ENDOU_HUMAN
ID ENDOU_HUMAN Reviewed; 410 AA.
AC P21128; B2RBJ3; B3KQS7; B7Z6E1; Q2NKJ4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Uridylate-specific endoribonuclease {ECO:0000305|PubMed:18936097};
DE EC=4.6.1.- {ECO:0000269|PubMed:18936097};
DE AltName: Full=Placental protein 11;
DE Short=PP11;
DE AltName: Full=Protein endoU;
DE Flags: Precursor;
GN Name=ENDOU;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF N-TERMINUS.
RC TISSUE=Placenta;
RX PubMed=2350438; DOI=10.1089/dna.1990.9.243;
RA Grundmann U., Roemisch J., Siebold B., Bohn H., Amann E.;
RT "Cloning and expression of a cDNA encoding human placental protein 11, a
RT putative serine protease with diagnostic significance as a tumor marker.";
RL DNA Cell Biol. 9:243-250(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [6]
RP DOMAIN SOMATOMEDIN-B.
RX PubMed=1710108; DOI=10.1016/0006-291x(91)90381-g;
RA Jenne D.E.;
RT "Homology of placental protein 11 and pea seed albumin 2 with
RT vitronectin.";
RL Biochem. Biophys. Res. Commun. 176:1000-1006(1991).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RNA-BINDING, COFACTOR,
RP AND MUTAGENESIS OF GLU-284; HIS-285; GLU-290; HIS-300 AND LYS-343.
RX PubMed=18936097; DOI=10.1074/jbc.m805759200;
RA Laneve P., Gioia U., Ragno R., Altieri F., Di Franco C., Santini T.,
RA Arceci M., Bozzoni I., Caffarelli E.;
RT "The tumor marker human placental protein 11 is an endoribonuclease.";
RL J. Biol. Chem. 283:34712-34719(2008).
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:0000269|PubMed:18936097}.
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:0000269|PubMed:18936097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67793;
CC Evidence={ECO:0000305|PubMed:18936097};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18936097};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P21128-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21128-2; Sequence=VSP_039216;
CC Name=3;
CC IsoId=P21128-3; Sequence=VSP_039215;
CC -!- TISSUE SPECIFICITY: Placental-specific, but also associated with
CC various malignant neoplasms.
CC -!- PTM: It has been suggested that the active SMB domain may be permitted
CC considerable disulfide bond heterogeneity or variability, thus two
CC alternate disulfide patterns based on 3D structures are described with
CC 1 disulfide bond conserved in both.
CC -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:2350438) thought to be a serine
CC protease. However, PubMed:18936097 showed it is not the case.
CC {ECO:0000305|PubMed:2350438}.
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DR EMBL; M32402; AAA36464.1; -; mRNA.
DR EMBL; M36109; AAA36465.1; -; mRNA.
DR EMBL; AK075446; BAG52139.1; -; mRNA.
DR EMBL; AK300169; BAH13227.1; -; mRNA.
DR EMBL; AK314688; BAG37240.1; -; mRNA.
DR EMBL; AC004241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW57940.1; -; Genomic_DNA.
DR EMBL; BC069715; AAH69715.1; -; mRNA.
DR EMBL; BC074763; AAH74763.1; -; mRNA.
DR EMBL; BC111782; AAI11783.1; -; mRNA.
DR CCDS; CCDS53784.1; -. [P21128-3]
DR CCDS; CCDS53785.1; -. [P21128-1]
DR CCDS; CCDS8754.1; -. [P21128-2]
DR PIR; A34614; A34614.
DR RefSeq; NP_001165910.1; NM_001172439.1. [P21128-1]
DR RefSeq; NP_001165911.1; NM_001172440.1. [P21128-3]
DR RefSeq; NP_006016.1; NM_006025.3. [P21128-2]
DR AlphaFoldDB; P21128; -.
DR SMR; P21128; -.
DR BioGRID; 114423; 29.
DR IntAct; P21128; 2.
DR STRING; 9606.ENSP00000397679; -.
DR MEROPS; X41.001; -.
DR iPTMnet; P21128; -.
DR PhosphoSitePlus; P21128; -.
DR BioMuta; ENDOU; -.
DR DMDM; 296434493; -.
DR MassIVE; P21128; -.
DR PaxDb; P21128; -.
DR PeptideAtlas; P21128; -.
DR PRIDE; P21128; -.
DR ProteomicsDB; 53846; -. [P21128-1]
DR ProteomicsDB; 53847; -. [P21128-2]
DR ProteomicsDB; 53848; -. [P21128-3]
DR TopDownProteomics; P21128-2; -. [P21128-2]
DR Antibodypedia; 2843; 56 antibodies from 19 providers.
