ID A0A915PFR4_9BILA Unreviewed; 2613 AA.
AC A0A915PFR4;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:sdigi.contig136.g5048.t1};
OS Setaria digitata.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Setariidae; Setaria.
OX NCBI_TaxID=48799 {ECO:0000313|Proteomes:UP000887581, ECO:0000313|WBParaSite:sdigi.contig136.g5048.t1};
RN [1] {ECO:0000313|WBParaSite:sdigi.contig136.g5048.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) 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:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR WBParaSite; sdigi.contig136.g5048.t1; sdigi.contig136.g5048.t1; sdigi.contig136.g5048.
DR Proteomes; UP000887581; Unplaced.
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:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0007411; P:axon guidance; IEA:UniProtKB-ARBA.
DR GO; GO:0048589; P:developmental growth; IEA:UniProtKB-ARBA.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:UniProtKB-ARBA.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:UniProtKB-ARBA.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 7.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR FunFam; 2.60.40.60:FF:000020; Dachsous cadherin-related 1b; 2.
DR FunFam; 2.60.40.60:FF:000033; FAT atypical cadherin 1; 1.
DR FunFam; 2.60.40.60:FF:000080; FAT atypical cadherin 1; 1.
DR FunFam; 2.60.40.60:FF:000039; FAT atypical cadherin 3; 1.
DR FunFam; 2.10.25.10:FF:000066; FAT atypical cadherin 4; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.60; Cadherins; 8.
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 InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR056286; Cadherin_CELSR1-3_9th.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR055928; Fmi-1_DUF7505.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
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; PF00028; Cadherin; 7.
DR Pfam; PF23592; Cadherin_CELSR2_9th; 1.
DR Pfam; PF24337; DUF7505; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
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; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000887581};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2265..2285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2297..2319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2331..2352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2364..2385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2397..2421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2441..2461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2473..2493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..262
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 263..367
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 368..470
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 471..576
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 577..677
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 678..778
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 779..884
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 885..992
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 1324..1538
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1541..1578
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1574..1746
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1779..1817
