CADN_DROME
ID CADN_DROME Reviewed; 3097 AA.
AC O15943; Q9VJB7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Neural-cadherin;
DE AltName: Full=Cadherin-N;
DE Short=dN-cadherin;
DE Flags: Precursor;
GN Name=CadN; ORFNames=CG7100;
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 D).
RC TISSUE=Embryo, and Head;
RX PubMed=9247265; DOI=10.1016/s0896-6273(00)80349-9;
RA Iwai Y., Usui T., Hirano S., Steward R., Takeichi M., Uemura T.;
RT "Axon patterning requires DN-cadherin, a novel neuronal adhesion receptor,
RT in the Drosophila embryonic CNS.";
RL Neuron 19:77-89(1997).
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 INTERACTION WITH ARM.
RX PubMed=9635189; DOI=10.1016/s0960-9822(98)70249-0;
RA Loureiro J., Peifer M.;
RT "Roles of Armadillo, a Drosophila catenin, during central nervous system
RT development.";
RL Curr. Biol. 8:622-632(1998).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types. May associate with arm neural isoform and
CC participate in the transmission of developmental information.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=D;
CC IsoId=O15943-1; Sequence=Displayed;
CC Name=A;
CC IsoId=O15943-2; Sequence=VSP_000667, VSP_000668;
CC Name=B;
CC IsoId=O15943-3; Sequence=VSP_000668;
CC Name=C;
CC IsoId=O15943-4; Sequence=VSP_000667, VSP_000668, VSP_000669;
CC Name=E;
CC IsoId=O15943-5; Sequence=VSP_000667;
CC Name=F;
CC IsoId=O15943-6; Sequence=VSP_000669;
CC Name=G;
CC IsoId=O15943-7; Sequence=VSP_000667, VSP_000669;
CC Name=H;
CC IsoId=O15943-8; Sequence=VSP_000668, VSP_000669;
CC -!- TISSUE SPECIFICITY: In the embryo, the protein first appears in the
CC mesoderm at stage 9 and is present in the myoblasts and muscle fibers
CC by stage 12 and stage 14, respectively. At stage 12 the protein is also
CC located in the axons of the entire CNS, but not in the glial cells. In
CC third instar larvae protein is expressed in the CNS neuropile,
CC photoreceptor axons and precursors of adult muscles.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB002397; BAA22151.1; -; mRNA.
DR EMBL; AE014134; AAF53635.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10992.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10993.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10994.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10995.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10996.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10997.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10998.1; -; Genomic_DNA.
DR PIR; T00021; T00021.
DR RefSeq; NP_724068.1; NM_165224.2. [O15943-8]
DR RefSeq; NP_724069.1; NM_165225.2. [O15943-3]
DR RefSeq; NP_724070.1; NM_165226.2. [O15943-6]
DR RefSeq; NP_724071.1; NM_165227.3. [O15943-1]
DR RefSeq; NP_724072.1; NM_165228.2. [O15943-4]
DR RefSeq; NP_724073.1; NM_165229.2. [O15943-2]
DR RefSeq; NP_724074.1; NM_165230.2. [O15943-7]
DR RefSeq; NP_724075.1; NM_165231.3. [O15943-5]
DR PDB; 3UBF; X-ray; 2.50 A; A=439-753.
DR PDB; 3UBG; X-ray; 2.50 A; A/B=439-753.
DR PDB; 3UBH; X-ray; 2.70 A; A=434-851.
DR PDBsum; 3UBF; -.
DR PDBsum; 3UBG; -.
DR PDBsum; 3UBH; -.
DR SMR; O15943; -.
DR BioGRID; 61066; 18.
DR IntAct; O15943; 8.
DR STRING; 7227.FBpp0099721; -.
DR GlyGen; O15943; 6 sites.
DR PaxDb; O15943; -.
DR PRIDE; O15943; -.
DR EnsemblMetazoa; FBtr0081013; FBpp0080566; FBgn0015609. [O15943-2]
DR EnsemblMetazoa; FBtr0081014; FBpp0080567; FBgn0015609. [O15943-4]
DR EnsemblMetazoa; FBtr0081015; FBpp0080568; FBgn0015609. [O15943-1]
DR EnsemblMetazoa; FBtr0081016; FBpp0080569; FBgn0015609. [O15943-5]
DR EnsemblMetazoa; FBtr0081017; FBpp0080570; FBgn0015609. [O15943-6]
DR EnsemblMetazoa; FBtr0081018; FBpp0080571; FBgn0015609. [O15943-7]
DR EnsemblMetazoa; FBtr0081019; FBpp0080572; FBgn0015609. [O15943-8]
DR EnsemblMetazoa; FBtr0081020; FBpp0080573; FBgn0015609. [O15943-3]
DR GeneID; 35070; -.
