ID A0A2A3EJU9_APICC Unreviewed; 3046 AA.
AC A0A2A3EJU9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protocadherin wing polarity protein stan {ECO:0000313|EMBL:PBC32045.1};
GN ORFNames=APICC_06752 {ECO:0000313|EMBL:PBC32045.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC32045.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC32045.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC32045.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-2014) 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; KZ288222; PBC32045.1; -; Genomic_DNA.
DR STRING; 94128.A0A2A3EJU9; -.
DR Proteomes; UP000242457; 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: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; -; 3.
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; 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; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF310; STARRY NIGHT; 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; 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; 4.
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 PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 9.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 2.
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:UP000242457};
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..3046
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012923596"
FT TRANSMEM 2391..2412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2424..2442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2462..2482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2494..2514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2526..2548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2569..2592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2598..2620
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 1142..1242
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1410..1553
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1556..1592
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1596..1760
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1797..1836
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1893..1940
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1925..1999
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2386..2621
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 2683..2804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2853..2897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2934..2979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2683..2724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2725..2756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2785..2804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2853..2875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2934..2974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1582..1591
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1893..1905
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1895..1912
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1914..1923
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3046 AA; 334047 MW; 7AA467305CD44170 CRC64;
MERWKWIVPL LAVFWTLTDA YLAVVSSNTP AGSVVFEAGV PQLGGRRKYE VSSERTAWFA
