SEM2A_DROME
ID SEM2A_DROME Reviewed; 724 AA.
AC Q24323; Q0E954; Q6NN47; Q7KRC9; Q8MLF1; Q9V7Q7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Semaphorin-2A {ECO:0000312|FlyBase:FBgn0011260};
DE AltName: Full=Semaphorin-II {ECO:0000303|PubMed:8269517};
DE Short=Sema II {ECO:0000303|PubMed:8269517};
DE Flags: Precursor;
GN Name=Sema2a {ECO:0000312|FlyBase:FBgn0011260};
GN Synonyms=Sema-2a {ECO:0000303|PubMed:16672342};
GN ORFNames=CG4700 {ECO:0000312|FlyBase:FBgn0011260};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8269517; DOI=10.1016/0092-8674(93)90625-z;
RA Kolodkin A.L., Matthes D.J., Goodman C.S.;
RT "The semaphorin genes encode a family of transmembrane and secreted growth
RT cone guidance molecules.";
RL Cell 75:1389-1399(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH PLEXB.
RX PubMed=16672342; DOI=10.1242/dev.02380;
RA Ayoob J.C., Terman J.R., Kolodkin A.L.;
RT "Drosophila Plexin B is a Sema-2a receptor required for axon guidance.";
RL Development 133:2125-2135(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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).
CC -!- FUNCTION: Plays a role in growth cones guidance. Required for both
CC proper adult behavior and survival. Can function in vivo as a selective
CC target-derived signal that inhibits the formation of specific synaptic
CC terminal arbors. {ECO:0000269|PubMed:8269517}.
CC -!- SUBUNIT: Interacts with PlexB. {ECO:0000269|PubMed:16672342}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A; Synonyms=B;
CC IsoId=Q24323-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q24323-2; Sequence=VSP_016075;
CC Name=D;
CC IsoId=Q24323-3; Sequence=VSP_016076;
CC Name=E;
CC IsoId=Q24323-4; Sequence=VSP_016077;
CC -!- TISSUE SPECIFICITY: Transiently expressed by a single large muscle
CC during motoneuron outgrowth and synapse formation.
CC {ECO:0000269|PubMed:8269517}.
CC -!- DEVELOPMENTAL STAGE: Expression begins around stage 10 in weak
CC epidermal stripes. Nervous system expression is first detected around
CC stage 15 and at stage 16 appears to remain restricted to a small subset
CC of neurons. Beginning around stage 14, it is also expressed at a very
CC high level in a single ventral thoracic muscle fiber in segment T3. It
CC is also expressed in the embryonic gonads and in anterior sensory
CC organs, including the maxillary complex. {ECO:0000269|PubMed:8269517}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; L26083; AAC37187.1; -; mRNA.
DR EMBL; AE013599; AAF57989.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68500.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64837.1; -; Genomic_DNA.
DR EMBL; AY095026; AAM11354.1; -; mRNA.
DR EMBL; AY128437; AAM75030.1; -; mRNA.
DR EMBL; BT011447; AAR99105.1; -; mRNA.
DR PIR; C49423; C49423.
DR RefSeq; NP_477507.1; NM_058159.5. [Q24323-1]
DR RefSeq; NP_599130.1; NM_134303.4. [Q24323-1]
DR RefSeq; NP_725586.1; NM_166178.3. [Q24323-2]
DR RefSeq; NP_995856.2; NM_206134.2. [Q24323-1]
DR PDB; 6QP7; X-ray; 1.96 A; A/B=27-671.
DR PDBsum; 6QP7; -.
DR AlphaFoldDB; Q24323; -.
DR SMR; Q24323; -.
DR BioGRID; 62559; 23.
DR IntAct; Q24323; 56.
DR STRING; 7227.FBpp0086237; -.
DR GlyGen; Q24323; 10 sites.
DR iPTMnet; Q24323; -.
DR PaxDb; Q24323; -.
DR PRIDE; Q24323; -.
DR DNASU; 36846; -.
DR EnsemblMetazoa; FBtr0087088; FBpp0086236; FBgn0011260. [Q24323-2]
DR EnsemblMetazoa; FBtr0087089; FBpp0086237; FBgn0011260. [Q24323-1]
DR EnsemblMetazoa; FBtr0087090; FBpp0086238; FBgn0011260. [Q24323-1]
DR EnsemblMetazoa; FBtr0345339; FBpp0311494; FBgn0011260. [Q24323-1]
DR GeneID; 36846; -.
DR KEGG; dme:Dmel_CG4700; -.
DR CTD; 36846; -.
DR FlyBase; FBgn0011260; Sema2a.