DR KEGG; dme:Dmel_CG7100; -.
DR CTD; 35070; -.
DR FlyBase; FBgn0015609; CadN.
DR VEuPathDB; VectorBase:FBgn0015609; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000173178; -.
DR HOGENOM; CLU_000347_1_0_1; -.
DR InParanoid; O15943; -.
DR OMA; YPQFYEV; -.
DR PhylomeDB; O15943; -.
DR SignaLink; O15943; -.
DR BioGRID-ORCS; 35070; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35070; -.
DR PRO; PR:O15943; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0015609; Expressed in brain and 18 other tissues.
DR ExpressionAtlas; O15943; baseline and differential.
DR Genevisible; O15943; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IPI:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007412; P:axon target recognition; IMP:FlyBase.
DR GO; GO:0007413; P:axonal fasciculation; TAS:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IPI:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR GO; GO:0045463; P:R8 cell development; IMP:FlyBase.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IMP:FlyBase.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:FlyBase.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 13.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 16.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 18.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00232; CADHERIN_1; 9.
DR PROSITE; PS50268; CADHERIN_2; 16.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT PROPEP 37..?
FT /id="PRO_0000003881"
FT CHAIN ?..3097
FT /note="Neural-cadherin"
FT /id="PRO_0000003882"
FT TOPO_DOM ?..2916
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2917..2937
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2938..3097
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 181..305
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 430..543
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 554..651
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 660..756
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 766..858
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 867..968
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 978..1078
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1087..1183
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1193..1299
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1307..1414
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1423..1514
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1523..1630
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1639..1742
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1749..1861
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1870..1966
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1974..2085
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2346..2377
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2379..2585
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2592..2627
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2631..2822
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2869..2902
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 2346..2357
FT /evidence="ECO:0000255"
FT DISULFID 2351..2366
FT /evidence="ECO:0000255"
FT DISULFID 2368..2377
