ID E2BTW3_HARSA Unreviewed; 1625 AA.
AC E2BTW3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Neural-cadherin {ECO:0000313|EMBL:EFN80862.1};
GN ORFNames=EAI_11895 {ECO:0000313|EMBL:EFN80862.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN80862.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN80862.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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:PRU00076}.
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DR EMBL; GL450531; EFN80862.1; -; Genomic_DNA.
DR STRING; 610380.E2BTW3; -.
DR EnsemblMetazoa; XM_025298006.1; XP_025153791.1; LOC105186472.
DR InParanoid; E2BTW3; -.
DR OMA; EPWCAKV; -.
DR Proteomes; UP000008237; 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:0030154; P:cell differentiation; 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; cd00053; EGF; 1.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.60; Cadherins; 7.
DR Gene3D; 2.10.25.10; Laminin; 2.
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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
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; 4.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 7.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 6.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
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, 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 Reference proteome {ECO:0000313|Proteomes:UP000008237};
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 1451..1474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..50
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 51..166
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 167..278
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 279..397
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 398..502
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 502..621
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 878..914
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 915..1121
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1129..1164
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1167..1358
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1401..1439
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1555..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 904..913
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1154..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1410..1427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1429..1438
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1625 AA; 182866 MW; 0A79EB1A8A64D094 CRC64;
MTGAIYVAGA LDYETRKRYE LRLTASDNLK ENYTTVVIHV KDVNDNPPVF ERPNYRTQIT
EEDDRTLPKR VLGVTATDGD KDRPQNIVYF LTGQGIDADN PTNSKFDINR TTGEIFVLKP
LDRDQPNGRP QWRFTVFAQD EGGEGLVGYA DVQVNLKDIN DNAPIFPQGV YFGNVTENGT
AGMVVMTMTA VDYDDPSEGT NARLVYSIEK NVIEEETGSP IFEIESDTGV IKTAVCCLDR
ERTPDYSIQV VAMDGGGLKG TGTASIRVKD INDMPPQFTK EEWFTEVDET EGPDLPEMPI
LTVTVHDEDE TNKFQYKVIE SSGYGADKFT MVRNNDGTGS LKIVQSLDYE DQLQSNGFRF
RIQVNDKGED NDNDKYHVAY SWVVVKLRDI NDNQPQFEKA NIETSVAENA RIGSTLETFK
ATDPDQGGKS KVSYSIDRSS DRKRQFFINE NGTVSIQRSL DREETPRHQV KILAIDDGIP
PKTATATLTV VVQDINDNPP RFLKDYRPVL PEYAQTKKVV EILATDDDDR SRSNGPPFTF
RMDPNANDVI RASFKVESDN KGANGDGMAV VSSLRSFDRE QQKEFLIPIV IKDSGNPSMS
GTSTLTVIIG DVNDNKMQPG SKEIFVYNYA GQSPDTEIGR VYVYDLDDWD LPDKKFYWEG
LEHNQFKLDE DTGMIYMKSG THDGKYHLRF KVYDRKHTQT DVPANVTVTV KSIPHEAVLN
SGSVRISGIT DEDFIRVWNY QNQTLSRSKV DLFRDKLSHL LNIDRDNVDV FSVQLRRMHP
PLTDVRFAAH GSLYYKPVRL NGIVLMHREE IEKDVGINIT MVGIDECYYE NEMCEGSCTN
TLDISSLPYM VNANRTALVG VRVDVIAECT CGARNFSKGE SCRNSPCYNG GRCVEDRFGL
SCQCPSGYNG PRCQQTARSF RGNGWAWYPA LEMCDNSHLS FEFITRKSDG LLLYNGPIVP
PESDEIMVSD FISVELERGI PRLLIDFGSG TLELKVKPKK TLDDGEWHRL DIFWNTETVK
LIIDYCKSAE ISELEDGSPP EFNDTSCQAQ GTVPPFNEYL NVNAPLQIGG LYVEQFDPTH
YKWKHMPVGK GFDGCIKNLF HNSKLYDLAH PGLSRNSVAG CPQTEEICNN QESTFRCWEH
GTCVGSFTEA RCQCNPGWTG PGCMTPTIPT TFKPQSYAKY ALSFEPDKYS TQVQLRFRTR
EIHGELFRVS DQHNREYAIL EIKDSRLHFR YNLNSLRTEE RDIWLSAIAV DDGQWHTVRV
SRYGSAATLE LDGGEGRRFN ETFSFEGHQW LLVDKQEGVY AGGKAEYTGV RTFEVYADYQ
KGCLDDIRLE GKHLPLPPAM NGTQWGQATM ARNLERNCPS NKPCANVICQ DPFECIDLWN
EYDCTCGEGR IPSPDNKGCM DKNECIDYPC LNGGRCINQD PRFRYRCICP DGFWGENCEL
VQEGQTLKLS MGALAAILVC LLIILVLVLV FVVYNRRREA HIKYPGPDDD VRENIINYDD
EGGGEDDMTA FDITPLQIPI GGPIPEMGGK LPPCKVTYPL GPEPNVGIFI EDHKKRADSD
PNAPPFDDLR NYAYEGGGST AGSLSSLASG TDDEQHEYQY LGAWGPRFDK LADMYGPAEE
SEEED
//
