ID T1KBB4_TETUR Unreviewed; 2616 AA.
AC T1KBB4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Neural-cadherin {ECO:0008006|Google:ProtNLM};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur08g03490.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur08g03490.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; CAEY01001946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 32264.T1KBB4; -.
DR EnsemblMetazoa; tetur08g03490.1; tetur08g03490.1; tetur08g03490.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_000347_1_0_1; -.
DR OMA; DFFRCDC; -.
DR Proteomes; UP000015104; 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; 13.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.60; Cadherins; 14.
DR Gene3D; 2.10.25.10; Laminin; 3.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF445; CADHERIN-87A; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 12.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 14.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 14.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00232; CADHERIN_1; 4.
DR PROSITE; PS50268; CADHERIN_2; 14.
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:UP000015104};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2616
FT /note="Neural-cadherin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004580483"
FT TRANSMEM 2438..2460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..119
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 122..227
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 228..332
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 382..491
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 493..601
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 602..706
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 708..822
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 822..938
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 939..1038
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1039..1154
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1155..1265
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1266..1384
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1385..1489
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1489..1608
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1864..1902
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1903..2110
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2113..2152
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2155..2344
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2387..2425
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1892..1901
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2142..2151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2396..2413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2415..2424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2616 AA; 294290 MW; 5E1E1F5A3D1D7FD8 CRC64;
