LORF1_MOUSE
ID LORF1_MOUSE Reviewed; 357 AA.
AC P11260; Q91V68;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=LINE-1 retrotransposable element ORF1 protein {ECO:0000305};
DE Short=L1-ORF1p {ECO:0000303|PubMed:28806172};
DE AltName: Full=LINE retrotransposable element 1;
DE AltName: Full=LINE1 retrotransposable element 1;
DE AltName: Full=Transposase element L1Md-A101/L1Md-A102/L1Md-A2;
GN Name=Lire1 {ECO:0000250|UniProtKB:Q9UN81};
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=11591644; DOI=10.1101/gr.198301;
RA Goodier J.L., Ostertag E.M., Du K., Kazazian H.H. Jr.;
RT "A novel active L1 retrotransposon subfamily in the mouse.";
RL Genome Res. 11:1677-1685(2001).
RN [3]
RP FUNCTION.
RX PubMed=11134335; DOI=10.1128/mcb.21.2.467-475.2001;
RA Martin S.L., Bushman F.D.;
RT "Nucleic acid chaperone activity of the ORF1 protein from the mouse LINE-1
RT retrotransposon.";
RL Mol. Cell. Biol. 21:467-475(2001).
RN [4]
RP SUBUNIT.
RX PubMed=14615577; DOI=10.1073/pnas.2336221100;
RA Martin S.L., Branciforte D., Keller D., Bain D.L.;
RT "Trimeric structure for an essential protein in L1 retrotransposition.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13815-13820(2003).
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).
RN [6]
RP FUNCTION, INTERACTION WITH TEX19.1 AND UBR2, UBIQUITINATION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=28806172; DOI=10.7554/elife.26152;
RA MacLennan M., Garcia-Canadas M., Reichmann J., Khazina E., Wagner G.,
RA Playfoot C.J., Salvador-Palomeque C., Mann A.R., Peressini P., Sanchez L.,
RA Dobie K., Read D., Hung C.C., Eskeland R., Meehan R.R., Weichenrieder O.,
RA Garcia-Perez J.L., Adams I.R.;
RT "Mobilization of LINE-1 retrotransposons is restricted by Tex19.1 in mouse
RT embryonic stem cells.";
RL Elife 6:0-0(2017).
RN [7]
RP STRUCTURE BY NMR OF 261-347, AND RNA-BINDING REGION.
RX PubMed=17569664; DOI=10.1074/jbc.m702023200;
RA Januszyk K., Li P.W., Villareal V., Branciforte D., Wu H., Xie Y.,
RA Feigon J., Loo J.A., Martin S.L., Clubb R.T.;
RT "Identification and solution structure of a highly conserved C-terminal
RT domain within ORF1p required for retrotransposition of long interspersed
RT nuclear element-1.";
RL J. Biol. Chem. 282:24893-24904(2007).
CC -!- FUNCTION: Nucleic acid-binding protein which is essential for
CC retrotransposition of LINE-1 elements in the genome. Functions as a
CC nucleic acid chaperone binding its own transcript and therefore
CC preferentially mobilizing the transcript from which they are encoded.
CC {ECO:0000269|PubMed:11134335, ECO:0000269|PubMed:28806172}.
CC -!- SUBUNIT: Homotrimer (via coiled coil domain). May also form larger
CC homooligomers. Interacts with Tex19.1 and UBR2 (PubMed:28806172).
CC Interacts with MOV10 (PubMed:28662698). {ECO:0000269|PubMed:14615577,
CC ECO:0000269|PubMed:28662698, ECO:0000269|PubMed:28806172}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9UN81}. Cytoplasm
CC {ECO:0000269|PubMed:28806172}. Cytoplasm, Cytoplasmic ribonucleoprotein
CC granule {ECO:0000250|UniProtKB:Q9UN81}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9UN81}. Note=Colocalizes with its encoding RNA
CC in cytoplasmic ribonucleoprotein particle. Mainly cytoplasmic, rarely
CC detected in the nucleus, possibly within the nucleolus.
