CAD87_DROME
ID CAD87_DROME Reviewed; 1975 AA.
AC Q9VGG5; Q8MQL5;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 4.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cadherin-87A;
DE Flags: Precursor;
GN Name=Cad87A; ORFNames=CG6977;
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] OF 443-1975.
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-424 AND ASN-1576, 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).
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; AE014297; AAF54717.4; -; Genomic_DNA.
DR EMBL; AY128505; AAM75098.1; -; mRNA.
DR RefSeq; NP_731649.2; NM_169440.3.
DR AlphaFoldDB; Q9VGG5; -.
DR SMR; Q9VGG5; -.
DR BioGRID; 66559; 1.
DR IntAct; Q9VGG5; 2.
DR STRING; 7227.FBpp0081987; -.
DR GlyGen; Q9VGG5; 16 sites.
DR iPTMnet; Q9VGG5; -.
DR PaxDb; Q9VGG5; -.
DR PRIDE; Q9VGG5; -.
DR EnsemblMetazoa; FBtr0082513; FBpp0081987; FBgn0037963.
DR GeneID; 41441; -.
DR KEGG; dme:Dmel_CG6977; -.
DR UCSC; CG6977-RA; d. melanogaster.
DR CTD; 41441; -.
DR FlyBase; FBgn0037963; Cad87A.
DR VEuPathDB; VectorBase:FBgn0037963; -.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_001354_1_0_1; -.
DR InParanoid; Q9VGG5; -.
DR OMA; FQGSTFQ; -.
DR OrthoDB; 19532at2759; -.
DR PhylomeDB; Q9VGG5; -.
DR SignaLink; Q9VGG5; -.
DR BioGRID-ORCS; 41441; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41441; -.
DR PRO; PR:Q9VGG5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037963; Expressed in wing disc and 25 other tissues.
DR Genevisible; Q9VGG5; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; ISM:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISM:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR Pfam; PF00028; Cadherin; 9.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 14.
DR SUPFAM; SSF49313; SSF49313; 14.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 14.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1975
FT /note="Cadherin-87A"
FT /id="PRO_0000004007"
FT TOPO_DOM 18..1775
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1776..1796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1797..1975
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 133..245
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 246..358
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 359..472
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 473..669
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 670..774
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 775..878
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 879..998
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 999..1103
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1104..1211
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1212..1318
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1319..1431
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1432..1553
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1554..1677
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 535..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 1691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 771
FT /note="V -> M (in Ref. 3; AAM75098)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110
FT /note="F -> S (in Ref. 3; AAM75098)"
FT /evidence="ECO:0000305"
FT CONFLICT 1650
FT /note="S -> R (in Ref. 3; AAM75098)"
FT /evidence="ECO:0000305"
FT CONFLICT 1690
FT /note="R -> C (in Ref. 3; AAM75098)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1975 AA; 217557 MW; 91BF71B0461D6E4F CRC64;
MKLPLGLLMI CLGLTLAKGE TNLPPVFTQT LNNIILYENV TVGTVVFRLE AYDPEGSPVT
YGAIGADHFS VDPVSGNITL IKPLDREEKD TLKFLVSIRD RVDPEGESER DNVVEVPITF
IILDLNDNPP EFQNTPYEAD VNEDAAVGTT IFDKITVKDR DIVGESLDLK CLPQQQSPEA
CRKFRLHIIK RDATILEAAV VLNDTLNYNQ RMVYHFQIEA TDGPHKTQTT FEARVKDVQD
KPPVFQGSLS TVIDEDSPIN TLVLTVHARD GDTGEPRKIV YDLRTNPNDY FLLDAQTGEL
RTAKPLDREA LEDSTGIISL VIRARELVNG VPSDDPLTSA TAKATVTIRD VNDSPPVFNH
KEYSVSLLEN TLPGTPLALD MSVSDADVGI NSKFALRLDD VSGVFDVEPK LVTGYSQVNI
RVANGTLDYE NPNQRKFIVL VVAEETDTNP RLSSTATITV SVLDANDNKP VFEQESYSAS
VSEAALPGQY IATITARDVD SGSYGDSGIR YSLSGTGAEL FHVNEQTGVI SLANCHDNGE
SNRRERRDLN EDEHVEEDDG EGHLEMLSME AATREIGTEP TVQYTLITQA PEEQASSVPL
PAPVPHAAPS GVPAATANDD KAPQTCLDYE SETTYFLSYK ATDDNGRGSA SVVSLRISVT
DANDSPPVCE SPLYRASVDE GAVVFDSPLI VKARDADTMS RISYRIRGSE QVESIFDIDR
ETGQIIIRPN ATLDVTNLNS DQLIFAVEAN DGLFTAHCGV NITVRDVNNH VPNFEQQSYS
AVVEENSEIG TSVERVHATD LDTGKNAELR YRIQQGSFDD FGIVETTGEV FVSRKLDFDR
RNTYQLQIQA SDQGTPSLTG TATLTINVQN SNDKDPYFVP ATQHAEVRAD APPGQLVYTL
IALDPDVANH NALEFAGTDD ITAIDKEGKE LPHYDQFKEY FKISRNGKVS VNKQLDRNLF
AVMRINVLVT DSTAPNVQQG RGLLIIQIID VNKNPPRFNA PWSVEQPQIK LQMVEEQPVG
TVLTTLQAND EDSSIGEFNI SDNDYFAINQ TSGMIYTIAR LDYEVVKEVK FQVTVSDTGV
PALTATADVV VDIINLNDND PKFSQSDYYF NVTENSPRGT VAGKVEAHDG DVGVFGEITY
TLIGENNKYF SIDAYTGNVM VANSSILDRE QIKELTLSVV AQDKAPAAVQ KSATATIHIN
ILDVNDNAPV FTRDVYNSTV AENAAYQPPA ALLQVQAIDQ DEGLYGDVRY IITAGNEMGL
FKLDAQSGIV YPAQSLSGKH GAYELTISAR DTQGSGTMES TTKAIITVLR VNRHKPEFVI
PALSNATIEI PGDIVQPDYL LLTVRAMDND TEENGKVSYH LQVNNRNEQQ TGEFKIDEVT
GELRAKTQLN RKNRANYDII LVARDAGNPP FESLRLLSVS IVDANENRPE FPDASNPYKV
SINENSGRDV KIGHIQAASR SKHNRDIFYY MLLGNEDGAF YVDKLTGDIY TNKSLDREET
DVYTLYILAS IKADLHISEE ERASFSIKTL NRDNTVAKVA ITVLDVNDNP PVFEKPIYYA
GVNANAKMGA AITLVNATDA DQGKNAKIEF MIVASNLYKF GATKSTGSIV PSPFAISQDG
RISANTIMAE YNQDRFELEI VARELEQPQS SASTKVNIWV FDGTQLVRVI LSRPPEEVYQ
EQEEIIAELR NATQHRIIVD EIRFHLDSIG RIRMDWCDLY FHAVDPQTQQ IAPVDEILKD
IDRNYDYLKD YYAGFAIENV VPAYIAIVQD EFDLAVAGLV ALVIVLFVGV ISFIVLCCCL
KHWNLSVPVE TRRKEALIKK QIIEDLNTTE NPLWIEQKLK LYEEQELTMQ VFSEPDHISN
SEAPGHLDHR SSLEQVHHVG QTVDNTYATI QPRNNQNRLT GGGGAGGGSM RSGGGASAGG
VGGAGLLLAR VDPHMNEFAD YATLRNNRAP SLYEFTGSTF QAPIRDGDDA VAELI
