NRG_DROME
ID NRG_DROME Reviewed; 1302 AA.
AC P20241; A4V452; O61541; O61542; Q1WWD5; Q24414; Q24415; Q95U64; Q9V3X0;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Neuroglian;
DE Flags: Precursor;
GN Name=Nrg; ORFNames=CG1634;
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 A), AND PROTEIN SEQUENCE OF 24-41 AND
RP 737-751.
RX PubMed=2805067; DOI=10.1016/0092-8674(89)90029-9;
RA Bieber A.J., Snow P.M., Hortsch M., Patel N.H., Jacobs J.R., Traquina Z.R.,
RA Schilling J., Goodman C.S.;
RT "Drosophila neuroglian: a member of the immunoglobulin superfamily with
RT extensive homology to the vertebrate neural adhesion molecule L1.";
RL Cell 59:447-460(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS A AND
RP B).
RX PubMed=9666073; DOI=10.1016/s0378-1119(98)00273-x;
RA Zhao G., Hortsch M.;
RT "The analysis of genomic structures in the L1 family of cell adhesion
RT molecules provides no evidence for exon shuffling events after the
RT separation of arthropod and chordate lineages.";
RL Gene 215:47-55(1998).
RN [3]
RP SEQUENCE REVISION.
RA Hortsch M.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1088-1302.
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1182-1302 (ISOFORMS A AND B), FUNCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=1693086; DOI=10.1016/0896-6273(90)90196-m;
RA Hortsch M., Bieber A.J., Patel N.H., Goodman C.S.;
RT "Differential splicing generates a nervous system-specific form of
RT Drosophila neuroglian.";
RL Neuron 4:697-709(1990).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH NRG AND CONT.
RX PubMed=15459097; DOI=10.1242/dev.01372;
RA Faivre-Sarrailh C., Banerjee S., Li J., Hortsch M., Laval M., Bhat M.A.;
RT "Drosophila contactin, a homolog of vertebrate contactin, is required for
RT septate junction organization and paracellular barrier function.";
RL Development 131:4931-4942(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198 AND ASN-411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 610-814, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-652 AND ASN-683.
RX PubMed=7512815; DOI=10.1016/0896-6273(94)90326-3;
RA Huber A.H., Wang Y.-M.E., Bieber A.J., Bjorkman P.J.;
RT "Crystal structure of tandem type III fibronectin domains from Drosophila
RT neuroglian at 2.0 A.";
RL Neuron 12:717-731(1994).
CC -!- FUNCTION: The long isoform may play a role in neural and glial cell
CC adhesion in the developing embryo. The short isoform may be a more
CC general cell adhesion molecule involved in other tissues and imaginal
CC disk morphogenesis. Vital for embryonic development. Essential for
CC septate junctions. Septate junctions, which are the equivalent of
CC vertebrates tight junctions, are characterized by regular arrays of
CC transverse structures that span the intermembrane space and form a
CC physical barrier to diffusion. Required for the blood-brain barrier
CC formation. {ECO:0000269|PubMed:1693086}.
CC -!- SUBUNIT: Forms a complex with Nrx and Cont.
CC {ECO:0000269|PubMed:15459097}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell junction, tight junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=180 kDa form;
CC IsoId=P20241-1; Sequence=Displayed;
CC Name=A; Synonyms=C, 167 kDa form;
CC IsoId=P20241-2; Sequence=VSP_002601, VSP_002602;
CC -!- TISSUE SPECIFICITY: Long isoform is restricted to surface of neurons
CC and glia in the developing nervous system and the short isoform to
CC other non-neuronal tissues. {ECO:0000269|PubMed:1693086}.
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DR EMBL; M28231; AAA28728.2; -; mRNA.
DR EMBL; AF050085; AAC28613.2; -; Genomic_DNA.
DR EMBL; AF050084; AAC28613.2; JOINED; Genomic_DNA.
DR EMBL; AF050085; AAC28614.2; -; Genomic_DNA.
DR EMBL; AF050084; AAC28614.2; JOINED; Genomic_DNA.
DR EMBL; AE014298; AAF46387.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09236.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65287.1; -; Genomic_DNA.
DR EMBL; AY058284; AAL13513.1; -; mRNA.
DR EMBL; BT024971; ABE01201.1; -; mRNA.
DR EMBL; X76243; CAA53822.1; -; mRNA.
DR EMBL; X76244; CAA53823.1; -; mRNA.
DR PIR; A32579; A32579.
