ID A0A091MMZ1_9PASS Unreviewed; 1460 AA.
AC A0A091MMZ1;
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:KFP76552.1};
DE Flags: Fragment;
GN ORFNames=N310_12600 {ECO:0000313|EMBL:KFP76552.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP76552.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP76552.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP76552.1};
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; KK831018; KFP76552.1; -; Genomic_DNA.
DR Proteomes; UP000053537; 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; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
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:SF40; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 6; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF14670; FXa_inhibition; 4.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00058; Ldl_recept_b; 10.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00135; LY; 17.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS51120; LDLRB; 13.
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:KFP76552.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFP76552.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1224..1244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 1..43
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 44..86
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 135..174
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 222..264
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 265..307
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 308..351
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 352..394
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 441..478
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 524..566
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 567..609
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 610..652
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 693..735
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 742..780
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REPEAT 876..918
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 919..963
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 964..1006
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1056..1100
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 1307..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1120..1135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1138..1150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1145..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1157..1172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1176..1188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1183..1201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1195..1210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP76552.1"
FT NON_TER 1460
FT /evidence="ECO:0000313|EMBL:KFP76552.1"
SQ SEQUENCE 1460 AA; 163342 MW; EC9EA010244011DD CRC64;
FMYWTDWGEV PKIERAGMDG SSRSVIVNTD IYWPNGLTLD YEEQKLYWAD AKLNFIHKSN
LDGSHRQAVV KGSLPHPFAL TLFGDTLYWT DWNTHSILAC SKYSGEDLRE IHSNIFSPMD
IHAFSQKRQP NATNPCGINN GGCSHLCLMS PTEPSYQCAC PTGVKLLENG KTCKDGATAL
LLLARRTDLR RISLDTPDFT DIVLPLEDIR HAIAIDFDPL EGYIYWTDDE VRAIRRSFID
GSGSQFVVTA QIAHPDGIAV DWVARNLYWT DTGTDRIEVT RLNGTMRKIL ISEDLEEPRA
IVLDPMVGYM YWTDWGEIPK IERAALDGSD RIVLVNTSLG WPNGLALDYA ESKIYWGDAK
TDKIEVMNAD GTGRRVLVED KLPHIFGFTL LGEYIYWTDW QRRSIERVHK RTAEREIIID
QLPDLMGLKA TNVHQIIGTN PCAEDNGGCS HLCLYRPQGL RCACPIGLEL INDMKTCIVP
EAFLLFSRRA DIRRISLETN NNNVAIPLTG VKEASALDFD VTDNRIYWTD ISLKTISRAF
MNGSALEHVV EFGLDYPEGM AVDWLGKNLY WADTGTNRIE VSKLDGQHRQ VLVWKDLDSP
RALALDPAEG FMYWTEWGGK PKIDRAAMDG SERTTLVPNV GRANGLTIDY AKRRLYWTDL
DTNLIESSNM LGLDREIIAD DLPHPFGLTQ YQDYIYWTDW SRRSIERANK TSGQNRTIIQ
GHLDYVMDIL VFHSSRQAGW NECASSNGHC SHLCLAVPIG GFVCGCPAHY SLNSDNRSCS
APTTFLLFSQ KNAINRMVID EQQSPDIILP IHSLRNVRAI DYDPLDKQLY WIDSRQNIIR
KAQEDGSQSL TVVTSPVPNQ NLDMQPYDLS IDIYSRYIYW TCEATNVINV TRLDGRPVGV
VLKGDQDRPR AIVVNPEKGY MYFTNLQERS PKIERAALDG TEREVLFFSG LSKPIAIAID
SQLGKLFWAD SDLRRIESSD LSGANRIVLE DSNILQPVGL TVFENWLYWI DRQQQMIEKI
DMTGREGRTK VQARIAQLSD IHAVKELNIQ EYRQHPCSQD NGGCSHICIV KGDGTTRCSC
PVHLVLLQDE LSCGEPPTCS PQQFTCFTGE IDCIPVAWRC DGFTECEDHS DEKNCPVCSD
TQFQCESGQC IDSALRCNGE ANCQDNSDEK NCEVLCLTDQ FRCASGQCIG KSKKCDHNLD
CSDSSDEQEC YTTEEPAPQP NNTIGSIIGV ILTVFVVGAM YFICQRVLCP RMKGDGETMT
NDYVVHGPAS VPLGYVPHPS SLSGSLPGMS RGKSVISSLS IMGGSSGPPY DRAHVTGASS
SSSSSTKGTY FPPILNPPPS PATERSQYTM EFGYSSNSPS THRSYSYRPY SYRHFAPPTT
PCSTDVCDSD YAPSRRGTAG TAXXXXXXXX XXPVPPPPTP RSQYLSAEEN YESCPPSPYT
ERSYSHHLYP PPPSPCTDSS
//
