CAD86_DROME
ID CAD86_DROME Reviewed; 1943 AA.
AC Q9VGW1; B3GN10; Q8MZ37;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cadherin-86C;
DE Flags: Precursor;
GN Name=Cad86C; ORFNames=CG4509;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18539010; DOI=10.1016/j.mod.2008.04.005;
RA Schlichting K., Dahmann C.;
RT "Hedgehog and Dpp signaling induce cadherin Cad86C expression in the
RT morphogenetic furrow during Drosophila eye development.";
RL Mech. Dev. 125:712-728(2008).
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.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 726-1943.
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
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 [5]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=17113384; DOI=10.1016/j.cub.2006.09.029;
RA Lovegrove B., Simoes S., Rivas M.L., Sotillos S., Johnson K., Knust E.,
RA Jacinto A., Hombria J.C.;
RT "Coordinated control of cell adhesion, polarity, and cytoskeleton underlies
RT Hox-induced organogenesis in Drosophila.";
RL Curr. Biol. 16:2206-2216(2006).
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 -!- TISSUE SPECIFICITY: As cell intercalation proceeds, a row of
CC stigmatophore cells surrounding the spiracular chamber show expression
CC of Cad86C. Expression is regulated by the Abd-B cascade, requiring sal.
CC Expressed in a broad region of the morphogenetic furrow and in clusters
CC of cells posterior to the morphogenetic furrow. Weakly expressed in the
CC epithelium of wing imaginal disks. In eye imaginal disk cells within
CC the morphogenetic furrow, expression is localized to the apical region.
CC {ECO:0000269|PubMed:17113384, ECO:0000269|PubMed:18539010}.
CC -!- INDUCTION: By hedgehog (hh) and dpp signal transduction in the
CC morphogenetic furrow. {ECO:0000269|PubMed:18539010}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM29379.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU707853; ACD79974.1; -; mRNA.
DR EMBL; AE014297; AAF54562.5; -; Genomic_DNA.
DR EMBL; AY113374; AAM29379.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001247031.1; NM_001260102.1.
DR RefSeq; NP_788635.3; NM_176458.4.
DR AlphaFoldDB; Q9VGW1; -.
DR SMR; Q9VGW1; -.
DR BioGRID; 66446; 2.
DR IntAct; Q9VGW1; 5.
DR STRING; 7227.FBpp0293207; -.
DR GlyGen; Q9VGW1; 9 sites.
DR PaxDb; Q9VGW1; -.
DR PRIDE; Q9VGW1; -.
DR GeneID; 41302; -.
DR KEGG; dme:Dmel_CG42601; -.
DR CTD; 41302; -.
DR FlyBase; FBgn0261053; Cad86C.
DR VEuPathDB; VectorBase:FBgn0261053; -.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_001960_1_0_1; -.
DR InParanoid; Q9VGW1; -.
DR BioGRID-ORCS; 41302; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41302; -.
DR PRO; PR:Q9VGW1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; Q9VGW1; baseline and differential.
