ID A0A1I8NR16_STOCA Unreviewed; 3805 AA.
AC A0A1I8NR16;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Protocadherin-like wing polarity protein stan {ECO:0008006|Google:ProtNLM};
GN Name=106087496 {ECO:0000313|EnsemblMetazoa:SCAU001284-PB};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU001284-PB, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU001284-PB}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU001284-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 RefSeq; XP_013108006.1; XM_013252552.1.
DR EnsemblMetazoa; SCAU001284-RB; SCAU001284-PB; SCAU001284.
DR VEuPathDB; VectorBase:SCAU001284; -.
DR OrthoDB; 4006628at2759; -.
DR Proteomes; UP000095300; 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; 9.
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; 2.60.220.50; -; 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; 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; 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; 3.
DR SMART; SM00180; EGF_Lam; 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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 9.
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 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 2984..3004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3016..3035
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3055..3075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3087..3107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3127..3147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3168..3190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3196..3219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 492..596
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 597..713
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 714..819
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 820..924
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 925..1027
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1028..1137
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1138..1243
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1244..1350
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1369..1469
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1612..1648
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1686..1883
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1886..1922
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1926..2092
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2094..2129
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2224..2271
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2256..2330
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2979..3220
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 45..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2747..2783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2814..2835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3252..3271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3276..3393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3454..3478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3519..3588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3661..3695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3708..3790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2749..2767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2768..2783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3276..3333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3375..3393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3551..3588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3672..3688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3708..3726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3736..3790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1638..1647
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1912..1921
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2098..2108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2119..2128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2224..2236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2226..2243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2245..2254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3805 AA; 422705 MW; 547FBADF54F67D57 CRC64;