DR DNASU; 8909; -.
DR Ensembl; ENST00000229003.7; ENSP00000229003.3; ENSG00000111405.9. [P21128-2]
DR Ensembl; ENST00000422538.8; ENSP00000397679.3; ENSG00000111405.9. [P21128-1]
DR Ensembl; ENST00000545824.2; ENSP00000445004.2; ENSG00000111405.9. [P21128-3]
DR GeneID; 8909; -.
DR KEGG; hsa:8909; -.
DR MANE-Select; ENST00000422538.8; ENSP00000397679.3; NM_001172439.2; NP_001165910.1.
DR UCSC; uc001rpt.3; human. [P21128-1]
DR CTD; 8909; -.
DR DisGeNET; 8909; -.
DR GeneCards; ENDOU; -.
DR HGNC; HGNC:14369; ENDOU.
DR HPA; ENSG00000111405; Group enriched (esophagus, salivary gland, skin, vagina).
DR MIM; 606720; gene.
DR neXtProt; NX_P21128; -.
DR OpenTargets; ENSG00000111405; -.
DR PharmGKB; PA165512645; -.
DR VEuPathDB; HostDB:ENSG00000111405; -.
DR eggNOG; KOG2849; Eukaryota.
DR GeneTree; ENSGT00530000063825; -.
DR HOGENOM; CLU_048034_0_0_1; -.
DR InParanoid; P21128; -.
DR OMA; MQFSWDG; -.
DR OrthoDB; 823332at2759; -.
DR PhylomeDB; P21128; -.
DR TreeFam; TF319848; -.
DR PathwayCommons; P21128; -.
DR SignaLink; P21128; -.
DR BioGRID-ORCS; 8909; 15 hits in 1069 CRISPR screens.
DR GenomeRNAi; 8909; -.
DR Pharos; P21128; Tbio.
DR PRO; PR:P21128; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P21128; protein.
DR Bgee; ENSG00000111405; Expressed in lower esophagus mucosa and 115 other tissues.
DR Genevisible; P21128; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; NAS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; TAS:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEP:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Hydrolase; Lyase; Manganese; Metal-binding; Nuclease;
KW Reference proteome; Repeat; RNA-binding; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2350438"
FT CHAIN 19..410
FT /note="Uridylate-specific endoribonuclease"
FT /id="PRO_0000036405"
FT DOMAIN 20..62
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 86..130
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 137..410
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 343
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 90..106
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 90..94
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 94..124
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 104..117
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 104..106
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 110..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 117..124
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT VAR_SEQ 19..82
FT /note="GKIESCASRCNEKFNRDAACQCDRRCLWHGNCCEDYEHLCTEDHKESEPLPQ
FT LEEETEEALASN -> D (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039215"
FT VAR_SEQ 19..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2350438"
FT /id="VSP_039216"
FT MUTAGEN 284
FT /note="E->Q: Abolishes endoribonuclease activity and
FT increases RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18936097"
FT MUTAGEN 285
FT /note="H->A: Abolishes endoribonuclease activity without
FT affecting RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18936097"
FT MUTAGEN 290
FT /note="E->Q: Abolishes endoribonuclease activity without
FT affecting RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18936097"
FT MUTAGEN 300
FT /note="H->A: Abolishes endoribonuclease activity without
FT affecting RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18936097"
FT MUTAGEN 343
FT /note="K->A: Strongly impairs endoribonuclease activity
FT without affecting RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:18936097"
FT CONFLICT 123
FT /note="L -> P (in Ref. 2; BAG37240)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="Y -> H (in Ref. 2; BAG37240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 46872 MW; CC19484F40355129 CRC64;
MRACISLVLA VLCGLAWAGK IESCASRCNE KFNRDAACQC DRRCLWHGNC CEDYEHLCTE
DHKESEPLPQ LEEETEEALA SNLYSAPTSC QGRCYEAFDK HHQCHCNARC QEFGNCCKDF
ESLCSDHEVS HSSDAITKEE IQSISEKIYR ADTNKAQKED IVLNSQNCIS PSETRNQVDR
CPKPLFTYVN EKLFSKPTYA AFINLLNNYQ RATGHGEHFS AQELAEQDAF LREIMKTAVM
KELYSFLHHQ NRYGSEQEFV DDLKNMWFGL YSRGNEEGDS SGFEHVFSGE VKKGKVTGFH
NWIRFYLEEK EGLVDYYSHI YDGPWDSYPD VLAMQFNWDG YYKEVGSAFI GSSPEFEFAL
YSLCFIARPG KVCQLSLGGY PLAVRTYTWD KSTYGNGKKY IATAYIVSST
