PLXA2_MOUSE
ID PLXA2_MOUSE Reviewed; 1894 AA.
AC P70207; Q6NVE6; Q6PHN4; Q80TZ7; Q8R1I4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Plexin-A2;
DE Short=Plex 2;
DE Short=Plexin-2;
DE Flags: Precursor;
GN Name=Plxna2; Synonyms=Kiaa0463;
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 TISSUE=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].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Colon;
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 366-1894.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH NRP1 AND SEMA3A.
RX PubMed=10520994; DOI=10.1016/s0092-8674(00)80062-8;
RA Takahashi T., Fournier A., Nakamura F., Wang L.-H., Murakami Y., Kalb R.G.,
RA Fujisawa H., Strittmatter S.M.;
RT "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.";
RL Cell 99:59-69(1999).
RN [5]
RP FUNCTION, AND INTERACTION WITH NRP1; NRP2 AND SEMA3A.
RX PubMed=10781943; DOI=10.1016/s0925-4773(00)00269-0;
RA Rohm B., Ottemeyer A., Lohrum M., Pueschel A.W.;
RT "Plexin/neuropilin complexes mediate repulsion by the axonal guidance
RT signal semaphorin 3A.";
RL Mech. Dev. 93:95-104(2000).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 35-701 IN COMPLEX WITH SEMA6A,
RP INTERACTION WITH SEMA6A, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP ASN-76; ASN-163; ASN-327 AND ASN-598, MUTAGENESIS OF PHE-221 AND ALA-396,
RP AND DISULFIDE BONDS.
RX PubMed=20877282; DOI=10.1038/nature09468;
RA Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H., Mitchell K.J.,
RA Siebold C., Jones E.Y.;
RT "Structural basis of semaphorin-plexin signalling.";
RL Nature 467:1118-1122(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-561 IN COMPLEX WITH SEMA6A,
RP INTERACTION WITH SEMA6A, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP ASN-76, MUTAGENESIS OF ASP-193; PHE-221 AND ALA-396, AND DISULFIDE BONDS.
RX PubMed=20881961; DOI=10.1038/nature09473;
RA Nogi T., Yasui N., Mihara E., Matsunaga Y., Noda M., Yamashita N.,
RA Toyofuku T., Uchiyama S., Goshima Y., Kumanogoh A., Takagi J.;
RT "Structural basis for semaphorin signalling through the plexin receptor.";
RL Nature 467:1123-1127(2010).
CC -!- FUNCTION: Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by
CC SEMA6A and class 3 semaphorins and subsequent remodeling of the
CC cytoskeleton. Plays a role in axon guidance, invasive growth and cell
CC migration. Class 3 semaphorins bind to a complex composed of a
CC neuropilin and a plexin. The plexin modulates the affinity of the
CC complex for specific semaphorins, and its cytoplasmic domain is
CC required for the activation of down-stream signaling events in the
CC cytoplasm. {ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943,
CC ECO:0000269|PubMed:20877282}.
CC -!- SUBUNIT: Homodimer. Interacts with RND1 (By similarity). Interacts
CC directly with NRP1 and NRP2. The PLXNA2 homodimer interacts with a
CC SEMA6A homodimer, giving rise to a heterotetramer. {ECO:0000250,
CC ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943,
CC ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}.
CC -!- INTERACTION:
CC P70207; P97333: Nrp1; NbExp=3; IntAct=EBI-771272, EBI-1555129;
CC P70207; P70207: Plxna2; NbExp=4; IntAct=EBI-771272, EBI-771272;
CC P70207; O35464-1: Sema6a; NbExp=5; IntAct=EBI-771272, EBI-15880936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20877282,
CC ECO:0000269|PubMed:20881961}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68155.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA13189.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86949; BAA13189.1; ALT_INIT; mRNA.
DR EMBL; BC024509; AAH24509.1; -; mRNA.
DR EMBL; BC056475; AAH56475.1; -; mRNA.
DR EMBL; BC068155; AAH68155.1; ALT_INIT; mRNA.
DR EMBL; AK122289; BAC65571.1; -; mRNA.
DR CCDS; CCDS35827.1; -.
DR PIR; JC4975; JC4975.
DR RefSeq; NP_032908.2; NM_008882.2.
DR PDB; 3AL8; X-ray; 3.60 A; B=31-561.
DR PDB; 3AL9; X-ray; 2.10 A; A/B=31-561.
DR PDB; 3OKT; X-ray; 2.30 A; A=35-703.
DR PDB; 3OKY; X-ray; 2.20 A; A=35-703.
DR PDB; 4GZA; X-ray; 7.00 A; A/B/C/D/E/F=33-703.
DR PDB; 5L5G; X-ray; 10.00 A; A/B/C/D=33-1231.
DR PDB; 5L74; X-ray; 1.36 A; A=655-803.
DR PDBsum; 3AL8; -.
