GenomeNet

Database: UniProt
Entry: A0A195DSY6_9HYME
LinkDB: A0A195DSY6_9HYME
Original site: A0A195DSY6_9HYME 
ID   A0A195DSY6_9HYME        Unreviewed;      3164 AA.
AC   A0A195DSY6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Protocadherin-like wing polarity protein stan {ECO:0000313|EMBL:KYN15907.1};
GN   ORFNames=ALC57_11876 {ECO:0000313|EMBL:KYN15907.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN15907.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN15907.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN15907.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN15907.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ980487; KYN15907.1; -; Genomic_DNA.
DR   STRING; 471704.A0A195DSY6; -.
DR   Proteomes; UP000078492; 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; 2.
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; PF01825; GPS; 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; 9.
DR   SMART; SM00181; EGF; 7.
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   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 8.
DR   PROSITE; PS00022; EGF_1; 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..3164
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008270528"
FT   TRANSMEM        2507..2528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2540..2558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2578..2598
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2610..2630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2650..2670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2691..2713
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2719..2742
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          262..366
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          367..483
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          484..590
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          591..701
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          702..804
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          805..912
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          913..1016
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1017..1123
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1386..1422
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1468..1668
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1671..1707
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1711..1875
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1877..1912
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1913..1952
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2009..2056
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2041..2115
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          2502..2743
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          2805..2906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2973..3019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3056..3103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2805..2846
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2847..2878
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2973..2997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3056..3097
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1412..1421
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1697..1706
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1881..1891
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1902..1911
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2009..2021
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2011..2028
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2030..2039
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   3164 AA;  348263 MW;  77FD7F9922079B62 CRC64;
