ID A0AA39H3U4_9BILA Unreviewed; 2590 AA.
AC A0AA39H3U4;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAK0398715.1};
GN ORFNames=QR680_002721 {ECO:0000313|EMBL:KAK0398715.1};
OS Steinernema hermaphroditum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=289476 {ECO:0000313|EMBL:KAK0398715.1, ECO:0000313|Proteomes:UP001175271};
RN [1] {ECO:0000313|EMBL:KAK0398715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PS9179 {ECO:0000313|EMBL:KAK0398715.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KAK0398715.1};
RA Schwarz E.M., Heppert J.K., Baniya A., Schwartz H.T., Tan C.-H.,
RA Antoshechkin I., Sternberg P.W., Goodrich-Blair H., Dillman A.R.;
RT "Genomic analysis of the entomopathogenic nematode Steinernema
RT hermaphroditum.";
RL Submitted (JUN-2023) 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: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}.
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:KAK0398715.1}.
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DR EMBL; JAUCMV010000005; KAK0398715.1; -; Genomic_DNA.
DR Proteomes; UP001175271; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProtKB-ARBA.
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:0007411; P:axon guidance; IEA:UniProtKB-ARBA.
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; 4.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR FunFam; 2.60.40.60:FF:000020; Dachsous cadherin-related 1b; 5.
DR FunFam; 2.10.25.10:FF:000247; Delta/notch like EGF repeat containing; 1.
DR Gene3D; 2.60.120.200; -; 2.
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 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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; 2.
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; 4.
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 SUPFAM; SSF111418; Hormone receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 9.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
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};
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:UP001175271};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2590
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041328151"
FT TRANSMEM 2219..2240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2252..2271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2283..2301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2322..2342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2354..2375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2396..2422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2428..2448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 157..261
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 262..364
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 365..467
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 468..570
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 571..671
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 672..772
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 773..880
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 881..988
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 999..1103
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1239..1275
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1319..1518
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1521..1558