FT /evidence="ECO:0000255"
FT DISULFID 2559..2585
FT /evidence="ECO:0000250"
FT DISULFID 2592..2607
FT /evidence="ECO:0000255"
FT DISULFID 2601..2616
FT /evidence="ECO:0000255"
FT DISULFID 2618..2627
FT /evidence="ECO:0000255"
FT DISULFID 2787..2822
FT /evidence="ECO:0000250"
FT DISULFID 2869..2880
FT /evidence="ECO:0000255"
FT DISULFID 2874..2891
FT /evidence="ECO:0000255"
FT DISULFID 2893..2902
FT /evidence="ECO:0000255"
FT VAR_SEQ 1147..1206
FT /note="ETYKLEAMAQDKGYPPLSRTVEVQIDVVDRANNPPVWDHTVYGPIYVKENMP
FT VGGKVVSI -> DRYRLRVSASDKGTPASAADVDVELDVVDRNNKPPIWDKSIYGPIHI
FT RENVTVGTVVTSV (in isoform A, isoform C, isoform E and
FT isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_000667"
FT VAR_SEQ 1486..1536
FT /note="RLAASDNLKENYTTVIIHVKDVNDNPPVFERPTYRTQITEEDDRNLPKRVL
FT -> KLVASDSLNENQTTIVINVRDVNDLPPQFPQTSYERTLDEGMTNTPFTIM (in
FT isoform A, isoform B, isoform C and isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_000668"
FT VAR_SEQ 2851..2930
FT /note="GEGRIMSPDSKGCMDRNECLDMPCMNGATCINLEPRLRYRCICPDGFWGENC
FT ELVQEGQTLKLSMGALAAILVCLLIILI -> PAGYKSSGSTCVNDNECLLFPCRNGGR
FT CRDHHPPKKYECHCPMGFTGMHCELELLASGVLTPSRDFIVALALCLGTLIL (in
FT isoform C, isoform F, isoform G and isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_000669"
FT VARIANT 1425
FT /note="E -> K (in allele CADN-M12; muscle defects)"
FT CONFLICT 1342
FT /note="P -> A (in Ref. 1; BAA22151)"
FT /evidence="ECO:0000305"
FT CONFLICT 2786
FT /note="S -> T (in Ref. 1; BAA22151)"
FT /evidence="ECO:0000305"
FT STRAND 440..450
FT /evidence="ECO:0007829|PDB:3UBF"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:3UBG"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:3UBF"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 505..513
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 525..534
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 546..554
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 578..589
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:3UBF"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 613..623
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:3UBG"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 650..661
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 683..692
FT /evidence="ECO:0007829|PDB:3UBF"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:3UBF"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 705..708
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 721..735
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 737..747
FT /evidence="ECO:0007829|PDB:3UBF"
FT STRAND 755..767
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 775..778
FT /evidence="ECO:0007829|PDB:3UBH"
FT HELIX 787..790
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 792..797
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 823..832
FT /evidence="ECO:0007829|PDB:3UBH"
FT STRAND 839..849
FT /evidence="ECO:0007829|PDB:3UBH"
SQ SEQUENCE 3097 AA; 347204 MW; 082242F28D9B5CC3 CRC64;
MAARRCLNQL RQRYITNRFN ICTCAIFLIS LPFILAIEET TFAGLSAENA ARMLAGSPGD
VEKSSLSHHS EMSLVLPHDT YPGFSIKKFK THPVKINGSS HSGAAAYHML DTDYSKYFTV
LEDGVVMTTA DISPLVNRPV QLVVVEQTPN ATNTHNLQLF VMHRNDMLRF SGSLLDASGE
