LORF2_MOUSE
ID LORF2_MOUSE Reviewed; 1281 AA.
AC P11369; Q60713; Q61787;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=LINE-1 retrotransposable element ORF2 protein;
DE Short=ORF2p;
DE AltName: Full=Long interspersed element-1;
DE Short=L1;
DE AltName: Full=Retrovirus-related Pol polyprotein LINE-1;
DE Includes:
DE RecName: Full=Reverse transcriptase;
DE EC=2.7.7.49;
DE Includes:
DE RecName: Full=Endonuclease;
DE EC=3.1.21.-;
GN Name=Pol; Synonyms=Gm17492;
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 [GENOMIC DNA].
RX PubMed=3023821; DOI=10.1128/mcb.6.1.168-182.1986;
RA Loeb D.D., Padgett R.W., Hardies S.C., Shehee W.R., Comer M.B.,
RA Edgell M.H., Hutchison C.A. III;
RT "The sequence of a large L1Md element reveals a tandemly repeated 5' end
RT and several features found in retrotransposons.";
RL Mol. Cell. Biol. 6:168-182(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7533116; DOI=10.1016/0378-1119(94)00785-q;
RA Martin S.L.;
RT "Characterization of a LINE-1 cDNA that originated from RNA present in
RT ribonucleoprotein particles: implications for the structure of an active
RT mouse LINE-1.";
RL Gene 153:261-266(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-484.
RX PubMed=3008107; DOI=10.1093/nar/14.7.3119;
RA Mottez E., Rogan P.K., Manuelidis L.;
RT "Conservation in the 5' region of the long interspersed mouse L1 repeat:
RT implications of comparative sequence analysis.";
RL Nucleic Acids Res. 14:3119-3136(1986).
RN [4]
RP PROTEIN SEQUENCE OF 99-108, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP INTERACTION WITH MOV10.
RX PubMed=28662698; DOI=10.1186/s12915-017-0387-1;
RA Skariah G., Seimetz J., Norsworthy M., Lannom M.C., Kenny P.J.,
RA Elrakhawy M., Forsthoefel C., Drnevich J., Kalsotra A., Ceman S.;
RT "Mov10 suppresses retroelements and regulates neuronal development and
RT function in the developing brain.";
RL BMC Biol. 15:54-54(2017).
CC -!- FUNCTION: Has a reverse transcriptase activity required for target-
CC primed reverse transcription of the LINE-1 element mRNA, a crucial step
CC in LINE-1 retrotransposition. Has also an endonuclease activity that
CC allows the introduction of nicks in the chromosomal target DNA. Cleaves
CC DNA in AT-rich regions between a 5' stretch of purines and a 3' stretch
CC of pyrimidines, corresponding to sites of LINE-1 integration in the
CC genome.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- SUBUNIT: Interacts with MOV10. {ECO:0000269|PubMed:28662698}.
CC -!- MISCELLANEOUS: An active LINE-1 encodes for 2 proteins translated from
CC a single RNA containing two non-overlapping ORFs, ORF1 and ORF2. ORF2p
CC is described in that entry as a representative of all ORF2p potentially
CC expressed by active elements in mouse genome. ORF1p is described in the
CC related entry AC P11260.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27363.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M13002; AAA66024.1; -; Genomic_DNA.
DR EMBL; U15647; AAA67727.1; -; mRNA.
DR EMBL; X03725; CAA27363.1; ALT_FRAME; Genomic_DNA.
DR PIR; B58927; GNMSLL.
DR AlphaFoldDB; P11369; -.
DR SMR; P11369; -.
DR STRING; 10090.ENSMUSP00000137421; -.
DR PhosphoSitePlus; P11369; -.
DR SwissPalm; P11369; -.
DR PaxDb; P11369; -.
DR PRIDE; P11369; -.
DR ProteomicsDB; 291958; -.
DR UCSC; uc029qyg.1; mouse.
DR eggNOG; ENOG502S9XJ; Eukaryota.
DR InParanoid; P11369; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11369; protein.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR013544; DUF1725.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000477; RT_dom.
