ID A0A0M4EQ25_DROBS Unreviewed; 1989 AA.
AC A0A0M4EQ25;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cad87A {ECO:0000313|EMBL:ALC46335.1};
GN ORFNames=Dbus_chr3Rg1085 {ECO:0000313|EMBL:ALC46335.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC46335.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC46335.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC46335.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012526; ALC46335.1; -; Genomic_DNA.
DR SMR; A0A0M4EQ25; -.
DR STRING; 30019.A0A0M4EQ25; -.
DR OMA; KEYFAIA; -.
DR Proteomes; UP000494163; Chromosome 3r sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 14.
DR Gene3D; 2.60.40.60; Cadherins; 15.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR Pfam; PF00028; Cadherin; 10.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 14.
DR SUPFAM; SSF49313; Cadherin-like; 14.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 14.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1989
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005793695"
FT TRANSMEM 1786..1812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..132
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 133..245
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 245..358
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 359..472
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 473..683
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 684..788
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 789..892
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 893..1012
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1019..1117
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1118..1225
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1226..1332
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1345..1443
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1446..1565
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1566..1689
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 590..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1989 AA; 218998 MW; FFD333D723504E1E CRC64;
MKRMLTWFII CLTTQLASSE TNLPPVFTQT LNNIVLYENV PVGTVVFRLE GYDPESSNVT
FGSIGSDHFS VDPVSGNITL VKPLDREEKD SLTFLVSIRD RVDAAGESEQ DNVVEQPITF
IILDENDNAP EFQNTPYETD VNEDAAVGTT IYNKILVTDR DTIGDSLDLK CLPQQQSPEA
CNKFRLQLLS REATVLTAAV VLNETLNYNQ RMIYHFQLEA SDGLHKTQTT FEARVKDVQD
KPPVFQGSLS TVIDEDSAIN TLVLTVHARD GDTGEPRKIV YDLISNPSDY FLLDSHSGEL
RTAKPLDREA LADSTGLITL VIRARELVNG VPSDDALTSA TARATVTIRD VNDSPPTFNK
KEYEVALLEN TPVGTPLALD MSVSDADVGV NSKFALRLED VSGVFDVEPK LVSGYSQVNI
RVANGTLDYE NPNQRKFIVL VIAEETDTNP KLSSTATITV SVLDANDNKP SFELESYSAS
VSEAALPGQF IATITAKDID SGSYGDAGIR YSLSGTGAEL FHVNEQTGVI TLADCQEQQQ
RNRRQRRDLH DNEHALQMLS LEANPQEQQQ SQQQPQINTE PSVQYTLITQ ADKQPQTTTM
ATTIEPTTTT TIGAEDAVAT ANDAKADSSS SSSRQAPSTC LDYETETTYF LSYKATDDNG
QGQTSVVSLR ISVTDANDSP PVCESPLYRG SVDEGALVFD SPLVVKARDA DTMSSISYRI
IGSPQIESIF DIDKQSGQIS IRSNASLDVT TLKSDQLIFV VEANDGLFTA NCGVNITVRD
VNNHAPSFVQ QSYSAVVEEN SEIGTSVEKL QATDLDTGKN AELRYRIQQG SFDDFGIDER
TGEVFVSRKL DYDRRNTYQL QVQAADQGTP SLTGTSTLTI NVQNSNDKDP YFVPATQHAE
VRADAPTGQL VYTLIALDPD VATHNALEFA ATDDITAIDK EGKELPQSEQ FKEYFAITRA
GKVLVNRQLD RNLFAVMRIN VLVTDSTAPN VQQGRGLLII QIIDVNKIPP RFNAPWTPAQ
PLIKLQMVEE QPVGTVLTTL QASDEDSSIG EFNISVNNYF AINATTGVIY TTARLDYEAV
KEVKFMATVS DTGVPALTAT ADIVVDIINL NDNEPQFSRS EYQFNITENS PEGTLAGQVQ
AQDADVGAFG ELTYTLIGEN HKYFNVDPYT GNVRVANASI LDREQLKQLT LTVVAQDKAP
ATVQKSATAT IHINILDVND NEPVFTRAVY NSTVSENAAY QPPAALLQVQ ANDQDEGLFG
DVRYVITAGN ELALFTLDAQ TGIVYPAQSL AGKAGSYRLT ISARDTQGSG SKESNAEALI
TVLRVNRHRP EFIIPALSNA TIEIPGDIVQ ADYLLLTVKA VDNDTDDSVS YHLQLNNQNV
QQTQEFKIDQ HSGELRAKQQ LNRKQRANYE IVLVARDAGN PPFESLRLLS VSIVDANENR
PEFPDAANPY QVSINENSGR DVKIGHIQAA SRSKHNRDIF YYMLLGNEDG AFYVDKLTGD
IYTNKSLDRE QTDAYTLYIL ASIKSDLHIS EEERASFSIK TLNRDNTVAK VAITVLDVND
NAPIFEKSIY YAGVNANAKM NAAITLVNAT DADQGKNSKI EYMIVASNLY KFDASKSTGS
IVPSPFAISQ DGRITANTIM AEYNQDRFEL EIVARELEEP QRSANTKVNI WVFDGTQLVR
VILSRPPEEV YQEQEEIIAE LRNATQHRII VDEIRFHLDS IGRIRMDWCD LYFHAVDPQT
QQIAPVDEIL KDIDRNYDYL KDYYAGFAIE NVVPAYIAIV QDEFDLAVAG LVALVIVLFV
GVISFIVLCC CLKHWNLSVP VETRRKEALI KKQIIEDLNT TENPLWIEQK LKLYEEQELT
MQVFSEPDHI SNSEAPGHLE HRSSLEQVHH GQSVDNTYAT IQPRNNQNRL NAGSNGGAGS
ISMRGTAGPA SAGGIGGAGL ILARVDPHGN DFSDYATLRN NRAPSMYEFT GSTFQAPIRD
GDDAVAELI
//