CC {ECO:0000250|UniProtKB:Q9UN81}.
CC -!- TISSUE SPECIFICITY: Expressed in meiotic spermatocytes and in the
CC cerebellum (at protein level). {ECO:0000269|PubMed:28806172}.
CC -!- DOMAIN: The coiled coil domain mediates homotrimerization.
CC {ECO:0000250}.
CC -!- DOMAIN: The RRM and the CTD domain are both required for proper RNA-
CC binding activity.
CC -!- PTM: Polyubiquitinated, probably by UBR2, which induces its
CC degradation. {ECO:0000269|PubMed:28806172}.
CC -!- MISCELLANEOUS: An active LINE-1 encodes for 2 proteins translated from
CC a single RNA containing two non-overlapping ORFs, ORF1 and ORF2. ORF1p
CC is described in that entry as a representative of all ORF1p potentially
CC expressed by active elements in mouse genome. ORF2p is described in the
CC related entry AC P11369.
CC -!- SIMILARITY: Belongs to the transposase 22 family. {ECO:0000305}.
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DR EMBL; M13002; AAA66023.1; -; Genomic_DNA.
DR EMBL; AY053455; AAL17969.1; -; mRNA.
DR EMBL; AY053456; AAL17971.1; -; mRNA.
DR PIR; A58927; QQMSLL.
DR PDB; 2JRB; NMR; -; A=261-347.
DR PDBsum; 2JRB; -.
DR AlphaFoldDB; P11260; -.
DR BMRB; P11260; -.
DR SMR; P11260; -.
DR PhosphoSitePlus; P11260; -.
DR MaxQB; P11260; -.
DR PeptideAtlas; P11260; -.
DR PRIDE; P11260; -.
DR ProteomicsDB; 291964; -.
DR EvolutionaryTrace; P11260; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11260; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0032197; P:transposition, RNA-mediated; IMP:UniProtKB.
DR Gene3D; 3.30.250.20; -; 1.
DR InterPro; IPR042566; L1_C.
DR InterPro; IPR035300; L1_dsRBD.
DR InterPro; IPR043636; L1_RRM_dom.
DR InterPro; IPR004244; Transposase_22.
DR PANTHER; PTHR11505; PTHR11505; 1.
DR Pfam; PF17490; Tnp_22_dsRBD; 1.
DR Pfam; PF02994; Transposase_22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..357
FT /note="LINE-1 retrotransposable element ORF1 protein"
FT /id="PRO_0000066358"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..274
FT /note="RNA recognition motif (RRM) domain"
FT /evidence="ECO:0000250"
FT REGION 278..339
FT /note="C-terminal domain (CTD)"
FT COILED 59..156
FT /evidence="ECO:0000255"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2JRB"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:2JRB"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:2JRB"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2JRB"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2JRB"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:2JRB"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:2JRB"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:2JRB"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:2JRB"
SQ SEQUENCE 357 AA; 41226 MW; 9103D341DA2E6FCC CRC64;
MAKGKRKNPT NRNQDHSPSS ERSTPTPPSP GHPNTTENLD PDLKTFLMMM IEDIKKDFHK
SLKDLQESTA KELQALKEKQ ENTAKQVMEM NKTILELKGE VDTIKKTQSE ATLEIETLGK
RSGTIDASIS NRIQEMEERI SGAEDSIENI DTTVKENTKC KRILTQNIQV IQDTMRRPNL
RIIGIDENED FQLKGPANIF NKIIEENFPN IKKEMPMIIQ EAYRTPNRLD QKRNSSRHII
IRTTNALNKD RILKAVREKG QVTYKGRPIR ITPDFSPETM KARRAWTDVI QTLREHKCQP
RLLYPAKLSI TIDGETKVFH DKTKFTQYLS TNPALQRIIT EKKQYKDGNH ALEQPRK
