ID W8ATM9_CERCA Unreviewed; 1560 AA.
AC W8ATM9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=DE-cadherin {ECO:0000313|EMBL:JAB89562.1};
GN Name=CADE {ECO:0000313|EMBL:JAB89562.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB89562.1};
RN [1] {ECO:0000313|EMBL:JAB89562.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB89562.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC membrane {ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane
CC protein {ECO:0000256|RuleBase:RU003318}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; GAMC01016993; JAB89562.1; -; mRNA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:UniProt.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd11304; Cadherin_repeat; 7.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 7.
DR Gene3D; 2.10.25.10; Laminin; 1.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
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; 5.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; Cadherin-like; 8.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 7.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|RuleBase:RU003318};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1382..1402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 160..266
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 293..354
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 385..465
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 465..575
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 584..676
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 676..785
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 795..896
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1142..1177
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1178..1366
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1541..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1167..1176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1560 AA; 176208 MW; 2A89219334AB59B8 CRC64;
MSPQHFQSQS ETQIYHLQQY RQTYQRPRKH LCRKLHKYHT IAFALALVNL HTVALVSAYI
GGSDAALAKS HRDDPFSAFY TPAATNVSID AHNSTYVSNN LIRQRRSPNP APDSVSSLYS
ALPAARTGNS AIYFSRSSSS AVTHENAKQY RDNRKPAFKK CASYKPSVRE EEPENTFVIM
VQAEDPDSDQ EIKYSLVQSA TERSKFHIDP KSGVIVTTHR FDRDEPTYEK MVYVTVQATD
NGNPQLDDVC TFKVVIEDVN DNAPVFNKAR YDESISEDKQ PDAIVMRISA SDLDDGNNSI
IYLNRPIDKR PGQYYTITVN AYNPTNPMSL ESKQESQIEV RIRVVESSKK PPSFVDPIED
PIYLKEDYRN YSTPIATLRA VSNVPDKPEV IFELVTGRTE QTNSKKTFVF NQTGTTVTIG
LGKILDYESV TEYTLTMIAR NTYDLVAEHV IKIKVVDVND NIPYFTEVNK GTLLENELPG
TPVMQVRAFD MDGTEANNIV SFELADNREY FKIDPHTGNI TALTTFDREE RDFYNVKVIA
SDNSPSSLYN NGEPNRGQQV FRIEIADKND HKPHFQLAEY VHDSLPEDAN INFIVTEVEA
VDEDNTAQIV YTIESGNVGN AFKIEKKTGQ ITVNQRLDYE NITEYVLKIR AFDGIYDDYA
TVTIKIANVN DNPPEFKEKY SITIKEEMVY DYCILNVEAY DPDIKDRTAD QHIKYSVVKE
EQKKMISIDN DGCVKLIQPL DRDPPDGHKS WQMLIAAVDE DGQGLKSVTH LTIDLEDIND
NAPFLVNKMP VIWQENRNPG QVVQLQADDY DEKQNGPPYT YGIDSEASAD IKTKFSIDND
YLFANVQFDR EEQKEYFIPI RISDSGKPKQ SKVSILHLII GDDNDNAMSE GSSRIFVYNY
KGEAPDTDVG RVFVDDPDDW DLDDKEFRWK NGFPHDNFRL NPSTGMITML ERTQEGEYLL
EFVVTEESTF IPRHSVDADV TVIVRELPEE AVDKSGSIRF YNVTKENFIS VPRDAQADDS
LSLKDRLQYS LAKLFNTSVT NVDVFTVLQN ANNTLDVRYS AHGSPYYAPE KLNGIVAQNQ
QKLERELGLQ MLMVNIDECL IEKYKCESSC MNTLHKSNIP YMIYSNTSSF VGVTAFIEWH
CVCEARISTY CLNGGTPRIG ENDMCDCIDG FTGPHCELVS VGFYGNGYAF YEPISPCENT
KISLEIAPQT DQGLIMYLGP LNYNPLLPLT DFLSLELVKG YPTLTVDYGT GAIRIEHRHV
QLQVGKSYQL DIILQKTSVE MVVDNCRLST CISLGAPQGP NEFLNVNAPL QLGGTPVDLL
QLGQKLNWTY TPSRQGFFGC IRNLTINNHT YNLGAPAISR NIDSGCQRAV AVAVSFGIDR
NFIIAIVACI LLLLIILLAV VVQKKQKNGW HEKDIDDIRE TIINYEDEGG GERDTDYDLN
VLRTQPFYEE KLYKDPHTLQ AMKDPNNEIP DIGGFLGDKK ENCDREAGTY PVDDVRNYAY
EGDGNSDGSL SSLASCTDDG DLNFDYLSNF GPRFRKLADM YGEEPSDTDS NVDDDQGWRI
//
