ID B0XD21_CULQU Unreviewed; 3396 AA.
AC B0XD21;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=Neural-cadherin {ECO:0000313|EMBL:EDS45256.1};
DE Flags: Fragment;
GN ORFNames=CpipJ_CPIJ017258 {ECO:0000313|EMBL:EDS45256.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS45256.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS45256.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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; DS232735; EDS45256.1; -; Genomic_DNA.
DR RefSeq; XP_001867543.1; XM_001867508.1.
DR STRING; 7176.B0XD21; -.
DR KEGG; cqu:CpipJ_CPIJ017258; -.
DR VEuPathDB; VectorBase:CPIJ017258; -.
DR VEuPathDB; VectorBase:CQUJHB007609; -.
DR eggNOG; KOG4289; Eukaryota.
DR InParanoid; B0XD21; -.
DR OrthoDB; 4006628at2759; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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; cd15441; 7tmB2_CELSR_Adhesion_IV; 1.
DR CDD; cd11304; Cadherin_repeat; 9.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR PANTHER; PTHR24026:SF51; PROTOCADHERIN-LIKE WING POLARITY PROTEIN STAN; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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 G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2702..2722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2734..2753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2773..2793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2805..2825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2845..2865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2886..2908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2914..2937
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..438
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 439..555
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 556..662
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 663..767
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 768..870
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 871..980
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 981..1086
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1087..1193
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1455..1491
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1530..1726
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1729..1766
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1770..1937
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1939..1974
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1975..2013
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2070..2116
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2089..2175
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2697..2938
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 2540..2564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2993..3110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3166..3187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3330..3396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2993..3038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3045..3078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3086..3104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3344..3359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3360..3375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3376..3396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1481..1490
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1756..1765
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1943..1953
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1964..1973
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2070..2082
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2090..2099
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDS45256.1"
FT NON_TER 3396
FT /evidence="ECO:0000313|EMBL:EDS45256.1"
