10.1038/nature08628;
RA Tran T.S., Rubio M.E., Clem R.L., Johnson D., Case L., Tessier-Lavigne M.,
RA Huganir R.L., Ginty D.D., Kolodkin A.L.;
RT "Secreted semaphorins control spine distribution and morphogenesis in the
RT postnatal CNS.";
RL Nature 462:1065-1069(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1170-1795, FUNCTION, AND
RP MUTAGENESIS OF LEU-1279; TYR-1300; PHE-1309; 1407-ARG-ARG-1408; ILE-1453;
RP LEU-1464; GLN-1506 AND 1631-HIS-HIS-1632.
RX PubMed=19717441; DOI=10.1073/pnas.0906923106;
RA He H., Yang T., Terman J.R., Zhang X.;
RT "Crystal structure of the plexin A3 intracellular region reveals an
RT autoinhibited conformation through active site sequestration.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15610-15615(2009).
CC -!- FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by
CC class 3 semaphorins and subsequent remodeling of the cytoskeleton.
CC Plays a role in axon guidance in the developing nervous system.
CC Regulates the migration of sympathetic neurons, but not of neural crest
CC precursors. Required for normal dendrite spine morphology in pyramidal
CC neurons. May play a role in regulating semaphorin-mediated programmed
CC cell death in the developing nervous system. Class 3 semaphorins bind
CC to a complex composed of a neuropilin and a plexin. The plexin
CC modulates the affinity of the complex for specific semaphorins, and its
CC cytoplasmic domain is required for the activation of down-stream
CC signaling events in the cytoplasm. {ECO:0000269|PubMed:11683995,
CC ECO:0000269|PubMed:18262512, ECO:0000269|PubMed:18804103,
CC ECO:0000269|PubMed:19020035, ECO:0000269|PubMed:19717441,
CC ECO:0000269|PubMed:20010807}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P70208-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70208-2; Sequence=VSP_041609;
CC -!- TISSUE SPECIFICITY: Detected in embryonic hindbrain, spinal cord,
CC dorsal root ganglion, trigeminal ganglion and superior cervical
CC ganglion. In newborns, detected throughout all layers of the
CC hippocampus. {ECO:0000269|PubMed:11683995, ECO:0000269|PubMed:18804103,
CC ECO:0000269|PubMed:8806646}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but causes subtle changes
CC in the central nervous system. Mice exhibit altered apical dendrite
CC spine morphology in pyramidal neurons. Mice exhibit defasciculation of
CC the facial branchiomotor nerve and of the ophthalmic branch of the
CC trigeminus, with variable severity. The number of neurons in the dorsal
CC root ganglion is higher than normal, probably due to reduced neuronal
CC apoptosis. In mice lacking both Plxna3 and Plxna4, migrating neurons do
CC not show the normal response to Sema3A and Sema3F and do not migrate
CC away from these semaphorins (in vitro). {ECO:0000269|PubMed:11683995,
CC ECO:0000269|PubMed:18262512, ECO:0000269|PubMed:18804103,
CC ECO:0000269|PubMed:19020035, ECO:0000269|PubMed:20010807}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; D86950; BAA13190.1; -; mRNA.
DR EMBL; BC093482; AAH93482.1; -; mRNA.
DR EMBL; AJ748653; CAG38687.1; -; mRNA.
DR EMBL; AK049319; BAC33681.1; -; mRNA.
DR CCDS; CCDS30228.1; -. [P70208-1]
DR PIR; JC4976; JC4976.
DR RefSeq; NP_032909.2; NM_008883.2. [P70208-1]
DR RefSeq; XP_006527963.1; XM_006527900.2.
DR PDB; 3IG3; X-ray; 1.99 A; A=1247-1872.
DR PDBsum; 3IG3; -.
DR AlphaFoldDB; P70208; -.
DR SMR; P70208; -.
DR BioGRID; 202263; 4.
DR DIP; DIP-48959N; -.
DR STRING; 10090.ENSMUSP00000004326; -.
DR GlyConnect; 2591; 1 N-Linked glycan (1 site).
DR GlyGen; P70208; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P70208; -.
DR PhosphoSitePlus; P70208; -.
DR MaxQB; P70208; -.
DR PaxDb; P70208; -.
DR PeptideAtlas; P70208; -.
DR PRIDE; P70208; -.
DR ProteomicsDB; 289630; -. [P70208-1]
DR ProteomicsDB; 289631; -. [P70208-2]
DR Antibodypedia; 31267; 61 antibodies from 18 providers.
DR DNASU; 18846; -.
