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Database: UniProt
Entry: A0A369SSL3_9METZ
LinkDB: A0A369SSL3_9METZ
Original site: A0A369SSL3_9METZ 
ID   A0A369SSL3_9METZ        Unreviewed;       845 AA.
AC   A0A369SSL3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Low-density lipoprotein receptor-related protein 4 {ECO:0000313|EMBL:RDD47933.1};
GN   ORFNames=TrispH2_000491 {ECO:0000313|EMBL:RDD47933.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD47933.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD47933.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD47933.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD47933.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
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:RDD47933.1}.
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DR   EMBL; NOWV01000001; RDD47933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369SSL3; -.
DR   STRING; 287889.A0A369SSL3; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
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; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
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; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00057; Ldl_recept_a; 7.
DR   Pfam; PF00058; Ldl_recept_b; 4.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 7.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57424; LDL receptor-like module; 7.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 5.
DR   PROSITE; PS50068; LDLRA_2; 7.
DR   PROSITE; PS51120; LDLRB; 3.
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:RDD47933.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:RDD47933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        744..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          303..343
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          344..383
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          477..518
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          519..562
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          563..605
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        61..73
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        68..86
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        80..95
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        101..113
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        108..126
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        120..135
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        140..152
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        147..165
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        159..174
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        183..195
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        190..208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        202..217
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        222..234
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        229..247
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        241..256
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        348..358
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   845 AA;  93075 MW;  6F6C6A4E804B32F3 CRC64;
     MPGIVETHQP AKQRTAQVTC HPNNEFTCND GKCITTSWVC DGQNDCIDGS DEGSHCLTKT
     CTPDEFSCGN GVCIKRDYVC DQVDDCGNSA DERNCTKVAT CSPQQFTCNN SHCINSAWRC
     DNDNDCGDNS DEWNCPNKTC GPELFQCSSG DCIKKSWLCD GERDCTDGSD EKNCSTSRPK
     HTCRAGEFQC KNWECIKSEW RCDGSTDCTD GSDELGCNKT TCKSGQFRCS AHICIDAHNV
     CDGISDCANS RDEQNCTTPT PPNLTCNSSQ FTCHTNKSCI SMKLVCNGKF DCEDKSDEPA
     TCNINECSEY NGHCSQNCVN TKVGYYCACN PGYTLDTDGR TCLDINECNI SNPCSQMCEN
     TKGSYKCTCA DGYRLDADFK SCKALGPEPV LFFANRRDIH RFTIKGSRYN DVMKGLKGAI
     GIDVHVRKRL LFWTDIVSEK IGRVTLHSNG TVAGKNKYII SDGVLSPECV AVDWIHDTIY
     WTDTGLDAIK MSDLDGRYVK TIISNIADPR GLAVDPVDGY IYFTDWGSSA KIERAKLDGT
     QRQILVSTNV EWPNGLTIDY PQRKMYWVDG KHHHIESANL DGSGRRVILS KGIPHPFSIT
     VFENSVYWTD WESKTVETAN KLTGANRSVL LSDLYAPMGI TTFQLQRQPR HYDACHLNKG
     GCSQICVKTG DYKRTCLCKD GWQLDSDGTG CVLLPTQSYN CKSIDCGYGS CLINSTNGVP
     YCSCSVGYGG DNCTVITSAS TGEAMTIGVA AGCAIGFLII IIIIGYIVRR RHGKNKKTFD
     EFDIQSMTNR AMINETTEDI SKRPVNNSRP VSLAISNGNF SYSSRQHLVG SRFSMVSSQS
     VATQV
//
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