VRENQPAGTR VRGVPLMQAF SGSILDEELA TPKKVRYTII DGNVDDAFAL QERKANKNIQ
ISAKSLVING DDESGVWLVT NRPLDREERA HYDLSVEASD VDGLDRTVSK IQITVLDEND
NRPIFKSLDY KFAIAGQKSA SMESNSSVTY QRFAIMGKVE ATDADGDKIA YRLKSPSNVV
IIVPQTGEIM LAGEPTSNEL LIEVIAHDLR YPSLVSAKPA KVLLEFLAAE PVSFIMQHLE
HDDINNHSHH REKRRVTRAV RPTKRIEFTE ADGDTEGKSV FQLEKETDKE TFKIRDDNPW
VTVETNGAVR VKKKWDYEEL GPEKTIDFWV IITNMGHNAG IKYTDNQRVI ILVKDVNDEP
PYFINRPLPM QAVVQLNAPP NTPVFTLQAR DPDTDHNIHY FIVRDRTGGR FEVDERSGVV
RTRGTDLFQL DMEYVLYVKA EDQNGKVDDR RFQSTPEERL SIVGGKRAPQ FYMPSYEAEI
PENQKKDSDI ISIKAKSFAD REIRYTLKAQ GQGAGTFNIG PTSGIVKLAK ELDFEDLRQP
HVYSLIVTAT EDSGGFSTSV DLTIRVTDVN DNAPKFELPD YQAHNVDEDI PLGTSILRVK
AMDSDSGSNA EIEYLVSDDH FAVDSNGIIV NNKQLDADNN NAYYEFIVTA KDKGEPPKSG
VATVRVYTKN KNDEEPKFSQ QVYTPNVDEN AGPNTLVTTV VASDKDGDNV RFGFVGGGTS
SGQFVIEDIT GVIRLHNKAI SLDKDKYELN VTAMDDGSCC VNGDQTIHTS TAVVVVFITD
VNDNKPVFKD CSTYYPKVEE GAPNGSPVIK VVATDEDKGV NGQVKYSIVQ QPNQKGTKFT
VDEETGEVST NKVFDREGDD GKFVSVTVKA TDQGDPSLEG VCSFTVEITD VNDNPPLFDR
QKYVENVKQD ASIGTNILRV SASDEDADNN GAIVYSLTAP FNPNDLEYFE IQAESGWIVL
KKPLDRETYK LEAMAQDKGY PPLSRTVEVQ IDVVDRANNP PVWDHTVYGP IYVKENMPVG
GKVVSIKASS GIEGNPTVFY RLMPGSTAQT NKFHTFYLQQ RPDNGDTWAD IKVNHPLDYE
SIKEYNLTIR VENNGAQQLA SEATVYIMLE DVNDEIPLFT EREQETVLEG EPIGTKVTQV
NAIDKDGTFP NNQVYYYIVD SPRNEGKEFF EINLQSGEIF TKTVFDREKK GAYALEVEAR
DGAPSARPNS NGPNSVTKFI RIGIADKNDN PPYFDKSLYE AEVDENEDIQ HTVLTVTAKD
HDESSRIRYE ITSGNIGGAF AVKNMTGAIY VAGALDYETR RRYELRLAAS DNLKENYTTV
IIHVKDVNDN PPVFERPTYR TQITEEDDRN LPKRVLQVTA TDGDKDRPQN IVYFLTGQGI
DPDNPANSKF DINRTTGEIF VLKPLDRDQP NGRPQWRFTV FAQDEGGEGL VGYADVQVNL
KDINDNAPIF PQGVYFGNVT ENGTAGMVVM TMTAVDYDDP NEGSNARLVY SIEKNVIEEE
TGSPIFEIEP DTGVIKTAVC CLDRERTPDY SIQVVAMDGG GLKGTGTASI RVKDINDMPP
QFTKDEWFTE VDETDGTALP EMPILTVTVH DEDETNKFQY KVIDNSGYGA DKFTMVRNND
GTGSLKIVQP LDYEDQLQSN GFRFRIQVND KGEDNDNDKY HVAYSWVVVK LRDINDNKPH
FERANVEVSV FEDTKVGTEL EKFKATDPDQ GGKSKVSYSI DRSSDRQRQF AINQNGSVTI
QRSLDREVVP RHQVKILAID DGSPPKTATA TLTVIVQDIN DNAPKFLKDY RPVLPEHVPP
RKVVEILATD DDDRSKSNGP PFQFRLDPSA DDIIRASFKV EQDQKGANGD GMAVISSLRS
FDREQQKEYM IPIVIKDHGS PAMTGTSTLT VIIGDVNDNK MQPGSKDIFV YNYQGQSPDT
PIGRVYVYDL DDWDLPDKKF YWEAMEHPRF KLDEDSGMVT MRAGTREGRY HLRFKVYDRK
HTQTDIPANV TVTVREIPHE AVVNSGSVRL SGISDEDFIR VWNYRTQSMS RSKMDRFRDK
LADLLNTERE NVDIFSVQLK RKHPPLTDVR FSAHGSPYYK PVRLNGIVLM HREEIEKDVG
INITMVGIDE CLYENQMCEG SCTNSLEISP LPYMVNANKT ALVGVRVDTI ADCTCGARNF
TKPESCRTTP CHNGGRCVDT RFGPHCSCPV GYTGPRCQQT TRSFRGNGWA WYPPLEMCDE
SHLSLEFITR KPDGLIIYNG PIVPPERDET LISDFIALEL ERGYPRLLID FGSGTLELRV
KTKKTLDDGE WHRIDLFWDT ESIRMVVDFC KSAEIAEMED GTPPEFDDMS CQARGQIPPF
NEYLNVNAPL QVGGLYREQF DQSLYFWHYM PTAKGFDGCI RNLVHNSKLY DLAHPGLSRN
SVAGCPQTEE VCAQTETTAR CWEHGNCVGS LSEARCHCRP GWTGPACNIP TIPTTFKAQS
YVKYALSFEP DRFSTQVQLR FRTREEYGEL FRVSDQHNRE YGILEIKDGH LHFRYNLNSL
RTEEKDLWLN AIVVNDGQWH VVKVNRYGSA ATLELDGGEG RRYNETFEFV GHQWLLVDKQ
EGVYAGGKAE YTGVRTFEVY ADYQKSCLDD IRLEGKHLPL PPAMNGTQWG QATMARNLEK
GCPSNKPCSN VICPDPFECV DLWNVYECTC GEGRIMSPDS KGCMDRNECL DMPCMNGATC
INLEPRLRYR CICPDGFWGE NCELVQEGQT LKLSMGALAA ILVCLLIILI LVLVFVVYNR
RREAHIKYPG PDDDVRENII NYDDEGGGED DMTAFDITPL QIPIGGPMPP ELAPMKMPIM
YPVMTLMPGQ EPNVGMFIEE HKKRADGDPN APPFDDLRNY AYEGGGSTAG SLSSLASGTD
DEQQEYDYLG AWGPRFDKLA NMYGPEAPNP HNTELEL