DR Ensembl; ENSMUST00000004326; ENSMUSP00000004326; ENSMUSG00000031398. [P70208-1]
DR GeneID; 18846; -.
DR KEGG; mmu:18846; -.
DR UCSC; uc009too.1; mouse. [P70208-1]
DR UCSC; uc012hku.1; mouse. [P70208-2]
DR CTD; 55558; -.
DR MGI; MGI:107683; Plxna3.
DR VEuPathDB; HostDB:ENSMUSG00000031398; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; P70208; -.
DR OMA; VYYNCSV; -.
DR PhylomeDB; P70208; -.
DR TreeFam; TF312962; -.
DR Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR BioGRID-ORCS; 18846; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Plxna3; mouse.
DR EvolutionaryTrace; P70208; -.
DR PRO; PR:P70208; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70208; protein.
DR Bgee; ENSMUSG00000031398; Expressed in cortical plate and 268 other tissues.
DR ExpressionAtlas; P70208; baseline and differential.
DR Genevisible; P70208; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; IMP:UniProtKB.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IGI:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021612; P:facial nerve structural organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IGI:ARUK-UCL.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IGI:MGI.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IGI:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:1990138; P:neuron projection extension; IGI:MGI.
DR GO; GO:0097485; P:neuron projection guidance; IMP:MGI.
DR GO; GO:0021628; P:olfactory nerve formation; IGI:ARUK-UCL.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0021860; P:pyramidal neuron development; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
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:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021637; P:trigeminal nerve structural organization; IMP:ParkinsonsUK-UCL.
DR Gene3D; 1.10.506.10; -; 1.
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; 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; IPR041362; TIG2_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; 4.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 4.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1872
FT /note="Plexin-A3"
FT /id="PRO_0000411104"
FT TOPO_DOM 20..1220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1221..1241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1242..1872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..489
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 841..934
FT /note="IPT/TIG 1"
FT DOMAIN 936..1021
FT /note="IPT/TIG 2"
FT DOMAIN 1024..1123
FT /note="IPT/TIG 3"
FT DOMAIN 1126..1212
FT /note="IPT/TIG 4"
FT COILED 1240..1294
FT /evidence="ECO:0000255"
FT MOD_RES 1597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51805"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 113..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 267..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 283..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 357..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 492..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 498..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 501..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 512..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 575..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 1072..1148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041609"
FT MUTAGEN 1279
FT /note="L->R: Strongly reduced response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT MUTAGEN 1300
FT /note="Y->A: Almost abolishes response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT MUTAGEN 1309
FT /note="F->A: Almost abolishes response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT MUTAGEN 1407..1408
FT /note="RR->AA: Abolishes response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT MUTAGEN 1453
FT /note="I->R: Abolishes response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT MUTAGEN 1464
FT /note="L->G: Almost abolishes response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT MUTAGEN 1506
FT /note="Q->A: Abolishes response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT MUTAGEN 1631..1632
FT /note="HL->AA: Abolishes response to semaphorin."
FT /evidence="ECO:0000269|PubMed:19717441"
FT CONFLICT 1627
FT /note="T -> A (in Ref. 4; BAC33681)"
FT /evidence="ECO:0000305"
FT CONFLICT 1861
FT /note="L -> P (in Ref. 1; BAA13190)"
FT /evidence="ECO:0000305"
FT HELIX 1248..1286
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1300..1308
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1316..1318
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1325..1337
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1341..1352
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1359..1372
