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Database: UniProt
Entry: A0A0V0ZZC7_9BILA
LinkDB: A0A0V0ZZC7_9BILA
Original site: A0A0V0ZZC7_9BILA 
ID   A0A0V0ZZC7_9BILA        Unreviewed;      2667 AA.
AC   A0A0V0ZZC7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Protocadherin-like wing polarity protein stan {ECO:0000313|EMBL:KRY17676.1};
GN   Name=stan {ECO:0000313|EMBL:KRY17676.1};
GN   ORFNames=T12_14422 {ECO:0000313|EMBL:KRY17676.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY17676.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY17676.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY17676.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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   -!- 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:KRY17676.1}.
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DR   EMBL; JYDQ01000058; KRY17676.1; -; Genomic_DNA.
DR   Proteomes; UP000054783; 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:0009653; P:anatomical structure morphogenesis; 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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   CDD; cd11304; Cadherin_repeat; 8.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00055; EGF_Lam; 1.
DR   CDD; cd00110; LamG; 1.
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; 4.
DR   InterPro; IPR039808; Cadherin.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00053; Laminin_EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 9.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00180; EGF_Lam; 2.
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; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 9.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS50026; EGF_3; 3.
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; 1.
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   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
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..2667
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006874178"
FT   TRANSMEM        2292..2312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2370..2391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2411..2432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2444..2464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..231
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          232..341
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          342..448
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          449..554
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          555..658
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          659..761
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          762..867
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          868..975
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          999..1099
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1243..1279
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1323..1531
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1527..1563
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1753..1788
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1881..1956
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          2286..2386
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          2576..2637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2576..2597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2605..2637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1269..1278