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1901..1979
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DISULFID 1269..1278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1788..1805
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1807..1816
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2613 AA; 293816 MW; E934B8C4D688FAE2 CRC64;
MKNFNHLERK LPVTICLIAS LPVITITSRL HPPIFGNCTA NCSLPTENGT IWLPYSYPPC
IHPGQPVLRW TNAVACSLPK FLISRSVSLD SSSGLLFTEE RVCFYLEPWH VTYSYDCSGN
DPPKRGTFFL DHKKYAARRR SKRWMRRRNP TVPRIHFKQE RYITEVPEDT PINSLIIKLY
ATHITNESMY YAMVAPEDSR SANIFTLDTI SGEIRVGKAL DRETLDRHVL KVTAYERLDP
AVSASSSVIV EILDVQDNAP IFERNSYYAE IREDAPIGTT LASVFARDLD IGLNGEIAYS
LGDELGAELL QIHSSTGVIQ TAQHLDRELM NLIRIYVYAT DKGVPPMTSR ALLEINLLDV
NDNAPVFEKE FCNVTIMENV TIPSNILQIK ATDNDSGQNG KVHYSIVASS VNGFSIDYDN
GWIKLYQKLD SQSNPITLLV RAKDSGQPAQ SSTINCAIHI IDINDHKPHF VASQQELSVE
ENIPIGYEIT RIFAIDEDSG INGLIAYTLE GENNANETFR IDKTTGIITT INKLDREDKE
KYILKVKAED GGEPPLFDTL LITVMVRDIN DNAPYFEPNF YNITVAENEI RGAPLITVKA
IDHDKDDKIV YRIERADKDI FSLIYSTDQG AILSLSGEIG RMDDTLSVSI TATDKGGLMG
TCVIAITVTD VNTAPVFQIH PFTIHIPENI PIGSEVIQLR AEDQDRLENA KLTYSIDSSE
FTINKDTGLV MIAEELDREE RSSYLLNVTA TDHATNPLSA STFLEIILDD VNDNAPEFTS
ENYTVAIAED APIGTSFAQV AAVDVDEGDN SIIDYYLIDE NGNSATFKLD RSSGTMRIVS
RLDREMVASY HLTVKAQDRG NPPLSSFCTV SVVIIDVNDN APQFESVRYD LWIAENSPIG
TTIGTIIARD QDEGDNALIQ FRIFGGIDAK LFDIEADSDQ DGVVHILSRT IFDYEAKKNN
FFLEIQASSG QLSSIVPVYV HVSDVNDNRP QLRDFTVLYA NHIDEPVERE IGYVPAFDPD
HNTTLEYSIE ANDILTVDQY KGSIMPMNVW KRYINVIYKI CVSDGPNNVC ANCRFIYIPI
DDAVIRDSVT IGFPDVRYEE LLDDNVFERI TGAISLLDDW HSDDIWIFSV HTHNKHTNIS
FVVHHAHNVQ RSEHVERLVR NGLAKLSDII GMKLILLKDA TCSSEPCPYF QQCRNTQKYV
KSTQNLRTDS FLMHSLDTVN SFQCECPAGF SSSDGIEQFC NRRLDMCFMS PCQHQGVCLP
LENGYRCDCP PQWTGKNCEE SIYVDSCLPN SCYSDSLCQL VNRTAKCIQC RWSPHDTDSQ
CRLRSISFGV NGGYIVLPVQ ITRMQWKLQF SIATVALDGV LLFAGNLSSD FLEVSLEDAL
VRGRFSLGHD IYQVTMDDWP ENRVSDGKWH QITLDYYNNK LIISLDDCDT YIAMKHHNIT
GYRKCAAEVI AKLPKKCEDP AVNCYRFFDL PGVVSLGGRS VTVAKQNYIS GIDGNRYGSA
RIQEPFIGCI SNLTLDGTLV DFSKFDEFEK VGDLQHGCKQ KRNDCEKNPC HSTAICEPAW
DGHHCRCKHT AHTDGPCTDE EDSFVSLYDE ESFVFWNLPD NVKFYNMSFE FRTRSRETQV
IATEFSKRSQ FIIFSISHGK GLISIGSEQN FLSFPNFSDG NLKSLAIIVE NQAVLIVIDH
LYKKRISVQN GDLYRDIRKI YSGLAPSTSY PQRFEGCLRN FKLNELQLKL AENMMTRPGC
QVPNGCNSPE ACPSNSICIR EWDRHRCECS PGFIGDGCVN ICSLPSLCSG GGVCHTKNSS
RGYECTCNRE LSGPNCERKA AMQICPKGWY GTFPKCKQCS CDIRKGFLEQ CNTKTGECYC
KSGTYYSSDE CISCECGYGS SGSTCTSKGQ CQCTGEAVGR RCDRCPSSDE ILDQKTLKCL
KIKNRCPSNI EYGIQWPTTI IGATARQSCP NGEVGLVLRK CLRSTYWDQV NSYNCTLAAF
TKLDSSDRMK LAHRLSNATA SVLRLKGINV AIARRALKRL IGEELTENDS PNNHLKSTDF
TNNLLKVADS LLGIKDYPNN AQLIRLFNDY GIHVANIHQH HPYLKPFMFC GQNMVFAVDD
MPVDGGRVLP KFRNFVDERK ENFRDIQIKL LCEDTVSYPG KVISYSMFNI DLFHSKAPIV
TVYYNATCAI QVLFPVNEEA WKYPECATVE NAPENGKWSK KTKNWQHGNL APATNVFLEW
SAKRTALVGL NRTHAICNFE RSGIYTILIR PDHGALIRFI PSKTIPYAGS LCVIFALVLL
LLSAIRTLYR PCLRLRLIRF GFILMFVLDV IAIFLVHRLQ PSIVFCLARN TIISLCTSAV
FGWLFMYSFH IYRLLATGGI KSIYWMIILS SVIIPMLLSL TAFFFAPGCS LSPSQPFFWI
LLTPVSLYIL FNFYAFSTAL LISFGKQFDY MVTEYSIRTT LYLHVILTVL CAFYNSFGLY
ILMDHADNPL YEIAFNSTLV FVATYIFLWT NYFGPKQSIR YENGLWMNNL PKSAEEVADP
QCQTPLLIQS SNTDAELNGN CLNGWMPDII PSATCIHQES LHNMPPPKIL SPPMKVLHHE
IYSSAEGIAL LYQDNVSSND IVLQALAIME HSA
//
