ID A0A085M2L6_9BILA Unreviewed; 1267 AA.
AC A0A085M2L6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Low-density lipoprotein receptor domain class A {ECO:0008006|Google:ProtNLM};
GN ORFNames=M513_07675 {ECO:0000313|EMBL:KFD51462.1}, M514_07675
GN {ECO:0000313|EMBL:KFD61924.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD51462.1, ECO:0000313|Proteomes:UP000030764};
RN [1] {ECO:0000313|EMBL:KFD51462.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD61924.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD51462.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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}.
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DR EMBL; KL363239; KFD51462.1; -; Genomic_DNA.
DR EMBL; KL367606; KFD61924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085M2L6; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; 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; 13.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 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:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 13.
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; 1.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..372
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 962..1202
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 252..298
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 395..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 402..420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 414..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 451..466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 468..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 475..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 487..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 504..516
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 542..554
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 549..567
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 561..576
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 578..590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 585..603
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 623..641
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 680..695
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 698..710
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 705..723
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 717..732
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 742..760
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 754..769
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 811..829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 823..838
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1214..1226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1221..1239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1267 AA; 141391 MW; 951B26DAE1AB72E3 CRC64;
MDTGLPGKYS YYGDSDRRNK AIKEAPSVLE HHRQASRTGH PIMAPPIDSR RQKMRTLYKF
GFVGVICLIF ILVIVLTSIL STDGSSKAGN TDSSTYDQHR KFSCYFACDN PNYRNESLPA
EETPSLESIY NKKIRAAFQN TTLQPYLDGI DFLGIDENDN HSVAKINAIL TFINSSKAEQ
FLNASFIADT LRTNVDCAQK ETVNVTEIEE PTKVTTQAPV PENTSTISPI SAETTLPPPT
KNYSVYPLLP FCNGHGWTDT CYPNYLGYKT PEEATASLSF FQIMTQQNCH HHIQYFSCAL
LQPPCSRTKG RIPICKPFCE GVKSSCWELL RLTEIGRKDL CSLENANYGP QCSQICSSSD
FICAKTKMCI DEKRRCDAKL DCGPGDLSDE LNCTCKSNQF RCSNGMCIKS SLRCNNVNDC
GEWEDEIGCT CREGWKNCSQ TGQCFPSSAW CDQKFDCADQ SDETECLCAP HQFKCQNGLC
RPALDRCNGV NDCGDFSDEF DCTCEADQFL CDKHLCKYYA TDWCNGKKNC ADGTDEPDKC
QCKPGQYKCD DGTCIPEHRA CDRSIDCPDG SDERHCKCSS LEFECEPGYC IPLEQVCDGV
EQCPNKADEL QNCECPMPTH FRCNNGQCLP LTRYCNFVSD CPDKEDEVEN CNRICPAGYA
LKCILRKNSE YACLPADKIC DGVPDCDQKE DEKNCGECRK DQFRCNDGTC LPLSAYCNGV
HDCVDLSDEG NCTCNPAFQF SCDDGWCYMK EQRCDGIAQC ADLSDEAQCS CAELLAKQHP
ERICDQVADC QDLSDEQNCD SIYTSANAFI CYAGRAIDVS KVCDGKKDCP LGDDERHCAT
LVANVTEDLN RYWEFRDTGT VYFRRNGVWA PVCALANNTE TLIVTAQHVC AQNLYQTVAS
IAMVAWNRTE AMYMPLSKYT SGQTLAPASR ECDSGQVLYV KCSHQTCGDN PYNLGEKSNV
ALLGSRTNTL PFFVSIYSDQ IHRCAGNLLG KMWVLTTASC LDGTNEKTLT VRVSVQRNSS
LSPYDQFSPV SHQLKHSMYA GRPGGTNDIA LLRLAVPLKS TPMAQPICLE SLDTIADDIR
STKGKTTTMF TLGMGRLRRK KITADYPDLG EITITNASSC RQHRTVRLER LNIGDEQFCA
FEQPDTYRCQ AELGSPILKK HSDNQWHLIG LTSRPHSCTS FKYPSIYMNI THYTKWIEHA
ADVLHAQKPY MRRCDNGMFA CLLGNCIDAS AICDGVRNCA FGEDEKCEVT LTKDDMTFRV
KPSSQLT
//
