SEM6A_MOUSE
ID SEM6A_MOUSE Reviewed; 1031 AA.
AC O35464; Q6P5A8; Q6PCN9; Q9EQ71;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Semaphorin-6A;
DE AltName: Full=Semaphorin Q;
DE Short=Sema Q;
DE AltName: Full=Semaphorin VIA;
DE Short=Sema VIA;
DE AltName: Full=Semaphorin-6A-1;
DE Short=SEMA6A-1;
DE Flags: Precursor;
GN Name=Sema6a; Synonyms=Semaq;
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 2), AND INTERACTION WITH EVL.
RC TISSUE=Brain;
RX PubMed=10993894; DOI=10.1074/jbc.m006316200;
RA Klostermann A., Lutz B., Gertler F., Behl C.;
RT "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
RT 1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like
RT protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
RL J. Biol. Chem. 275:39647-39653(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [MRNA] OF 1-888 (ISOFORM 1).
RX PubMed=9204478; DOI=10.1006/mcne.1997.0607;
RA Zhou L., White F.A., Lentz S.I., Wright D.E., Fisher D.A., Snider W.D.;
RT "Cloning and expression of a novel murine semaphorin with structural
RT similarity to insect semaphorin I.";
RL Mol. Cell. Neurosci. 9:26-41(1997).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16205717; DOI=10.1038/nn1555;
RA Kerjan G., Dolan J., Haumaitre C., Schneider-Maunoury S., Fujisawa H.,
RA Mitchell K.J., Chedotal A.;
RT "The transmembrane semaphorin Sema6A controls cerebellar granule cell
RT migration.";
RL Nat. Neurosci. 8:1516-1524(2005).
RN [5]
RP FUNCTION.
RX PubMed=19063725; DOI=10.1186/1749-8104-3-34;
RA Runker A.E., Little G.E., Suto F., Fujisawa H., Mitchell K.J.;
RT "Semaphorin-6A controls guidance of corticospinal tract axons at multiple
RT choice points.";
RL Neural Dev. 3:34-34(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-571 IN COMPLEX WITH PLXNA2,
RP FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-65; ASN-282 AND ASN-434, DISULFIDE
RP BONDS, AND MUTAGENESIS OF LEU-191 AND ILE-322.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-570 IN COMPLEX WITH PLXNA2,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-282 AND
RP ASN-434, DISULFIDE BONDS, AND MUTAGENESIS OF HIS-212; LYS-393 AND MET-415.
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: Cell surface receptor for PLXNA2 that plays an important role
CC in cell-cell signaling. Required for normal granule cell migration in
CC the developing cerebellum. Promotes reorganization of the actin
CC cytoskeleton and plays an important role in axon guidance in the
CC developing central nervous system. Can act as repulsive axon guidance
CC cue. Has repulsive action towards migrating granular neurons. May play
CC a role in channeling sympathetic axons into the sympathetic chains and
CC controlling the temporal sequence of sympathetic target innervation.
CC {ECO:0000269|PubMed:16205717, ECO:0000269|PubMed:19063725,
CC ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}.
CC -!- SUBUNIT: Active as a homodimer or oligomer. The SEMA6A homodimer
CC interacts with a PLXNA2 homodimer, giving rise to a heterotetramer.
CC Interacts with EVL. {ECO:0000269|PubMed:10993894,
CC ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}.
CC -!- INTERACTION:
CC O35464; Q80UG2: Plxna4; NbExp=3; IntAct=EBI-8057848, EBI-8057809;
CC O35464-1; P70207: Plxna2; NbExp=5; IntAct=EBI-15880936, EBI-771272;
CC O35464-1; O35464-1: Sema6a; NbExp=9; IntAct=EBI-15880936, EBI-15880936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20881961};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:20881961}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O35464-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35464-2; Sequence=VSP_012097;
CC Name=3;
CC IsoId=O35464-3; Sequence=VSP_012098;
CC -!- TISSUE SPECIFICITY: Particularly high levels in spinal cord,
CC cerebellum, metencephalon, superior and inferior colliculus,
CC diencephalon, olfactory bulb and eye. {ECO:0000269|PubMed:16205717}.
