SERR_DROME
ID SERR_DROME Reviewed; 1404 AA.
AC P18168; Q9VB65;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein serrate;
DE AltName: Full=Protein beaded;
DE Flags: Precursor;
GN Name=Ser; Synonyms=Bd; ORFNames=CG6127;
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].
RX PubMed=2125287; DOI=10.1101/gad.4.12a.2188;
RA Fleming R.J., Scottgale T.N., Diederich R.J., Artavanis-Tsakonas S.;
RT "The gene Serrate encodes a putative EGF-like transmembrane protein
RT essential for proper ectodermal development in Drosophila melanogaster.";
RL Genes Dev. 4:2188-2201(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=1840519; DOI=10.1242/dev.111.3.749;
RA Thomas U., Speicher S.A., Knust E.;
RT "The Drosophila gene Serrate encodes an EGF-like transmembrane protein with
RT a complex expression pattern in embryos and wing discs.";
RL Development 111:749-761(1991).
RN [3]
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 [4]
RP GENOME REANNOTATION.
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 [5]
RP INTERACTION WITH MIB.
RX PubMed=15829515; DOI=10.1242/dev.01825;
RA Lai E.C., Roegiers F., Qin X., Jan Y.N., Rubin G.M.;
RT "The ubiquitin ligase Drosophila Mind bomb promotes Notch signaling by
RT regulating the localization and activity of Serrate and Delta.";
RL Development 132:2319-2332(2005).
RN [6]
RP PROBABLE UBIQUITINATION.
RX PubMed=15760269; DOI=10.1371/journal.pbio.0030096;
RA Le Borgne R., Remaud S., Hamel S., Schweisguth F.;
RT "Two distinct E3 ubiquitin ligases have complementary functions in the
RT regulation of delta and serrate signaling in Drosophila.";
RL PLoS Biol. 3:688-696(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Acts as a ligand for Notch (N) receptor. Essential for proper
CC ectodermal development. Serrate represents an element in a network of
CC interacting molecules operating at the cell surface during the
CC differentiation of certain tissues.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Restricted exclusively to cells of ectodermal
CC origin.
CC -!- PTM: Ubiquitinated by mind-bomb, leading to its endocytosis and
CC subsequent degradation. {ECO:0000305}.
CC -!- MISCELLANEOUS: Separation of neuroblasts from the ectoderm into the
CC inner part of embryo is one of the first steps of CNS development in
CC insects, this process is under control of the neurogenic genes.
CC -!- MISCELLANEOUS: Notch and Serrate may interact at the protein level, it
CC is conceivable that the Serrate and Delta proteins may compete for
CC binding with the Notch protein.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF56678.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M35759; AAA28938.1; -; mRNA.
DR EMBL; X56811; CAA40148.1; -; mRNA.
DR EMBL; AE014297; AAF56678.2; ALT_INIT; Genomic_DNA.
DR PIR; S16148; S16148.
DR RefSeq; NP_001287558.1; NM_001300629.1.
DR RefSeq; NP_524527.3; NM_079803.3.
DR PDB; 7ALT; X-ray; 2.03 A; A/B=80-349.
DR PDBsum; 7ALT; -.
DR AlphaFoldDB; P18168; -.
DR SMR; P18168; -.
DR BioGRID; 68163; 36.
DR IntAct; P18168; 2.
DR MINT; P18168; -.
DR STRING; 7227.FBpp0084498; -.
DR GlyGen; P18168; 13 sites.
DR iPTMnet; P18168; -.
DR PaxDb; P18168; -.
DR PRIDE; P18168; -.
DR EnsemblMetazoa; FBtr0085128; FBpp0084498; FBgn0004197.
DR GeneID; 43275; -.
DR KEGG; dme:Dmel_CG6127; -.
DR CTD; 107980446; -.
DR FlyBase; FBgn0004197; Ser.
DR VEuPathDB; VectorBase:FBgn0004197; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000170138; -.
DR HOGENOM; CLU_004732_0_0_1; -.
DR InParanoid; P18168; -.
DR PhylomeDB; P18168; -.
DR SignaLink; P18168; -.
DR BioGRID-ORCS; 43275; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43275; -.
