SIDT2_RAT
ID SIDT2_RAT Reviewed; 832 AA.
AC D3ZEH5; D3ZSU1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=SID1 transmembrane family member 2;
DE Flags: Precursor;
GN Name=Sidt2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=20965152; DOI=10.1016/j.bbrc.2010.09.133;
RA Jialin G., Xuefan G., Huiwen Z.;
RT "SID1 transmembrane family, member 2 (Sidt2): A novel lysosomal membrane
RT protein.";
RL Biochem. Biophys. Res. Commun. 402:588-594(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mediates the translocation of RNA and DNA across the
CC lysosomal membrane during RNA and DNA autophagy (RDA), a process in
CC which RNA or DNA is directly imported into lysosomes in an ATP-
CC dependent manner, and degraded. Involved in the uptake of single-
CC stranded oligonucleotides by living cells, a process called gymnosis
CC (By similarity). In vitro, mediates the uptake of linear DNA more
CC efficiently than that of circular DNA, but exhibits similar uptake
CC efficacy toward RNA and DNA. Binds long double-stranded RNA (dsRNA)
CC (500 - 700 base pairs), but not dsRNA shorter than 100 bp (By
CC similarity). {ECO:0000250|UniProtKB:Q8CIF6,
CC ECO:0000250|UniProtKB:Q8NBJ9}.
CC -!- SUBUNIT: Interacts with adapter protein complex 1 (AP-1) and AP-2, but
CC not AP-3 and AP-4 (By similarity). Interacts with LAMP2 (By
CC similarity). {ECO:0000250|UniProtKB:Q8CIF6,
CC ECO:0000250|UniProtKB:Q8NBJ9}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBJ9};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NBJ9}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8NBJ9}. Note=Mainly localizes to
CC lysosomes and only partly to the plasma membrane (By similarity).
CC Lysosomal localization is required for SIDT2-mediated intracellular
CC degradation of endogenous RNA (By similarity).
CC {ECO:0000250|UniProtKB:Q8CIF6, ECO:0000250|UniProtKB:Q8NBJ9}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, brain, kidney and
CC intestine (at protein level). {ECO:0000269|PubMed:20965152}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:20965152}.
CC -!- SIMILARITY: Belongs to the SID1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDL95388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC096909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473975; EDL95388.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001101612.1; NM_001108142.1.
DR AlphaFoldDB; D3ZEH5; -.
DR STRING; 10116.ENSRNOP00000024239; -.
DR GlyGen; D3ZEH5; 10 sites.
DR iPTMnet; D3ZEH5; -.
DR PhosphoSitePlus; D3ZEH5; -.
DR SwissPalm; D3ZEH5; -.
DR PaxDb; D3ZEH5; -.
DR PeptideAtlas; D3ZEH5; -.
DR PRIDE; D3ZEH5; -.
DR GeneID; 315617; -.
DR KEGG; rno:315617; -.
DR CTD; 51092; -.
DR RGD; 1308311; Sidt2.
DR VEuPathDB; HostDB:ENSRNOG00000017871; -.
DR eggNOG; ENOG502QUXZ; Eukaryota.
DR HOGENOM; CLU_357018_0_0_1; -.
DR InParanoid; D3ZEH5; -.
DR OrthoDB; 139174at2759; -.
DR PhylomeDB; D3ZEH5; -.
DR TreeFam; TF313076; -.
DR PRO; PR:D3ZEH5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000017871; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; D3ZEH5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0035650; F:AP-1 adaptor complex binding; ISS:UniProtKB.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0051032; F:nucleic acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0051033; F:RNA transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; ISO:RGD.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0050658; P:RNA transport; ISS:UniProtKB.
DR GO; GO:0003323; P:type B pancreatic cell development; ISO:RGD.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; ISO:RGD.
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 Cell membrane; DNA-binding; Glycoprotein; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; RNA-binding; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..832
FT /note="SID1 transmembrane family member 2"
FT /id="PRO_0000404154"
FT TOPO_DOM 16..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..746
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 818..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ9"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ9"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ9"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 832 AA; 94527 MW; 20E333A5E215DF03 CRC64;
MIAWRLPLCV LLVAAVESHL GALGPKNVSQ KDAEFERTYA DDVNSELVNI YTFNHTVTRN
RTEGVRVSVN VLNKQKGAPL LFVVRQKEAV VSFQVPLILR GLYQRKYLYQ KVERTLCQPP
TKNESEIQFF YVDVSTLSPV NTTYQLRVNR VDNFVLRTGE LFTFNTTAAQ PQYFKYEFPD
GVDSVIVKVT SKKAFPCSVI SIQDVLCPVY DLDNNVAFIG MYQTMTKKAA ITVQRKDFPS
NSFYVVVVVK TEDQACGGSL PFYPFVEDEP VDQGHRQKTL SVLVSQAVTS EAYVGGMLFC
LGIFLSFYLL TVLLACWENW RQRKKTLLVA IDRACPESGH PRVLADSFPG SAPYEGYNYG
SFENGSGSTD GLVESTGSGD LSYSYQDRSF DPVGARPRLD SMSSVEEDDY DTLTDIDSDK
NVIRTKQYLC VADLARKDKR VLRKKYQIYF WNIATIAVFY ALPVVQLVIT YQTVVNVTGN
QDICYYNFLC AHPLGNLSAF NNILSNLGYI LLGLLFLLII LQREINHNRA LLRNDLYALE
CGIPKHFGLF YAMGTALMME GLLSACYHVC PNYTNFQFDT SFMYMIAGLC MLKLYQKRHP
DINASAYSAY ACLAIVIFFS VLGVVFGKGN TAFWIVFSVI HIISTLLLST QLYYMGRWKL
DSGIFRRILH VLYTDCIRQC SGPLYTDRMV LLVMGNIINW SLAAYGLIMR PNDFASYLLA
IGICNLLLYF AFYIIMKLRS GERIKLIPLL CIVCTSVVWG FALFFFFQGL STWQKTPAES
REHNRDCILL DFFDDHDIWH FLSSIAMFGS FLVLLTLDDD LDTVQRDKIY VF
