ID A0A0L0BPI5_LUCCU Unreviewed; 3725 AA.
AC A0A0L0BPI5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Protocadherin-like wing polarity protein stan {ECO:0000313|EMBL:KNC21967.1};
GN ORFNames=FF38_12122 {ECO:0000313|EMBL:KNC21967.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC21967.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC21967.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC21967.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC21967.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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}.
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:KNC21967.1}.
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DR EMBL; JRES01001567; KNC21967.1; -; Genomic_DNA.
DR STRING; 7375.A0A0L0BPI5; -.
DR EnsemblMetazoa; KNC21967; KNC21967; FF38_12122.
DR OMA; YTFLRGN; -.
DR Proteomes; UP000037069; 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: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; 8.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
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; 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; 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; 5.
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; 2.
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; 3.
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 Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
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 2910..2930
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2942..2961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2981..3001
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3013..3033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3053..3073
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3094..3116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3122..3145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 460..564
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 565..681
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 682..787
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 788..892
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 893..995
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 996..1105
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1106..1211
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1212..1318
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1580..1616
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1654..1851
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1854..1890
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1894..2060
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2062..2097
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2192..2239
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2224..2298
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2905..3146
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 2739..2769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3201..3321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3381..3413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3428..3516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3590..3725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2746..2765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3201..3260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3261..3282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3304..3321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3460..3516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3595..3631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3632..3653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3672..3713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1606..1615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1880..1889
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2066..2076
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2087..2096
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2192..2204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2194..2211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2213..2222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3725 AA; 415386 MW; 907F4BDA0A9DA60D CRC64;