DR PRO; PR:P18168; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004197; Expressed in wing disc and 26 other tissues.
DR ExpressionAtlas; P18168; baseline and differential.
DR Genevisible; P18168; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0030673; C:axolemma; IDA:FlyBase.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043208; F:glycosphingolipid binding; IDA:FlyBase.
DR GO; GO:0005112; F:Notch binding; IDA:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0042688; P:crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0035214; P:eye-antennal disc development; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IGI:FlyBase.
DR GO; GO:0014009; P:glial cell proliferation; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IEP:FlyBase.
DR GO; GO:0007436; P:larval salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
DR GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IMP:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 6.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR02059; JAGGEDFAMILY.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..79
FT /evidence="ECO:0000255"
FT CHAIN 80..1404
FT /note="Protein serrate"
FT /id="PRO_0000007718"
FT TOPO_DOM 80..1219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1246..1404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 235..279
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 280..313
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 311..345
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 347..385
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 387..485
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 487..523
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 525..605
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 607..642
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 644..680
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 682..717
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 719..793
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 795..831
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 833..873
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 875..911
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 913..949
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 961
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 237..246
FT /evidence="ECO:0000250"
FT DISULFID 250..262
FT /evidence="ECO:0000250"
FT DISULFID 270..279
FT /evidence="ECO:0000250"
FT DISULFID 284..295
FT /evidence="ECO:0000250"
FT DISULFID 288..301
FT /evidence="ECO:0000250"
FT DISULFID 303..312
FT /evidence="ECO:0000250"
FT DISULFID 315..326
FT /evidence="ECO:0000250"
FT DISULFID 321..333
FT /evidence="ECO:0000250"
FT DISULFID 335..344
FT /evidence="ECO:0000250"
FT DISULFID 351..363
FT /evidence="ECO:0000250"
FT DISULFID 357..373
FT /evidence="ECO:0000250"
FT DISULFID 375..384
FT /evidence="ECO:0000250"
FT DISULFID 391..402
FT /evidence="ECO:0000250"
FT DISULFID 396..473
FT /evidence="ECO:0000250"
FT DISULFID 475..484
FT /evidence="ECO:0000250"
FT DISULFID 491..502
FT /evidence="ECO:0000250"
FT DISULFID 496..511
FT /evidence="ECO:0000250"
FT DISULFID 513..522
FT /evidence="ECO:0000250"
FT DISULFID 529..584
FT /evidence="ECO:0000250"
FT DISULFID 578..593
FT /evidence="ECO:0000250"
FT DISULFID 595..604
FT /evidence="ECO:0000250"
FT DISULFID 611..621
FT /evidence="ECO:0000250"
FT DISULFID 615..630
FT /evidence="ECO:0000250"
FT DISULFID 632..641
FT /evidence="ECO:0000250"
FT DISULFID 648..659
FT /evidence="ECO:0000250"
FT DISULFID 653..668
FT /evidence="ECO:0000250"
FT DISULFID 670..679
