ID A0A3P6T5F5_LITSI Unreviewed; 2709 AA.
AC A0A3P6T5F5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Cadherin domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NLS_LOCUS2663 {ECO:0000313|EMBL:VDK74890.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK74890.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK74890.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004251}.
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; UYRX01000127; VDK74890.1; -; Genomic_DNA.
DR STRING; 42156.A0A3P6T5F5; -.
DR OMA; DAYYTYT; -.
DR OrthoDB; 26203at2759; -.
DR Proteomes; UP000277928; 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: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; 1.
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; 2.10.25.10:FF:000066; FAT atypical cadherin 4; 1.
DR FunFam; 2.60.40.60:FF:000005; Protocadherin 9; 1.
DR Gene3D; 2.60.120.200; -; 1.
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 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; 6.
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 SUPFAM; SSF111418; Hormone receptor domain; 1.
DR PROSITE; PS00232; CADHERIN_1; 4.
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; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
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 2345..2363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2375..2397
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..2464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2476..2500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2520..2542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2554..2573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..305
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 306..410
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 411..513
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 514..619
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 620..772
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 773..873
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 874..979
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 980..1087
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1338..1374
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1418..1620
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1623..1660
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1859..1897
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2006..2059
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DISULFID 1364..1373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1868..1885
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1887..1896
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2709 AA; 304921 MW; CD86CAD2DC114511 CRC64;
MTVVEMMMMD ATVEIEMMQL QRLATIWSAE AVSAHSYFFL LIIIDVTTNN GKFKVTALTY
FIELLIIAIA FHLDPPILDI CITGCLVPAR NNTIWLPYSY PPCVDPGQPL LRWSNNVTCN
