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   27-MAR-2024, entry version 203.
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}.
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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; 19.
DR   IntAct; O15943; 8.
DR   STRING; 7227.FBpp0099721; -.
DR   GlyCosmos; O15943; 6 sites, No reported glycans.
DR   GlyGen; O15943; 6 sites.
DR   PaxDb; 7227-FBpp0099721; -.
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   AGR; FB:FBgn0015609; -.
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   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 cell types or tissues.
DR   ExpressionAtlas; O15943; baseline and differential.
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:0016020; C: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; cd11304; Cadherin_repeat; 15.
DR   CDD; cd00053; EGF; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.40.60; Cadherins; 17.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
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   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 14.
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; Cadherin-like; 18.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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.
DR   Genevisible; O15943; DM.
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
//