DR PDBsum; 3AL9; -.
DR PDBsum; 3OKT; -.
DR PDBsum; 3OKY; -.
DR PDBsum; 4GZA; -.
DR PDBsum; 5L5G; -.
DR PDBsum; 5L74; -.
DR AlphaFoldDB; P70207; -.
DR SMR; P70207; -.
DR BioGRID; 202262; 12.
DR DIP; DIP-32252N; -.
DR IntAct; P70207; 2.
DR STRING; 10090.ENSMUSP00000027952; -.
DR GlyConnect; 2590; 6 N-Linked glycans (3 sites).
DR GlyGen; P70207; 11 sites, 6 N-linked glycans (3 sites).
DR iPTMnet; P70207; -.
DR PhosphoSitePlus; P70207; -.
DR MaxQB; P70207; -.
DR PaxDb; P70207; -.
DR PeptideAtlas; P70207; -.
DR PRIDE; P70207; -.
DR ProteomicsDB; 289629; -.
DR Antibodypedia; 4060; 188 antibodies from 27 providers.
DR DNASU; 18845; -.
DR Ensembl; ENSMUST00000027952; ENSMUSP00000027952; ENSMUSG00000026640.
DR GeneID; 18845; -.
DR KEGG; mmu:18845; -.
DR UCSC; uc007een.1; mouse.
DR CTD; 5362; -.
DR MGI; MGI:107684; Plxna2.
DR VEuPathDB; HostDB:ENSMUSG00000026640; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; P70207; -.
DR OMA; GQHHFTA; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; P70207; -.
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; 18845; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Plxna2; mouse.
DR EvolutionaryTrace; P70207; -.
DR PRO; PR:P70207; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P70207; protein.
DR Bgee; ENSMUSG00000026640; Expressed in ganglionic eminence and 277 other tissues.
DR ExpressionAtlas; P70207; baseline and differential.
DR Genevisible; P70207; 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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017154; F:semaphorin receptor activity; IMP:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0021935; P:cerebellar granule cell precursor tangential migration; IMP:MGI.
DR GO; GO:0060174; P:limb bud formation; IEP:BHF-UCL.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0021915; P:neural tube development; IEP:BHF-UCL.
DR GO; GO:0060037; P:pharyngeal system development; IEP:BHF-UCL.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
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:0001756; P:somitogenesis; IEP:BHF-UCL.
DR CDD; cd11272; Sema_plexin_A2; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 6.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR042826; Plexin-A2_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; 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; 1.
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; Cell membrane; Coiled coil; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1894
FT /note="Plexin-A2"
FT /id="PRO_0000232748"
FT TOPO_DOM 35..1237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1238..1258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1259..1894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..508
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 858..951
FT /note="IPT/TIG 1"
FT DOMAIN 954..1037
FT /note="IPT/TIG 2"
FT DOMAIN 1041..1139
FT /note="IPT/TIG 3"
FT DOMAIN 1143..1228
FT /note="IPT/TIG 4"
FT COILED 1261..1310
FT /evidence="ECO:0000255"
FT MOD_RES 1612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75051"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20877282,
FT ECO:0000269|PubMed:20881961"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20877282"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20877282"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20877282"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT DISULFID 129..137
FT DISULFID 284..405
FT DISULFID 300..356
FT DISULFID 374..393
FT DISULFID 511..528
FT DISULFID 517..559
FT DISULFID 520..537
FT DISULFID 531..543
FT DISULFID 594..613
FT MUTAGEN 193
FT /note="D->K: Abolishes interaction with SEMA6A."
FT /evidence="ECO:0000269|PubMed:20881961"
FT MUTAGEN 221
FT /note="F->A,R: Abolishes interaction with SEMA6A."
FT /evidence="ECO:0000269|PubMed:20877282,
FT ECO:0000269|PubMed:20881961"
FT MUTAGEN 396
FT /note="A->E: Abolishes interaction with SEMA6A."