RPNFLTSQSV SLDSSSGVLF AEERMCFYVK PWYMTYLYDC SGDGVPQEGI VFLDHKKYVT
KRRSKRWIRR RNPAVPRIHF KQEHYVTEIP EDTPINSLII QLHATHITNE SIYYAMVAPE
DSRSANIFTL DTVSGDIRVG KALDREALDR HVLKVMAYER LDPAVSASSS VIVEVLDVQD
NAPIFERNSY YVEIREDAPI GTTIASVFAR DLDIGLNGEI AYSLGEQDGA KLLQIHSSTG
LIQTAQHLDR ESMNIIRVYI YATDKGVPPM TSRALLEIFL LDVNDNAPVF EEEFYNATIM
ENITIPYNIL QIKATDRDSG QNGKVHYSIV ASSINGFSID YESGWIKLHR KLDPRSNLAT
LLVRAKDSGQ PAQSSTINCA IHIIDINDHK PHFVSSQQKL FVEENVPIGF EITRIFAIDE
DNGMNGVISY ILEGEDGANE TFRIDEATGI ITTIGKLDRE EREKYIFKVK AEDGGKPPLS
DSLLVTVIVR DVNDNAPYFE PNFYNVTIPE NEVRGTPLLS VKAIDHDNDD KIAYRIEGAD
KDIFSLIHST DQNMVILSRE QKGSIHRGAC KGLYGSTENK STIGLETGNR LKPSGVKDMC
LQCMGAILSL SGEIDRMDDI LRVMITAIDK GGLTGTCTVT IIVTDVNAAP VFLTHPFTVH
IPENVPIGAE VIQLRAEDED RHENAKLTYS LDSKEFNIDK ETGLIIVAKE IDREECSSYL
LNITVTDHAT NPLSASTFLE IVPDDVNDNA PEFTSENYTV AIAEDTPIGT SFTQISAVDV
DEGDNAIIDY FLVEENGNGD TFKLDRSSGT LRVVTKLDRE MTARYQLTVK AQDRGNPPLS
SFSTISVVII DVNDNAPQFE SLRYDLWIAE NSPMGSTVGT IIARDQDEGD NALIQFRIFG
GIDAKLFDIE ADSNQNGVAN ILSRTVFDYE AKKNLFFVEV QASSDQLSSV VPVYVHVSDV
NDNRPQLRDF TVLYANHIEE PVEREIGYVP AFDPDHNATL EYSIETNDIL MVDQYKGSIM
PMNVWRRYIN VVYKICVSDG PNNICARCRF VYIPLDDAII RDTVTVGFPN TRYEELLDNV
VFERFTSAIS LLDDWHSDDI WVFSVHTENE YTNVSLVVHQ GRTVHKSEYV EGLIRNGLAK
LSDMIGMRLT IHKDATCFNE PCPYFQQCRN TQKYVKTTQD FKTDSFLMHS LDTVNSFQCQ
CPVGFSSSDG LQQLCNHRLD MCFTSPCEHQ GTCVPLENGY RCHCSPQWIG ENCEKSVYVD
SCLPNSCFSN SICKLVNRTT KCVQCRWHSH DTDSQCRLLS ISFGEDGGYI VLPLQITRMQ
WKLQFSIATV ASNGVLFFTG NLSLDFLEVS LQDALVIMDD WPENRVSDGK WHQITLEYYD
NKLIISLDDC DAHIAMKYSN ITGYRKCAAE ITAKLLEKCN DPAVSCYRFF DLPAAVNLGG
RAITIARQNY ISGIDGDQYG SARIQEPFVG CISNLTFDGR LVDFSNFEEF EKAGDIQHGC
KQKRNDCLNN PCHHTAVCEP MWDGYHCRCK QTAHTDGPCI DDEDSFVSLY DEESYVFWNI
PDNIKFYNLS FEFRTRLHET QISHGKGVIS IGSKQYFLPF PNFADGNLKS FSIAVEKYVT
LIVIDHLYKK RIVMPNNGLY RDIRKVYSGL APSTSYPQRF EGCLRNVKIN DVRLKLAENM
MAKPGCQVLI SHPLLSEKCS KAPNGCSLPK ACPLNSVCVR EWDRHRCECN PGFVGDGCVN
ICLLPNLCGA EGVCHTTNNS RGYECTCKGG LSGRNCERKA ALQICPKGWY GTFPKCKQCS
CDTWRGFLEQ CNAETGECYC KSGAYHSGGE CISCECGYGS SGSTCTSKGQ CQCAGEAVGR
RCDRCPGKDQ VLDRKTLKCL KIMNRCPSNI EYGIQWPTTI VGTTARQSCP NGKVGFALRK
CLKSAHWDRV NDYNCTLPAL TKLDLTDRMK FAQSLLNATS SALQLKGINV VIARKALEQL
IDEELSGNDP HPSSHLKSTE YTNNILKVGD SLLKIEGYPN NAQLIHLFND YGIHVANVHQ
MHSYLKPFIF CGQNMVFAVD DMPAQGRALP KFNNFVDKRV ESFRSIQMKL LCEDTAAYPK
VIFYSMFSNI HCFRCKAPVV AVFYNTTCTI QVLFPVSEEV WRYPECAIAK DSAENNKLFG
TKDWEDRNVE RENIFLEWSA QGTTLVGLNR THVICNFERS GIYTIIVRPE RGALIRFIPS
KTMPYAELLC VLFSLILLSL SAVRTLYRSC LSLRLIRFGF IVMFSLNVIA VSFIHRLQPS
IIFCLARNTI ISLCTSAVFA WLFMYSFHIY RLLATERAES NYWMVILCSV IIPILLSLAS
FFFAPGCCSL SPNQSFFWVL LVPVVLYILF DFYAFSTALL ISFSKQFDYI VTEYSIRTAL
CLHIILPILC AFYNSFGLYI LFDHADSPLY EITFNSTLVF ISTYIFLWTN YFGPKRNMRY
DNGLWVNNLA KSTGTLGHQC QTPLLLQSQN ADSNLLITSK YHAEISGDCV NGWMPDIIPS
TTYVHHQSTH GVPHPKILSP PMKILNQEAY CSAEGIALLY QDNAPSIDTD HIYGTRSSEH
HYPSFTFTH
//