CC -!- DEVELOPMENTAL STAGE: Temporally and spatially regulated during
CC development.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and
CC fertile, and do not show any major behavioral defects. In developing
CC cerebellum, migration of granule cells is impaired. Granule cells can
CC form normal cell processes, but the movement of the nucleus seems to be
CC impaired. {ECO:0000269|PubMed:16205717}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AF288666; AAG29494.1; -; mRNA.
DR EMBL; BC059238; AAH59238.1; -; mRNA.
DR EMBL; BC062979; AAH62979.1; -; mRNA.
DR EMBL; AF030430; AAB86408.1; -; mRNA.
DR CCDS; CCDS37813.1; -. [O35464-1]
DR CCDS; CCDS79642.1; -. [O35464-3]
DR RefSeq; NP_001298026.1; NM_001311097.1. [O35464-3]
DR RefSeq; NP_061214.2; NM_018744.2. [O35464-1]
DR PDB; 3AFC; X-ray; 2.50 A; A/B=19-570.
DR PDB; 3AL8; X-ray; 3.60 A; A=19-570.
DR PDB; 3OKW; X-ray; 2.30 A; A/B=19-571.
DR PDB; 3OKY; X-ray; 2.20 A; B=19-571.
DR PDBsum; 3AFC; -.
DR PDBsum; 3AL8; -.
DR PDBsum; 3OKW; -.
DR PDBsum; 3OKY; -.
DR AlphaFoldDB; O35464; -.
DR SMR; O35464; -.
DR BioGRID; 203173; 7.
DR DIP; DIP-59220N; -.
DR ELM; O35464; -.
DR IntAct; O35464; 2.
DR MINT; O35464; -.
DR STRING; 10090.ENSMUSP00000019791; -.
DR GlyConnect; 2701; 1 N-Linked glycan (1 site).
DR GlyGen; O35464; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O35464; -.
DR PhosphoSitePlus; O35464; -.
DR MaxQB; O35464; -.
DR PaxDb; O35464; -.
DR PRIDE; O35464; -.
DR ProteomicsDB; 256773; -. [O35464-1]
DR ProteomicsDB; 256774; -. [O35464-2]
DR ProteomicsDB; 256775; -. [O35464-3]
DR Antibodypedia; 25481; 323 antibodies from 30 providers.
DR DNASU; 20358; -.
DR Ensembl; ENSMUST00000019791; ENSMUSP00000019791; ENSMUSG00000019647. [O35464-1]
DR Ensembl; ENSMUST00000076043; ENSMUSP00000075420; ENSMUSG00000019647. [O35464-3]
DR Ensembl; ENSMUST00000156422; ENSMUSP00000121442; ENSMUSG00000019647. [O35464-1]
DR GeneID; 20358; -.
DR KEGG; mmu:20358; -.
DR UCSC; uc008ewa.1; mouse. [O35464-1]
DR UCSC; uc008ewb.1; mouse. [O35464-3]
DR CTD; 57556; -.
DR MGI; MGI:1203727; Sema6a.
DR VEuPathDB; HostDB:ENSMUSG00000019647; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000156565; -.
DR HOGENOM; CLU_009051_2_0_1; -.
DR InParanoid; O35464; -.
DR OMA; KDMPPMA; -.
DR PhylomeDB; O35464; -.
DR TreeFam; TF316102; -.
DR BioGRID-ORCS; 20358; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Sema6a; mouse.
DR EvolutionaryTrace; O35464; -.
DR PRO; PR:O35464; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O35464; protein.
DR Bgee; ENSMUSG00000019647; Expressed in embryonic post-anal tail and 251 other tissues.
DR ExpressionAtlas; O35464; baseline and differential.
DR Genevisible; O35464; MM.
DR GO; GO:0030424; C:axon; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030215; F:semaphorin receptor binding; IGI:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0106089; P:negative regulation of cell adhesion involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1031
FT /note="Semaphorin-6A"
FT /id="PRO_0000032340"
FT TOPO_DOM 19..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..1031
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..512
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 754..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2E6"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2E6"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20877282"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20877282,
FT ECO:0000269|PubMed:20881961"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20877282,
FT ECO:0000269|PubMed:20881961"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..117
FT DISULFID 135..144
FT DISULFID 258..369
FT DISULFID 283..328
FT DISULFID 477..506
FT DISULFID 515..533
FT DISULFID 521..568
FT DISULFID 525..542
FT VAR_SEQ 439..464
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10993894"
FT /id="VSP_012097"
FT VAR_SEQ 577..631
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012098"
FT MUTAGEN 191
FT /note="L->R: Strongly reduced affinity for PLXNA2."
