P29240 (5NTD_DISOM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: 5'-nucleotidase EC=3.1.3.5 Alternative name(s): Ecto-nucleotidase
Organism	Discopyge ommata (Electric ray)
Taxonomic identifier	7785 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Narcinoidei › Narcinidae › Discopyge

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Cofactor	Zinc.
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Gene Ontology (GO)
Biological process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide 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
	Signal peptide	1 – 30	30
	Chain	31 – 552	522	5'-nucleotidase		PRO_0000000024
	Propeptide	553 – 577	25	Removed in mature form		PRO_0000000025
Regions
	Region	500 – 506	7	Substrate binding By similarity
Sites
	Metal binding	39	1	Zinc 1 By similarity
	Metal binding	41	1	Zinc 1 By similarity
	Metal binding	86	1	Zinc 1 By similarity
	Metal binding	86	1	Zinc 2 By similarity
	Metal binding	118	1	Zinc 2 By similarity
	Metal binding	221	1	Zinc 2 By similarity
	Metal binding	244	1	Zinc 2 By similarity
	Binding site	417	1	Substrate By similarity
	Site	119	1	Transition state stabilizer By similarity
	Site	122	1	Transition state stabilizer By similarity
Amino acid modifications
	Lipidation	552	1	GPI-anchor amidated serine By similarity
	Glycosylation	135	1	N-linked (GlcNAc...) Potential
	Glycosylation	311	1	N-linked (GlcNAc...) Potential
	Glycosylation	347	1	N-linked (GlcNAc...) Potential
	Glycosylation	403	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P29240 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 3B52535C2F70C0DB	FASTA	577	63,613
	10 20 30 40 50 60 MPRVPSASAT GSSALLSLLC AFSLGRAAPF QLTILHTNDV HARVEETNQD SGKCFTQSFA 70 80 90 100 110 120 GVARRWTKIE ELRARDKNVL LLDAGDQYQG TIWFNYYKGA EAAHFIEAVG YNAMALGNHE 130 140 150 160 170 180 FDNGAEGLLD PFLLNVSFPV LSANLEQGED QVPSLIGYYK PSTVLDVNGE KIGVVGYTSK 190 200 210 220 230 240 ETPTLSSPGP HLIFKDEIQA VQHEVDILVS QGIDKIIALG HSGFETDKLI AQKVRGVDVV 250 260 270 280 290 300 VGGHSNTFLY TGKAPSNDVP VGPYPFLVNS DDQRTIPVVQ AYAYGKYLGY LKLTFDKGEV 310 320 330 340 350 360 IKREGNPILL NSSIIQDPVL LAEVNKWKES LANFGKEVIG RTVVYLNGTT EECRNRECNM 370 380 390 400 410 420 GNLICDAMIQ QNIRNPDEKF WNHVSICIFQ GGGIRAPINE QNNGTIQVDS LLAVLPFGST 430 440 450 460 470 480 IDLLEVYGST LRAAFDHSVR RYGQNTGEFL QVSGIQVQFN LKRPPGSRVV KIDVLCADCR 490 500 510 520 530 540 VPHYQPLLDN KIYKIVTNSY IAEGGDGFTM LKNERLRYDT GSTDISVVSS YIKQMKVVYP 550 560 570 AVEGRILFVE NSATLPIINL KIGLSLFAFL TWFLHCS

References

[1]

"5'-nucleotidase from the electric ray electric lobe. Primary structure and relation to mammalian and procaryotic enzymes." Volknandt W., Vogel M., Pevsner J., Misumi Y., Ikehara Y., Zimmermann H. Eur. J. Biochem. 202:855-861(1991) [PubMed: 1765099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Electric lobe.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X62278 mRNA. Translation: CAA44168.1.
PIR	S19564.
3D structure databases
ProteinModelPortal	P29240.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG000026.
Family and domain databases
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. Metallo_PEstase_dom. [Graphical view]
Gene3D	G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.
PANTHER	PTHR11575. 5_nucleotidase. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
SUPFAM	SSF55816. 5'-Nucleotdase_C. 1 hit.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

5NTD_DISOM

Accession

Primary (citable) accession number: P29240

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	September 21, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program