ID A0A0V1P1X4_9BILA Unreviewed; 2665 AA.
AC A0A0V1P1X4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Protocadherin-like wing polarity protein stan {ECO:0000313|EMBL:KRZ90163.1};
GN Name=stan {ECO:0000313|EMBL:KRZ90163.1};
GN ORFNames=T08_16028 {ECO:0000313|EMBL:KRZ90163.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ90163.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ90163.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ90163.1};
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:KRZ90163.1}.
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DR EMBL; JYDM01000060; KRZ90163.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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; 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; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR PANTHER; PTHR24026:SF125; FAT-LIKE CADHERIN-RELATED TUMOR SUPPRESSOR HOMOLOG; 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:UP000054924};
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..2665
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006883865"
FT TRANSMEM 2290..2310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2368..2389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2409..2430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2442..2462
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 2284..2384
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 2574..2635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2574..2595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2603..2635
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 2665 AA; 299082 MW; DDBAF4EE25ADD4DA CRC64;
MLAGVLCCSL LFQASLFSSA AVHPQSTLLR KVLYVNSTCI GAGGPVFPSF DRWLLKRFNV
PVTANSICLG EWFISTVDGE 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 FEQSTYVVEI 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 HEPVFNDFYL VVYNHESDPW NKDLSKRPIG 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
HLYIDYKMIN LNHYISNQMT VPGCAAMTKN CRRNPCQRNS ACQGIWEDYI CKCPTDYAGK
NCSDYVGKPI SLPTSSSSVS FKVPPHAEIP LVFGIQFRTA QTDADIVVVE LTSGKKIILQ
ITDQLASVTL ERKHQQLAQR LVSDSKWHSL LCEMQNDQII LNVDYVYQLT IPLSEKLNGI
VKKIKINISS SKNNNNHNHP 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 NCTTDEFQTL ENKIKDLQSN FKIDPIIITA
VAEKLKNATQ RKSLYGHDLF AVGRILLKIL TLELSDQHAL PVAYQHDRNF ASNIIASLDE
AFSVNIRQNA GDADGQFLEQ TLELVNQFHD YGIKIAAYQQ KSHVDSMEYT GKSVVYAIQT
VDLKNSDFQR TATLGRSKKS VAIQLDIQPE VKDLHKARTL FYAVYENAYD AELQRLSPSF
AKCNVHNIHS PLLSVGVIDN AGKQVISIKK PAFFTFPLPS WMKNNYLIPF CMFWNAKNTY
DDDDESEPKW NTQGCYVDYF NRSHVICACN HLSTFAVSMR DFMTTDTVLS YFALTVTTLS
MLKCSVIGNA LLFVNVALFT WLVVVPVEIF KTSTPLKQTN NYHTWLRHML IWSKEHTIPT
VYVAIRILKD SFKATHEECW FSFYDPTLIF FAAPVVVLML LSLYASTMAL IFDCKHKQKL
FPNGSKNRLY IFICFQLGIV AQWWFSYFAF NLTSYGLYYT YYGMSLVNMP LGAFLIFSII
VINTQTSRKA NQCNTKQTAD ADLWLSMNVS QFEMSMKQST VSDACCAEES TEMDRLMITT
VDGHEIHQFS CEDMKLQNLN HDEKIYWKKA YSEQQPLDSS RVYLLEKVCN SENSQRYPEN
SWPKLPTQTQ GYNSPRGRPV ALITGTNRSQ MDGLPSRRPS IGRSPTSPSS GQISPAILSS
PIKVLQYGTS AHNSPVLEIG EKLDR
//
