ID B4DJ13_HUMAN Unreviewed; 1158 AA.
AC B4DJ13;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=cDNA FLJ50970, highly similar to Sortilin-related receptor {ECO:0000313|EMBL:BAG58675.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG58675.1};
RN [1] {ECO:0000313|EMBL:BAG58675.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Hippocampus {ECO:0000313|EMBL:BAG58675.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) 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; AK295878; BAG58675.1; -; mRNA.
DR AlphaFoldDB; B4DJ13; -.
DR PeptideAtlas; B4DJ13; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 5.
DR CDD; cd00112; LDLa; 11.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR24270:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF00057; Ldl_recept_a; 10.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00192; LDLa; 11.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 11.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 11.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:BAG58675.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1080..1103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 501..593
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 597..689
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 693..788
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 878..973
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DISULFID 22..34
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 29..47
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 41..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 82..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 102..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 109..127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 121..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 143..155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 150..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 188..206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 200..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 269..281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 276..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 288..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 320..338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 332..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 363..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 370..388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 382..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 435..450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 478..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1158 AA; 129748 MW; 7434B012FE5FC151 CRC64;
MCDCPQGYQL KNNTCVKEEN TCLRNQYRCS NGNCINSIWW CDFDNDCGDM SDERNCPTTI
CDLDTQFRCQ ESGTCIPLSY KCDLEDDCGD NSDESHCEMH QCRSDEYNCS SGMCIRSSWV
CDGDNDCRDW SDEANCTAIY HTCEASNFQC RNGHCIPQRW ACDGDTDCQD GSDEDPVNCE
KKCNGFRCPN GTCIPSSKHC DGLRDCSDGS DEQHCEPLCT HFMDFVCKNR QQCLFHSMVC
DGIIQCRDGS DEDAAFAGCS QDPEFHKVCD EFGFQCQNGV CISLIWKCDG MDDCGDYSDE
ANCENPTEAP NCSRYFQFRC ENGHCIPNRW KCDRENDCGD WSDEKDCGDS HILPFSTPGP
STCLPNYYRC SSGTCVMDTW VCDGYRDCAD GSDEEACPLL ANVTAASTPT QLGRCDRFEF
ECHRPKTCIP NWKRCDGHQD CQDGRDEANC PTHSTLTCMS REFQCEDGEA CIVLSERCDG
FLDCSDESDE KACSDELTVY KVQNLQWTAD FSGDVTLTWM RPKKMPSASC VYNVYYRVVG
ESIWKTLETH SNKTNTVLKV LKPDTTYQVK VQVQCLSKAH NTNDFVTLRT PEGLPDAPRN
LQLSLPREAE GVIVGHWAPP IHTHGLIREY IVEYSRSGSK MWASQRAASN FTEIKNLLVN
TLYTVRVAAV TSRGIGNWSD SKSITTIKGK VIPPPDIHID SYGENYLSFT LTMESDIKVN
GYVVNLFWAF DTHKQERRTL NFRGSILSHK VGNLTAHTSY EISAWAKTDL GDSPLAFEHV
MTRGVRPPAP SLKAKAINQT AVECTWTGPR NVVYGIFYAT SFLDLYRNPK SLTTSLHNKT
VIVSKDEQYL FLVRVVVPYQ GPSSDYVVVK MIPDSRLPPR HLHVVHTGKT SVVIKWESPY
DSPDQDLLYA IAVKDLIRKT DRSYKVKSRN STVEYTLNKL EPGGKYHIIV QLGNMSKDSS
IKITTVSLSA PDALKIITEN DHVLLFWKSL ALKEKHFNES RGYEIHMFDS AMNITAYLGN
TTDNFFKISN LKMGHNYTFT VQARCLFGNQ ICGEPAILLY DELGSGADAS ATQAARSTDV
AAVVVPILFL ILLSLGVGFA ILYTKHRRLQ SSFTAFANSH YSSRLGSAIF SSGDDLGEDD
EDAPMITGFS DDVPMVIA
//