FT /evidence="ECO:0000250"
FT DISULFID 686..696
FT /evidence="ECO:0000250"
FT DISULFID 691..705
FT /evidence="ECO:0000250"
FT DISULFID 707..716
FT /evidence="ECO:0000250"
FT DISULFID 766..781
FT /evidence="ECO:0000250"
FT DISULFID 783..792
FT /evidence="ECO:0000250"
FT DISULFID 799..810
FT /evidence="ECO:0000250"
FT DISULFID 804..819
FT /evidence="ECO:0000250"
FT DISULFID 821..830
FT /evidence="ECO:0000250"
FT DISULFID 837..848
FT /evidence="ECO:0000250"
FT DISULFID 842..861
FT /evidence="ECO:0000250"
FT DISULFID 863..872
FT /evidence="ECO:0000250"
FT DISULFID 879..890
FT /evidence="ECO:0000250"
FT DISULFID 884..899
FT /evidence="ECO:0000250"
FT DISULFID 901..910
FT /evidence="ECO:0000250"
FT DISULFID 917..928
FT /evidence="ECO:0000250"
FT DISULFID 922..937
FT /evidence="ECO:0000250"
FT DISULFID 939..948
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="S -> SSLSS (in Ref. 2; CAA40148)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="A -> P (in Ref. 2; CAA40148)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="P -> S (in Ref. 1; AAA28938 and 2; CAA40148)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="K -> T (in Ref. 1; AAA28938 and 2; CAA40148)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="F -> S (in Ref. 1; AAA28938 and 2; CAA40148)"
FT /evidence="ECO:0000305"
FT CONFLICT 1348
FT /note="S -> T (in Ref. 2; CAA40148)"
FT /evidence="ECO:0000305"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:7ALT"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:7ALT"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:7ALT"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:7ALT"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:7ALT"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:7ALT"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7ALT"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:7ALT"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:7ALT"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:7ALT"
SQ SEQUENCE 1404 AA; 150344 MW; E988604001DAAC84 CRC64;
MFRKHFRRKP ATSSSLESTI ESADSLGMSK KTATKRQRPR HRVPKIATLP STIRDCRSLK
SACNLIALIL ILLVHKISAA GNFELEILEI SNTNSHLLNG YCCGMPAELR ATKTIGCSPC
TTAFRLCLKE YQTTEQGASI STGCSFGNAT TKILGGSSFV LSDPGVGAIV LPFTFRWTKS
FTLILQALDM YNTSYPDAER LIEETSYSGV ILPSPEWKTL DHIGRNARIT YRVRVQCAVT
YYNTTCTTFC RPRDDQFGHY ACGSEGQKLC LNGWQGVNCE EAICKAGCDP VHGKCDRPGE
CECRPGWRGP LCNECMVYPG CKHGSCNGSA WKCVCDTNWG GILCDQDLNF CGTHEPCKHG
GTCENTAPDK YRCTCAEGLS GEQCEIVEHP CATRPCRNGG TCTLKTSNRT QAQVYRTSHG
RSNMGRPVRR SSSMRSLDHL RPEGQALNGS SSPGLVSLGS LQLQQQLAPD FTCDCAAGWT
GPTCEINIDE CAGGPCEHGG TCIDLIGGFR CECPPEWHGD VCQVDVNECE APHSAGIAAN
ALLTTTATAI IGSNLSSTAL LAALTSAVAS TSLAIGPCIN AKECRNQPGS FACICKEGWG
GVTCAENLDD CVGQCRNGAT CIDLVNDYRC ACASGFKGRD CETDIDECAT SPCRNGGECV
DMVGKFNCIC PLGYSGSLCE EAKENCTPSP CLEGHCLNTP EGYYCHCPPD RAGKHCEQLR
PLCSQPPCNE GCFANVSLAT SATTTTTTTT TATTTRKMAK PSGLPCSGHG SCEMSDVGTF
CKCHVGHTGT FCEHNLNECS PNPCRNGGIC LDGDGDFTCE CMSGWTGKRC SERATGCYAG
QCQNGGTCMP GAPDKALQPH CRCAPGWTGL FCAEAIDQCR GQPCHNGGTC ESGAGWFRCV
CAQGFSGPDC RINVNECSPQ PCQGGATCID GIGGYSCICP PGRHGLRCEI LLSDPKSACQ
NASNTISPYT ALNRSQNWLD IALTGRTEDD ENCNACVCEN GTSRCTNLWC GLPNCYKVDP
LSKSSNLSGV CKQHEVCVPA LSETCLSSPC NVRGDCRALE PSRRVAPPRL PAKSSCWPNQ
AVVNENCARL TILLALERVG KGASVEGLCS LVRVLLAAQL IKKPASTFGQ DPGMLMVLCD
LKTGTNDTVE LTVSSSKLND PQLPVAVGLL GELLSFRQLN GIQRRKELEL QHAKLAALTS
IVEVKLETAR VADGSGHSLL IGVLCGVFIV LVGFSVFISL YWKQRLAYRT SSGMNLTPSL
DALRHEEEKS NNLQNEENLR RYTNPLKGST SSLRAATGME LSLNPAPELA ASAASSSALH
RSQPLFPPCD FERELDSSTG LKQAHKRSSQ ILLHKTQNSD MRKNTVGSLD SPRKDFGKRS
INCKSMPPSS GDEGSDVLAT TVMV