DR Pfam; PF08333; DUF1725; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA recombination; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; Reference proteome; RNA-directed DNA polymerase;
KW Transferase.
FT CHAIN 1..1281
FT /note="LINE-1 retrotransposable element ORF2 protein"
FT /id="PRO_0000058509"
FT DOMAIN 505..780
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 1247..1266
FT /note="DUF1725"
FT REGION 1..245
FT /note="Endonuclease activity"
FT /evidence="ECO:0000250"
FT REGION 318..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 607
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 710
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT CONFLICT 86
FT /note="S -> L (in Ref. 2; AAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="N -> K (in Ref. 3; CAA27363)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="T -> K (in Ref. 2; AAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="L -> F (in Ref. 2; AAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="V -> A (in Ref. 2; AAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="R -> W (in Ref. 2; AAA67727)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="A -> D (in Ref. 2; AAA67727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1281 AA; 149581 MW; A6D2894DA364AB19 CRC64;
MPTLTTKIKG SNNYFSLISL NINGLNSPIK RHRLTDWLHK QDPTFCCLQE THLREKDRHY
LRVKGWKTIF QANGLKKQAG VAILISDKID FQPKVIKKDK EGHFILIKGK ILQEELSILN
IYAPNARAAT FIRDTLVKLK AYIAPHTIIV GDFNTPLSSK DRSWKQKLNR DTVKLTEVMK
QMDLTDIYRT FYPKTKGYTF FSAPHGTFSK IDHIIGHKTG LNRYKNIEIV PCILSDHHGL
RLIFNNNINN GKPTFTWKLN NTLLNDTLVK EGIKKEIKDF LEFNENEATT YPNLWDTMKA
FLRGKLIALS ASKKKRETAH TSSLTTHLKA LEKKEANSPK RSRRQEIIKL RGEINQVETR
RTIQRINQTR SWFFEKINKI DKPLARLTKG HRDKILINKI RNEKGDITTD PEEIQNTIRS
FYKRLYSTKL ENLDEMDKFL DRYQVPKLNQ DQVDHLNSPI SPKEIEAVIN SLPTKKSPGP
DGFSAEFYQT FKEDLIPILH KLFHKIEVEG TLPNSFYEAT ITLIPKPQKD PTKIENFRPI
SLMNIDAKIL NKILANRIQE HIKAIIHPDQ VGFIPGMQGW FNIRKSINVI HYINKLKDKN
HMIISLDAEK AFDKIQHPFM IKVLERSGIQ GPYLNMIKAI YSKPVANIKV NGEKLEAIPL
KSGTRQGCPL SPYLFNIVLE VLARAIRQQK EIKGIQIGKE EVKISLLADD MIVYISDPKN
STRELLNLIN SFGEVVGYKI NSNKSMAFLY TKNKQAEKEI RETTPFSIVT NNIKYLGVTL
TKEVKDLYDK NFKSLKKEIK EDLRRWKDLP CSWIGRINIV KMAILPKAIY RFNAIPIKIP
TQFFNELEGA ICKFVWNNKK PRIAKSLLKD KRTSGGITMP DLKLYYRAIV IKTAWYWYRD
RQVDQWNRIE DPEMNPHTYG HLIFDKGAKT IQWKKDSIFN NWCWHNWLLS CRRMRIDPYL
SPCTKVKSKW IKELHIKPET LKLIEEKVGK SLEDMGTGEK FLNRTAMACA VRSRIDKWDL
MKLQSFCKAK DTVNKTKRPP TDWERIFTYP KSDRGLISNI YKELKKVDFR KSNNPIKKWG
SELNKEFSPE EYRMAEKHLK KCSTSLIIRE MQIKTTLRFH LTPVRMAKIK NSGDSRCWRG
CGERGTLLHC WWECRLVQPL WKSVWRFLRK LDIVLPEDPA IPLLGIYPED APTGKKDTCS
TMFIAALFII ARSWKEPRCP STEEWIQKMW YIYTMEYYSA IKKNEFMKFL AKWMDLEGII
LSEVTHSQRN SHNMYSLISG Y
