ID A0A0V0VDK3_9BILA Unreviewed; 1069 AA.
AC A0A0V0VDK3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Chloride intracellular channel exc-4 {ECO:0000313|EMBL:KRX61584.1};
GN Name=hmr-1 {ECO:0000313|EMBL:KRX61584.1};
GN ORFNames=T09_14821 {ECO:0000313|EMBL:KRX61584.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61584.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX61584.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX61584.1};
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 -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
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:KRX61584.1}.
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DR EMBL; JYDN01000046; KRX61584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VDK3; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR43920; CHLORIDE INTRACELLULAR CHANNEL, ISOFORM A; 1.
DR PANTHER; PTHR43920:SF5; CHLORIDE INTRACELLULAR CHANNEL, ISOFORM A; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 534..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..240
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 259..289
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 292..474
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 604..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 279..288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1069 AA; 121212 MW; 85E34A1A7E7A3848 CRC64;
MLKYTSGGKI WPSSTSLNTV TKLGGGCECR GLYKGPRCAG HVRSFRGLGW AWFEPVQTCQ
KWNISLEFIT QNSNGIILYN GPMLARRHDV REMFVKDFLY IAVVRGQLVV NVDFGGMPMS
VTSTLDDWKV DDGRWHTLEL FASGKEVRVI LDKCRRGNRR QHFDWNRCEL KQVVQLDNDQ
LNSIYPLQLG GIAPVHSGIA FRDFFNTTDG FDGCIRNVYL NGKILDLANP LRFDNSEMGC
PQTDHFCETN RLSEQHQQAV THCLHGECVA SFHDYTCHCE PGWYGPKCDI EARWKTFGPM
SYVRYLMALA DTDIPLQYSK LEVSFFPDSG AGTLFSASHT EKNHSMHLMI EDRILNYLLS
FGPDVMTKAK MAHFQLARNQ TYHVVVERTR EIVRFNVDGL VYYLSMFELN NKNKQFFMDY
DSNSFRVGST NHGNSGFRGC IRKVTFDDYW LPLDSDTAVD YAKIDETFGV SDGCTLLQTC
ASLPGYCSPP LVCVDFWKGP FCTCPPDSNH WIQNGQLYCG RPLAAMHLGI THGAVAAILV
TLLTLIVLVL LLVVYSRRRH QSPLLIRPED DIRENIINYA EEGGGEEDQD AYNIAALRKP
VLPIEDDPSM QLPNTDDHNG THRRPAAKDP LSSGGDLNSF IKNRLNNADQ DPMVPPFDEL
RVYANEDDAA SVGSLSSLSS PSSGSEIDWD EVNKWGGEAF KKLADMYANF LLACFTFVKF
VHSFIEQQRP PSHVIYVQKT SKPQTKTTDV HNLTTWHLPA AQFGSACSLV AVVMSDSVNE
SDGMCASRND GCIDAVGDGS KPFLELFVMA SGIDHRRIGA CLFCQEFWME LYALYEINLV
RVEVKTVNVN SEPFKRSFLG ALPPILFEAE NGSMFTDNRE IERRIFHIAK EFKVPLFEKD
VTVDKSIESL YRNFKLFLRS KTDYERGKEV VSNDIPACAQ PAYNKLIEQL TNIDKLLAQR
NTRYLVGSSM TMYDCELMPR LHHIRIAGEH LCGVEIPHAL THLWNYMLTA YRTAAFIESC
PADQDICYHY REQLNWPHRL KEYLQTPTKT HTIPDDVLSE IKQLGLDKL
//
