SMBP2_MESAU
ID SMBP2_MESAU Reviewed; 989 AA.
AC Q60560;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DNA-binding protein SMUBP-2;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P38935};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P38935};
DE AltName: Full=ATP-dependent helicase IGHMBP2;
DE AltName: Full=Immunoglobulin mu-binding protein 2;
DE AltName: Full=Insulin II gene enhancer-binding protein;
DE AltName: Full=RIPE3B-binding complex 3B2 p110 subunit;
DE Short=RIP-1;
GN Name=IGHMBP2; Synonyms=RIP1, SMUBP2;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Insulinoma;
RX PubMed=7665561; DOI=10.1074/jbc.270.37.21503;
RA Shieh S.-Y., Stellrecht C.M.M., Tsai M.-J.;
RT "Molecular characterization of the rat insulin enhancer-binding complex
RT 3b2. Cloning of a binding factor with putative helicase motifs.";
RL J. Biol. Chem. 270:21503-21508(1995).
CC -!- FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplexes in an
CC ATP-dependent reaction (By similarity). Specific to 5'-phosphorylated
CC single-stranded guanine-rich sequences (By similarity). May play a role
CC in RNA metabolism, ribosome biogenesis or initiation of translation (By
CC similarity). May play a role in regulation of transcription (By
CC similarity). Interacts with tRNA-Tyr (By similarity).
CC {ECO:0000250|UniProtKB:P38935, ECO:0000250|UniProtKB:Q9EQN5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P38935};
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with RUVBL1 (By
CC similarity). Interacts with RUVBL2 (By similarity). Interacts with
CC GTF3C1 (By similarity). Interacts with ABT1 (By similarity). Interacts
CC with ribosomes (By similarity). {ECO:0000250|UniProtKB:P38935}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7665561}. Cytoplasm
CC {ECO:0000269|PubMed:7665561}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P40694}.
CC -!- TISSUE SPECIFICITY: High expression in brain and testis, moderate in
CC heart, spleen, and kidney, and low in other tissues.
CC {ECO:0000269|PubMed:7665561}.
CC -!- DOMAIN: The R3H domain recognizes phosphorylated 5'-ends of single-
CC stranded nucleic acids which promotes binding of nucleic acids and
CC stimulates ATPase activity. {ECO:0000250|UniProtKB:P38935}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; L15625; AAB00104.1; -; mRNA.
DR PIR; T48845; T48845.
DR RefSeq; NP_001268318.1; NM_001281389.1.
DR AlphaFoldDB; Q60560; -.
DR SMR; Q60560; -.
DR STRING; 10036.XP_005064163.1; -.
DR GeneID; 101836074; -.
DR CTD; 3508; -.
DR eggNOG; KOG1803; Eukaryota.
DR OrthoDB; 633768at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; ISS:UniProtKB.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IEA:Ensembl.
DR CDD; cd02641; R3H_Smubp-2_like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 4.10.1110.10; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034072; R3H_Smubp-2.
DR InterPro; IPR004483; SMUBP-2/Hcs1-like.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; SSF118310; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR TIGRFAMs; TIGR00376; TIGR00376; 2.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Cell projection; Cytoplasm;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Transcription; Transcription regulation; tRNA-binding; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P38935"
FT CHAIN 2..989
FT /note="DNA-binding protein SMUBP-2"
FT /id="PRO_0000080702"
FT DOMAIN 721..784
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 885..934
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 637..783
FT /note="SS DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 650..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 860..864
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 765..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q92900"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 924
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 926
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P38935"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40694"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40694"
SQ SEQUENCE 989 AA; 108439 MW; 9489671E46DAD04E CRC64;
MALSTVESFV AQQLELLELE RDAEVEERRS WQEHSSLKEL QSRGVCLLKL QVSSQCTGLY
GQRLVTFEPR KLGPVVVLPS NSFTSGDIVG LYDANESSQL ATGVLTRITQ KSVTVAFDES
HDFQLNLDRE NTYRLLKLAN DVTYKRLKKA LMTLKKYHSG PASSLIDVLL GGSSPSPTTE
IPPFTFYNTA LDPSQKEAVS FALAQKEVAI IHGPPGTGKT TTVVEIILQA VKQGLKILCC
APSNVAVDNL VERLALCKKR ILRLGHPARL LESAQQHSLD AVLARSDNAQ IVADIRKDID
QVFGKNKKTQ DKREKSNFRN EIKLLRKELK EREEAAIVQS LTAADVVLAT NTGASSDGPL
KLLPENHFDV VVVDECAQAL EASCWIPLLK APKCILAGDH RQLPPTTISH KAALAGLSRS
LMERLVEKHG AGAVRMLTVQ YRMHQAITRW ASEAMYHGQL TAHPSVAGHL LKDLPGVADT
EETSVPLLLI DTAGCGLLEL DEEDSQSKGN PGEVRLVTLH IQALVDAGVH AGDIAVIAPY
NLQVDLLRQS LSNKHPELEI KSVDGFQGRE KEAVILTFVR SNRKGEVGFL AEDRRINVAV
TRARRHVAVI CDSRTVNNHA FLKTLVDYFT EHGEVRTAFE YLDDIVPENY THEGSQGHSH
APKPRGPVTS IRKPTNEQEN GQEARAAAGQ GRRKPNERPP GSQVHSQPSS GARGCDRTGA
IDRTEHFRAM IEGFVASKES QLEFPASLSS HDRLLVHQIA EEHGLRHDST GEGKARHITV
SRKSPAGSGG VAPQLPSPPS PAQAEPEPLS QQPLGQPHCS TQLDLKALHL QRLQRQQGSQ
AQPAKAQPGV GLHPQKTQQK KKKKETKGPA LPCEEDFDAL VSAVIKADNT CSFAKCTAST
TTLGQFCMHC SRRYCLSHHL PEIHGCGEKA RAHARQMISR EGVLYAGSGT RDRALDPAKR
AQLQRRLDKK LGELSSQRTS KRKEKERGT