FT /evidence="ECO:0000269|PubMed:20877282"
FT MUTAGEN 212
FT /note="H->N: Strongly reduced affinity for PLXNA2."
FT /evidence="ECO:0000269|PubMed:20881961"
FT MUTAGEN 322
FT /note="I->E: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:20877282"
FT MUTAGEN 393
FT /note="K->E: Strongly reduced affinity for PLXNA2."
FT /evidence="ECO:0000269|PubMed:20881961"
FT MUTAGEN 415
FT /note="M->C: Formation of disulfide-linked homodimer."
FT /evidence="ECO:0000269|PubMed:20881961"
FT CONFLICT 172
FT /note="A -> V (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="L -> P (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="N -> D (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="S -> N (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="Q -> R (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 703..704
FT /note="TK -> SE (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="P -> S (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="Q -> E (in Ref. 3; AAB86408)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="I -> T (in Ref. 1; AAG29494)"
FT /evidence="ECO:0000305"
FT CONFLICT 863..888
FT /note="KSPNHGVNLVENLDSLPPKVPQREAS -> ESSPYVLKQFSEAFNRQGIILS
FT VAVE (in Ref. 3; AAB86408)"
FT /evidence="ECO:0000305"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:3OKW"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 435..442
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 445..452
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:3AFC"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 507..512
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:3OKY"
FT HELIX 522..527
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:3OKY"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:3OKY"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:3OKW"
SQ SEQUENCE 1031 AA; 114433 MW; 38565A81A4DA3BDB CRC64;
MRPAALLLCL TLLHCAGAGF PEDSEPISIS HGNYTKQYPV FVGHKPGRNT TQRHRLDIQM
IMIMNRTLYV AARDHIYTVD IDTSHTEEIY CSKKLTWKSR QADVDTCRMK GKHKDECHNF
IKVLLKKNDD TLFVCGTNAF NPSCRNYRVD TLETFGDEFS GMARCPYDAK HANIALFADG
KLYSATVTDF LAIDAVIYRS LGDSPTLRTV KHDSKWLKEP YFVQAVDYGD YIYFFFREIA
VEYNTMGKVV FPRVAQVCKN DMGGSQRVLE KQWTSFLKAR LNCSVPGDSH FYFNILQAVT
DVIRINGRDV VLATFSTPYN SIPGSAVCAY DMLDIANVFT GRFKEQKSPD STWTPVPDER
VPKPRPGCCA GSSSLEKYAT SNEFPDDTLN FIKTHPLMDE AVPSIINRPW FLRTMVRYRL
TKIAVDNAAG PYQNHTVVFL GSEKGIILKF LARIGSSGFL NGSLFLEEMN VYNPEKCSYD
GVEDKRIMGM QLDRASGSLY VAFSTCVIKV PLGRCERHGK CKKTCIASRD PYCGWVRESG
SCAHLSPLSR LTFEQDIERG NTDGLGDCHN SFVALNGHAS SLYPSTTTSD SASRDGYESR
GGMLDWNDLL EAPGSTDPLG AVSSHNHQDK KGVIRESYLK SNDQLVPVTL LAIAVILAFV
MGAVFSGIIV YCVCDHRRKD VAVVQRKEKE LTHSRRGSMS SVTKLSGLFG DTQSKDPKPE
AILTPLMHNG KLATPSNTAK MLIKADQHHL DLTALPTPES TPTLQQKRKP NRGSREWERN
QNIINACTKD MPPMGSPVIP TDLPLRASPS HIPSVVVLPI TQQGYQHEYV DQPKMSEVVA
QMALEDQAAT LEYKTIKEHL SSKSPNHGVN LVENLDSLPP KVPQREASLG PPGTSLSQTG
LSKRLEMQHS SSYGLEYKRS YPTNSLTRSH QTTTLKRNNT NSSNSSHLSR NQSFGRGDNP
PPAPQRVDSI QVHSSQPSGQ AVTVSRQPSL NAYNSLTRSG LKRTPSLKPD VPPKPSFAPL
STSMKPNDAC T