MHFHQQHHLQ KHGLPSTAIA TTTTKTSSSS SSASFHSSSQ SSKSFFSSCS TVKTSKTKGT
FMKITNKTSC CSCSNISSCC PHSKATRTSS PALQLLLKHI LILLLTICHT VQITNAYLII
VHESTEPGTV IFNASVYKLG SERHYKINAH KSAHFVHHLV AVNHKDGQIQ LKKSLKCDGI
YYPNLFTFYV DSTSNRLRSI DYYSLPIRIF VSGHTCNEDR RVEEEIHARH YEEEDNGYSR
RRKRRDLLEL EDDLSNSKSL QPITTITSNT LDLYNHNHSR NDFREGDLIF GDAYDNEMRH
RILSRKRRGF SDINPFALET NLHRRITDAK QWISETYASY AIHTTDKWNQ ICLRKSQFIN
NLNAFLPRSI CQYCKVNFLD VNDERFAIEH QNRDLVASRD VCIHESMWKV SITFNIRCDR
NDIVDSDHRL KIVYHHQEFN DTDIAKRVRR ELRNQSPFFE QALYVASVLE EQPAGSTVTT
VRARDPEDSP VVYSMVSLLD SRSQSLFKVD SRTGVVTTSA SLDRELMDVH YFRVVATDDS
FPPRSGTTTL QVNVLDCNDH SPTFEAEQFE TSIREGATVG STVITLRATD QDIGKNAEIE
YGIESVTDGT GTLQDQEIPI FRIDARSGVI ATRTSLDRET SDSYNIVVTA SDMASAQSER
KTATASVLVK ILDDNDNYPQ FSERTYTVQV PEDRWGDDNV VAHIRATDAD QGNNAAIRYA
IIGGNTQSQF AIDSMSGDVS LVKPLDYESV RSYRLVIRAQ DGGSPSRSNT TQLLVNVLDT
NDNAPRFYTS QFQESVLENV PVGYNIIRVQ AYDSDEGANA EIQYSILERD DNFPLAVDSR
TGWIQTIKQL DREEQSRFAF QVIAKDGGIP PKSASSTVVI TVQDVNDNDP VFNPKYYEAN
VGEDQPPGTP VCTVTATDPD EDSRLHYEIT SGNTRGRFAI TSQNGRGLIT IAQSLDYKQE
KRFLLTITAT DSGGRADTAT VNINITDANN FAPIFENAPY SASVFEDAPI GTTVLVVSAT
DSDVGINAQI TYSLNEESIN GLSSPDPFSI NPQTGAIITN ALLDRETTSG YLLTVTAKDG
GNPSLSDTTD VEISVTDVND NPPQFKNPLY QASILEDALV GTSVLQVSAS DPDIGLNGRI
KYLLSDRDVE DGSFVIDPTS GTIRTNKGLD RESVAIYHLT ALAVDKGSPS MSSSVEVQIR
LEDVNDSPPT FPSDKITLYV PENSPVGSVV GEIHAHDPDE GVNAVVHYSI IGGDDSNSFS
LVTRPGSERA QLLTMTELDY ESNRKRFELV IRAASPPLRN DAHVEILVTD VNDNAPVLRD
FQVIFNNFRD HFPSGDIGRI PAFDADVSDK LTYRILSGNN ANLIRLNQTS GGLSLSPQLN
TNVPKFATME VSVTDGINEA KAIMQLAVRL ITEDMLFNSV TVRLNEMTEE AFLSPLLNFF
LDGLAAIIPC PKENIFIFSI QDDTDVTSRI LNVSFSAKRP DVSHEEFYTP QYLQERVYLN
RAILARLATV EVLPFDDNLC VREPCLNFEE CLTVLKFGNA SDFIHSDTVL FRPIYPVNTF
ACSCPEGFTG SKEHYLCDTE VDLCYSDPCE NGGSCIRREG GYTCVCPASH TGVNCETDIR
KLKPCMSDIC EGGLSCMNNY LSSQPPPYTA TCELRSRSFS RNSFLTFESL KQRHRFNVKL
RFATVHENGL LLYNGRYNEL HDFIALEIVQ GHITFTFSLG DRIEKVSIVQ HSKVSDGQWH
EVEVVYLNRT VTLILDNCDT AIALAGNLGE RWNCANQTTL KLDKKCSLLT ETCHRFLDLT
GPLQVGGLPR IPAHFPIENQ DYVGCISDLR IDERFIDLNS YVADNGTISG CPQKNPLCSS
EPCFNGGVCR EGWNVYTCEC PEGYAGNQCQ DTIPAPWRFA GDGSLSFNPL LRPIQLPWVT
SLSLRTRQED AFIIQIQIGQ NSSAVICLKN GILYYIYDNE PMFLAGAYLS DGEWHRIEIK
WQSSELQFSV DFGQRVGSVP ISQKIQGLYV GKIVIGNADS SIGHVGDLLP YEGCIQDVRI
GAAQSVLSRP TIRENVEDGC ISKAECPQSC PSHSTCTTSW DESKCECLPG YVGSECLPIC
TVKPCAAGVC RANISDLRGY HCECNSTYQH GEYCEKTVQQ PCPGGWWGEK VCGPCKCNVK
QGYHPDCHKT TGQCHCKTNH YQPPNETACI PCDCYSIGSF NSACNPLTGQ CECREGVIGR
RCDSCSNPYA EVTLNGCEVV YDACPRSFAA GVWWPRTPLG STTVENCPTP AKGKGQRTCD
NLSGGWNIPD MFNCTSEPFV ELRKQLSQME KLELELNSFV AIKTAENLQK ACITVDRTKV
QKKPPIKDHR RYKMESSFLL NENNNVWSNE IEMEYLSDEM KFSHDRLYGA DLLVTEGLLQ
ELINYELMQN GLNLTHSQDK YFIKNLVEAA SVILDRKYGQ EWKRASELIQ RGPDDLLDAF
NKYMVVLARS QHDTYTNPFE IVQPNMAFGL DIVTMESLFG YEPEQLSEYH KTKYLKPNAF
TTESVILPDT SAFLQHSAKQ KPVITFPKYN NYIQDKTKFD KYTKVLVPLD MLGISPPESN
EVTHGSSDYK AIVSYAQYKD VGQLLPDMFD ETITRRWGVD IEVASPILSL AILVPSTEAE
EKRIEIPYRK ISSQKTFSVS GSSEQEFIEV FDVPKKPGQS SGNSASGSEE HMIENIRITA
HEIPPPSSKA EDSNEAVEIE DVEEPHLKVR FDDNIEFHGN SGEEVIDSPE NMNGGNNNNN
NYEGSIEHED SMEKGENEAF YRNRRLVKRQ VEVIYPNEQQ QQNKHITYRS LGSPHLSQPI
KLQMWLDIDV TRFGPRSNPQ CVRWNSFTNQ WTRLGCQTDI PDYENMHLLP PQPILVNCTC
THISNYAVIV DVIDPEDIPE PSLLVQITSY SAFLVSLPVL LSVLIALALL RGQQTNSNTI
HQNIVLCVFF AELLFFVGMQ SRRNLLENEF PCKLIAICLH YFWLAAFGWT TVDCVHLYRM
LTEMRDINHG PMGFYFAMGY GAPAIVVGLS VGVRAHEYGN SLFCWLSVYE PVVWWLVGPI
AGMSIVNLLI LFVSVKAAFT LKDHVLGFGN LRTLLWLSVV SLPLMGVMWV LAVLAASESS
QLLSMLLSGV VVLHAIFCLV GYCIINKRVR ENLQRTFLRC MGRKVPLLDS SMVVSNSSHN
VNGTTRPNNF LNANGYDTQR RNVGISVSST TSRSTAKTSS SPYSISSPSD GQLRQTSTST
SNYNSNSDAP SFLRGFDSST TSGQHERKSR RHRKDSDSGS ETDGRSLELA SSHSSDDDES
RTNRSSTTGT GTSTHRSTAV SITPSFLPNI TEHVQATTPP ELNVVQSPQL FPSVNKPVYA
PRWSSQLPDA YMQPPANMGR WSQETGSDNE HIHHGQKITI SPNPLPNPDL TDTSYLQQHH
NKINMTPSIL ENLQNARPTD SYDGLERESL YGRRPDNYVQ YEGITSNISN YKPPSHYGSE
HDYNGSNNGN QSNGSNGSGN IANGNNGSNG GGGGTQIVNH MRTFHNDNAY LSDSIYDKQR
TIGSPYMSKD RIAPDIYGSR ENHYSLKKQQ PIYAGDSVHS VHSLLRNDYQ QQQRHLQQHN
DHHSDRMSEG SDKNGYHFPY TAEEDHLSSA RKLSLQHNPS PALHSSQQIL NGHQTHHHGH
HAGGMVNDIN NPGLMNRHTL NGSSRHSSRA SSPPSSSIVA PMQPLAPLTS ITDTERNIDD
DETTV
//