RKLLKVHPHT GRVTLARPLS CDGLQYPRIF TFYVDSTSSR LGRPTIDYYS LPLRILITGC
GGENRDLAAT RGWTAETLAS YAMPSTERFT EVCLRTSQLV AALRDFLPQT ALKECETRWG
GVADPRFLIE GAAGDLVSAT EQCLVDPLWK VSVSMNLRCG MESRLTDAEH RFKIVFHHRQ
LDDTDLGRRV RRELKNQSPY FEQSLYVAVV EEEKEPGVYV TSVRARDPEG GTVRYSMSSL
LDARSQALLV LDPVTGRVTT RARLDRESVD VHYFRVLAVD DSFPPRTGTT TLQVNVLDTN
DHAPSFEWPE EEASIREGVP VGSTVVTVKA TDQDAGRNAE VEYSILSTTS NSGTANTEDA
LIFRIDPRTG VVTTRTPLDR EKTEVYTVIL SVSDQATPPS ARKTANATLV VRVLDDNDNY
PQFTERTYSA WIPEDLDYTA NPVIARIRAT DADSGNNAAV RYAIIGGNTQ NTFSIDSMVG
DVALVKPLDY ESTRSYKIVI RAQDGGSPAR SNTTQLLVHV GDVNDNAPRF YTSHFQESVS
ENVPVGYSIL RIQAYDADEG ANAQIKYTIG ARDFTGASTE NFPITVNAET GWLYTTKQLD
REQCSRYQFT VIAADSGEIS KSASATVILT VTDVNDNDPY FDPKNYESVV SEDDPPGTPV
ASVTATDPDE DARIHYEITA GNTRGRFAIA SQNGRGLITI AQPLDYKQEK RFVLTVTASD
SGGRTDTALV YVNISDANNF SPVFENAPYS VSVFEDAPIG TTVLVVSATD SDVGKNAQVA
YSLDTDSGDR AASEFVINPQ TGAITTTRPL DRELVPAYLL TVTARDGGVP PLSDTTDVEI
SVTDVNDNAP VFEAPQYQGS IPEDVLVGTS VLRVSATDAD TDLNGRVRYA LEEDGDGAFA
VDSTTGIIRT AKPLDRESVA KYALKAVATD RGSPSLSTVM PVTIRIEDVN DSPPAFENDK
IVLYIAENSP IGSTVGEICA HDPDEGANAV VQYSVIGGED SNSFALNVRP GADRGELITL
EELDYESPKK KFELVVRAAS PPLRSDALVQ ILVTDVNDNA PVLKDFQIIF NNFKDFFPAA
PIGKIPAADA DVTDKLTYTV LAGNNANLIE LNRTSGEIRL SPQLNTNVPR VATMEVSVTD
GINEVKATMT LSVRLITDKM LLNSITVRLD DMTAEAFLSP LLGYFLDGLA AIIPCPRENI
FLFSVQEDAN VDGKILNVSF SARKVEPGVA DEFYSPQFLQ ERVYLNRGIL ARLATVTVLP
FDDNLCVREP CLNFEECLTV LKFGNASGFA SSDTVLFRPI YPVTTFACRC ATGFTGSKES
YLCDTETTGG FTCEGCPVAA LESATPLCEL RARSFGPATF LTFASLRQRH RLQVKLRFAT
EAANGLLLYN GRYNEKHDFI ALEIVDSEVQ FSFSLGDEIT RTSASIPGGV SDGQWHEVEV
SYMNKTLGGL PAIPSSFRVR NKDFVGCVSD LYIDHTFVDL NSFVADNGTN PGCPEKLSFC
SSSPCKNNGK CREMWAGFVC ECEETFAGPT CADEVGQPWN FHGDGMISFN PLLRPIQLPW
LTALSLRTRS RQAFVMSVQI GQNSSALLQI REGKLVALLD GADVVRTSND IADGEWHRVE
IVWQSGHVSL DIDYRGRPAL SSLPAKLQGL YIGRILVGGP EQSAGVELPH FDGCLQDIRI
GSNQSVLLRP TVQENVATGC SSEAECNVDC PEASICVPKW KAGECVCATG RVGRSCERVC
DLNPCNNGGA CVEDAASRRG YRCECDSPEY SGNYCEIKAD QPCPATWWGS PVCGPCHCDE
AKGYDPACNK TTGECYCKEN HYQPSGRKEC IPCECYATGS FGPRCDTETG QCRCRVGVIG
RSCTACPNPY AEVTLRGCEV VYDGCPRSYS EGLWWPRTKF GMVAVEDCPE TAEGKTCRSC
DDKLGGWQEP DLFNCTSEAF IEQRHQLAAL ETKELTLNTY VAVKIAKDVY RAVNVTKELY
GADLLVAESL LVALLRYEES LVGLNLTHSQ DKDYVSYLVG IAGGILKSKY LEKWSRIETL
NGDTPDQVLN AMGNYLKTLT ASQHDTFTNP FEIVDVNVVL GLDVVTSESL FGYETAEYTE
DPSASTARPT EADQKVVLPD TSAFLSSPAH FGPSITFPKY NNYMADPNRF DPYSKIRVPL
DILGIKTLMQ GELNVKKSLV NRKAVLSYVQ YKQLGALLPQ RFDDSVTVRW GVEVAVGSPV
ITVSVLVPSN DGYVSLTGIP LQSPVQISLW LSEKDDIKTR TNPQCVHWST ARGVGEWSRM
GCTTESEDDS LSFGTIVNCS CFQLSTFAIL TDVLDPEYVP EPSLLEDVTS YSAFMLALPL
LLSALLILAL IRGGGTNSNS IHKNLVMCVF FAEVLYLIAL KARSPLVSNE FPCKLTAIGL
HYAWLSTFSW TLVDSIHLYR MLTEMRDVNH GQMRFYYAMG YGAPAIIVGL TIGVRADHCW
LSIYETVIWS LIGPICLAIF VNFCILVMSI RAAFTLKEHI MGFGNLRTLL WLSVASLPLL
GSTWTLTVLN ASENSPTLSY LLSIAVVVHA SFSLIGYCFI NGRVRRNLYL SLLRCIGKKT
PLLEGSMGNG SSSQNVNGHS RSALAYSSTY SGAESVCRRV HVGVSTSSTT SRSTNKTGSS
PYRSDTHLRH TSTSTSNYNS DRDPYLSSRS HRSTLHSRQE TTEPRNQRRD SESDSDGSQA
EGGGRSLDLA SSHSSDEEDV TSRSHRNMGV STQQPVTHSY LPNIHSNPTE HLNILCSNTE
LFPNIKPIYA PRWSSQLPEA YLSSNAMDVR GSQWSGGTIS DNEMASNKTS SPNPLPYPDM
NSPQKSQPDE NYSEGEEKLH HLGEKYLFPY TAEEDHTVSP TPYMLPMSSR ILASSMSHHS
QNSNHENMSG SERYGSLKRG QSLHGSQHDN LSGSERYGSL KRGKITPTVL EDSPEYILPM
SGRILSSSLT HDLQHSNELA ALRQQQQQYE QTITETEKDT NAETSV
//