DR Genevisible; Q9VGW1; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
DR GO; GO:0035003; C:subapical complex; IDA: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:0098609; P:cell-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 GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR Pfam; PF00028; Cadherin; 3.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 1.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..1943
FT /note="Cadherin-86C"
FT /id="PRO_0000004010"
FT TOPO_DOM 1..934
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 956..1943
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 238..366
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 367..483
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 484..600
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 601..708
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 709..832
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..90
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 926
FT /note="D -> DTLTPLQ (in Ref. 4; AAM29379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1943 AA; 220408 MW; 16ADFDBB8C0EED30 CRC64;
MASTSSSQPE KNRSHVPLCR LGTEPVSRTG AAEEPSGQRE CYYYAPATSP HHHHHHHHQH
HHHHRLKQHH RHHHHHHRLQ HHHHHHQQQH NHQNQQMQHH WPSRLGPIGP WLGAMTAYRL
LTISLLIGIL CPHHVQGADP KFDPTTRMRL VLVPADAQVN SVIYRLRATD EEFDYPLTFE
FVGDASASTV KVESLPCTKY NSVCQANIVL QRRLEPGRYY DFQVSVKDTK GGMTTQLCSI
TATNFTTPHD LIFPHKPGII MIPEDAKRGT ELDYVIARKN PLFQKPVYLE LWGSPLFAIR
QKIVSSETTE GTVFLLGPLD FEKQAMYHLT ILANDAYAEP GQDSRNIAGM EIVVIVQDVQ
DQPPVFTSAP PVTKLPPGIL PGDKILQVHA EDGDKGNPRE VRYGLVSENN PFTSFFDINE
TSGEIFLMRP LEDIAFITHV GDPVLLTVIA EEVKVGRDEP PALASTVQLA FFLPDRTNSP
PYFENDHYVS RVDENAPQGT ALTFVDPYVP RVYDDDTGKN GVFSLTLLNN NGTFEISPNV
AERSAGFLIR VRDNSMLDYE QQQSVQFQIL AQELGPATNL SALVNVTVYI NDVNDNAPVF
EQPAYSVELP ENMTAGTKVV QVLATDPDSG LGGKVRYTAI LGYLNTSLNL DAETGLITVS
TNKHGFDREV MPEYHLYVEA RDMDGEGNRA QVPLIIKLID VNDETPIFDK DLYEFILTHD
LMGFTTTAVI HAEDKDATAP NNEVRYEIIN GNYDNQFVLD KVTGELTVRE KIHLRSKKNA
KTRRRRQAGS DDEDTDIFIL TARAYDLGVP VRFSTTTIRV YPPESRKRSV KFVVPGHNPD
KAKTEETLSA LSGGKVYIHN IRPLSPDEPG AKDIPAGNPG IKERSVVTAT VIYDSSSVVD
ISEIQQRLSH HNNSYAIMPQ DTSSTDTQYK AENKVLFWLL ILLATLVALT ILILLLCCIC
SWCPLYGAAT KRIVNISRTE DDVHLVHREM ANGKQTKSVQ VAEWMGRRDA WSAEKPPDTR
TKPTRWEFHD GREQLDEDVG RGQDIGEGDR RHIQSAEEQQ RRVRIKHNRT AKDDLHLNFH
NSRTNLINDR DVYMEDVIEN RDLAGDREHI TRTRVNRQEY ARRKQYDSEV RHIDDDSMRR
HEIDRGSDID FNTAHNSLKS KRELFIKDGN VEILQLMTRD KTRDGLNLDD DNIYVNVPLK
PAGNLSHPQL LMVDNTGKEI LMRRFIEEQP DGKQIIREHY QIVPGATYIQ SMPNEVQQGS
TLKGDTFPLG KSGPNSIVYS QLEPEVKVIH TQPVQAGEGV SLDQQMQPAV SNQSLTHELE
HSLKQQNALL RQILMEKEKL ENAYTQHEVA LETQSLPGQS MAIGTQTDCD AGTQTEGFDG
VLDPEISLAK PSRRRARSEN DESMSEDGYE YVRFNPPNSP EGVYWIKRRR TKKRPRQPRK
RIVMVEEVKR KIRTPIKEEE EVQERKKRVP PKKPLRETKT SILRKQLSDE SRKDQSRNGE
SQTGNRHRSE SDSHNRDMFM EITDSMDELA SPGSHSIRKI QVEKYYKHSD GDFDEDDTEY
SIDSDGDEIV IRTNYPSRAQ ENERYRRQER TYAEPENPVD RKRPARKSSP TDSQPEAMPR
LSRRDSSKRG SRKQTSSEPP HNRVSISKYE STVTENGRKL MSTSTEIVGS KRSLTDRSYQ
SETELAGLEH EERNVPKYME WYYNKKKSSV SGRTSTESSK SQPSSKKKVG AAEKRVSKTR
ITAQPKDVEE YDETGGRYKP EPAPRKSPPK GSRLLKEDRA LNKQHKPKIE TDTNHPLLQH
SEHRFERENA LEVPAAPTKL PHYMYPETPP HAAAGGKESK SGRESKTSKE AKPKPSPIRE
NEVKVSNSKI YVEHRGTGHP TQKQLNASTL EDDHDSGIAM NSLLNSLGRR NPIAEKKSVF
SIAYDDVSRV KKINSGGESP QYS
