ID G0PLM7_CAEBE Unreviewed; 541 AA.
AC G0PLM7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Chitin-binding type-2 domain-containing protein {ECO:0000259|PROSITE:PS50940};
GN ORFNames=CAEBREN_19313 {ECO:0000313|EMBL:EGT35375.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; GL381134; EGT35375.1; -; Genomic_DNA.
DR AlphaFoldDB; G0PLM7; -.
DR STRING; 135651.G0PLM7; -.
DR EnsemblMetazoa; CBN19313.1; CBN19313.1; WBGene00158038.
DR eggNOG; ENOG502S85J; Eukaryota.
DR HOGENOM; CLU_535566_0_0_1; -.
DR InParanoid; G0PLM7; -.
DR OMA; PTTRVMT; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
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; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00192; LDLa; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..541
FT /note="Chitin-binding type-2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003407549"
FT DOMAIN 36..109
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 286..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 137..152
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 175..190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 213..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 252..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 541 AA; 59608 MW; 51D899299079E9C0 CRC64;
MNNPIVLIFL SSGVLLLTVT GNGMEQMMTA EGPINPNFCN SSDLLEEAGL IKSTLGQFLG
YECSEEFYHC RWQSDGFRTY RKKCKPGLVY DVLGTQNCNY DYNVKSCGVR SGGPVQCNGT
DFYCSLSEQC VPMSSRCDGH YDCSMEEDEQ NCPLCTAGEF ACKVSEQCIS LDRRCNGLIE
CDDGTDERDC DVCGHGLFHC GKSNECIPMD ERCDGRRQCP HGEDEMLCKK PEMEKKFTCQ
SRDYEIPSNQ VCDGMAQCPD GSDEAYCEYP GSPKSQAAIS FSSNLTPVLE SKPGPPPPAP
QQPEPEETEE DYEYEQIKDE NAPAAFPMIS LVPLPPTTTT TTTYIPPTTR IITRAPAPLP
ATRMVAKPAF SRPRPKLPST DDNRPTISQK TIQAISTRST RPPKTLETSR SSSLRTTSQT
LPPSRLTTNF EKKMPQAIVQ PPRSPALPQP KGEKVFIMQV TASPSVRPPL QELPRASSGS
RPLSKSLPIK VPGADSDNIL AQITSQLNGG MSPELLAKIE TIIKSEMQGG EPRHRRFQPR
L
//