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1564..1728
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1761..1799
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1883..1961
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DISULFID 1265..1274
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1770..1787
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1789..1798
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2590 AA; 290595 MW; 4B2CFD64DF26F08B CRC64;
MFATSVIISF IFSCLLSTLE ATVNHKPLYL SGLESQCKAS CLIPDRVAVH WIASSRSPCL
HAGQAVFEWP KNSTSSCITP EWFHSEDLSF DPESGLAFTK HRICFYSRIW EPDYLFKCKN
GKVQSSRIRL GHKIYSKRRR MKRWMRRRNP PSVIHFQQDR YVAEIPEDAA VKDFVLKVTA
QHNGNQPLYY SMVAPEDTRS FNTFTLDTST GEIWLAKPLD REVLDTHVIK VTAYERLDPS
VMASTTVVID VLDVQDNMPM FERDSYFTEV REDAPIGTTV LSVFARDLDA GANGEVEYSI
TDDTGFFAIN AKTGVLQTTR ALDRENISMY RFQAIASDKG TPVMSSKAVL EINVVDVNDN
APQFEQVHYN ITILETVDTP SVIAKLTAED QDIGDNGKVH YSIVASSTNA FSIDYRSGEL
SVLRKPDPRF SPIMLVVRAK DSAQPALSST ATCSINIIDV NDHAPSFVAS QRDVFIDEGV
PVGSLCCSVL AVDEDTGKNG EVRYRFLNDV GDFKINPETG KIEVLRQLDR ETNNRYVLQI
IAEDGGDPPL NSTVNITIHI RDVNDNAPQF AQHEYNVTFP EDSPVGTEII RLQASDADAD
AKLVYRLETD DRDIFALIDL GNEGAVINLA KSFHSNDMVV HLVLVATDEG GLQGRCKINI
FIDDVNRPPY FLENPLSVRI PENSPIDFHV AKIRAMDNDR GANSEITYFI DLEEFRIDNE
TGLITVARKL DRELRSSYTL MVSVSDKADP PLVSTTILEV ILEDENDNSP VFTSLNYTVS
ISEDIPVGTS FLQVTANDDD IGNNAIVDYY FEEDDEFVKM DLFRIDRSSG TVRVDSKLDR
ETTPRVILPV LARDRGDPSL VGRSVVTITL ADVNDNAPQF QFPMYNLWVA ENSPIGTTVG
QLVANDLDEG ENARISFRIF GGNDAKLFGI ETDPSKNGVV NIVTRSEFDC EAKIRQFHIE
LQAISGQLSA TVPVTVFISD ENDNKPQIRD FNIITVTFEN EEGRNEIASI PAFDPDINAT
LEYFIVENDI LNVDKSSGML SFKYTLERNL NMPFKAGVSD GPNTACARAR LMNIFMNDED
LRNSVTVRID DTDVEDFLDL STFDKFVEAI SIAANTNASN VYVFSVQEAH DAVNISFFVY
RANKPISSWK LEEILTEQRR NISETIDREV QMVRDNMCVD EPCQYYQRCR QTLKYTRNHE
HFSTDNFIMH GLRTTKTFYC ECPRGFTSAD ITQGRCDRRL DLCFSSPCQN NGTCTSLEND
YKCDCPREYT GQNCEQSIFV DTCIPSTCKS GSVPFLNKRR QECRFCPWNE NDRDEYCNLR
SVSFDGDGYI TLTKVPSRLE WTMELSIATI TSNGVLAFAG SREHDFIELF LSGGLPKMEL
SLGGDIYTVE IEDWRENRIN DGEWHTVRVK YFEHTVQLIV DDCDEHISLN LGVTTGYRRC
ASKTELDLPA RCKDMSLPCD RFLDLASPLY IGGKPNRDTR GVINGYSGCI RDVNLDGSIL
NFGDFSSLEM RGSVTAGCKE RHDFCSKNPC PEKSQCVNKW NGFHCACHNR IHSQKPCDRI
DAHMPSLLLK EASYAHFQTP PKLSYPFQLL FEFRTREKIN QIMVLEFEIK SQIFIFSLES
GLAVVQIDSE RYLLPYPYLA DGGWHGVTVD FQMDYVNVTL DYIYDRKLPV YGIAKLSQLD
KVYTGIAPST NHPSSFVGCL RNVEITNHPL KITTHSGVKP GCGVENQCQI AGICPKKSTC
VRKWDRHICR CDRGFVGDTC TDFCALNGIC ANNGTCVKSS SGKGYECLCA EGFRGANCEM
KAPLRYCPEG WFGEWPQCMR CQCDQRMGFS GRCNKASGEC QCKSGSYLKN GMCVPCDCGY
GSVGKSCNSL GQCRCSGEAK GLRCDRCLDS SLHLDPKTHK CRRIPGRCPS NIESGIQWPS
TMFGMMSRQS CRKGEVGFAS RTCSSEGVWD MPTTENCSLS EVQTLYDMTV KKQDNVQIAR
RLANTTSYVQ LTGKSVITAS TVLSNLIKSE LDADFPKLGH IRDSKFVNNI VVSTSQLIKK
LPSVRFLELS SLLFDYGRKL ALAHQRMPFL QPIAVSADNL MYIVDDIVSP TIELPVFSDS
HKNQIRLPEL QKESVPVFYF IVQSHHCIAC GSYLVGVFGA PMPVRVAFSL GDRNSWSYQE
CAILANSDQP KWSVSDAKLT GLNDTHAICE FSADGVYSVL SKPDSGVFLK LSSVYRIPYF
APASGIFSLF LCTVSFITTV FKTTLDTKVS RLCVIMSFIL NATATIFTTH VELNMVFCPV
RNAVISFCSS TLFAWTFLYS WSVYKIIAKT CHYHQKRSRF GVAFDLFVGL IIPISITISV
FVLSESCMIS PKDLIFLLFV GPIAILVLLS FYSSATSLMV ALTDMHAPKA YIARSIFLHW
FLMALFCVFN VLGLGMAFKF FYGPLLEVIL NLVLMFSAIA IFLWSTYFTE TIHVQRSKHV
ELWVEDSAKP DLDESAYHCD TPLLQTSCQD VSIDSTDNPH HHITHPHWMP DVIPPTAETR
SVPLAAAHIL SSPQKALLLD SQHYALSSPS STLRKNYESP YGTLEDNDVE DAYYTYSATR
YKTPSSTFKR
//
