GenomeNet

Database: UniProt
Entry: A0A212F954_DANPL
LinkDB: A0A212F954_DANPL
Original site: A0A212F954_DANPL 
ID   A0A212F954_DANPL        Unreviewed;      1433 AA.
AC   A0A212F954;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=DE-cadherin like protein {ECO:0000313|EMBL:OWR50260.1};
DE   Flags: Fragment;
GN   ORFNames=KGM_216145B {ECO:0000313|EMBL:OWR50260.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR50260.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR50260.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR50260.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC       {ECO:0000256|RuleBase:RU004357}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU003318};
CC       Single-pass type I membrane protein {ECO:0000256|RuleBase:RU003318}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWR50260.1}.
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DR   EMBL; AGBW02009647; OWR50260.1; -; Genomic_DNA.
DR   STRING; 278856.A0A212F954; -.
DR   KEGG; dpl:KGM_216145B; -.
DR   InParanoid; A0A212F954; -.
DR   Proteomes; UP000007151; Unassembled WGS sequence.
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   CDD; cd11304; Cadherin_repeat; 6.
DR   CDD; cd00054; EGF_CA; 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   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; 6.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 7.
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; 4.
DR   PROSITE; PS50268; CADHERIN_2; 7.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   4: Predicted;
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};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007151};
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        1263..1283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..129
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          130..235
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          270..346
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          346..455
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          464..556
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          556..668
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          678..775
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1059..1247
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OWR50260.1"
SQ   SEQUENCE   1433 AA;  160616 MW;  E1FC97ACD49C846E CRC64;
     FTPASPKLAV KDNHKPLFTE CLNYRPTLKE EQPVGTYVFT VHAEDRDPPE MGGTVTYKFV
     STPGEKERFH VDPETGRITT ADIFDHDEPS REKEAYITVR ASDNGQPQLD DACTIKILIE
     DINDNQPVFD KVSYSESVPQ DLPSGREVMR ISATDIDDGN NSIVHYSLDS NSPDQAYFYI
     DPDNGVIFLN KTIDKVPGYK FKLSAIVKDM GDPPQQSSIT LDIQVVESNK KSPSFIEVPD
     EPIRLKENYA DFNTPIATVR AVSNIPEEKK LQFELVMGQT EQTNKWHTFV LEPEADSAYI
     KLGNHLDYEK ITDYTLTVRI QNNYKLAAET IIQIEIEDVN DNIPIFSEIR SGSVLENEPP
     GTPVMQVRAF DADGTSANNQ VTYELGDPSD PFAIDSITGN ITTLKMFDRE ERSFYNIKII
     ATDNSESALI PGKHNAGQQV FLIEIADKND NPPHFTQDTY VAESIAENAN INELVTQVTA
     LDIDTASVVT YSIVAGNTYD AFVIRNFTGE IRVNNELDYE NITSYSLDVR AFDGLYEDYA
     KVLIKIENLN DNPPVFLANY TKTIEEEKLY EGCIVKVEAY DPDLDRNEPQ NIVYSLVKHE
     QKEFLQIDND GCLRLTKPLD RDQPSGFTRW QILIMAADHG GRLGSDSLRS TTEVILELTD
     INDNAPFLTN TQPIIWYENE PPGQVVILTA KDYDSAENGP PFTFALNESA SFDIRSKFHI
     QGNILSTLVS FDREQRKEYK IPVAITDSGT PRLTGVSILH IVIGDRNDNS MEPGHSDIFV
     YNYKGEAPDT EIGRVFVNDP DDWDLPDKRF MWLPSYEQRS PYFDVHSNTG MITMKEGTPN
     GTYMLRFNVT EVNEPLVPFH WVEATVNVTI KEIPEEAVDK SGSIRFLNIT AEEFIIPEAD
     GTSKKDKLHR RLAELYNKSM DNVDVFTVFT KLTVKDAFLD VRFSAHGSPY FEAEKLDSMV
     VGIQEKLEDE LGVRIYMVKI DECLIEKEQC EDSCRNVLIK NNVPLSVYTN TTSFVGVSAR
     VESECTCDVE EPLICLNGGT PFADKCECPE GWNGPHCEQT SIGFHGDGWA MYPSPPACHE
     GHVTLTVTSH TSNALVFYLG PLKFNPLLDV QDFMSLELVD GYPILLVNYG SGTTRLNNSV
     VHVADGKPHL IEIVLMRSSI EMFVDRCKLS TCMSLAAPTG PREILNVNGP LQLGGASVDL
     QSLARSFGWR YVPTNQHFMG CISNFTYNDY MYNLGKPSVE RNADPGCQKS VFTAVTFGID
     TNFLVAILVC IAILIILLLA VVVHRKRADA WAEKELDDIR ENIIAYEDEG GGEGDAGYDL
     HVLRQMYDGP PPDNEPAFMH VPVVGAAPDI SGFLDDKKSV LDRDPDINPY DDVRHYAYEG
     DGNTSGSLSS LASCTDDEDL KFNYLSTFGP RFRKLADMYG DDGEDRQHEE SWC
//
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