ID Q59H02_HUMAN Unreviewed; 793 AA.
AC Q59H02;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Suppression of tumorigenicity variant {ECO:0000313|EMBL:BAD92194.1};
DE Flags: Fragment;
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:BAD92194.1};
RN [1] {ECO:0000313|EMBL:BAD92194.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:BAD92194.1};
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane, coated pit
CC {ECO:0000256|ARBA:ARBA00037878}.
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; AB208957; BAD92194.1; -; mRNA.
DR RefSeq; NP_001129175.1; NM_001135703.2.
DR RefSeq; NP_038465.1; NM_013437.4.
DR AlphaFoldDB; Q59H02; -.
DR PeptideAtlas; Q59H02; -.
DR DNASU; 29967; -.
DR GeneID; 29967; -.
DR KEGG; hsa:29967; -.
DR CTD; 29967; -.
DR PharmGKB; PA134921850; -.
DR OrthoDB; 2916406at2759; -.
DR BioGRID-ORCS; 29967; 12 hits in 1164 CRISPR screens.
DR GenomeRNAi; 29967; -.
DR Genevisible; Q59H02; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF47; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 12; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 5.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 5.
PE 2: Evidence at transcript level;
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|ARBA:ARBA00023176}.
FT DOMAIN 1..93
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 193..306
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 557..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 100..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 107..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 119..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 173..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 329..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 367..382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 385..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 392..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 404..419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAD92194.1"
SQ SEQUENCE 793 AA; 87909 MW; E3B82E6D458917FA CRC64;
ACDYPAKINC SWFIRANPGE IITISFQDFD IQGSRRCNLD WLTIETYKNI ESYRACGSTI
PPPYISSQDH IWIRFHSDDN ISRKGFRLAY FSGKSEEPNC ACDQFRCGNG KCIPEAWKCN
NMDECGDSSD EEICAKEANP PTAAAFQPCA YNQFQCLSRF TKVYTCLPES LKCDGNIDCL
DLGDEIDCDV PTCGQWLKYF YGTFNSPNYP DFYPPGSNCT WLIDTGDHRK VILRFTDFKL
DGTGYGDYVK IYDGLEENPH KLLRVLTAFD SHAPLTVVSS SGQIRVHFCA DKVNAARGFN
ATYQVDGFCL PWEIPCGGNW GCYTEQQRCD GYWHCPNGRD ETNCTMCQKE EFPCSRNGVC
YPRSDRCNYQ NHCPNGSDEK NCFFCQPGNF HCKNNRCVFE SWVCDSQDDC GDGSDEENCP
VIVPTRVITA AVIGSLICGL LLVIALGCTC KLYSLRMFER RSFETQLSRV EAELLRREAP
PSYGQLIAQG LIPPVEDFPV CSPNQASVLE NLRLAVRSQL GFTSVRLPMA GRSSNIWNRI
FNFARSRHSG SLALVSADGD EVVPSQSTSR EPERNHTHRS LFSVESDDTD TENERRDMAG
ASGGVAAPLP QKVPPTTAVE ATVGACASSS TQSTRGGHAD NGRDVTSVEP PSVSPARHQL
TSALSRMTQG LRWVRFTLGR SSSLSQNQSP LRQLDNGVSG REDDDDVEML IPISDGSSDF
DVNDCSRPLL DLASDQGQGL RQPYNATNPG VRPSNRDGPC ERCGIVHTAQ IPDTCLEVTL
KNETSDDEAL LLC
//
