ENDOU_BOVIN
ID ENDOU_BOVIN Reviewed; 413 AA.
AC A6QLQ8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Uridylate-specific endoribonuclease {ECO:0000305};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE AltName: Full=Protein endoU;
DE Flags: Precursor;
GN Name=ENDOU;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
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DR EMBL; BC148052; AAI48053.1; -; mRNA.
DR RefSeq; NP_001095560.1; NM_001102090.1.
DR AlphaFoldDB; A6QLQ8; -.
DR SMR; A6QLQ8; -.
DR STRING; 9913.ENSBTAP00000043168; -.
DR PaxDb; A6QLQ8; -.
DR GeneID; 525399; -.
DR KEGG; bta:525399; -.
DR CTD; 8909; -.
DR eggNOG; KOG2849; Eukaryota.
DR HOGENOM; CLU_048034_0_0_1; -.
DR InParanoid; A6QLQ8; -.
DR OrthoDB; 823332at2759; -.
DR TreeFam; TF319848; -.
DR Proteomes; UP000009136; Unplaced.
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:0006955; P:immune response; IEA:InterPro.
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 Disulfide bond; Endonuclease; Hydrolase; Lyase; Manganese; Metal-binding;
KW Nuclease; Reference proteome; Repeat; RNA-binding; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..413
FT /note="Uridylate-specific endoribonuclease"
FT /id="PRO_0000394221"
FT DOMAIN 20..63
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 88..130
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 139..412
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 345
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 92..108
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 92..96
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 96..126
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 106..119
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 106..108
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 112..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 119..126
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
SQ SEQUENCE 413 AA; 47188 MW; ECBC928F474B51FB CRC64;
MRACVPLTVA ILCGLAWAGK RESCASRCNE RFDRDAVCQC DRRCPQHGDC CEDYEQLCTA
EENPKEPELF LELEEETEGA PASSLYLAPN SCQGRCLEAF DKHHSCHCNA RCPEFGNCCE
DFESLCGHEG FSHSSDAITK EELQSVSEKI YRADTNKARK EDIVLNSQNC ISPSETRDQV
DRCPEPLFTY VNEKLFSKPT YSAFLNLLNN YQRATGRGEH FTAQELAEQD TFLREIMKTA
VMKELYGFLH QQNRYSSEQE FVSDLKNMWF GLYSRSKEER DSSGFEHVFS GEVKKGKVTG
FHNWIRFYMQ EKEGLVDYYS HIYDGPWDSY PDVLAMQFNW DGYYKEVGSA FIGSSPEFEF
ALYSLCFIAR PGKVCQLSLG GHPLAIQTYT WNKSTYGNGK KYIATAYVVS STH
