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Protein

Zinc phosphodiesterase ELAC protein 1

Gene

Elac1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (By similarity).By similarity

Catalytic activityi

Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Zinc 1; catalyticBy similarity
Metal bindingi64 – 641Zinc 1; catalyticBy similarity
Active sitei66 – 661Proton acceptorSequence analysis
Metal bindingi66 – 661Zinc 2; catalyticBy similarity
Metal bindingi67 – 671Zinc 2; catalyticBy similarity
Metal bindingi181 – 1811Zinc 1; catalyticBy similarity
Metal bindingi252 – 2521Zinc 1; catalyticBy similarity
Metal bindingi252 – 2521Zinc 2; catalyticBy similarity
Metal bindingi312 – 3121Zinc 2; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc phosphodiesterase ELAC protein 1 (EC:3.1.26.11)
Alternative name(s):
ElaC homolog protein 1
Ribonuclease Z 1
Short name:
RNase Z 1
tRNA 3 endonuclease 1
tRNase Z 1
Gene namesi
Name:Elac1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1890495. Elac1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Zinc phosphodiesterase ELAC protein 1PRO_0000155826Add
BLAST

Proteomic databases

EPDiQ8VEB6.
MaxQBiQ8VEB6.
PaxDbiQ8VEB6.
PRIDEiQ8VEB6.

PTM databases

PhosphoSiteiQ8VEB6.

Expressioni

Gene expression databases

BgeeiQ8VEB6.
CleanExiMM_ELAC1.
GenevisibleiQ8VEB6. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041793.

Structurei

3D structure databases

ProteinModelPortaliQ8VEB6.
SMRiQ8VEB6. Positions 3-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase Z family.Curated

Phylogenomic databases

eggNOGiKOG2121. Eukaryota.
COG1234. LUCA.
GeneTreeiENSGT00730000111224.
HOGENOMiHOG000272419.
HOVERGENiHBG050040.
InParanoidiQ8VEB6.
KOiK00784.
OMAiPVPGKMD.
OrthoDBiEOG7HF1KG.
PhylomeDBiQ8VEB6.
TreeFamiTF324462.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
HAMAPiMF_01818. RNase_Z_BN.
InterProiIPR001279. Metallo-B-lactamas.
IPR013471. RNase_Z/BN.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
PF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 2 hits.
TIGRFAMsiTIGR02651. RNase_Z. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VEB6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSMDVTFLGT GAAYPSPTRG ASAVVLRCEG ECWLFDCGEG TQTQLMKSQL
60 70 80 90 100
KAGRITKIFI THLHGDHFFG LPGLLCTISL QSGSVVARQP IEIYGPVGLR
110 120 130 140 150
DFIWRTMELS HTELVFPYVV HELVPTADQC PVEELREFAH MDETDSSPKG
160 170 180 190 200
QGRTILLDAE ENSYCLVDDE QFVVKAFRLF HRIPSFGFSV VEKKRAGKLN
210 220 230 240 250
AQKLRDLGVP PGPAYGKLKN GISVVLDNGV TISPQDVLKK PMVGRKVCIL
260 270 280 290 300
GDCSGVVGDG GVKLCFEADL LIHEATLDDS QMDKAREHGH STPQMAAAFA
310 320 330 340 350
KLCRAKRLVL THFSQRYKPT ALAREGEADG IAELRKQAEA VLELQEVTLA
360
EDFMVIGIPI KK
Length:362
Mass (Da):39,740
Last modified:March 1, 2002 - v1
Checksum:iDC3D437211D6810C
GO
Isoform 2 (identifier: Q8VEB6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-241: Missing.

Note: No experimental confirmation availalbe.
Show »
Length:121
Mass (Da):13,179
Checksum:i6434F54E0626FF2B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771T → P in AAG24919 (PubMed:11175785).Curated
Sequence conflicti263 – 2631K → N in BAB31204 (PubMed:16141072).Curated
Sequence conflicti276 – 2761T → G in AAG24919 (PubMed:11175785).Curated
Sequence conflicti282 – 2821M → I in AAG24919 (PubMed:11175785).Curated
Sequence conflicti287 – 2871E → D in AAG24919 (PubMed:11175785).Curated
Sequence conflicti303 – 3031C → S in AAG24919 (PubMed:11175785).Curated
Sequence conflicti314 – 3141S → I in AAG24919 (PubMed:11175785).Curated
Sequence conflicti321 – 3211A → P in AAG24919 (PubMed:11175785).Curated
Sequence conflicti340 – 3401A → P in AAG24919 (PubMed:11175785).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 241241Missing in isoform 2. 1 PublicationVSP_009167Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308697 mRNA. Translation: AAG24919.1.
AK018424 mRNA. Translation: BAB31204.1.
BC019371 mRNA. No translation available.
CCDSiCCDS37855.1. [Q8VEB6-1]
RefSeqiNP_444485.2. NM_053255.3. [Q8VEB6-1]
UniGeneiMm.50642.

Genome annotation databases

EnsembliENSMUST00000041138; ENSMUSP00000041793; ENSMUSG00000036941. [Q8VEB6-1]
GeneIDi114615.
KEGGimmu:114615.
UCSCiuc008fow.1. mouse. [Q8VEB6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308697 mRNA. Translation: AAG24919.1.
AK018424 mRNA. Translation: BAB31204.1.
BC019371 mRNA. No translation available.
CCDSiCCDS37855.1. [Q8VEB6-1]
RefSeqiNP_444485.2. NM_053255.3. [Q8VEB6-1]
UniGeneiMm.50642.

3D structure databases

ProteinModelPortaliQ8VEB6.
SMRiQ8VEB6. Positions 3-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041793.

PTM databases

PhosphoSiteiQ8VEB6.

Proteomic databases

EPDiQ8VEB6.
MaxQBiQ8VEB6.
PaxDbiQ8VEB6.
PRIDEiQ8VEB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041138; ENSMUSP00000041793; ENSMUSG00000036941. [Q8VEB6-1]
GeneIDi114615.
KEGGimmu:114615.
UCSCiuc008fow.1. mouse. [Q8VEB6-1]

Organism-specific databases

CTDi55520.
MGIiMGI:1890495. Elac1.

Phylogenomic databases

eggNOGiKOG2121. Eukaryota.
COG1234. LUCA.
GeneTreeiENSGT00730000111224.
HOGENOMiHOG000272419.
HOVERGENiHBG050040.
InParanoidiQ8VEB6.
KOiK00784.
OMAiPVPGKMD.
OrthoDBiEOG7HF1KG.
PhylomeDBiQ8VEB6.
TreeFamiTF324462.

Miscellaneous databases

NextBioi368567.
PROiQ8VEB6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VEB6.
CleanExiMM_ELAC1.
GenevisibleiQ8VEB6. MM.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
HAMAPiMF_01818. RNase_Z_BN.
InterProiIPR001279. Metallo-B-lactamas.
IPR013471. RNase_Z/BN.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
PF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 2 hits.
TIGRFAMsiTIGR02651. RNase_Z. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryonic lung.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Mammary tumor.

Entry informationi

Entry nameiRNZ1_MOUSE
AccessioniPrimary (citable) accession number: Q8VEB6
Secondary accession number(s): Q9CXB1, Q9ERF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.