ID A0A0V1A6S7_9BILA Unreviewed; 930 AA.
AC A0A0V1A6S7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Low-density lipoprotein receptor-related protein 2 {ECO:0000313|EMBL:KRY20560.1};
GN Name=Lrp2 {ECO:0000313|EMBL:KRY20560.1};
GN ORFNames=T12_5596 {ECO:0000313|EMBL:KRY20560.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY20560.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY20560.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY20560.1};
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: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:KRY20560.1}.
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DR EMBL; JYDQ01000024; KRY20560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A6S7; -.
DR STRING; 990121.A0A0V1A6S7; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR24270:SF61; CD320 ANTIGEN; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF00058; Ldl_recept_b; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 1.
PE 4: Predicted;
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}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipoprotein {ECO:0000313|EMBL:KRY20560.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KRY20560.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..930
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006874412"
FT TRANSMEM 820..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 615..657
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 768..811
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 908..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 52..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 94..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 101..119
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 113..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 160..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 179..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 186..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 198..213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 228..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 235..253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 247..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 288..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 313..325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 320..338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 801..810
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 930 AA; 105665 MW; 7E4F2B215C231998 CRC64;
MKCKNNLCKL LFLYVLFLAN SRSKATETEK LKSEDLFECW KSETYIPVEK VCDGKVDCQD
NEDENICPNV KNVTTEEDVE KHQRSIKAKN EKKCGIHKFR CKNGKCISKK KLCDGEFDCI
DGSDEQNCSA KMGLMKSDCP SNTFHCNSEP SICLPVDLIC DFERDCPNGE DEMHCEHECL
ENQLKCKNNR CIDKEFICNG MDDCGDGTDE ESCMDHLLFE EYSNRLECKG FEYKCYMGPC
IPTSVVCDGF RDCPNGDDEH KCPTFHICHE NEFQCKDKLF CFPESWVCDG IADCRDKSDE
IDCPNKDFLY DLCSSDSFIC NDGSCIAREK MCDGSADCND KSDEHIHCGA CKTENGGCPN
KCREGAFGVE CQCGNTWRQA SLFSSEDHCP KVDYCELHTD ECDHFCHSNA TNFSCSCSEG
YDLEYNLRTC KLKHKHLGHL LFSIGHQIRN ISINSKEYIG ADYTILFDEE CSKEKDNGRM
MALDYNYKKK EILFSRKTSV YSLANNEEKC LFGEFLSFVN VAVDWVTSNI YFADEMLSRI
GVCNEDGRYC TVFDKLSLRR PRGLATHPKY GYLFLCDWGT NASIIRVAMD GQSWQVLHHN
KLSWPNSVAV DYVRDMVYWM DAKYKLIERS RLDGSEREVV ASKGVHHPFD MVVFDGRVFW
SDWTAKSLLW VSIFNGSEEG SVQSVEFDPY GIAINHPVYQ NQTLENPCAE NDCSHLCTIS
PRDSPKGPLK HTCLCPSGYT MYNDKKQCHI SPNSTRLRGT LKWCTRTFEE NCNKGTACKN
GGTCHMLYDA ENHQTDIVCD CPKNHAGLYC EISPIVPSKW PLITLIFTGV SVAIAIVYSL
IKFTKNHSQS STYRNGVKFS MHPFNPALAE VQFLEKESEN TEEKIHLAAM QPCESLTEKC
AFINASYSPS SSNEQEEICS INDSQNSSFS
//