     MARWRWMLLI LTTIWTLGDG YLTVLPSSTP VGTVVFEAGV PQLGGRRKYE ASSERTAWFA
     RKLLKVHPHT GRVTLAKTLS CEGLQYPRVF TFYVDSTSSR LGRPTIDYYS LPLRILITGC
     GGENHDLAAT RGWMAETLAS YAMPSTDRFT EVCLRTSQLV AALRDFLPQT TLKECETRWG
     GVADPRFLVE GAAGDLVSAT EQCLVDPLWK VSVSMNLRCT GDSRLTDAEH RLKIVFHHHQ
     LDDTDLGRRV RRELKNQSPY FEQHLYLAAV EEEKEPGMYV TSVKARDPEN GAVRYSMSSL
     VDARSQALLA LDPVTGRVTT RARLDRENVD VHYFRVLAVD DSFPPRTGTT TLQVNVLDAN
     DHTPSFEGPE YDASVREGVP VGSTVITVKA TDQDTGRNAE VEYSIVSITA GSSITHMEDA
     ATFRIDPRSG VVTTRTPLDR EQTEIYTVVL SVTDQATPPS TRRSSNATLV VRVLDDNDNY
     PQFTERTYSA TVPEDLDYTT NPVIARIRAM DADAGANAAV RYAIIGGNTQ NTFSIDSMSG
     DVALVKPLDY ESTRSYKIVI RAQDGGSPAR SNTTQLLVMV RDVNDNAPRF YTSHFQEAVS
     ESVPVGYSIL RVQAYDADEG NNALIKYTIG ARDFTGASTE NFPITVKAET GWIYTTKQLD
     REQCSKYQFT VIAADSGEEP KSASATVFLT VTDVNDNDPY FEPKTYEAVV SEDSLAGTPV
     TTVTATDPDE DSRIHYEITG GNTRGRFSIS SQNGRGLITI AQTLDYKQEK RFVLTVTASD
     TGSRTDTALV YVNVSDANNY SPEFENAPYS VSVFEDAPIG VTVLVVSATD ADVGKNAQIT
     YSLATDNGEQ VITEFTINPQ TGAITTTKAL DRESVPSYLL TVTARDGGVP SLSDTTDVEI
     SVTDVNDNAP VFEAPHYHGS ILEDVLLSTS VLRVAATDAD TDLNGRVKYG LEDDGDGAFT
     IDSTTGIIRT AKILDRESVA YYTLKAVATD RGSPALSSVV PVTIKIEDIN DSPPAFENDK
     IILYIAENSP IGSTVGEIYA HDPDEGPNAV VQYSIIGGED SNSFSLNVRQ GADRAELITL
     EELDYESPKK KFELVVRAAS PPLRSDAVVQ ILVTDVNDNA PVLKDFQIIF NNFKDFFPTI
     PIGRIPAVDA DVTDNLVYSI LAGNNANLID LNRTSGEIRL SPQLNTNVPR VATMEVAVTD
     GINEAKATMT LSVRLITDEM LLNSITVRLD DMTVEAFLSP LLGYFLDGLA AIIPCPRENI
     FLFSVQEDAN VQGKILNVSF SARKVEPGTV DEFYSPQFLQ ERVYLNRGIL ARLATVTVLP
     FDDNLCVREP CLNFEECLTV LKFGNASGFA SSDTVLFRPI YPVTTFACRC ARGFTGSREA
     YMCDTEVNLC YSNPCMNGGI CHRREGGYSC TCQPDFTGVN CEISMNRDAC SPGICKGDSQ
     CTVKNTAGFT CEGCPVSALE SVTPFCELKA RSFGPATFLT FASLKQRHRF HLRLKFATEL
     ADGLLLYNGR YNERHDFIAL EIVDSRVQFS FSLGNEVTRA MATVPGGVSD GQWHEVVVSY
     INRTVTVSLD DCDVALALKH GEKRLGPKWT CAGRSERVLE ERCGLVTETC HRFLDLTGPL
     QLGGLPAIPS SFQIRNKDYV GCISDLYIDH VFVDLNSFVA DNGTNAGCPE KAAFCASSPC
     RNNGKCREIW SGFVCECEHN FAGPICAEEI GAPYSFHSNG MLGFNPLLRP IQLPWTTALS
     FRTRAQLAFV MSVQIGQNSS VLLEIRNGKL VASLDGADVI RSGCTVADGE WHRMEIVWQS
     GHVSLDTDYR ERPVTVPLPA KLQGLYVGRI LVGGPDQATN IDLPFFDGCL QDIRIGTNQS
     VLQRPTIQEN VDAGCPSETY CNTECPQASI CIAQWRSSEC VCAAGHVGSN CERICNLEPC
     SDAGTCIEDT SDLRRGYQCK CVSSDISGEY CETKSEQPCP ATWWGSPICG PCHCDETKGY
     DPACNKTTGE CHCKENHYQP NGRKECIPCE CYTTGSFGPR CDSETGQCRC RTGVIGRSCT
     DCPNSYAEVT LRGCEVVYDG CPRSYSDGLW WPRTLFGLTA IEDCPGTAEG KTSRSCDDKL
     GGWQPPDLFN CTSEAFIEHR YQLAALETKD LTLNTYVAVK MAKDVYRAVN ITREMYGADL
     LVTESLLVAL LRYEESLVGL NLTHSQDKDY VAHLIGIAGA ILRSKYKEKW DKIGELNGDS
     PDKILDAMAR YLKTLTASQH DTFTNPFEVV NDNVVLGLDI VTSESLFGYE TIEYKEDPTV
     STARPVEADR KVILPDTSAF LSSSAHFGPS ISFPKYNNYM ADPSRFDPHS KIQVPLNTLG
     IKPVIQGELN VKNSLNNRKA VLSYVQYKEL GALLPQRFDD SVSVRWGVEV AVGSPVMTIS
     VLVPSDNGYE SLTGIPLQSP IQVRLWLHEN DDFKTRTNPQ CVHWSTARGS GEWSRMGCTT
     EIEDNSLSFG TIVNCSCMKL STFAILTDVL DLEYVPEPSL LEDVTSYSAF MLALPLLLSA
     LLILALIRGG GTNSNSIHKN LVLCVFMAEI LYLIALKARN PLVSNEFPCK LTAIGLHYAW
     LSTFAWTLVD SVHLYRMLTE MRDVNHGQMR FYYTMGYGLP AVIVGLTIGV RADQYGNFYF
     CWLSIYETVI WSLIGPVCAA VLVNFCILVM CIRAAFTLKE HIMGFGNLRT LLWLSVASLP
     LLGSTWTLAV LNASENSPML SYLLSVAIVV HAAFSLIGYC FINSRVRRNL YQSLLRCIGK
     KTPLLEGSMG NGSSSQNVNG HSRSALAYSS TYNGAESVCK RVHVGVSTSS TTSRSTNKTG
     SSPYRSDTHL RHTSTSTSNY NSDRDPYLSS RSHRSALHSR QESTEVRGQR RESESDSDGS
     QAEGGGRSLD LASSHSSDED DVTSRSHRNM GVSTQQHVAH NYLPNIHTNP AEHLNILCSN
     AELFPNIKPI YAPRWSSQLP EAYLSSNVMD VRSSQWSGGT MSDNEIASNK TSSPNPLPYP
     EMNSPQKNQP DENYSEGEEK MHHLGEKYLF PYTAEEDHTV SPTPYMLSMS SRILASSMSH
     HSQNSNHENL SGSEQRYGSL KRGQSLHGSQ HDNLSGSERY GSLKRGKMVT PTVLEDRPEY
     ILPMSGRILS SSLTHDLQHS NELAALRQQQ QQQQQYEQTI TETE
//
DBGET integrated database retrieval system