MLLRPQTKEW LATSSLTSAA VKSVLSTSSS TVATTNASVA ASTSTSFSSS SFSSSSTSTP
TPTPKGLQPH VVTAFKPRQG FDNRQHNNRT PAALATTTTC RRSGFVRPSS ATAAAATLAS
AYTHLMLFAT IVCLTVQMSN AYLIIVHEDA TPGTVIFNAS VYKLGSERHY KINAHKSAHF
VHHLVAVNHK DGQIQLKKSL KCDGIYYPNL FTFYVDSTSN RLRSIDYYSL PIRIFVSGHT
CNEDRRVEEE MHARHYEEED TGYSKRRRKR FIEELDPVLE YERTYGEFRE SGVQANSLAL
NYNHNHSLNE FRDGDLLFGN SFDNEMRHRI LNRKRRSLLS SELATSSATS AINLHRRISE
AKQWISETYA SYAIHTTDKW NQICLRKSQF INNLNAFLPR SICQHCKVNF LDVNDERFVI
EHQNRDLVAS RDVCIHESIW KVSITFNIRC DRSDIVDSDH RLKIVYHYQE FNDTDIARRV
RRELRNQSPY FEQALYVASV LEEQPAGSSV TTVRARDPED SPVVYSMVSL LDSRSQSLFK
VDSRTGIVTT SASLDRELMD VHYFRVVATD DSFPPRSGTT TLQVNVLDCN DHSPTFEAEQ
FEASIREGAT VGSTVITLRA TDQDIGKNAE IDYGIESITD GTGTLQDQEI PIFRIDARTG
VIATRTSLDR ETSDSYNIVV TASDMASAQS ERKTATASVL VKILDDNDNY PQFSERTYTV
QVPEDQWGDD NVVAHIRATD ADQGNNAAIR YAIIGGNTQS QFSIDSMSGD VSLVKPLDYE
SVRSYRLVIR AQDGGSPSRS NTTQLLVNVI DTNDNAPRFY TSQFQESVLE NVPVGYNIIR
VQAYDSDEGA NAEIAYSILE RDDNFPLAVD ARTGWIQTIK QLDREEQNRF AFQVIAKDGG
VPPKSASSTV VITVQDVNDN DPVFNPKYYE ANVGEDQPPG TPVCTVTATD PDEDSRLHYE
ITSGNTRGRF AITSQNGRGL ITIAQSLDYK QEKRFLLTIT ATDSGGRADT ASVNINITDA
NNFAPIFENA PYSASVFEDA PIGTTVLVVS ATDSDVGINA QITYSLNDES INGLSSPDPF
SINAQTGAIV TSALLDRETT SGYLLTVTAK DGGNPSLSDT TDVEISVTDV NDNPPQFKNP
LYQASILEDA LVGTSVLQIS ASDPDIGLNG RIKYLLSDRD VEDGSFVVDP TSGTIRTNKN
LDRESVAIYH LTAIAVDKGS PAMSSTVEVQ IRLEDVNDSP PTFPSDKITL YVPENSPVGS
VVGEIHAHDP DEGVNAVVHY SIIGGDDSNS FSLVTRPGSE RAQLLTMTEL DYESNRKRFE
LVIRAASPPL RNDAHVEILV TDVNDNAPVL RDFQVIFNNF RDHFPSGDIG RIPAFDADVS
DKLTYRILSG NNANLIRLNQ TTGGLSLSPQ LNTNVPKFAT MEVSVTDGIN EAKAIMQLAV
RLITEDMLFN SVTVRLNEMT EEAFLSPLLN FFLDGLAAII PCPKENIFIF SIQDDTDVTS
RILNVSFSAK RPDVSHEEFY TPQYLQERVY LNRAILARLA TVEVLPFDDN LCVREPCLNF
EECLTVLKFG NASDFIHSDT VLFRPIYPVN TFACSCPEGF TGSKEHYLCD TEVDLCYSDP
CHNGGSCVRR EGGYTCVCPP SHTGVNCEND IKKLKPCMSD ICEGGLSCMN NYMSSQPPPY
TPTCELRSRS FSRNSFLTFE SLKQRHRFNV KLRFATVHEN GLLLYNGRYN ELHDFVALEV
VQGHVTFTFS LGDRSEKVAV VQNRKVSDGQ WHEVELVYLN RTVTLIVDKC DTAIALAGNL
GNRWNCANQT TLKLDKRCAL LTETCHRFLD LTGPLQIGGL PRIPAHFPID NQDYVGCISD
LRIDERYIDL NSYVADNGTI SGCPQRNPLC SSEPCFNGGA CHEGWNTYTC ECPEGYAGNN
CQESIPAPWR FSGDGSLSFN PLLRPIQMPW VTSLALRTRQ RNAFLIQIQI GQNSSAVICL
KDGILYYIFD NEPMFLAGAF LADGEWHRVE IKWMGSELMF SVDFGQRSGA VPVAQKIQGL
YVGKIVIGSA DSSIGHVDDL LPYEGCIQEV RIGASQAVLS RPTIRENVED GCLSKAECPA
MCTAHSSCTT SWDHAECECL PGYVGPDCLP ICTVKPCVAG VCRANISEPK GYRCECNSTY
QHGEYCEKTV QQPCPGGWWG EKVCGPCKCN VKQGYHPDCH KTTGHCHCKT NHYQPPNETA
CIPCDCYSIG SFNSACNPLT GQCECREGVI GRRCDSCSNP YAEVTLNGCE VVYDACPRSF
AAGVWWPRTP LGSTTVENCP APSRGKGQRS CNILSGGWNV ADMFNCTSEP FVELRKQLSQ
LEKLELELNS FVAIKTAENL QKACTTVDRS TKVHKKPSNK DHRRYKMESS FLLNEQHAAT
NIKDNNVWSH ELELEYLSDE MKFSHDRLYG ADLLVTEGLL QELINYELMQ NGLNLTHSQD
KYFIKNLVEA ASVILDRKYA GEWRRASELI QRGPDDLLDA FNKYMVVLAR SQHDTYTSPF
EIVQPNMAFG LDIVTAESLF GYEPEQLSEY HKTKYFKPNA FTTESIILPD TSGFLQHSAK
QKPVITFPKY NNYIQDKTKF DKFSKVLVPL DMLGITPPES NEVTYGSGND YKAIVSYAQY
KDVGQLLPDM FDETITRRWG VDIEVASPIL SLAILVPSTE AEEKRIEIPY RKISTQKTYS
ATGSSEQEFI EVFDVPKKHG QGQTSAAASN SGSEEHMIEN IRITAHEIPP ATSVSSASSS
SSSSSREHDS NEAVEIEDGE EPHINVHFED NIEFHGNSGE EVIISSPEDM AHEYDQSQEM
HEEHESEEHS SKGENEAFYR HRRLVKRQVE VIYPSEQMQT PQHISYRSLG SPHLSQPIKL
QMWLDIEAAR FGPRSNPQCV RWNSFTNQWT RLGCQTDIPD YESMHLAASA AGASTSASGS
NSSPAPAIIV NCTCTHISNY AVIVDVIDPE DIPEPSLLVQ ITSYSAFLVS LPVLLSVLIA
LALLRGQQTN SNTIHQNIVL CVFFAELLFF VGMQSRRNLL ENEFPCKLIA ICLHYFWLAA
FAWTTVDCVH LYRMLTEMRD INHGPMGFYF AMGYGAPAIV VGLSVGVRAH EYGNSLFCWL
SVYEPVVWWL VGPIAGMSVV NLLILFVSVQ AAFTLKDHVL GFGNLRTLLW LSVVSLPLMG
VMWVLAVLAA SESSQLLSML LSGVVVLHAI FCLVGYCIIN KRVRENLQRT FLRCMGRKVP
LLDSSMVVSN SSHNVNGGQA RPNNFLNANG YDTQRRNVGI SVSSTTSRST AKTSSSPYSD
GQLRQTSTST SNYNSNSDAP SFLRGFDSST TSGQRENKSR RHHRKDSDSG SETDGRSLEL
ASSHSSDDDE SRTNRSSTTG TATSTHRSTA VSITPSYLPN ITEHVQATTP PELNVVQSPQ
LFPSVNKPVY AARWSSQLPD AYLQSPANVG RWSQNTESDN EHVHHGQKIT ISPNPLPNPD
LTDTSYLQQH HNKINMTPSI LENLQNARPS ESYDALERES LYGRRPDNYV QYDGLPPNIT
NYKPPSHYGS EHDYNGSNGN NSSSNGSNHT SNGTGNGANG NGGTQIVNHM RTFNNDNAYL
SDSIYDKQPR TLGSPYMSKD RIAPDIYGSR ENHYSLKKHQ PPPMYGADSV HSVHSLLRND
YHHQQQQHQQ QRLHQQDHHS DRLSENSDKN GYHFPYTAEE DHLTTTARKL SLQHSHSSSL
HGSSHQILNG HHPHHMTAPN NGSHSMVNDI NNPGLMGRHT LNGSRHSSRG SSPPTSSIAP
MQPLAPLTSI TDTDSSWSWD RLKKI
//
