Q9H777 (RNZ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc phosphodiesterase ELAC protein 1
EC=3.1.26.11

Alternative name(s):
Deleted in Ma29
ElaC homolog protein 1
Ribonuclease Z 1
Short name=RNase Z 1
tRNA 3 endonuclease 1
tRNase Z 1

Gene names

Name:	ELAC1
Synonyms:	D29

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Catalytic activity	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. Ref.5
Cofactor	Binds 2 zinc ions By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Nucleus Probable.
Tissue specificity	Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.1
Sequence similarities	Belongs to the RNase Z family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA 3'-trailer cleavage Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endoribonuclease activity, producing 5'-phosphomonoesters Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 363

363

Zinc phosphodiesterase ELAC protein 1

PRO_0000155825

Sites

Active site

66

1

Proton acceptor Potential

Metal binding

62

1

Zinc 1; catalytic By similarity

Metal binding

64

1

Zinc 1; catalytic By similarity

Metal binding

66

1

Zinc 2; catalytic By similarity

Metal binding

67

1

Zinc 2; catalytic By similarity

Metal binding

182

1

Zinc 1; catalytic By similarity

Metal binding

253

1

Zinc 1; catalytic By similarity

Metal binding

253

1

Zinc 2; catalytic By similarity

Metal binding

313

1

Zinc 2; catalytic By similarity

Natural variations

Natural variant

355

1

M → V. Ref.1
Corresponds to variant rs34524743 [ dbSNP | Ensembl ].

VAR_017424

Experimental info

Sequence conflict

314

1

F → S in BAB15021. Ref.3

Sequence conflict

358

1

S → G in BAB15021. Ref.3

Secondary structure

1

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363

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Beta strand

11 – 14

4

Beta strand

17 – 19

3

Beta strand

21 – 28

8

Beta strand

31 – 35

5

Helix

41 – 47

7

Beta strand

48 – 50

3

Helix

52 – 54

3

Beta strand

55 – 59

5

Helix

65 – 67

3

Turn

68 – 70

3

Helix

71 – 81

11

Beta strand

91 – 96

6

Helix

99 – 109

11

Beta strand

118 – 123

6

Helix

127 – 129

3

Turn

160 – 163

4

Beta strand

164 – 169

6

Beta strand

171 – 184

14

Beta strand

186 – 193

8

Beta strand

247 – 251

5

Beta strand

255 – 257

3

Helix

261 – 265

5

Turn

266 – 268

3

Beta strand

270 – 275

6

Helix

280 – 282

3

Helix

283 – 288

6

Helix

294 – 303

10

Beta strand

307 – 312

6

Beta strand

347 – 350

4

Beta strand

356 – 358

3

Sequences

	Sequence		Length	Mass (Da)
	Q9H777 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: 125A8416502D4C79	FASTA	363	40,019
	10 20 30 40 50 60 MSMDVTFLGT GAAYPSPTRG ASAVVLRCEG ECWLFDCGEG TQTQLMKSQL KAGRITKIFI 70 80 90 100 110 120 THLHGDHFFG LPGLLCTISL QSGSMVSKQP IEIYGPVGLR DFIWRTMELS HTELVFHYVV 130 140 150 160 170 180 HELVPTADQC PAEELKEFAH VNRADSPPKE EQGRTILLDS EENSYLLFDD EQFVVKAFRL 190 200 210 220 230 240 FHRIPSFGFS VVEKKRPGKL NAQKLKDLGV PPGPAYGKLK NGISVVLENG VTISPQDVLK 250 260 270 280 290 300 KPIVGRKICI LGDCSGVVGD GGVKLCFEAD LLIHEATLDD AQMDKAKEHG HSTPQMAATF 310 320 330 340 350 360 AKLCRAKRLV LTHFSQRYKP VALAREGETD GIAELKKQAE SVLDLQEVTL AEDFMVISIP IKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Physical and transcriptional map of a 311-kb segment of chromosome 18q21, a candidate lung tumor suppressor locus." Yanaihara N., Kohno T., Takakura S., Takei K., Otsuka A., Sunaga N., Takahashi M., Yamazaki M., Tashiro H., Fukuzumi Y., Fujimori Y., Hagiwara K., Tanaka T., Yokota J. Genomics 72:169-179(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT VAL-355.
[2]	"A candidate prostate cancer susceptibility gene at chromosome 17p." Tavtigian S.V., Simard J., Teng D.H.F., Abtin V., Baumgard M., Beck A., Camp N.J., Carillo A.R., Chen Y., Dayananth P., Desrochers M., Dumont M., Farnham J.M., Frank D., Frye C., Ghaffari S., Gupte J.S., Hu R. , Iliev D., Janecki T., Kort E.N., Laity K.E., Leavitt A., Leblanc G., McArthur-Morrison J., Pederson A., Penn B., Peterson K.T., Reid J.E., Richards S., Schroeder M., Smith R., Snyder S.C., Swedlund B., Swensen J., Thomas A., Tranchant M., Woodland A.-M., Labrie F., Skolnick M.H., Neuhausen S., Rommens J., Cannon-Albright L.A. Nat. Genet. 27:172-180(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Smooth muscle.
[4]	"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]. Tissue: Muscle.
[5]	"A candidate prostate cancer susceptibility gene encodes tRNA 3' processing endoribonuclease." Takaku H., Minagawa A., Takagi M., Nashimoto M. Nucleic Acids Res. 31:2272-2278(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB029151 mRNA. Translation: BAA96799.1.
AF308695 mRNA. Translation: AAG24917.1.
AK024822 mRNA. Translation: BAB15021.1.
BC014624 mRNA. Translation: AAH14624.1.

IPI

IPI00302979.

RefSeq

NP_061166.1. NM_018696.2.

UniGene

Hs.657360.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ZWF	X-ray	1.70	A/B	3-363	[»]

ProteinModelPortal

Q9H777.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000269466.

PTM databases

PhosphoSite

Q9H777.

Polymorphism databases

DMDM

41017799.

Proteomic databases

PaxDb

Q9H777.

PRIDE

Q9H777.

Protocols and materials databases

DNASU

55520.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269466; ENSP00000269466; ENSG00000141642.

GeneID

55520.

KEGG

hsa:55520.

UCSC

uc002lez.3. human.

Organism-specific databases

CTD

55520.

GeneCards

GC18P048429.

HGNC

HGNC:14197. ELAC1.

HPA

HPA040867.

MIM

608079. gene.

neXtProt

NX_Q9H777.

PharmGKB

PA27738.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1234.

HOGENOM

HOG000272419.

HOVERGEN

HBG050040.

InParanoid

Q9H777.

KO

K00784.

OMA

EGTQHQF.

OrthoDB

EOG4FN4J3.

PhylomeDB

Q9H777.

Enzyme and pathway databases

BRENDA

3.1.26.11. 2681.

Gene expression databases

Bgee

Q9H777.

CleanEx

HS_ELAC1.

Genevestigator

Q9H777.

GermOnline

ENSG00000141642. Homo sapiens.

Family and domain databases

InterPro

IPR001279. Beta-lactamas-like.
IPR013471. RNase_Z.
[Graphical view]

SMART

SM00849. Lactamase_B. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02651. RNase_Z. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

ELAC1. human.

GenomeRNAi

55520.

NextBio

59936.

SOURCE

Search...

Entry information

Entry name

RNZ1_HUMAN

Accession

Primary (citable) accession number: Q9H777
Secondary accession number(s): Q9NS99

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.