ID A0A0V1DAN1_TRIBR Unreviewed; 694 AA.
AC A0A0V1DAN1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Sortilin-related receptor {ECO:0000313|EMBL:KRY58656.1};
GN Name=SORL1 {ECO:0000313|EMBL:KRY58656.1};
GN ORFNames=T03_7327 {ECO:0000313|EMBL:KRY58656.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58656.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY58656.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY58656.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:KRY58656.1}.
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DR EMBL; JYDI01000019; KRY58656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DAN1; -.
DR STRING; 45882.A0A0V1DAN1; -.
DR Proteomes; UP000054653; 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; IPR036508; Chitin-bd_dom_sf.
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; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00192; LDLa; 4.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
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}; Receptor {ECO:0000313|EMBL:KRY58656.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..694
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006876591"
FT DOMAIN 450..521
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|SMART:SM00494"
FT REGION 158..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 555..570
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 639..654
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 677..692
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 694 AA; 79003 MW; FA40FBD8B94863AE CRC64;
MMHFLILLVL LKIHQTEAVN KDDTTLNATS TPTSVEDIRH NLVQNDRPQI FVPPFFSNIF
NKGATAAETH ENAAKAGIPP VPVRKLPELQ ESQHPMQTKM MLPKTALPKY QPYFVMPPFL
QQRAQFNQQP QNPYSNGPPQ TAAWKNFSNR SNFNQRISTS ANEKPSQQWS QQSTDGAAPP
PPPPVQLQQE NNLYTSQQKK NNFQMPFQFP ILQPYPFWSL LQNIHSNNMH NPSPSGPTLP
RTYNVDKGKL QNQNLFENGM NFIPSLYPTN NIKPWPMVNS QPNAMPMMSN SRPSEALLQQ
FDPQSGLFFE KPKIPMQPPP PPPPLPAPRP VMTKQFQYPV PQFELPRPKP TPPTFILRTQ
LPPTANFKTV NEIEDKQQHQ HTQMINYLDR TNSIVNPETR PIQYQMEPPL LNVDDLQQPM
KASGYYHQPS SSINNDSTTY MLSLEQSPIN FCNPLEFNEQ VLASLNLKRV DYFIANMSCS
SVFFQCSMQT TFVRRCAGAD QVFDESTVNC NYRHSVKSCL EYDHVLHCTI KNQCLSDEYA
CCAAPQQCIP YAKRCDGIVD CADGEDENNC PTCSINEFPC LIGGTCIPME RRCNGMPDDC
FDNSNADEKY CEYCGVGKFY CYKSDPNYEY SCIDANQRCD GVKDCQGGED ELNCKRQGAQ
FLLCENQRQS VPRKQWCDGN EDCADGSDEI YCEY
//
