ID A0A0V1P2J3_9BILA Unreviewed; 1259 AA.
AC A0A0V1P2J3;
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 1B {ECO:0000313|EMBL:KRZ90426.1};
GN Name=Lrp1b {ECO:0000313|EMBL:KRZ90426.1};
GN ORFNames=T08_15050 {ECO:0000313|EMBL:KRZ90426.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ90426.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ90426.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ90426.1};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
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:KRZ90426.1}.
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DR EMBL; JYDM01000056; KRZ90426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1P2J3; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07066; CRD_FZ; 1.
DR CDD; cd00112; LDLa; 11.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 12.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF60; PROTEIN CBG07635; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 14.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 11.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 13.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Lipoprotein {ECO:0000313|EMBL:KRZ90426.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Receptor {ECO:0000313|EMBL:KRZ90426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..364
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 963..1211
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 244..290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 387..399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 394..412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 406..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 443..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 460..472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 467..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 479..494
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 496..508
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 534..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 541..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 553..568
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 593..605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 600..618
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 638..656
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 695..710
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 712..724
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 719..737
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 731..746
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 756..774
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 768..783
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 829..847
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 841..856
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1230..1248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1259 AA; 143288 MW; A8DCBB0DEF7701C9 CRC64;
MEAGVPGKYS QRGETDRRTS RGMKITHPTS LEHHEQRHIN RIQLNNENEH NRRFRGNLYK
FGCIISICVV FILVIVLSAL LSSEGNSSSA EEMTENMKRK FWCTFIQENS LEESTKMELE
LSTLLYLEMK FHSLQIASVL RSFFLINCRD NLNGVNVTCI LEFINEPSLE ELNVDFLKTL
FQTTIPRINV ESVQVEEIKQ PIIPVPTPES NSTEPTISTN TTIPSTPNQT TPSVITLFDL
VPFCTDFGWQ KTCYPNHLGY RNKYEVLASL SFFQILNKQQ CHKHVQIFAC LLLQPPCKEN
TGIVSVCRPF CEEVVSACSK SLDMTEIGEK NLCSDVISNY GPNCMQFCDK DNFICEQTRL
CINATRRCDG NLDCGANDIS DELNCECKSN EFRCRNGLCI SQSKTCNNEN DCGDWEDEKN
CTCRENWKKC TETGQCFPAS FWCDGEFHCG DKSDELQCEC PREQFICQNG ACMPENVRCN
GVNDCGDFSD EFDCECQAEQ FRCDKYLCKY FDNDWCNGKA DCVDGTDEPA NCTCKPGQFK
CDDGFCLAKH RVCDRYIDCK DGSDELHCGL EKKSLQKKTN IQLNQLHISN LDCTPEEFQC
EPGICIPVEK VCDGEANCAN RKDELQQCEC NSKEQFRCKN GQCMDINRYC NHRTDCLDGD
DEFQNCEGKC PPGYGKKCNL RTTGEYKCLP ESMMCDGVSD CERNEDEENC KCREDQFQCN
DGACKPWSLY CNSIHDCLDF SDETNCTCNE KYQETCHDGW CYDKNHRCDG KAQCADLSDE
YNCTCAEYLR KSNPEKLCDY VQDCADRTDE LNCSYIPNNL KNKYDTFLCY GGAALDRSKI
CDGNIDCPMG DDEYHCYFLM PKEGYDLNKP WVFQDAGVIF VQSKGSWGIV CAPSNENNNS
LNALAEHVCK RNLFHSVDYI SRVPLDNTQQ IPTYQLNSFN PKDFVQTDCP SKQTIAVMCK
SEICGQDPYK LSSPSVSLLQ STAMRTLPFF ASIYTDGKHR CSGIIYQRRW ILTSASCVEK
NDLFTMRVRV GQQRNSSLSP FDQFFYVAQA IKHSMYKPIP NVEHDIALLQ LDKNIQYTPF
VQPICLGNGK VDVSKLDTHT IGMGRLRRKA IKAEHADLTR LSVKNADICK SNLIVRLERV
KIAENQFCTL ERDKSYLCQG ETGSPILTQY SNGTWAVVGL TTDVNYCFKK KFPTIFTDLS
HYSEWIQYIT DYASKQKERK IVHCEGSFSC LLGNCIESAS VCDGIRDCAF GEDEICSYP
//