DR VEuPathDB; VectorBase:FBgn0011260; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000172789; -.
DR InParanoid; Q24323; -.
DR OMA; GDYENTW; -.
DR PhylomeDB; Q24323; -.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-DME-399956; CRMPs in Sema3A signaling.
DR Reactome; R-DME-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-DME-416700; Other semaphorin interactions.
DR SignaLink; Q24323; -.
DR BioGRID-ORCS; 36846; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Sema-2a; fly.
DR GenomeRNAi; 36846; -.
DR PRO; PR:Q24323; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0011260; Expressed in wing disc and 32 other tissues.
DR ExpressionAtlas; Q24323; baseline and differential.
DR Genevisible; Q24323; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; ISS:FlyBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0070983; P:dendrite guidance; IGI:FlyBase.
DR GO; GO:0042756; P:drinking behavior; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0071678; P:olfactory bulb axon guidance; IMP:FlyBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR GO; GO:0097374; P:sensory neuron axon guidance; IMP:FlyBase.
DR GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR GO; GO:0007632; P:visual behavior; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
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; PF01403; Sema; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Neurogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..724
FT /note="Semaphorin-2A"
FT /id="PRO_0000032301"
FT DOMAIN 45..522
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 552..663
FT /note="Ig-like C2-type"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..129
FT /evidence="ECO:0000250"
FT DISULFID 291..399
FT /evidence="ECO:0000250"
FT DISULFID 315..358
FT /evidence="ECO:0000250"
FT DISULFID 525..541
FT /evidence="ECO:0000250"
FT DISULFID 535..550
FT /evidence="ECO:0000250"
FT DISULFID 590..647
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..55
FT /note="MSLLQLSPLLALLLLLCSSVSETAADYENTWNFYYERPCCTGNDQGNNNYGK
FT HGA -> MNGIHWLLFGSCLMLISQIEAVTEELSP (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_016075"
FT VAR_SEQ 103..125
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_016076"
FT VAR_SEQ 110..127
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:8269517"
FT /id="VSP_016077"
FT CONFLICT 105
FT /note="V -> A (in Ref. 1; AAC37187)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="P -> S (in Ref. 5; AAR99105)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="A -> G (in Ref. 1; AAC37187)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="S -> C (in Ref. 1; AAC37187)"
FT /evidence="ECO:0000305"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 125..129
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 362..370
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 440..450
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 455..464
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 480..490
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 504..507
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 525..528
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 575..581
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 586..593
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 603..609
FT /evidence="ECO:0007829|PDB:6QP7"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 621..627
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:6QP7"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 643..649
FT /evidence="ECO:0007829|PDB:6QP7"
FT STRAND 652..662
FT /evidence="ECO:0007829|PDB:6QP7"
SQ SEQUENCE 724 AA; 82998 MW; 600DB0AEA82E677E CRC64;
MSLLQLSPLL ALLLLLCSSV SETAADYENT WNFYYERPCC TGNDQGNNNY GKHGADHVRE
FNCGKLYYRT FHMNEDRDTL YVGAMDRVFR VNLQNISSSN CNRDVINLEP TRDDVVSCVS
KGKSQIFDCK NHVRVIQSMD QGDRLYVCGT NAHNPKDYVI YANLTHLPRS EYVIGVGLGI
AKCPYDPLDN STAIYVENGN PGGLPGLYSG TNAEFTKADT VIFRTDLYNT SAKRLEYKFK
RTLKYDSKWL DKPNFVGSFD IGEYVYFFFR ETAVEYINCG KAVYSRIARV CKKDVGGKNL
LAHNWATYLK ARLNCSISGE FPFYFNEIQS VYQLPSDKSR FFATFTTSTN GLIGSAVCSF
HINEIQAAFN GKFKEQSSSN SAWLPVLNSR VPEPRPGTCV NDTSNLPDTV LNFIRSHPLM
DKAVNHEHNN PVYYKRDLVF TKLVVDKIRI DILNQEYIVY YVGTNLGRIY KIVQYYRNGE
SLSKLLDIFE VAPNEAIQVM EISQTRKSLY IGTDHRIKQI DLAMCNRRYD NCFRCVRDPY
CGWDKEANTC RPYELDLLQD VANETSDICD SSVLKKKIVV TYGQSVHLGC FVKIPEVLKN
EQVTWYHHSK DKGRYEIRYS PTKYIETTER GLVVVSVNEA DGGRYDCHLG GSLLCSYNIT
VDAHRCTPPN KSNDYQKIYS DWCHEFEKYK TAMKSWEKKQ AQCSTRQNFS SNQHPNEIFR
KPNV
