ENDOU_MOUSE
ID ENDOU_MOUSE Reviewed; 412 AA.
AC Q3V188; Q01084;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Uridylate-specific endoribonuclease {ECO:0000305};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE AltName: Full=Placental protein 11-related protein;
DE Short=PP11-related protein;
DE AltName: Full=Protein endoU;
DE AltName: Full=T-cell-specific protein 30;
DE Short=Tcl-30;
DE Flags: Precursor;
GN Name=Endou; Synonyms=Pp11r;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=1506680;
RA Baughman G., Lesley J., Trotter J., Hyman R., Bourgeois S.;
RT "Tcl-30, a new T cell-specific gene expressed in immature glucocorticoid-
RT sensitive thymocytes.";
RL J. Immunol. 149:1488-1496(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 TISSUE SPECIFICITY.
RX PubMed=8104059; DOI=10.1007/bf00296822;
RA Kingsmore S.F., Bieniarz M.C., Watson M.L., Seldin M.F.;
RT "Genetic mapping of Pp11r, a thymocyte gene expressed during apoptosis, to
RT mouse chromosome 15.";
RL Mamm. Genome 4:459-460(1993).
CC -!- FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at 5' of
CC uridylates and releases a product with a 2',3'-cyclic phosphate at the
CC 3'-end. The UU and GU sites are more efficiently cleaved than CU and AU
CC sites. {ECO:0000250|UniProtKB:P21128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ribonucleotidyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-
CC ribonucleotide-RNA + a 5'-end dephospho-uridine-RNA;
CC Xref=Rhea:RHEA:67792, Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:17354,
CC Rhea:RHEA-COMP:17356, ChEBI:CHEBI:83064, ChEBI:CHEBI:173117,
CC ChEBI:CHEBI:173224; Evidence={ECO:0000250|UniProtKB:P21128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67793;
CC Evidence={ECO:0000250|UniProtKB:P21128};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3V188-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3V188-2; Sequence=VSP_039224;
CC -!- TISSUE SPECIFICITY: Specifically expressed in T-cells during apoptosis.
CC Expressed in surface heat stable antigen (HSA)-containing T-cells
CC populations (CD4(-)CD8(-)HSA(+), CD4(+)CD8(-)HSA(+),
CC CD4(-)CD8(+)HSA(+), and CD4(+)CD8(+)HSA(+)) and not in the HSA(-)
CC single positive T-cell populations of the thymus or spleen, suggesting
CC that expression is lost during T-cell maturation and is absent at the
CC most mature stages of T-cell development. {ECO:0000269|PubMed:1506680,
CC ECO:0000269|PubMed:8104059}.
CC -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
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DR EMBL; M95545; AAA40405.1; -; mRNA.
DR EMBL; AK132616; BAE21263.1; -; mRNA.
DR CCDS; CCDS27783.1; -. [Q3V188-2]
DR CCDS; CCDS49712.1; -. [Q3V188-1]
DR PIR; A46498; A46498.
DR RefSeq; NP_001162164.1; NM_001168693.1. [Q3V188-1]
DR RefSeq; NP_032928.1; NM_008902.3. [Q3V188-2]
DR AlphaFoldDB; Q3V188; -.
DR SMR; Q3V188; -.
DR STRING; 10090.ENSMUSP00000023105; -.
DR PhosphoSitePlus; Q3V188; -.
DR EPD; Q3V188; -.
DR MaxQB; Q3V188; -.
DR PaxDb; Q3V188; -.
DR PRIDE; Q3V188; -.
DR ProteomicsDB; 275617; -. [Q3V188-1]
DR ProteomicsDB; 275618; -. [Q3V188-2]
DR Antibodypedia; 2843; 56 antibodies from 19 providers.
DR DNASU; 19011; -.
DR Ensembl; ENSMUST00000023105; ENSMUSP00000023105; ENSMUSG00000022468. [Q3V188-2]
DR Ensembl; ENSMUST00000100249; ENSMUSP00000097820; ENSMUSG00000022468. [Q3V188-1]
DR GeneID; 19011; -.
DR KEGG; mmu:19011; -.
DR UCSC; uc007xkw.1; mouse. [Q3V188-2]
DR UCSC; uc007xkx.1; mouse. [Q3V188-1]
DR CTD; 8909; -.
DR MGI; MGI:97746; Endou.
DR VEuPathDB; HostDB:ENSMUSG00000022468; -.
DR eggNOG; KOG2849; Eukaryota.
DR GeneTree; ENSGT00530000063825; -.
DR HOGENOM; CLU_048034_0_0_1; -.
DR InParanoid; Q3V188; -.
DR OMA; MQFSWDG; -.
DR OrthoDB; 823332at2759; -.
DR PhylomeDB; Q3V188; -.
DR TreeFam; TF319848; -.
DR BioGRID-ORCS; 19011; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Endou; mouse.
DR PRO; PR:Q3V188; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3V188; protein.
DR Bgee; ENSMUSG00000022468; Expressed in thymus and 79 other tissues.
DR ExpressionAtlas; Q3V188; baseline and differential.
DR Genevisible; Q3V188; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd21159; XendoU; 1.
DR InterPro; IPR039787; ENDOU.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR018998; EndoU_C.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR12439; PTHR12439; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR Pfam; PF09412; XendoU; 1.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS51959; ENDOU; 1.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW Manganese; Metal-binding; Nuclease; Reference proteome; Repeat;
KW RNA-binding; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..412
FT /note="Uridylate-specific endoribonuclease"
FT /id="PRO_0000394222"
FT DOMAIN 20..63
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 85..128
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 138..411
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT DISULFID 24..40
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 24..28
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 28..58
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..51
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..40
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 44..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 51..58
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 89..105
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 89..93
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 93..123
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 103..116
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 103..105
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 109..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 116..123
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT VAR_SEQ 1..59
FT /note="MKARVPFIVAMLCGLAWAGNLESCASRCHEKFNRDAVCQCDRRCPQHDDCCD
FT DYEHLCT -> MLNCSIHVGQLKLVFNPEGAPLSLPFFTYFSFYIFWVQWAPNARMVEN
FT LSPGEIIFVLFCLSFPSSDLGKPSIFSVLSLLCQIGGWDGMCEYPFNTCACLQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:1506680"
FT /id="VSP_039224"
SQ SEQUENCE 412 AA; 47010 MW; 27C954A35490B8EF CRC64;
MKARVPFIVA MLCGLAWAGN LESCASRCHE KFNRDAVCQC DRRCPQHDDC CDDYEHLCTA
EEGPPEPEAF LDPEDKIPTS HLYSAPSSCQ GRCREAYDKH HPCHCNDRCP EFGNCCEDFD
SLCGGDHEGF SHSSDAVTKE ELESISETIY RVDTNKAQKE DIVLNSQNRI SPSETGNQVD
RSPEPLFTYV NEKLFSKPTY AAFINLLNNY QRATGHGEHF SAQQLEEQGV FLREVMKTAV
MKELYSFLHH QNRYSSEQEF VDDLKNMWFG LYSRGNDEGD SSGFEHVFSG EVKKGKVTGF
HNWIRFYLQE KEGLLDYYSH NYDGPWDSYP DVLAMQFNWD GYYKEVGSVF IGSSPEFEFA
LYSLCFITRP GKKCHLSLGG YPLAIQTYTW DKTTYGNGKK YIATAYVVSS SQ