MAGWVWLFVI FYAPLCISSS TRSIKNFDFK ESEGSITGAT VFTLEKKQDA ERFELESPNR
WVTVEPNGDV KVKEPWDYEQ LNKDKTIDFW VLVKRQNYDT EKQHVVINVR DVNDEPPYFV
NRPLPMQAVV QLNAPPGTSV FKLQARDPDT GHNLHYFLVR DRTGGRFEVD ERSGEVRTRG
NEPFMLDQEY AIYVKAEDHA GTINDRQYQS TKEERLSIMG GTRPPQFYMP KYDATIPENQ
RKDSDIIEIK AKSFADREIR YTLRAQGKGA GTFNIGPTSG VVKLAKELDF EDLRQPKQYS
LIVTATEDSG GFSTTVELTI KVTDVNDNAP RFELPDYQAH NVHEDIDVGT KILETRRGCQ
QHLSNGCTIY TENKNDEPPK FSQDVYTPNV DENAGPSTLV TTVVASDKDG DAIHFGFANG
SNKSGVFEIE ERTGVIRLQS NPFSLDKDKY ELHITARDDG SCCKDGSRMI HTSTALVVVF
ITDVNDNKPV FEECGSYAPT AQEGAPAGTH VITVKATDSD KGHNGQVRYS IVQQPNQKGT
KFTVDEVSGE IKTNKVFDRE GEDGRFVSIT VKAVDKGVPP LEGVCSFKVE ITDINDNPPL
FDRQEYRENV KQDTQVGTNI LRVSASDDDA DNNGAILYNL TAGRDPSDLD YFYISPDSGW
IRLQRPLDRT NYNLQAIAVD KGIPQHTATV AIIIEVVDRA NNPPVWDQPV YGPVSVKENI
KVGETIQSVR ASSGIADNPT VFYTLIRGNT EQTNKHNHFY LTQRADDEGI WADLKVNYPL
DFEKLAHYNL TVRVENNGVQ QLASECTVYV VVEDVNDEIP LFTEREQETV LEGMPAGTKV
TQVHAVDRDG TKPFNQVYYA IEKSKDGSER FFTIDKESGE IFTKDEFDRE EKQAYAVLVR
AYDGAPSSRP GSKPNEPNSV TKYIRIGIGD KNDNPPYFDQ ALYEAEVNED EDIQHTVITV
TAKDKDESSK IRYEITRGNT GGAFAVKNET GAIYVAGPLD YETRKEYKLR LAASDNLNEN
YTQVVIRVKD VNDHPPVFDR PVYETQITEE DNTNLPKKIL QVTATDGDKD RPQGIVYFLT
GQGTEDKGLS DRKFEVNSTT GEIYVLKPLD RDLPRGRSQW RFTVFAEDEG GNGLVGFAEV
LVNLKDINDN APFFPSNIYT GNVTENGTAG MTVMTMTATD YDDINEGQNA KLRYSIEQNQ
VNENGELIFN IDEDTGVIST AVCCLDRETN PEYTIKVVAI DGGHLKGTGT ATIKIKDIND
MPPDFTKKEW YVEVDETEGD QLPEFPILVV SVNDGDLLET NRFNYKVEPG QFGSDKFTMV
TNNDGTGSLK VAKPLDYEDP RQRYGFNITI IVSDHGGETT DPSHISRAKV FIRPKDINDN
KPEFEKPNIE VTVIENSPIG QTLTKFAATD ADQGGKSKVS YMIDRSSDKK RQFTIDQEGI
VRIQRTLDRE DIPRHHVKIL AVDDGYPPRT ATATLTVIVG DVNDNYPRFL KDYRPVIMEH
EPPQKVEEIL ATDDDDRSKH NGPPFTFRMD PNAPDMIKNF FDLTHDHNGA NGDGMAIVRS
KVKFDREVQK EYQIPIIIKD NGTPSMTGTS TLTVIIGDIN DNKMNPGSKS IFVYSFKGHS
PPTEIGRVHV EDQDDWDLPD KKFLWEDHIA HENFELNAHT GMIMMKNVTE GSYFLRFKVF
DRKHTQEVLA NVTVTVREIP EEAIYKSGSL RVSGVTAEDF VRTYDWQTPT YQKISKYDKF
KNALSEIMKT KPDNIDVFSV ITRQERPPIT DIRFAVHGSP YYESTYLDGT VAVNRDHIER
EVGINITMVG IDECLIEGLC EGSCTNELKI SRTPVLVNAN RTSFVGVNTW IERKCVCGAR
DFSEPETCRK YPPPCANGGR CTDSSVGALC KCLKGYDGPQ CQVTTRTFNG HGWAWFPPLQ
QCQESHLSLD FMTPSPNGLI FYNGPIVRPD IGVQVVSDFI SLELYNGYPR LLIDFGSGTT
EVTVRTFGDL HDGEWHHIDI FWDKETVRMM VDHCSGTATD VKDSREPLHI DRSKCENISH
IVPFNEFLNV NSPLQLGGIY KLPEDLDQYF NWMYKPTKIG FTGCIRNFIH NSQMYDLGSP
GSLSNSMVGC QPAKDRCDSN PIARNCQHGT CVASYHNARC VCQPGYFGPR CDRETQSKMF
QHSSYIKYAL SFEPDPYKTD IQLMFRTRQK AGELFRATSK HGREYVILDI KDKKLRFRFN
LNSLKSSEER ELWLPNITVS DGQWHTVQVL RFGSTASIAL DGGGGRRFNE IIDYIGLHQL
MTVERQNVVA GGDVQYLGPG VTMVDNDFQE GCMNDIRLEQ RYLPMENGSE NAAVVEFRSL
IDGCPSNNPC HSVACSRPFV CYDLWLLPDC SCEPGFIRTE DQNNCTDANE CLTDPCLNGG
TCINRDKGQG FYCICPEGFS GDVCNALRQE KVMRLSNAAL ATILICLLNI LILLLVIFAY
SRTRRTDQKF GHGDMDDDVR ENIINYDDEG GGEDDMNAYD ITPLRIPIDP HGLKQDPKGT
LLKSGRQRQY PPGAHLDIGE FIQENLNKVD SDPNAPPFDD LRNYAYEGCG SNAGSLSSLA
SGNEDNEQDF DYLNGWGPRF QNLARMYERG ESKIED
//