FT /evidence="ECO:0000269|PubMed:20877282,
FT ECO:0000269|PubMed:20881961"
FT CONFLICT 211
FT /note="A -> P (in Ref. 2; AAH68155)"
FT /evidence="ECO:0000305"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3OKT"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 275..286
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 305..316
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 334..344
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 360..375
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 432..440
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 453..462
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 466..474
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 500..508
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:3AL9"
FT TURN 544..547
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:3AL9"
FT HELIX 557..561
FT /evidence="ECO:0007829|PDB:3AL9"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 592..596
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 630..639
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 645..654
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:5L74"
FT HELIX 662..666
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:5L74"
FT TURN 676..679
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 680..683
FT /evidence="ECO:0007829|PDB:5L74"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:5L74"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:5L74"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 710..713
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 718..725
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 737..743
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 746..756
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 759..765
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 775..785
FT /evidence="ECO:0007829|PDB:5L74"
FT TURN 786..788
FT /evidence="ECO:0007829|PDB:5L74"
FT STRAND 799..802
FT /evidence="ECO:0007829|PDB:5L74"
SQ SEQUENCE 1894 AA; 211535 MW; 9F6C34F48BC29CEE CRC64;
MEQRRFYLRA MQADNLSVVL LSVAWLLLAR GTTGMPQYST FHSENRDWTF NHLTVHRRTG
AVYVGAINRV YKLTGNLTIQ VAHKTGPEED NKACYPPLIV QPCSEVLTLT NNVNKLLIID
YSENRLLACG SLYQGVCKLL RLDDLFILVE PSHKKEHYLS SVNKTGTMYG VIVRSEGEDG
KLFIGTAVDG KQDYFPTLSS RKLPRDPESS AMLDYELHSD FVSSLIKIPS DTLALVSHFD
IFYIYGFASG GFVYFLTVQP ETPDGMAINS AGDLFYTSRI VRLCKDDPKF HSYVSLPFGC
TRAGVEYRLL QAAYLAKPGE ALAQAFNISS DEDVLFAIFS KGQKQYHHPP DDSALCAFPI
RAINLQIKER LQSCYHGEGN LELNWLLGKD VQCTKAPVPI DDNFCGLDIN QPLGGSTPVE
GLTLYTTSRD RLTSVASYVY NGYSVVFVGT KSGKLKKIRA DGPPHGGVQY EMVSVFKDGS
PILRDMAFSI NQLYLYVMSE RQVTRVPVES CEQYTTCGEC LSSGDPHCGW CALHNMCSRR
DKCQRAWEAN RFAASISQCM SLEVHPNSIS VSDHSRLLSL VVNDAPNLSE GIACAFGNLT
EVEGQVSGSQ VICISPGPKD VPVIPLDQDW FGLELQLRSK ETGKIFVSTE FKFYNCSAHQ
LCLSCVNSAF RCHWCKYRNL CTHDPTTCSF QEGRINVSED CPQLVPTEEI LIPVGEVKPI
TLKARNLPQP QSGQRGYECV LSIQGAVHRV PALRFNSSSV QCQNSSYQYD GMDISNLAVD
FAVVWNGNFI IDNPQDLKVH LYKCAAQRES CGLCLKADHK FECGWCSGER RCTLHQHCPS
TSSPWLDWSS HNVKCSNPQI TEILTVSGPP EGGTRVTIHG VNLGLDFSEI AHHVQVAGVP
CTPIPGEYII AEQIVCEMGH AVIGTTSGPV RLCIGECKPE FMTKSHQQYT FVNPSVLSLS
PIRGPESGGT MVTITGHYLG AGSSVAVYLG NQTCEFYGRS MNEIVCVSPP SSNGLGPVPV
SVSVDRARVD SSLQFEYIDD PRVQRIEPEW SITSGHTPLT ITGFNLDVIQ EPRVRVKFNG
KESVNVCTVV NTTTLTCLAP SLTSDYRPGL DTVERPDEFG FLFNNVQSLL IYNDTKFIYY
PNPTFELLSP TGILDQKPGS PIILKGKNLC PPASGGAKLN YTVMIGETPC TVTVSETQLL
CEPPNLTGQH KVMVHVGGMV FSPGSVSVIS DSLLTLPAII SIAAGGSLLL IIVIIVLIAY
KRKSRENDLT LKRLQMQMDN LESRVALECK EAFAELQTDI NELTSDLDRS GIPYLDYRTY
AMRVLFPGIE DHPVLRELEV QGNGQQHVEK ALKLFAQLIN NKVFLLTFIR TLELQRSFSM
RDRGNVASLI MTGLQGRLEY ATDVLKQLLS DLIDKNLENK NHPKLLLRRT ESVAEKMLTN
WFAFLLHKFL KECAGEPLFM LYCAIKQQME KGPIDAITGE ARYSLSEDKL IRQQIEYKTL
ILNCVNPDNE NSPEIPVKVL NCDTITQVKE KILDAVYKNV PYSQRPRAVD MDLEWRQGRI
ARVVLQDEDI TTKIEGDWKR LNTLMHYQVS DRSVVALVPK QTSSYNIPAS ASISRTSISR
YDSSFRYTGS PDSLRSRVPM ITPDLESGVK VWHLVKNHDH GDQKEGDRGS KMVSEIYLTR
LLATKGTLQK FVDDLFETLF STVHRGSALP LAIKYMFDFL DEQADRHSIH DTDVRHTWKS
NCLPLRFWVN VIKNPQFVFD IHKGSITDAC LSVVAQTFMD SCSTSEHRLG KDSPSNKLLY
AKDIPSYKNW VERYYADIAK LPAISDQDMN AYLAEQSRLH ATEFNMLSAL NEIYSYVSKY
SEELIGALEQ DEQARRQRLA YKVEHLINAM SIES
