SMBP2_MOUSE
ID SMBP2_MOUSE Reviewed; 993 AA.
AC P40694;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA-binding protein SMUBP-2 {ECO:0000303|PubMed:8493094};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P38935};
DE EC=3.6.4.13 {ECO:0000305|PubMed:22965130};
DE AltName: Full=ATP-dependent helicase IGHMBP2;
DE AltName: Full=Cardiac transcription factor 1;
DE Short=CATF1;
DE AltName: Full=Immunoglobulin mu-binding protein 2;
GN Name=Ighmbp2; Synonyms=Smbp-2, Smbp2;
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 [MRNA], DNA-BINDING, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=8493094; DOI=10.1093/nar/21.8.1761;
RA Mizuta T.-R., Fukita Y., Miyoshi T., Shimizu A., Honjo T.;
RT "Isolation of cDNA encoding a binding protein specific to 5'-phosphorylated
RT single-stranded DNA with G-rich sequences.";
RL Nucleic Acids Res. 21:1761-1766(1993).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RIBOSOMES.
RX PubMed=19158098; DOI=10.1093/hmg/ddp028;
RA Guenther U.P., Handoko L., Laggerbauer B., Jablonka S., Chari A.,
RA Alzheimer M., Ohmer J., Ploettner O., Gehring N., Sickmann A., von Au K.,
RA Schuelke M., Fischer U.;
RT "IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular
RT disorder distal SMA type 1 (DSMA1).";
RL Hum. Mol. Genet. 18:1288-1300(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TRNA-BINDING.
RX PubMed=19299493; DOI=10.1093/hmg/ddp134;
RA de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
RA Mourelatos Z.;
RT "Biochemical and genetic evidence for a role of IGHMBP2 in the
RT translational machinery.";
RL Hum. Mol. Genet. 18:2115-2126(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797 AND SER-800, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, Spleen, and Testis;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=22965130; DOI=10.1093/nar/gks792;
RA Lim S.C., Bowler M.W., Lai T.F., Song H.;
RT "The Ighmbp2 helicase structure reveals the molecular basis for disease-
RT causing mutations in DMSA1.";
RL Nucleic Acids Res. 40:11009-11022(2012).
CC -!- FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplexes in an
CC ATP-dependent reaction (PubMed:22965130, PubMed:8493094). Specific to
CC 5'-phosphorylated single-stranded guanine-rich sequences
CC (PubMed:8493094). May play a role in RNA metabolism, ribosome
CC biogenesis or initiation of translation (PubMed:19299493,
CC PubMed:19158098). May play a role in regulation of transcription (By
CC similarity). Interacts with tRNA-Tyr (PubMed:19299493).
CC {ECO:0000250|UniProtKB:Q9EQN5, ECO:0000269|PubMed:19158098,
CC ECO:0000269|PubMed:19299493, ECO:0000269|PubMed:22965130,
CC ECO:0000269|PubMed:8493094}.
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:0000269|PubMed:22965130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:22965130};
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:0000250|UniProtKB:P38935}. Cytoplasm
CC {ECO:0000269|PubMed:19158098}. Cell projection, axon
CC {ECO:0000269|PubMed:19158098}.
CC -!- TISSUE SPECIFICITY: In all tissues examined.
CC {ECO:0000269|PubMed:8493094}.
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:0000269|PubMed:22965130}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; L10075; AAA40143.1; -; mRNA.
DR CCDS; CCDS29393.1; -.
DR PIR; S35633; S35633.
DR AlphaFoldDB; P40694; -.
DR SMR; P40694; -.
DR IntAct; P40694; 1.
DR STRING; 10090.ENSMUSP00000025751; -.
DR iPTMnet; P40694; -.
DR PhosphoSitePlus; P40694; -.
DR EPD; P40694; -.
DR MaxQB; P40694; -.
DR PaxDb; P40694; -.
DR PeptideAtlas; P40694; -.
DR PRIDE; P40694; -.
DR ProteomicsDB; 257262; -.
DR UCSC; uc008fwa.1; mouse.
DR MGI; MGI:99954; Ighmbp2.
DR eggNOG; KOG1803; Eukaryota.
DR InParanoid; P40694; -.
DR PhylomeDB; P40694; -.
DR PRO; PR:P40694; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P40694; protein.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA: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; IDA: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:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:1990955; F:G-rich single-stranded DNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA: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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
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 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; 1.
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..993
FT /note="DNA-binding protein SMUBP-2"
FT /id="PRO_0000080703"
FT DOMAIN 721..784
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 889..938
FT /note="AN1-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 637..783
FT /note="SS DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 650..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 862..866
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 683..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 837..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..993
FT /note="Basic and acidic 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 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 914
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 930
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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:0007744|PubMed:21183079"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 993 AA; 109466 MW; 2FA0850DBABDE35B CRC64;
MASSTVESFV AQQLQLLELE RDAEVEERRS WQEHSSLREL QSRGVCLLKL QVSSQRTGLY
GQRLVTFEPR KFGPAVVLPS NSFTSGDIVG LYDTNENSQL ATGVLTRITQ KSVTVAFDES
HDLQLNLDRE NTYRLLKLAN DVTYKRLKKA LMTLKKYHSG PASSLIDILL GSSTPSPAME
IPPLSFYNTT LDLSQKEAVS FALAQKELAI IHGPPGTGKT TTVVEIILQA VKQGLKVLCC
APSNIAVDNL VERLALCKKR ILRLGHPARL LESVQHHSLD AVLARSDNAQ IVADIRRDID
QVFGKNKKTQ DKREKGNFRS EIKLLRKELK EREEAAIVQS LTAADVVLAT NTGASSDGPL
KLLPEDYFDV VVVDECAQAL EASCWIPLLK APKCILAGDH RQLPPTTVSH RAALAGLSRS
LMERLAEKHG AGVVRMLTVQ YRMHQAIMCW ASEAMYHGQF TSHPSVAGHL LKDLPGVTDT
EETRVPLLLI DTAGCGLLEL EEEDSQSKGN PGEVRLVTLH IQALVDAGVQ AGDIAVIAPY
NLQVDLLRQS LSNKHPELEI KSVDGFQGRE KEAVLLTFVR SNRKGEVGFL AEDRRINVAV
TRARRHVAVI CDSHTVNNHA FLETLVDYFT EHGEVRTAFE YLDDIVPENY THEGSQGHSR
VPKPKCPSTS IRKPASDQES GQETRAAPRH GRRKPSEKPP GSHVQSQHSS SANGSDRTGG
PDRTEHFRAT IEEFVASKES QLEFPTSLSS HDRLRVHQLA EEFGLRHDST GEGKARHITV
SRRSPASSGS VAPQPSSPPS PAQAEPEPRA EEPVTVVQAH CPVQLDLKAL HLERLQRQQS
SQAQTAKGQP GGDSRPQKAS QKKKKKEPKG PVMALPCEED FDALVSAVVK ADNTCSFSKC
SVSTTTLGQF CMHCSHRYYL SHHLPEIHGC GEKARAHARQ RISREGVLYA GSGTKDRALD
PAKRAQLQRR LDKKLGELSS QRTSRKKEKE RGT
