SAMD1_RABIT
ID SAMD1_RABIT Reviewed; 550 AA.
AC Q6SPE9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Atherin;
DE AltName: Full=Sterile alpha motif domain-containing protein 1;
DE Short=SAM domain-containing protein 1;
GN Name=SAMD1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RX PubMed=16159594; DOI=10.1016/j.atherosclerosis.2005.01.041;
RA Lees A.M., Deconinck A.E., Campbell B.D., Lees R.S.;
RT "Atherin: a newly identified, lesion-specific, LDL-binding protein in human
RT atherosclerosis.";
RL Atherosclerosis 182:219-230(2005).
CC -!- FUNCTION: Unmethylated CpG islands (CGIs)-binding protein which
CC localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional
CC repressor. Tethers L3MBTL3 to chromatin and interacts with the KDM1A
CC histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at
CC CGIs. Plays a role in atherogenesis by binding with LDL on cell surface
CC and promoting LDL oxidation which leads to the formation of foam cell.
CC {ECO:0000250|UniProtKB:Q6SPF0}.
CC -!- SUBUNIT: Homopolymerize into a closed pentameric ring. Interacts (via
CC SAM domain) with L3MBTL3 (via SAM domain); the interaction mediates
CC L3MBTL3 binding to chromatin. Interacts (via WH domain) with KDM1A; the
CC interaction modulates KDM1A function. {ECO:0000250|UniProtKB:Q6SPF0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6SPF0}.
CC Chromosome {ECO:0000250|UniProtKB:Q6SPF0}. Secreted
CC {ECO:0000250|UniProtKB:Q6SPF0}. Note=In atherosclerotic lesions, it is
CC found in the extracellular compartment and in foam cells cytoplasm.
CC {ECO:0000250|UniProtKB:Q6SPF0}.
CC -!- DOMAIN: Winged-helix (WH) domain directly recognizes and binds
CC unmethylated CpG-containing DNA via simultaneous interactions with both
CC the major and the minor groove of DNA. {ECO:0000250|UniProtKB:Q6SPF0}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY453841; AAR24088.1; -; mRNA.
DR RefSeq; NP_001075633.1; NM_001082164.1.
DR AlphaFoldDB; Q6SPE9; -.
DR SMR; Q6SPE9; -.
DR PRIDE; Q6SPE9; -.
DR GeneID; 100008923; -.
DR KEGG; ocu:100008923; -.
DR CTD; 90378; -.
DR InParanoid; Q6SPE9; -.
DR OrthoDB; 619766at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:UniProtKB.
DR GO; GO:0090077; P:foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0034439; P:lipoprotein lipid oxidation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0090308; P:regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Nucleus; Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..550
FT /note="Atherin"
FT /id="PRO_0000279495"
FT DOMAIN 474..542
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..99
FT /note="Winged-helix domain"
FT /evidence="ECO:0000250|UniProtKB:Q6SPF0"
FT REGION 93..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..358
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6SPF0"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6SPF0"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6SPF0"
SQ SEQUENCE 550 AA; 57020 MW; AF1CF2B780D879A7 CRC64;
MAGPPALPPP ETAAAATTAA AAASSSAASP HYQEWILDTI DSLRSRKARP DLERICRMVR
RRHGPEPERT RAELEKLIQQ RAVLRVSYKG SISYRNAARV QPPRRGATPP APPRAPRGGP
AAAAAPPPTP APPPPPAPVA AAAAPARAPR AAAAAAAATA PPSPGPAQPG PRAQRAAPLA
APPPAPAAPP AAAPPAGPRR APPPAAAVAA RESPLPPPPQ PPAPPQQQQQ PPPPPPPQQP
QPPPEGGAAR AGGPARPVSL REVVRYLGGS SGAGGRLTRG RVQGLLEEEA AARGRLERTR
LGALALPRGD RPGRAPPAAS ARAARNKRAG EERVLEKEEE EEEEEDDEDD DDDVVSEGSE
VPESDRPAGA QHHQLNGGER GPQTAKERAK EWSLCGPHPG QEEGRGPAAG SGTRQVFSMA
ALSKEGGSAS STTGPDSPSP VPLPPGKPAL PGADGTPFGC PAGRKEKPAD PVEWTVMDVV
EYFTEAGFPE QATAFQEQEI DGKSLLLMQR TDVLTGLSIR LGPALKIYEH HIKVLQQGHF
EDDDPEGFLG
