SIDT1_HUMAN
ID SIDT1_HUMAN Reviewed; 827 AA.
AC Q9NXL6; Q17RR4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=SID1 transmembrane family member 1;
DE Flags: Precursor;
GN Name=SIDT1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXL6-2; Sequence=VSP_039174;
CC -!- SIMILARITY: Belongs to the SID1 family. {ECO:0000305}.
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DR EMBL; AK000181; BAA90994.1; -; mRNA.
DR EMBL; AC055740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117222; AAI17223.1; -; mRNA.
DR CCDS; CCDS2974.1; -. [Q9NXL6-1]
DR CCDS; CCDS77790.1; -. [Q9NXL6-2]
DR RefSeq; NP_001295279.1; NM_001308350.1. [Q9NXL6-2]
DR RefSeq; NP_060169.2; NM_017699.2. [Q9NXL6-1]
DR AlphaFoldDB; Q9NXL6; -.
DR BioGRID; 120197; 2.
DR IntAct; Q9NXL6; 2.
DR MINT; Q9NXL6; -.
DR STRING; 9606.ENSP00000264852; -.
DR TCDB; 1.A.79.1.2; the cholesterol uptake protein (chup) or double stranded rna uptake family.
DR GlyGen; Q9NXL6; 8 sites.
DR iPTMnet; Q9NXL6; -.
DR PhosphoSitePlus; Q9NXL6; -.
DR SwissPalm; Q9NXL6; -.
DR BioMuta; SIDT1; -.
DR DMDM; 296452905; -.
DR jPOST; Q9NXL6; -.
DR MassIVE; Q9NXL6; -.
DR PaxDb; Q9NXL6; -.
DR PeptideAtlas; Q9NXL6; -.
DR PRIDE; Q9NXL6; -.
DR ProteomicsDB; 83110; -. [Q9NXL6-1]
DR ProteomicsDB; 83111; -. [Q9NXL6-2]
DR Antibodypedia; 32584; 155 antibodies from 28 providers.
DR DNASU; 54847; -.
DR Ensembl; ENST00000264852.9; ENSP00000264852.4; ENSG00000072858.11. [Q9NXL6-1]
DR Ensembl; ENST00000393830.4; ENSP00000377416.4; ENSG00000072858.11. [Q9NXL6-2]
DR GeneID; 54847; -.
DR KEGG; hsa:54847; -.
DR MANE-Select; ENST00000264852.9; ENSP00000264852.4; NM_017699.3; NP_060169.2.
DR UCSC; uc003eak.4; human. [Q9NXL6-1]
DR CTD; 54847; -.
DR DisGeNET; 54847; -.
DR GeneCards; SIDT1; -.
DR HGNC; HGNC:25967; SIDT1.
DR HPA; ENSG00000072858; Tissue enhanced (intestine, salivary gland).
DR MIM; 606816; gene.
DR neXtProt; NX_Q9NXL6; -.
DR OpenTargets; ENSG00000072858; -.
DR PharmGKB; PA134923837; -.
DR VEuPathDB; HostDB:ENSG00000072858; -.
DR eggNOG; ENOG502QUXZ; Eukaryota.
DR GeneTree; ENSGT00390000010091; -.
DR HOGENOM; CLU_357018_0_0_1; -.
DR InParanoid; Q9NXL6; -.
DR OMA; CPNHSNF; -.
DR OrthoDB; 139174at2759; -.
DR PhylomeDB; Q9NXL6; -.
DR TreeFam; TF313076; -.
DR PathwayCommons; Q9NXL6; -.
DR SignaLink; Q9NXL6; -.
DR BioGRID-ORCS; 54847; 7 hits in 1063 CRISPR screens.
DR ChiTaRS; SIDT1; human.
DR GenomeRNAi; 54847; -.
DR Pharos; Q9NXL6; Tbio.
DR PRO; PR:Q9NXL6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NXL6; protein.
DR Bgee; ENSG00000072858; Expressed in right hemisphere of cerebellum and 153 other tissues.
DR Genevisible; Q9NXL6; HS.
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; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
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 2: Evidence at transcript 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_0000032575"
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 355..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 655
FT /note="I -> IDVSDT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039174"
FT VARIANT 3
FT /note="G -> S (in dbSNP:rs9879313)"
FT /id="VAR_061793"
FT VARIANT 78
FT /note="V -> M (in dbSNP:rs2271496)"
FT /id="VAR_057184"
FT VARIANT 363
FT /note="T -> I (in dbSNP:rs33990195)"
FT /id="VAR_057185"
FT CONFLICT 572
FT /note="Q -> R (in Ref. 1; BAA90994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 827 AA; 93839 MW; E7C383DF74378B8C CRC64;
MRGCLRLALL CALPWLLLAA SPGHPAKSPR QPPAPRRDPF DAARGADFDH VYSGVVNLST
ENIYSFNYTS QPDQVTAVRV YVNSSSENLN YPVLVVVRQQ KEVLSWQVPL LFQGLYQRSY
NYQEVSRTLC PSEATNETGP LQQLIFVDVA SMAPLGAQYK LLVTKLKHFQ LRTNVAFHFT
ASPSQPQYFL YKFPKDVDSV IIKVVSEMAY PCSVVSVQNI MCPVYDLDHN VEFNGVYQSM
TKKAAITLQK KDFPGEQFFV VFVIKPEDYA CGGSFFIQEK ENQTWNLQRK KNLEVTIVPS
IKESVYVKSS LFSVFIFLSF YLGCLLVGFV HYLRFQRKSI DGSFGSNDGS GNMVASHPIA
ASTPEGSNYG TIDESSSSPG RQMSSSDGGP PGQSDTDSSV EESDFDTMPD IESDKNIIRT
KMFLYLSDLS RKDRRIVSKK YKIYFWNIIT IAVFYALPVI QLVITYQTVV NVTGNQDICY
YNFLCAHPLG VLSAFNNILS NLGHVLLGFL FLLIVLRRDI LHRRALEAKD IFAVEYGIPK
HFGLFYAMGI ALMMEGVLSA CYHVCPNYSN FQFDTSFMYM IAGLCMLKLY QTRHPDINAS
AYSAYASFAV VIMVTVLGVV FGKNDVWFWV IFSAIHVLAS LALSTQIYYM GRFKIDLGIF
RRAAMVFYTD CIQQCSRPLY MDRMVLLVVG NLVNWSFALF GLIYRPRDFA SYMLGIFICN
LLLYLAFYII MKLRSSEKVL PVPLFCIVAT AVMWAAALYF FFQNLSSWEG TPAESREKNR
ECILLDFFDD HDIWHFLSAT ALFFSFLVLL TLDDDLDVVR RDQIPVF
