CADN2_DROME
ID CADN2_DROME Reviewed; 1799 AA.
AC Q9VJB6; G4LU36; Q0E8P8;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Putative neural-cadherin 2;
DE AltName: Full=Cadherin-N2;
DE Short=dN2-cadherin;
GN Name=CadN2; ORFNames=CG42829, CG7527;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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; AE014134; AAF53636.4; -; Genomic_DNA.
DR EMBL; AE014134; ABI31322.2; -; Genomic_DNA.
DR EMBL; BT132666; AEQ05568.1; -; mRNA.
DR RefSeq; NP_001036368.2; NM_001042903.4.
DR RefSeq; NP_609855.3; NM_136011.4.
DR AlphaFoldDB; Q9VJB6; -.
DR SMR; Q9VJB6; -.
DR BioGRID; 61067; 1.
DR IntAct; Q9VJB6; 6.
DR STRING; 7227.FBpp0300935; -.
DR GlyGen; Q9VJB6; 16 sites.
DR PaxDb; Q9VJB6; -.
DR PRIDE; Q9VJB6; -.
DR EnsemblMetazoa; FBtr0303836; FBpp0292843; FBgn0262018.
DR EnsemblMetazoa; FBtr0308770; FBpp0300935; FBgn0262018.
DR GeneID; 35071; -.
DR KEGG; dme:Dmel_CG42829; -.
DR UCSC; CG7527-RB; d. melanogaster.
DR CTD; 35071; -.
DR FlyBase; FBgn0262018; CadN2.
DR VEuPathDB; VectorBase:FBgn0262018; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000173178; -.
DR HOGENOM; CLU_000347_0_1_1; -.
DR InParanoid; Q9VJB6; -.
DR OMA; LCQESHL; -.
DR OrthoDB; 6237at2759; -.
DR PhylomeDB; Q9VJB6; -.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-418990; Adherens junctions interactions.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-525793; Myogenesis.
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q9VJB6; -.
DR BioGRID-ORCS; 35071; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35071; -.
DR PRO; PR:Q9VJB6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0262018; Expressed in brain and 3 other tissues.
DR Genevisible; Q9VJB6; DM.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISM:FlyBase.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IMP:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:FlyBase.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISM:FlyBase.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS: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 CDD; cd00110; LamG; 2.
DR Gene3D; 4.10.900.10; -; 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_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; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24027; PTHR24027; 2.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; SSF49313; 7.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00232; CADHERIN_1; 4.
DR PROSITE; PS50268; CADHERIN_2; 7.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1799
FT /note="Putative neural-cadherin 2"
FT /id="PRO_0000003883"
FT TRANSMEM 1549..1569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 37..136
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 137..252
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 253..364
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 368..485
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 486..590
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 590..709
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 708..812