DR RefSeq; NP_001162704.1; NM_001169233.2. [P20241-2]
DR RefSeq; NP_001162705.1; NM_001169234.3. [P20241-1]
DR RefSeq; NP_001162706.1; NM_001169235.1. [P20241-2]
DR RefSeq; NP_001259336.1; NM_001272407.2. [P20241-2]
DR RefSeq; NP_001259337.1; NM_001272408.1. [P20241-1]
DR RefSeq; NP_511090.1; NM_078535.3. [P20241-2]
DR RefSeq; NP_727274.1; NM_167160.2. [P20241-1]
DR RefSeq; NP_996380.1; NM_206657.4. [P20241-2]
DR PDB; 1CFB; X-ray; 2.00 A; A=610-814.
DR PDBsum; 1CFB; -.
DR AlphaFoldDB; P20241; -.
DR SMR; P20241; -.
DR BioGRID; 58251; 28.
DR DIP; DIP-22412N; -.
DR IntAct; P20241; 79.
DR STRING; 7227.FBpp0297081; -.
DR GlyGen; P20241; 8 sites.
DR iPTMnet; P20241; -.
DR PaxDb; P20241; -.
DR DNASU; 31792; -.
DR EnsemblMetazoa; FBtr0071207; FBpp0071154; FBgn0264975. [P20241-2]
DR EnsemblMetazoa; FBtr0071208; FBpp0071155; FBgn0264975. [P20241-1]
DR EnsemblMetazoa; FBtr0071209; FBpp0089326; FBgn0264975. [P20241-2]
DR EnsemblMetazoa; FBtr0301762; FBpp0290976; FBgn0264975. [P20241-2]
DR EnsemblMetazoa; FBtr0301763; FBpp0290977; FBgn0264975. [P20241-1]
DR EnsemblMetazoa; FBtr0301764; FBpp0290978; FBgn0264975. [P20241-2]
DR EnsemblMetazoa; FBtr0333522; FBpp0305702; FBgn0264975. [P20241-2]
DR EnsemblMetazoa; FBtr0333523; FBpp0305703; FBgn0264975. [P20241-1]
DR GeneID; 31792; -.
DR KEGG; dme:Dmel_CG1634; -.
DR UCSC; CG1634-RC; d. melanogaster.
DR CTD; 31792; -.
DR FlyBase; FBgn0264975; Nrg.
DR VEuPathDB; VectorBase:FBgn0264975; -.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; P20241; -.
DR OMA; AGRGDYP; -.
DR PhylomeDB; P20241; -.
DR BioGRID-ORCS; 31792; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Nrg; fly.
DR EvolutionaryTrace; P20241; -.
DR GenomeRNAi; 31792; -.
DR PRO; PR:P20241; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0264975; Expressed in oviduct (Drosophila) and 44 other tissues.
DR ExpressionAtlas; P20241; baseline and differential.
DR Genevisible; P20241; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0030175; C:filopodium; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IMP:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005919; C:pleated septate junction; IDA:FlyBase.
DR GO; GO:0005918; C:septate junction; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:FlyBase.
DR GO; GO:0008366; P:axon ensheathment; IMP:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:FlyBase.
DR GO; GO:0048036; P:central complex development; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0008050; P:female courtship behavior; IMP:FlyBase.
DR GO; GO:0007560; P:imaginal disc morphogenesis; IMP:UniProtKB.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0021682; P:nerve maturation; IMP:FlyBase.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0045924; P:regulation of female receptivity; IMP:FlyBase.
