REXO1_MOUSE
ID REXO1_MOUSE Reviewed; 1213 AA.
AC Q7TT28; Q3UMP1; Q69ZR0; Q6NSQ6; Q6PI95; Q9DA29;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=RNA exonuclease 1 homolog;
DE EC=3.1.-.-;
DE AltName: Full=Transcription elongation factor B polypeptide 3-binding protein 1;
GN Name=Rexo1; Synonyms=Kiaa1138, Tceb3bp1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Lung, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-279; SER-353 AND
RP SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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).
CC -!- FUNCTION: Seems to have no detectable effect on transcription
CC elongation in vitro. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TCEA2 and ELOA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TT28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TT28-2; Sequence=VSP_019121, VSP_019122, VSP_019123;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the REXO1/REXO3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32386.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173108; BAD32386.1; ALT_INIT; mRNA.
DR EMBL; AK006228; BAB24471.1; -; mRNA.
DR EMBL; AK144769; BAE26057.1; -; mRNA.
DR EMBL; BC039623; AAH39623.1; -; mRNA.
DR EMBL; BC052424; AAH52424.1; -; mRNA.
DR EMBL; BC069964; AAH69964.1; -; mRNA.
DR CCDS; CCDS24025.1; -. [Q7TT28-1]
DR RefSeq; NP_080128.2; NM_025852.3. [Q7TT28-1]
DR AlphaFoldDB; Q7TT28; -.
DR SMR; Q7TT28; -.
DR BioGRID; 211819; 1.
DR IntAct; Q7TT28; 1.
DR STRING; 10090.ENSMUSP00000049705; -.
DR iPTMnet; Q7TT28; -.
DR PhosphoSitePlus; Q7TT28; -.
DR EPD; Q7TT28; -.
DR jPOST; Q7TT28; -.
DR MaxQB; Q7TT28; -.
DR PaxDb; Q7TT28; -.
DR PeptideAtlas; Q7TT28; -.
DR PRIDE; Q7TT28; -.
DR ProteomicsDB; 255238; -. [Q7TT28-1]
DR ProteomicsDB; 255239; -. [Q7TT28-2]
DR Antibodypedia; 22810; 183 antibodies from 27 providers.
DR DNASU; 66932; -.
DR Ensembl; ENSMUST00000057910; ENSMUSP00000049705; ENSMUSG00000047417. [Q7TT28-1]
DR GeneID; 66932; -.
DR KEGG; mmu:66932; -.
DR UCSC; uc007gdq.1; mouse. [Q7TT28-2]
DR UCSC; uc007gds.1; mouse. [Q7TT28-1]
DR CTD; 57455; -.
DR MGI; MGI:1914182; Rexo1.
DR VEuPathDB; HostDB:ENSMUSG00000047417; -.
DR eggNOG; KOG2248; Eukaryota.
DR GeneTree; ENSGT00940000158590; -.
DR HOGENOM; CLU_006810_2_1_1; -.
DR InParanoid; Q7TT28; -.
DR OMA; YKRPTPQ; -.
DR OrthoDB; 227856at2759; -.
DR PhylomeDB; Q7TT28; -.
DR TreeFam; TF350172; -.
DR BioGRID-ORCS; 66932; 8 hits in 70 CRISPR screens.
DR ChiTaRS; Rexo1; mouse.
DR PRO; PR:Q7TT28; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q7TT28; protein.
DR Bgee; ENSMUSG00000047417; Expressed in undifferentiated genital tubercle and 251 other tissues.
DR ExpressionAtlas; Q7TT28; baseline and differential.
