ENDOU_PAROL
ID ENDOU_PAROL Reviewed; 385 AA.
AC Q9PTU6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Uridylate-specific endoribonuclease {ECO:0000305};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE AltName: Full=Pancreatic protein with two somatomedin-B domains;
DE AltName: Full=Protein endoU;
DE Flags: Precursor;
GN Name=endou; Synonyms=ppsb;
OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC Paralichthys.
OX NCBI_TaxID=8255;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=12431400; DOI=10.1016/s1096-4959(02)00158-6;
RA Suzuki T., Srivastava A.S., Kurokawa T.;
RT "A homologue of human placental protein, PP11, and mouse T cell-specific
RT protein, Tcl-30, in exocrine pancreas of a teleost (Paralichthys
RT olivaceus).";
RL Comp. Biochem. Physiol. 133:325-329(2002).
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 -!- TISSUE SPECIFICITY: Specifically expressed by the exocrine pancreatic
CC acinar cells. {ECO:0000269|PubMed:12431400}.
CC -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
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DR EMBL; AB035673; BAA88246.1; -; mRNA.
DR RefSeq; XP_019965028.1; XM_020109469.1.
DR AlphaFoldDB; Q9PTU6; -.
DR SMR; Q9PTU6; -.
DR GeneID; 109644140; -.
DR KEGG; pov:109644140; -.
DR CTD; 8909; -.
DR OrthoDB; 823332at2759; -.
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; Repeat; RNA-binding; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..385
FT /note="Uridylate-specific endoribonuclease"
FT /id="PRO_0000394226"
FT DOMAIN 22..61
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 62..105
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 112..385
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT DISULFID 25..41
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 25..29
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 29..59
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 39..52
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 39..41
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 45..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 52..59
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 66..82
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 66..70
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 70..100
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 80..93
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 80..82
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 86..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 93..100
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
SQ SEQUENCE 385 AA; 43256 MW; A1AE0AA4C461C4C9 CRC64;
MKVIALLTLC VTLFCQGYSN SLDSCQGRCG YGTDNNFSCQ CNTSCERFKD CCSDYAEQCK
AGATSCKGRC DEKYNSQNKC HCNSKCSRYN NCCSDYTDIC DSDAGGGGSV ITDADIKAVS
EVLYALDSNK ATASELIIDP QALVHDSQTS SQRDLSSRPL FRYVDGTLLS RPTYAAFLAV
LDNYHRMTGQ VEDFSPQQLS EQETFIKEAM SNTELGRELF AFLYTKGVYA SENEFLHDLK
MMWFGLYSRY NNKMDSSGFE HIFAGEIKGG KVSGFHNWIQ FYRLEKRGQL NYYSHSFNGP
WTTFPDVMGM QFKWDGYFKQ VGSAVIGCSP EFDFALYSLC YITRPGKQCR LSLGGKELII
QTYTWDKTTY GNGKKFIASA FPSTP