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 973..1010
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1011..1217
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1220..1260
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1263..1454
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1497..1535
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1726..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 977..988
FT /evidence="ECO:0000250"
FT DISULFID 982..997
FT /evidence="ECO:0000250"
FT DISULFID 1000..1009
FT /evidence="ECO:0000250"
FT DISULFID 1191..1217
FT /evidence="ECO:0000250"
FT DISULFID 1224..1239
FT /evidence="ECO:0000250"
FT DISULFID 1233..1248
FT /evidence="ECO:0000250"
FT DISULFID 1250..1259
FT /evidence="ECO:0000250"
FT DISULFID 1419..1454
FT /evidence="ECO:0000250"
FT DISULFID 1501..1512
FT /evidence="ECO:0000250"
FT DISULFID 1506..1523
FT /evidence="ECO:0000250"
FT DISULFID 1525..1534
FT /evidence="ECO:0000250"
SQ SEQUENCE 1799 AA; 200480 MW; 6ECD9723887BCAF6 CRC64;
MVDPLKIFWV LTNSTYLVTK FVRIGIADKN DSPPYFDRFL YETEIDENAD LQSTVLTVNA
KDHNESTNIR YQITGGNIGN AFAVQNTTGV IYVASPLDYE TRPRYELRLE ATRNRKNNYT
TVVINVRDVN DNPPVFDRQT YRTQITEEDD RNLPKRILQV TATDGDVDRP INIVYFLTGQ
GIDPDNPANS KFDINRTTGD IFVLKPLDRD QPNGRPQWRF TVFAQDEGGE GLVGYADIQV
NLKDINDNAP QFPQGIYFGN VTENGTAGSS VMTMSAVDYD DPNESTNAKL IYSIEKNVIE
EETGAPIFEI EPETGLIKTA VCCLDRERTP DYSIQVVAMD GGGLKGTGTA SIRVKDLNDM
PPQFTKDEWV TEVDETNGTY IPETPILTVT VQDEDETNTF QYKVVPNSGF GADKFAMVRN
GDGTGSLKII QPLDYEDPLQ SSGFRFRIQV NDKGDDGPGG SDKYHVAYSW VVVKLRDIND
NVPKFDREHI EVSIYEDTKV GTILEQFKAT DADQGGHSKV AYKIVRSTNR KRQFAISDRG
AVSIQRPLDR ETQDRHHIQI LAIDDGSPAR TATATLTVIV KDVNDNAPTF AQDYKPTLPE
NVSGKKILEV AAKDPDDRLR GNGGPFTFRL DPLASDEIKA GFKVEYDRRG DNENGVAIIS
SLRPFDREAQ KSYAIPIEIK DNGAPAMTGT STLTVTIGDV NDNKMQPGSK SVLVYNYQGQ
SQDTPIGRVY VNDPDDWDVP DKKYYWEVQE HQRFKLDTDT GILTMRAGTR RGRYQLRFKV
YDREHGQEDI PANLSVTVRD ITAEAVQQAG SMRLSHITDE DFVRTWNPVK NQVEPSKLER
FRNKLAELLY TDRDNVDVFS VQLKEGSPYP LTDVHFAARS ATQQPYFKAV RLNGVVQMHR
EEIEKDVGLN ITMVNINECL HEGKGKCGSN SCTSKVELGK KPYTVSVNRT ALVGVRLDIS
AQCVCRARNF THQDHNCRTH LCYNGGRCVE TRNGPKCVAC PVGYNGPRCQ QSTRSFRGNG
WAWYPPLQLC QESHLSLEFI TRVADGLILY NGPIVPPKPE ETVISDFIAL ELEQGYPRLL
IDFGSGTLEL RVKTKKTLDD GVWHRLDIFW DTENVRMVVD FCRTALVSEM EDGTPPEFDD
NACQARGQIP PFAESLNLNQ PLQLGGLYRQ HFDQTLYNWQ YAFSSKGFDG CIRNVIHNSE
HYDLAFPALA RNSFPACPQT DEVCLKTEHT ARCWEHGNCV ASLVQAKCHC QPGWMGPGCN
VPTIPTTFKA QSYVKFALSF EPDRFSTQLQ LRFRTREQGG ELFRVSDQHH REYAILELRR
GHLQFRYNLN SMRNEEQLLT LTAIAVNDGQ WHVIRISRYG SAALMELDGG ESRRYNESFH
FTGHQWLTID KQEGVYAGGK AEYTGIKTFE VQSDFQRSCL DDIRLDGKHL PLPPAMNGTQ
WGQATMARNL ERNCPSNRPC SNVICPDPFD CVDLWNEYEC TCSEGRIMSS DTKGCVDRNE
CLDLPCLNGA TCINLEPRLR YRCICPEGYW GENCELVQEG QRLKLSMGAL GAIFVCLIII
LILALIFVLY SRKRKTTKKK KRSGPEKDVR ETVISYEDEG GGEDDMTAFD ITPLQIPISA
QGGPPDIAAC KMPIIYPVMT LLPPGQELNV AYLMEERKQR IDKDNNAPPF DDLRNFTFEG
SGSIAESLSS LASGTDDENQ DFNYLQNWGP RFNALAAMYV HDKAKASSQL PSDGGGGSGD
GPGPGASSSS PLGGGGTGGG SGIPGNVLAV VATGSGAGPG GGGGSSGLMP LPEVDKVVL