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1553..1562
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1778..1787
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   2667 AA;  299122 MW;  08E0F94621A379CA CRC64;
     MLAGVLCCSL LFQASLFSSA AVHPQSTLLR KVLYVNSTCI GAGGPVFPSF DRWLLKRFNV
     PVTANSICLG EWFITTVDGE LSTGEEEGSV SAFSVQLKLR RRRRASRHRR AQSNDGDQWS
     GFSKSRYEVS VLEEQDPPIS LLNFAQLSSA ANVETVSSCS VTGAGNVQSQ NLFTVEKETG
     RLITTGRLDR EQADKHTLRI TCYEMTSNGR RSTTAIVLVN VLDLNDHEPV FERSNYAASI
     SESVEPGTTV LHVHAQDEDA GRNGRIQYSV QRTNPETPLP FSLGSDDGVL RVEKPLDRET
     CPFYRFEVLA CDQPLTITER LCAKALVEVT VDDENDNAPE FEQSSYVVEI DENLDPNDKP
     VIANVMARDR DFGHNGEVKY SIVSGNAEGR FSIDYNTGEV RLVDRVDYRQ TDHYELVIRA
     QDSAIFSLSN TTLLEIRIRD VNDHAPQFYA PVFQESVRED VPVGYRLLRL AAYDLDSGRN
     SEIRFRFTGP EANNCPLEVD SVTGWVTVAK PLDHELEPTI ELQVEAVDLG NPPLASNAKL
     IVNVLDVDDN VPVFPEKQLN VSVPETARRG SLLLRIAAHD PDNNSGRLQY SIISGNDDRA
     FILLNEENNY CSLAVDQPLS YTSKPIHVLS IKVTDSAGHW DTMTVRVQVE DVNSAPTFAE
     HSSTIHVRES EPVGSTVTVV RATDSDDGEN ARLQYQLEGG EPVFAIEPST GVLFVNGTLD
     RESQSRFKLK VIATDHGQPP LSGSMDLEVV LDDVNDNAPV FSRTRYVTNV SEDAAVGVSL
     LHLTATDSDY GINSRITYHF SDEDPENDAF QIDPSSGVVR VARPLDRERR AVYEITVLAK
     DKGEPPLIGR TTLVINVDDV NDNAPKFDRE AYQFEVYENV PIGTIVGHVL AVDPDVGEHA
     LVSYKILGGD DAAAFEIHSP MSKSEGMDLV TRIELDFESD RRTYQFHIQA SSGQLSSMAE
     VLVRILDLND HEPVFDDFYL VVYNHESDSW NKDLSKRSIG RVPAFDLDLN DTLHYKIAAG
     NEADLIQLDS NTGELRLSAA LNTNRRIRLL LLIQVSDGIN AVQATCTVIV EMITNSALLN
     SVTFRISGLT MNSFLNPTAY GRLLDSLSAL IPSDRRDVLI FSVRQDNELH GEPTLNVSLV
     LRKANSDRFL SGEELHELVD FNRKRLSEAS NLNILPLADE LCSREPCLNN ERCRNVLKFD
     GTGDFIVTEN FIFKPVHCIS TFICECPIGF AELSKQRPGC NIEINLCYSS PCKAGGTCLS
     RENGYSCICR PDFTGKNCEF PISNSYCIAD ICHGGSLCTL VQGKQKCQNC TYDADSTNEY
     CELTTRTFQP NSFVEFPTLN QRNRFNITFQ FTTTVLDGML FYAGRQKAEN DFIVLELANG
     RLKLSMSLGE SDIKVLNLDS DYTLNDGQWH KVQVIYFNRT VTLILDDCDP YLALNPNRIF
     RYSQCAAHME LKLDEKCNDP MVPCYRFLDI TSPLYLGGLP SRNRHQRFRI MPVGFVGCMG
     HLHIDHKMIN LNHYISNQMT VPGCAAMTKN CRRNPCQRNS ACQGIWEDYI CKCPTDYAGK
     NCSDYVGKPI SLPTSSSSVS FKVPPHAEIP LVFGIQFRTA QTDADIVVVE LTSGKKIILQ
     ITDQLASVTL ERKHQQLAQR LVSDSKWHSL LCEMQNDQII LNVDYVYQLT IPLSEKLNGI
     VKKIKINISS SKNNNNHNHL SNPFTGCLKG AFVDKPMQNK KAYLQILHQK NIIKQCTLPD
     NFCPKRDADG YCMNLCTLHP CLNGGTCNDQ WNSYVCQCVE NFTGRNCEHR LSTIGGRCPK
     GWWGNSTCGP CNCDTTKGYD ANCDKYTGIC KCTDKTYFDD EKKQCTPCNC FYPAGALNMS
     CNSETGQCHC RGNAVGKRCD ICADPRAQIS RISGYCEIVT NGCPENWMSD ILWPAMKSNR
     TSTKPCPRGW QGRATRYCNE KGFWGKPRLE NCTTAEFQTL ENKIKDLQSN FKIDPITITA
     VAEKLKNATQ RKSLYGHDLF AVGRILLKIL TLELSDQHAL PVAYQHDRNF ASNIIASLDE
     AFSVNIRQNA GDADGQFLEQ TLELVNQFHD YGIKIAAYQQ KSHVDSMEYT GKSVVYAIQT
     VDLKNSDFQR TATLGRSKKS VAIQLDIQPE EVKDLHKART LFYAVYENAY DAELQRLSPS
     FAKCNVHNIH SPLLSVGVID NAGKQVISIE KPAFFTFPLP SWMKNNYLIP FCMFWNAKNT
     YDDDDDESEP KWSTQGCYVD YFNRSHVICA CNHLSTFAVS MRDFMTTDTV LSYFALTVTT
     LSMLKCSVIG NALLFVNVAL FTWLVVVPVE IFKTSTPLKQ TNNYHTWLRH MLIWSKEHTI
     PTVYVAIRIL KDSFKATHEE CWLSFYDPTL IFFAAPVVVL MLLSLYASAM ALIFDCKHKQ
     KLFPNGSKNR LYIFICFQLG IVAQWWFSYF AFNLTSYGLY YTYYGMSLVN MPLGAFLIFS
     IIVINTQTSR KANQCNTKQT ADADLWLSMN VSQFEMSMKQ STVSDACCTE EPTEMDRLMI
     TTVDGHEIHQ FSCEDMKLQN LNHDEKIYWK KAYAEQQPLD SSRVYLLEKV CNSENSQRYP
     ENSWPKLPTQ TQGYNSPRGR PVALITGTNR SQMDGLPSRR PSIGRSPTSP SSGQISPAIL
     SSPIKVLQYG TSAHSSPVLE IGEKLDR
//
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