SQ SEQUENCE 3396 AA; 380506 MW; 517385D2D9F2138C CRC64;
LFPYVSSYMV ILNENDNPGK IVFNASVYKL GSERHYKINA HKSAHFVHHL LNIDAKNGEI
SLRRPVRCDG IHYPSLFTFY VDSTSNRLHS IDYYSLPLRI FIVGINCIDD AEAESFRKLF
MEDDAGKNHR FKRRLTTNGL FEGGLVNTQH LKSSNITSYT TLQDGDVLFE TIENNKHRSE
IISRKKRSSP ISSDERIHRK INEARQWISE TFASYAIHTT DKWNQICLKK SQYINSVNSF
LPKTVLKYCT VKYIDVNNGL FKIEPHSGDL VASGDVCISE SWKLSITFSV KCDRMDVVDA
DHRLKVIYHH QNLNDTDIAT RVKRELRNQS PYFEQALYVV SAQEEQPAGT EITTVRARDP
EHSVVSYTMV SLLDSRSQSM FQINTKSGTV KTVAILDREV MDVHYFRIIA TDDSFPPRSG
TSTLQVNVLD CNDHTPAFES EEFHANVREG TSVGSSVITI RATDQDIGKN GEIEYSIASV
SGDNVTVGEN ADNLFRIEAR TGTITTRGAL DREISEMYVI QVMATDMAIP QSERKSTTAT
VFVNVLDDND NYPQFSERTY TVHVSEDQWT NENNVIAQIR ATDADKGNNA AVRYAIIGGN
TQSQFSMDSI SGDVLLVKPL DYESIRSYRL VIRAQDGGSP SRSNTTQLLV NVQDANDNAP
RFYTTQFQEA VLESVPVGYN IVRVQAYDSD EGVNSEISYR IQDRDENSPL AIDSRTGWIH
TTSPLDREEK SRYVFQVVAI DGGIPPKSAS TSVVVTIQDI NDNDPIFNPK YYEASIAEDQ
PPGTPVTTVT ATDLDEDSRL HYEITSGNTR GRFSITSQNG RGLITIAQSL DYKQEQRFAL
TVSATDSGQR SDQAIVNINI TDANNFAPVF ENAPYTASVF EDAPVGTTVL MVFASDNDVG
LNAQITYSLN EGSSNGLGSN EPFSVHVQTG AIVTTAALDR ETTSTFLLTV TAKDSGNPSL
ADTTDVEISI TDINDNSPQF DVPLYQATIA EDAFIGTSVL QISATDDDMG LNGRVKFMLS
SKDVEDGSFV IDPSSGVIRT NKGLDRESIA VYHLIAIAAD RGTPTLSSSV EVQIRLNDIN
DSPPTFASDK LTMYVPENSP VGSAIGEIYA HDPDEGVNAI VHYSIIGGDD LNAFSLVTRP
GSERAQLLTM TELDFESNKK RFELVVRAAS PPLRSDVLVE IFVTDVNDNA PTLRDFQIIF
NNFKDCFPSG IIGRIPAFDA DVTDRLNYRI LSGNNANLVL LNSSTGGLTL SPQLNTNVPR
FATMEVSVND GINEAKAIMQ LIVRLVTEDM LFNSITVRLN EMTEEAFMSP LLNFFMDGLA
AIIPCPRENI YLFSIQDDTD VNSRILNVSF SARKSNLAAE EYYSPQYLQE KVYLNRAILA
RLATVQVLPF DDNLCVREPC LNYEKCLSVL KFGNASGFIS SETVLFRPIH PVNTFACKCP
EGFTGSKEHY LCDTEVDLCY SEPCQNGGSC VRNEGGYTCV CTALFTGVSC ETEINSLKSC
AAEVCGEGYS CLADKQTMSH SPLYTKTCEL MARSFTRNSF LTFPSINKRH RLNIQLKFAT
MRDNGLLLYN GRYNDENDFI ALEIINGRVT FSFSLGERIE SVMVDQHKKV SDGNWHTVEV
NYFNRSVQLS IDNCDTALAY SNLGQSWNCA NRTTLVLERR CASLTESCHR FLDLTGPLQL
GGLPKIATQF QIHSHDFIGC IKDVYLDHRY VDLNSYIADN GTIAGCPQKS ASCSSEPCFN
GGTCREGWGE GWQCECLDGF SGNACQETVA LPWRFNGDGI LSFNPLLRPI QLPWLTALTI
RTRQKDAFLM QIQIGQNSSA VLSLRNGVLY YTYNSSPMFL TGTNLADGQS HRIEVKWLMS
NEISLSVDYG QQTGVLPMTQ KIQGLYVGRI MIGGTDGNLP NEDNDGYFKG CIHDVRIGNS
QSILNRPTIR ENVIDGCTSN ARCPESCPEH STCVKNWDQS YCECKQGYVG VNCAPVCTVH
PCHENGRCRY DKMARKGYVC ECNSTTSSGE YCEIIVEKPC PAGWWGERGC GPCKCNVKNG
YHPVCNKNTG ECFCQEHHYQ LSKDSACLAC ECYAIGSYGK SCSSTGQCEC REGVIGRRCD
SCSNPYAEVT LNGCEVVYDA CPKSFAAGLW WPRTSFNEVA IENCPSAARG KVTRKCDLEN
GGWGQPDVFN CTSEPFLNLR KQLSQIETKE LEINTFVSVK IAATLEDACD RIGRVDEDHS
KNEQNRYLYI FEGEQASNNI FWEANEFGFS YLSDERNKKQ HSFYGSDLLI TERLLHELLN
YESNQSGLNL SHSQDKHYIK NLVTSAGMIL DKRYKQEWKR LTELTQRNPN DLVEAFNRYL
MILGKSQQDT YTDPFEIVQD NMVFGLDVVD EESHLQHETQ LHVINRNSQK LDTQKTEHES
RKQKLSMISF PKYNNYIQDK NKFDLYSKII VPLENRSNNV RGHRAIVGYA QYKDAGDIYA
ANFDETIMRR WGVEVIIASP LISINILVPN NIKKTEEKPS FNDVSQYKEN DNISDTLLNH
DNEKISNDLK VSIHDLSGQQ DLNIQGNGEK EENNNPFEDS SIPNTLSISS ENINAYRLEG
KTKRSVIQQY MDAGQYNTLI EYKPIGNPYL THPIKLQMWL QVPRHKFGPR SNPQCVRWNS
HMNFWTRLGC QTEVPPYEHF SWNQTILITC TCNQISSYAV LIDVTDPDDI AEPSMPVRIT
SYSAYVLSLT MLFSVILSLA LLRGLQTNSN TIHQNLVFCI FIAELLFFAG TNARQTLIVN
EFACKLVAIA LHYAWLAAFA WTTVDCVHLY RMLTEMRDVN HGPMGFYYAL GYGSPALLVG
LSIGVRAHEY GNSVFCWLSV YESVIWWLVG PVVAMSVISL LILFMSVKAA FTIKDHVLEF
GNLRTLLWLS VVSLPLMGIL WVLSVLVASE SSQMLQVLLS GSVIVHALFS VVGYCIINKR
VRENLHRSFL ICTGRKVPLL DSSMAISISS QNVGPTTKTP GFTGHYETAR RNIGISASST
TSRSTTKTSS IPYRSDSQFR HTSTSTSNYN SNSDGGPTYV RGYESRGMRK SKVTGQDGTS
HHQKDRHHKR DSDSGSETDG RSFELASSHS SDDEESRVGR NSSTHRSNER NSTFYLSNIM
EHVATTPPEL HVVQSPQLFP NVNDPRWSNR VPDSYINRPN VGRWSQETGS DNEMHPQNVT
STLPRPDLTD TSYLLQDRMG VQPSLLENIH ESCNFSSQNF MHENNSHNIR EYRDFEDIPQ
HITMPYIADA GTNNLPGSAQ VVNHMRAYNY DTPYTMKDIC YDPSKTNNSI PQSSYIGKER
ISSELYSPRI DNVGSFKSSV QSLLKNDYQR HKQHNETDRM SESSDKNPYN FPYTAEEDHS
SHNYATRHED TRRHQLNNPS SIQPEASLTI VNNDTE
//
