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Database: UniProt
Entry: A0A183BQJ6_GLOPA
LinkDB: A0A183BQJ6_GLOPA
Original site: A0A183BQJ6_GLOPA 
ID   A0A183BQJ6_GLOPA        Unreviewed;       733 AA.
AC   A0A183BQJ6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=C3H1-type domain-containing protein {ECO:0000313|WBParaSite:GPLIN_000288200};
OS   Globodera pallida (Potato cyst nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Globodera.
OX   NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000288200};
RN   [1] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Aslett M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA   Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA   Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA   Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT   "The genome and life-stage specific transcriptomes of Globodera pallida
RT   elucidate key aspects of plant parasitism by a cyst nematode.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:GPLIN_000288200}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   AlphaFoldDB; A0A183BQJ6; -.
DR   WBParaSite; GPLIN_000288200; GPLIN_000288200; GPLIN_000288200.
DR   Proteomes; UP000050741; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 5.
DR   Gene3D; 4.10.1220.10; EGF-type module; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR24270:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 5.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 6.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   TRANSMEM        218..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          118..146
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         118..146
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        321..336
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        384..399
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        464..479
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        582..597
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        624..639
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        662..677
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   733 AA;  81519 MW;  5350194D08BAC86D CRC64;
     MDQRISTTTG NSSSRPKQQQ NPAYFVVSPV GNAALPPPLL SDCNRGSGCA AWWGRFQLIY
     PDSQQPVPLS HYVHGPPAPI VLPMQHSKYT STQPKALPKT SHHQPSNKRP ADPLVNEKYK
     TMLCKSYTIS GYCAYGAQCL FAHGDRELRP CPGRQRRPSK IRTFALLNME PIEFKLSEHT
     NTVNVTPTVM ERMRYRADEF RLWLSTTCCA CLSSVPSYAL VFIAALLVMM IVSAIPLTLI
     LTRMRSQPST ADSSQQDSKN ILSTQRIHHA WPDASVVPIH KYSDWEDAEE LIVQAKLFVP
     PNISLCSEFG FACLEQPNYR CDGYSDCLDM SDEKGCKEHL CDGVKHCGNG EDEDPKTYCR
     SKCDGKNEFS CRKADICLPI EAVCDGVQHC PFGDDELNCK ECRGEAKRCG DHCLSRRVLC
     DGIMDCREDG GSDEKDCDCA SCSGKTSMLC DGEQKFCVDR RRMCDGRVDC PGGEDEFECH
     GVCPSLMNIN SSGSHKKDVI MKTKKEGKDS NEALVKCSDG VLREWGVACG GLYPECRGSC
     RHCNPQSAFQ CGLRNSTTEP KVRNDDNNTP NGRECIHRSL ICDGKQDCFD GSDELNCDCE
     NALQCQDYGR GLPTGRCYSE DQKCDGYTDC VGGEDERNCA KCKNGAFLCQ SEKRCISSMA
     RCNGLDDCED ASDELHCTCD ECTRHSSRPM YMCQETQRCF PLDKVCNPTS SCPNATKMDE
     LFCAVQKRGI EHL
//
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