DR Genevisible; Q7TT28; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd06145; REX1_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR031736; EloA-BP1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR034922; REX1-like_exo.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF15870; EloA-BP1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Exonuclease; Hydrolase; Methylation;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1213
FT /note="RNA exonuclease 1 homolog"
FT /id="PRO_0000239233"
FT DOMAIN 1052..1201
FT /note="Exonuclease"
FT REGION 38..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..112
FT /evidence="ECO:0000255"
FT COMPBIAS 236..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 181
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G1"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G1"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G1"
FT VAR_SEQ 1..679
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019121"
FT VAR_SEQ 680..735
FT /note="PTAQEVCYRRAQLAQRDSASWLQAAPRPTERLSSVHISAPGEKRRIAHVPNP
FT RLAA -> MSFHTPSPVPRPPLRCEMRVLLTLNDRSFLVLRSSVMGLLSSCTHVPCPPS
FT A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019122"
FT VAR_SEQ 875..876
FT /note="SK -> STFLYFLLE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019123"
FT CONFLICT 187
FT /note="G -> S (in Ref. 3; AAH69964)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="T -> A (in Ref. 3; AAH69964)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="S -> P (in Ref. 3; AAH69964)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="E -> K (in Ref. 3; AAH39623/AAH69964)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="P -> L (in Ref. 1; BAD32386)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1213 AA; 130790 MW; 2ECFAAA7A1B54363 CRC64;
MLRSTGFFRS IDCPYWAGAP GGPCRRPYCH FRHRGARGPG APGSGGAASP ASGLGYDPYN
PELPQPPVQR ENGALGQGDG MLELELVNQA IEAVRGEVEL EQRRYQELLE TARGHSAGPS
ALAPCSPATS IDDDDTFSLA LTYTPGGLLS PDAAYQPTPL AVPAEPGHKY SLAPSDRSQG
RAAGGAGALE YVPKAVGQPR RCGRPVSGGK YVVDSSKPST DLEYDPLSNY SARHLGRASA
RDERATKRPR GSRGAEPYTP ALKKPCDPFG GCEARFSDSE DDVTSPPKAD VSSPKAGADP
ESKAPGKPVS KEGREHEDGG LRGTKEMAVQ YDVEDLGQPP KAPDTVSVVK PGSPARASQD
ARVPKEGKAK KKKSGTSASL SHKDKVRKKD KKKEKDPARP RGKEKVCTDK KKLPASNPRG
KAQGPEGTKK KPSSATTVAS SGKGGSGRPS STGPQDSGPG PHAPLAWKAG SAKKMSSGKL
VERKARSLDE GAPQDTPKLK KRALSHAELF GDESEEEDSS LGAGAPRVWP PTLPSLSSDS
ESDSDSSLGL DETKVPKRLK AAPPASPVPP SPLSSSSSSS GASQCAEEDV DYSALEKEVD
FDVDPMEECL RIFNESTSVK TEDKGRLARQ PPKEKAEEKT HAGLTTLFPG QKRRVSHLCK
PGKESEAPKR TPVAPPARPP TAQEVCYRRA QLAQRDSASW LQAAPRPTER LSSVHISAPG
EKRRIAHVPN PRLAAAPTGA KRALSASSSQ ASHGPEPGSQ PLKTRTLSGM ASKTTTTVTP
KRIAHSPSLQ SLKKPVIPKE FGGKVPTVVR QRYLNLFIEE CLKFCSSNQE AIEKALNEEK
VAYDRSPSKN IYLNVAVNTL KKLRGLVPNT VPNLSKASGR RVVSHEVVLG GKLAAKTSFS
LSRPSSPRVE ELKGTALYSR LREYLLTQEQ LKENGYPFPH PERPGGAIIF TAEEKKPKDP
SCRICCRCGT EYLVSSSGRC VRSEECYYHW GRLRRNRVAG GWETQYMCCS AAVGSVGCQV
AKQHVQDGRK ENLEGFVRTF QKELPEDAHA GVFALDCEMS YTTYGLELTR VTVVDTDMQV
VYDTFVKPDN EVVDYNTRFS GVTEADLVDT SITLRDVQAV LLSMFSADTI LIGHSLESDL
LALKVIHGTV VDTSVLFPHR LGLPYKRSLR NLMADYLRQI IQDNVDGHSS SEDASACMHL
VIWKIREDAK TKR
