ID A0A093GZC4_TYTAL Unreviewed; 915 AA.
AC A0A093GZC4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Low-density lipoprotein receptor-related protein 6 {ECO:0000313|EMBL:KFV47848.1};
DE Flags: Fragment;
GN ORFNames=N341_02167 {ECO:0000313|EMBL:KFV47848.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV47848.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV47848.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV47848.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK379919; KFV47848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093GZC4; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
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; PTHR46513:SF36; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00135; LY; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF63825; YWTD domain; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS51120; LDLRB; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipoprotein {ECO:0000313|EMBL:KFV47848.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFV47848.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 37..79
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 80..122
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 163..205
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 212..250
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 346..388
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 389..433
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 434..476
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 526..570
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 784..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 590..605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 608..620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 615..633
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 627..642
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 646..658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 653..671
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 665..680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV47848.1"
FT NON_TER 915
FT /evidence="ECO:0000313|EMBL:KFV47848.1"
SQ SEQUENCE 915 AA; 101881 MW; 91E8C8E83049DBB6 CRC64;
VSLQTISRAF MNGSALEHVV EFGLDYPEGM AVDWLGKNLY WADTGTNRIE VSKLDGQHRQ
VLVWKDLDSP RALALDPAEG FMYWTEWGGK PKIDRAAMDG SERTTLVPNV GRANGLTIDY
AKRRLYWTDL DTNLIESSNM LGLDREIIAD DLPHPFGLTQ YQDYIYWTDW SRRSIERANK
TSGQNRTIIQ GHLDYVMDIL VFHSSRQAGW NECASSNGHC SHLCLAVPVG GFVCGCPAHY
SLNSDNRTCS APTTFLLFSQ KNAINRMVID EQQSPDIILP IHSLRNVRAI DYDPLDKQLY
WIDSRQNIIR KAQEDGSQSL TVVTSPVPNQ NLDMQPYDLS IDIYSRYIYW TCEATNVINV
TRLDGRPMGV VLKGDQDRPR AIVVNPEKGY MYFTNLQERS PKIERAALDG TEREVLFFSG
LSKPIALAID SQLGKLFWAD SDLRRIESSD LSGANRIVLE DSNILQPVGL TVFENWLYWI
DRQQQMIEKI DMTGREGRTK VQARIAQLSD IHAVKELNVQ EYRQHPCSQD NGGCSHICIV
KGDGTTRCSC PVHLVLLQDE LSCGEPPTCS PQQFTCFTGE IDCIPVAWRC DGFTECEDHS
DEKNCPVCSD TQFQCESGQC IDSALRCNGE ANCQDNSDEK NCEVLCLTDQ FRCASGQCIG
KSKKCDHNLD CSDSSDEQGC YTTEEPAPQP NNTIGSIIGV ILTVFVVGAM YFICQRVLCP
RMKGDGETMT NDYVVHGPAS VPLGYVPHPS SLSGSLPGMS RGKSVISSLS IMGGSSGPPY
DRAHVTGASS SSSSSTKGTY FPPILNPPPS PATERSHYTM EFGYSSNSPS THRSYSYRPY
SYRHFAPPTT PCSTDVCDSD YAPSRRLTAA TAQGYTRQYL SAEENYESCP PSPYTERSYS
HHLYPPPPSP CTDSS
//