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1374..1376
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1377..1397
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1403..1407
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1412..1424
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1426..1431
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1434..1448
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1455..1457
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1466..1468
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1478..1484
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1486..1488
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1493..1499
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1504..1515
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1516..1518
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1521..1523
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1527..1529
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1530..1536
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1541..1544
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1546..1548
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1557..1559
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1563..1567
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1573..1578
FT /evidence="ECO:0007829|PDB:3IG3"
FT STRAND 1628..1632
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1653..1677
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1682..1684
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1689..1703
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1704..1706
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1710..1720
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1721..1724
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1725..1731
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1733..1735
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1743..1759
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1773..1777
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1778..1781
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1782..1798
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1804..1817
FT /evidence="ECO:0007829|PDB:3IG3"
FT TURN 1818..1820
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1824..1837
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1839..1848
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1850..1854
FT /evidence="ECO:0007829|PDB:3IG3"
FT HELIX 1857..1869
FT /evidence="ECO:0007829|PDB:3IG3"
SQ SEQUENCE 1872 AA; 207958 MW; 39D57886A0C4830A CRC64;
MPTVCLLPLL FFTIGGCLGS SRPFRTFVVT DTTLTHLAVH RVTGEVFVGA VNRVFKLAPN
LTELRAHVTG PIEDNARCYP PPSMRVCSHR LVPVDNVNKL LLIDYAARRL VACGSIWQGI
CQFLRLDDLF KLGEPHHRKE HYLSGAQEPD SMAGVIVEQV QGPSKLFVGT AVDGKSEYFP
TLSSRKLIDD EDSGDMFSLV YQDEFVSSQI KIPSDTLSLY PAFDIYYIYG FVSASFVYFL
TLQLDTQQTL LDTAGEKFFT SKIVRMCAGD SEFYSYVEFP IGCSWRGVEY RLVQSAHLAK
PGLLLAQALG VPADEDVLFT IFSQGQKNRA NPPRQTILCL FTLSSINAHI RRRIQSCYRG
EGTLALPWLL NKELPCINTP LQINGNFCGL VLNQPLGGLH VIEGLPLLAD STDGMASVAA
YTYHQHSVVF IGTRSGNLKK VRVDGSQDAQ LYETVSVVQG SPILRDLLFS PDHRHIYLLS
EKQVSQLPVE TCEQYLSCAA CLGSGDPHCG WCVLQHRCCR EGACPGASAP HGFAEELSKC
IQVRVRPNNV SVTSSGVQLT VAMRNVPDLS VGVSCSFEEV TESEAILLPS GELRCPSPSL
QELQTLTRGH GATHTVRLQL LSMETGVRFA GVDFVFYNCS ALQSCMSCVG SPYPCHWCKY
RHVCTSHPHE CSFQEGRVHS PEGCPEILPQ GDLLIPVGVM QPLTLRAKNL PQPQSGQKNY
ECVVRVQGRQ HRVPAVRFNS SSVQCQNASY FYEGDEFGDT ELDFSVVWDG DFPIDKPPSF
RALLYKCWAQ RPSCGLCLKA DPRFNCGWCI SEHRCQLRAH CPAPKSNWMH PSQKGARCSH
PRITQIHPLT GPKEGGTRVT IVGENLGLTS REVGLRVAGV RCNSIPTEYV SAERIVCEME
ESLVPSPPPG PAELCVGDCS ADFRTQSQQL YSFVTPTFDR VSPSRGPASG GTRLTISGIS
LDAGSRVTVI IRDGECQFVR RDAEAIVCIS PVSTLGPSQS PITLAIDHAN ISNTGVIYTY
TQDPTVTHLE PTWSIINGST SITVSGTHLL TVQEPRVRAK YRGIETTNTC QVINDTAMLC
KAPGIFLGHP QPRAQGEHPD EFGFLLDHVQ AARSLNRSSF TYYPDPSFEP LGPSGVLDVK
PGSHVVLKGK NLIPAAAGSS RLNYTVLIGG QPCALTVSDT QLLCDSPSQT GRQPVMVLVG
GLEFWLGTLH ITADRALTLP AMVGLAAGGG LLLLAITVVL VAYKRKTQDA DRTLKRLQLQ
MDNLESRVAL ECKEAFAELQ TDINELTNHM DGVQIPFLDY RTYAVRVLFP GIEAHPVLKE
LDTPPNVEKA LRLFGQLLHS RAFLLTFIHT LEAQSSFSMR DRGTVASLTM VALQSRLDYA
TGLLKQLLAD LIEKNLESKN HPKLLLRRTE SVAEKMLTNW FTFLLHKFLK ECAGEPLFLL
YCAIKQQMEK GPIDAITGEA RYSLSEDKLI RQQIDYKTLT LHCVCPESEG SAQVPVKVLN
CDSITQAKDK LLDTVYKGIP YSQRPKAEDM DLEWRQGRMA RIILQDEDIT TKIECDWKRV
NSLAHYQVTD GSLVALVPKQ VSAYNMANSF TFTRSLSRYE SLLRAASSPD SLRSRAPMLT
PDQEAGTKLW HLVRNHDHTD HREGDRGSKM VSEIYLTRLL ATKGTLQKFV DDLFETVFST
AHRGSALPLA IKYMFDFLDE QADQRQISDP DVRHTWKSNC LPLRFWVNVI KNPQFVFDIH
KNSITDACLS VVAQTFMDSC STSEHRLGKD SPSNKLLYAK DIPNYKSWVE RYYRDIAKMA
SISDQDMDAY LVEQSRLHAN DFNVLSALSE LYFYVTKYRQ EILTSLDRDA SCRKHKLRQK
LEQIITLVSS SS
