SIDT1_RAT
ID SIDT1_RAT Reviewed; 831 AA.
AC Q6Q3F5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=SID1 transmembrane family member 1;
DE Flags: Precursor;
GN Name=Sidt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen L., Shao N., Shen B., Yang G., Liu Z., Cao G., Li J., Li S., Sun W.,
RA Zhou H.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: In vitro binds long double-stranded RNA (dsRNA) (500 and 700
CC base pairs), but not dsRNA shorter than 300 bp. Not involved in RNA
CC autophagy, a process in which RNA is directly imported into lysosomes
CC in an ATP-dependent manner, and degraded.
CC {ECO:0000250|UniProtKB:Q6AXF6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SID1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS87380.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY562215; AAS87380.1; ALT_INIT; mRNA.
DR RefSeq; NP_001094123.1; NM_001100653.1.
DR AlphaFoldDB; Q6Q3F5; -.
DR SMR; Q6Q3F5; -.
DR STRING; 10116.ENSRNOP00000002759; -.
DR GlyGen; Q6Q3F5; 7 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q6Q3F5; -.
DR PaxDb; Q6Q3F5; -.
DR GeneID; 288109; -.
DR KEGG; rno:288109; -.
DR UCSC; RGD:1559616; rat.
DR CTD; 54847; -.
DR RGD; 1559616; Sidt1.
DR eggNOG; ENOG502QUXZ; Eukaryota.
DR InParanoid; Q6Q3F5; -.
DR OrthoDB; 139174at2759; -.
DR PhylomeDB; Q6Q3F5; -.
DR PRO; PR:Q6Q3F5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0051033; F:RNA transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0050658; P:RNA transport; IBA:GO_Central.
DR InterPro; IPR025958; SID1_TM_fam.
DR PANTHER; PTHR12185; PTHR12185; 1.
DR Pfam; PF13965; SID-1_RNA_chan; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; RNA-binding; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..831
FT /note="SID1 transmembrane family member 1"
FT /id="PRO_0000032577"
FT TOPO_DOM 20..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..571
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..625
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..714
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..795
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 817..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 354..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 831 AA; 94145 MW; BC4F6B3EC0E668C0 CRC64;
MLDCPRLALL CALPWLLRAA VPGHRAEPLK RSAELPRNPR DPARGADFDR VYSGVVSLST
ENIYSFNHTS HPGQVTAVRV HVNSSSDNLD YPVLVVVRQQ KQVLSWQVPL PFQGLYQRSY
NYQEVSRTLC PSKATNETGP LEQLIFVDVA SMAPHGAHYK LLVTKIKHFQ LRTNVAFYFT
ASPSQPQYFL YKFPEDVDSV IIKVVSEKAY PCSVVSVQNI MCPVYDLDHD VEFNGVYQSM
TKQAAITLQK DFPDEQFFVV FVIKPEDYAC GGSFSIQENE NQTWNLQRSK NLKVTIVPSV
KGSVYVKSSL FSVFVFLSFY LGCLLVVFVH HMRFQRKPVD GSFGSGDGSG NMAVSHPITA
STPEGSNYGA IDESSSSPGR QMSSSDGGQP CHSDTDSSVE ESDFDTMPDI ESDKNVIRTK
MFLYLSDLSR KDRRIVSKKY KIYFWNIITI AVFYALPVMQ LVITYQTVVN VTGNQDICYY
NFLCAHPLGV LSAFNNILSN LGHVLLGFLF LLIVLRRDLL HRRALEAKDI FAMEYGIPKH
FGLFYAMGIA LMMEGVLSAC YHVCPNYSNF QFDTSFMYMI AGLCMLKLYQ TRHPDINASA
YSAYASFAVV ITLTVLGVVF GKNDVWFWII FSAIHVLASL ALSTQIYYMG RFKIDVSDTD
LGIFRRAAMV FYTDCIQQCS RPLYMDRMVL LIVGNLVNWS FALFGLIYRP RDFASYMLGI
FICNLLLYLA FYIIMKLRSS EKVLPLPVFC IVATAVVWAA ALYFFFQNLS SWEGTPAESR
EKNRECVLLG FFDDHDIWHF LSATALFFSF LVLLTLDDDL DVVRRDQIPV F