DR GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 11.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 2.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Developmental protein; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2805067"
FT CHAIN 24..1302
FT /note="Neuroglian"
FT /id="PRO_0000015055"
FT TOPO_DOM 24..1138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1139..1154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1155..1302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..133
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..225
FT /note="Ig-like C2-type 2"
FT DOMAIN 245..330
FT /note="Ig-like C2-type 3"
FT DOMAIN 339..426
FT /note="Ig-like C2-type 4"
FT DOMAIN 432..524
FT /note="Ig-like C2-type 5"
FT DOMAIN 521..610
FT /note="Ig-like C2-type 6"
FT DOMAIN 614..711
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 716..813
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 818..915
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 916..1017
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1021..1119
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1172..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7512815"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7512815"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..212
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 268..317
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 360..410
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 625..706
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:7512815"
FT VAR_SEQ 1224..1239
FT /note="QFTEDGSFIGQYVPGK -> MNEDGSFIGQYGRKGL (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1693086, ECO:0000303|PubMed:2805067"
FT /id="VSP_002601"
FT VAR_SEQ 1240..1302
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1693086, ECO:0000303|PubMed:2805067"
FT /id="VSP_002602"
FT CONFLICT 85..86
FT /note="NR -> KP (in Ref. 2; AAC28613/AAC28614)"
FT /evidence="ECO:0000305"
FT CONFLICT 1232
FT /note="Missing (in Ref. 7; ABE01201)"
FT /evidence="ECO:0000305"
FT CONFLICT 1282
FT /note="Missing (in Ref. 8; CAA53823)"
FT /evidence="ECO:0000305"
FT CONFLICT 1299
FT /note="A -> V (in Ref. 7; ABE01201)"
FT /evidence="ECO:0000305"
FT STRAND 619..625
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 627..635
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 646..656
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 661..668
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 672..677
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 680..692
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 730..733
FT /evidence="ECO:0007829|PDB:1CFB"
FT HELIX 739..741
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 748..757
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 763..767
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 785..794
FT /evidence="ECO:0007829|PDB:1CFB"
FT STRAND 806..812
FT /evidence="ECO:0007829|PDB:1CFB"
SQ SEQUENCE 1302 AA; 143618 MW; 59BD9DF286756F1A CRC64;
MWRQSTILAA LLVALLCAGS AESKGNRPPR ITKQPAPGEL LFKVAQQNKE SDNPFIIECE
ADGQPEPEYS WIKNGKKFDW QAYDNRMLRQ PGRGTLVITI PKDEDRGHYQ CFASNEFGTA
TSNSVYVRKA ELNAFKDEAA KTLEAVEGEP FMLKCAAPDG FPSPTVNWMI QESIDGSIKS
INNSRMTLDP EGNLWFSNVT REDASSDFYY ACSATSVFRS EYKIGNKVLL DVKQMGVSAS
QNKHPPVRQY VSRRQSLALR GKRMELFCIY GGTPLPQTVW SKDGQRIQWS DRITQGHYGK
SLVIRQTNFD DAGTYTCDVS NGVGNAQSFS IILNVNSVPY FTKEPEIATA AEDEEVVFEC
RAAGVPEPKI SWIHNGKPIE QSTPNPRRTV TDNTIRIINL VKGDTGNYGC NATNSLGYVY
KDVYLNVQAE PPTISEAPAA VSTVDGRNVT IKCRVNGSPK PLVKWLRASN WLTGGRYNVQ
ANGDLEIQDV TFSDAGKYTC YAQNKFGEIQ ADGSLVVKEH TRITQEPQNY EVAAGQSATF
RCNEAHDDTL EIEIDWWKDG QSIDFEAQPR FVKTNDNSLT IAKTMELDSG EYTCVARTRL
DEATARANLI VQDVPNAPKL TGITCQADKA EIHWEQQGDN RSPILHYTIQ FNTSFTPASW
DAAYEKVPNT DSSFVVQMSP WANYTFRVIA FNKIGASPPS AHSDSCTTQP DVPFKNPDNV
VGQGTEPNNL VISWTPMPEI EHNAPNFHYY VSWKRDIPAA AWENNNIFDW RQNNIVIADQ
PTFVKYLIKV VAINDRGESN VAAEEVVGYS GEDRPLDAPT NFTMRQITSS TSGYMAWTPV
SEESVRGHFK GYKIQTWTEN EGEEGLREIH VKGDTHNALV TQFKPDSKNY ARILAYNGRF
NGPPSAVIDF DTPEGVPSPV QGLDAYPLGS SAFMLHWKKP LYPNGKLTGY KIYYEEVKES
YVGERREYDP HITDPRVTRM KMAGLKPNSK YRISITATTK MGEGSEHYIE KTTLKDAVNV
APATPSFSWE QLPSDNGLAK FRINWLPSTE GHPGTHFFTM HRIKGETQWI RENEEKNSDY
QEVGGLDPET AYEFRVVSVD GHFNTESATQ EIDTNTVEGP IMVANETVAN AGWFIGMMLA
LAFIIILFII ICIIRRNRGG KYDVHDRELA NGRRDYPEEG GFHEYSQPLD NKSAGRQSVS
SANKPGVESD TDSMAEYGDG DTGQFTEDGS FIGQYVPGKL QPPVSPQPLN NSAAAHQAAP
TAGGSGAAGS AAAAGASGGA SSAGGAAASN GGAAAGAVAT YV
