SIDT1_MOUSE
ID SIDT1_MOUSE Reviewed; 827 AA.
AC Q6AXF6; Q8R397;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=SID1 transmembrane family member 1;
DE Flags: Precursor;
GN Name=Sidt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF PHE-169 AND PRO-186.
RX PubMed=26067272; DOI=10.1074/jbc.m115.658864;
RA Li W., Koutmou K.S., Leahy D.J., Li M.;
RT "Systemic RNA interference deficiency-1 (SID-1) extracellular domain
RT selectively binds long double-stranded RNA and is required for RNA
RT transport by SID-1.";
RL J. Biol. Chem. 290:18904-18913(2015).
RN [4]
RP FUNCTION.
RX PubMed=27046251; DOI=10.1080/15548627.2016.1145325;
RA Aizawa S., Fujiwara Y., Contu V.R., Hase K., Takahashi M., Kikuchi H.,
RA Kabuta C., Wada K., Kabuta T.;
RT "Lysosomal putative RNA transporter SIDT2 mediates direct uptake of RNA by
RT lysosomes.";
RL Autophagy 12:565-578(2016).
CC -!- FUNCTION: In vitro binds long double-stranded RNA (dsRNA) (500 and 700
CC base pairs), but not dsRNA shorter than 300 bp (PubMed:26067272). Not
CC involved in RNA autophagy, a process in which RNA is directly imported
CC into lysosomes in an ATP-dependent manner, and degraded
CC (PubMed:27046251). {ECO:0000269|PubMed:26067272,
CC ECO:0000269|PubMed:27046251}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AXF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AXF6-2; Sequence=VSP_013522;
CC -!- SIMILARITY: Belongs to the SID1 family. {ECO:0000305}.
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DR EMBL; BC025888; AAH25888.1; -; mRNA.
DR EMBL; BC079584; AAH79584.1; -; mRNA.
DR CCDS; CCDS28185.1; -. [Q6AXF6-1]
DR RefSeq; NP_001152891.1; NM_001159419.1.
DR RefSeq; NP_932151.2; NM_198034.3. [Q6AXF6-1]
DR AlphaFoldDB; Q6AXF6; -.
DR STRING; 10090.ENSMUSP00000038433; -.
DR GlyConnect; 2711; 5 N-Linked glycans (2 sites).
DR GlyGen; Q6AXF6; 7 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; Q6AXF6; -.
DR PhosphoSitePlus; Q6AXF6; -.
DR PaxDb; Q6AXF6; -.
DR PRIDE; Q6AXF6; -.
DR ProteomicsDB; 261400; -. [Q6AXF6-1]
DR ProteomicsDB; 261401; -. [Q6AXF6-2]
DR Antibodypedia; 32584; 155 antibodies from 28 providers.
DR DNASU; 320007; -.
DR Ensembl; ENSMUST00000136381; ENSMUSP00000115372; ENSMUSG00000022696. [Q6AXF6-1]
DR GeneID; 320007; -.
DR KEGG; mmu:320007; -.
DR UCSC; uc007zhd.1; mouse. [Q6AXF6-1]
DR CTD; 54847; -.
DR MGI; MGI:2443155; Sidt1.
DR VEuPathDB; HostDB:ENSMUSG00000022696; -.
DR eggNOG; ENOG502QUXZ; Eukaryota.
DR GeneTree; ENSGT00390000010091; -.
DR HOGENOM; CLU_059625_0_0_1; -.
DR InParanoid; Q6AXF6; -.
DR OMA; CPNHSNF; -.
DR OrthoDB; 139174at2759; -.
DR BioGRID-ORCS; 320007; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Sidt1; mouse.
DR PRO; PR:Q6AXF6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6AXF6; protein.
DR Bgee; ENSMUSG00000022696; Expressed in primary visual cortex and 85 other tissues.
DR ExpressionAtlas; Q6AXF6; baseline and differential.
DR Genevisible; Q6AXF6; MM.
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:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:WormBase.
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 Alternative splicing; Glycoprotein; Membrane; Reference proteome;
KW RNA-binding; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..827
FT /note="SID1 transmembrane family member 1"
FT /id="PRO_0000032576"
FT TOPO_DOM 20..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..572
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..626
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..710
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..741
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 763..791
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 792..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 813..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 344..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..396
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:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..382
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013522"
FT MUTAGEN 169
FT /note="F->T: Decreased affinity for 700-bp RNA."
FT /evidence="ECO:0000269|PubMed:26067272"
FT MUTAGEN 186
FT /note="P->L: Decreased affinity for 700-bp RNA."
FT /evidence="ECO:0000269|PubMed:26067272"
SQ SEQUENCE 827 AA; 93896 MW; 7B92AD693E134D87 CRC64;
MLDCLRLALL CALPWLLRAA VPGHQEEPLA KSAELRRDPR DPARGADFDR VYSGVVSLST
ENIYSFNHTS HPGQVTAVRV HVNSSSDNLD YPVLVVVRQQ KEVLSWQVPL LFQGLYQRSY
NYQEVSRTLC PSKATNETGP LEQLIFVDVA SMAPHGAHYK LLVTKIKHFQ LPTNVAFYFT
ASPSQPQYFL YKFPEDVDSV IIKVVSEKAY PCSVVSVQNI MCPVYDLDHN VEFNGVYQSM
TKKAAITLQK KDFPDEQFFV VFVIKPEDYA CGGSFSIQEN ENQTWNLQRS KNLKVTIVPS
IKESVYVKSS LFSIFVFLSF YLGCLLVVLV HHVRFQRKSI DGSFGSSDGS GNMAVSHPIT
ASTPEGSNYG AIDESSSSPG RQMSSSDGGQ PCHSDTDSSV EESDFDTMPD IESDKNVIRT
KMFLYLSDLS RKDRRIVSKK YKIYFWNIIT IAVFYALPVM QLVITYQTVV NVTGNQDICY
YNFLCAHPLG VLSAFNNILS NLGHVLLGFL FLLIVLRRDL LHRRALEAKD IFAMEYGIPK
HFGLFYAMGI ALMMEGVLSA CYHVCPNYSN FQFDTSFMYM IAGLCMLKLY QTRHPDINAS
AYSAYASFAV VITLTVLGVV FGKNDVWFWI IFSAIHILSS LALSTQIYYM GRFKIDLGIF
RRAAMVFYTD CIQQCSRPLY MDRMVLLIVG NLVNWSFAFF GLIYRPRDFA SYMLGIFICN
LLLYLAFYII MKLRSSEKVL PLPVFCIAAT AVVWAAALYF FFQNLSSWEG TPAESREKNR
ECVLLDFFDD HDIWHFLSAT ALFFSFLVLL TLDDDLDVVR RDQIPVF
