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Protein

5'-nucleotidase

Gene

Nt5e

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi38 – 381Zinc 1By similarity
Metal bindingi40 – 401Zinc 1By similarity
Metal bindingi87 – 871Zinc 1By similarity
Metal bindingi87 – 871Zinc 2By similarity
Metal bindingi119 – 1191Zinc 2By similarity
Sitei120 – 1201Transition state stabilizerBy similarity
Sitei123 – 1231Transition state stabilizerBy similarity
Metal bindingi222 – 2221Zinc 2By similarity
Metal bindingi245 – 2451Zinc 2By similarity
Binding sitei247 – 2471SubstrateBy similarity
Binding sitei356 – 3561SubstrateBy similarity
Binding sitei392 – 3921SubstrateBy similarity
Binding sitei397 – 3971SubstrateBy similarity
Binding sitei419 – 4191SubstrateBy similarity

GO - Molecular functioni

  • 5'-nucleotidase activity Source: CACAO
  • ferrous iron binding Source: RGD
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • adenosine metabolic process Source: RGD
  • AMP catabolic process Source: RGD
  • brain development Source: RGD
  • dephosphorylation Source: GOC
  • positive regulation of lipid biosynthetic process Source: RGD
  • purine nucleotide biosynthetic process Source: RGD
  • response to aluminum ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
Alternative name(s):
Ecto-5'-nucleotidase
CD_antigen: CD73
Gene namesi
Name:Nt5e
Synonyms:Nt5, Nte
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61956. Nt5e.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cell surface Source: RGD
  • integral component of membrane Source: RGD
  • plasma membrane Source: CACAO
  • synaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075214.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Add
BLAST
Chaini29 – 5515235'-nucleotidasePRO_0000000019Add
BLAST
Propeptidei552 – 57625Removed in mature formPRO_0000000020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 59By similarity
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence analysis
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence analysis
Disulfide bondi355 ↔ 360By similarity
Disulfide bondi367 ↔ 389By similarity
Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi478 ↔ 481By similarity
Lipidationi551 – 5511GPI-anchor amidated serine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP21588.
PRIDEiP21588.

PTM databases

PhosphoSiteiP21588.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015057.

Chemistry

BindingDBiP21588.

Structurei

3D structure databases

ProteinModelPortaliP21588.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni502 – 5087Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4419. Eukaryota.
COG0737. LUCA.
HOGENOMiHOG000247215.
HOVERGENiHBG000026.
InParanoidiP21588.
PhylomeDBiP21588.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21588-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPAAATAPK WLLLALSALL PLWPTAKSWE LTIMHTNDVH SRLEQTSDDS
60 70 80 90 100
TKCLNASLCV GGVARLFTKV QQIRKEEPNV LLLDAGDQYQ GTIWFTVYKG
110 120 130 140 150
LEVAHFMNLL GYDAMALGNH EFDNGVEGLI DPLLRNVKFP ILSANIKARG
160 170 180 190 200
PLAPQISGLY LPYKVLSVGG EVVGIVGYTS KETPFLSNPG TNLVFEDEVT
210 220 230 240 250
ALQPEVDKLK TLNVNKIIAL GHSGFEMDKL IAQKVRGVDV VVGGHTNTFL
260 270 280 290 300
YTGNPPSKEV PAGKYPFIVT SDDGRKVPVV QAYAFGKYLG YLKVEFDDKG
310 320 330 340 350
NVVTSYGNPI LLNSTIREDA AIKADINQWR IKLDNYSTQE LGRTIVYLNG
360 370 380 390 400
SAQECRFREC NMGNLICDAM INNNLRHPDE MFWNHVSMCI VNGGGIRSPI
410 420 430 440 450
DERNNGTITW ENLAAVLPFG GTFDLVQLKG STLKKAFEHS VHRYGQSTGE
460 470 480 490 500
FLQVGGIHVV YDISRKPWDR VVQLKVLCTK CRVPIYEPLE MDKVYKVVLP
510 520 530 540 550
SYLVNGGDGF QMIKDELLKH DSGDQDISVV SEYISKMKVI YPAVEGRIKF
560 570
SAASHYQGSF PLIILSFWAV ILVLYQ
Length:576
Mass (Da):63,969
Last modified:May 1, 1991 - v1
Checksum:i9EB75DD51E678AA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05214 mRNA. Translation: AAA40621.1.
PIRiA35036.
UniGeneiRn.40132.

Genome annotation databases

UCSCiRGD:61956. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05214 mRNA. Translation: AAA40621.1.
PIRiA35036.
UniGeneiRn.40132.

3D structure databases

ProteinModelPortaliP21588.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015057.

Chemistry

BindingDBiP21588.
ChEMBLiCHEMBL1075214.

PTM databases

PhosphoSiteiP21588.

Proteomic databases

PaxDbiP21588.
PRIDEiP21588.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:61956. rat.

Organism-specific databases

RGDi61956. Nt5e.

Phylogenomic databases

eggNOGiKOG4419. Eukaryota.
COG0737. LUCA.
HOGENOMiHOG000247215.
HOVERGENiHBG000026.
InParanoidiP21588.
PhylomeDBiP21588.

Miscellaneous databases

PROiP21588.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of rat liver 5'-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid."
    Misumi Y., Ogata S., Hirose S., Ikehara Y.
    J. Biol. Chem. 265:2178-2183(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Membrane-anchoring domain of rat liver 5'-nucleotidase: identification of the COOH-terminal serine-523 covalently attached with a glycolipid."
    Ogata S., Hayashi Y., Misumi Y., Ikehara Y.
    Biochemistry 29:7923-7927(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 538-551, GPI-ANCHOR AT SER-551.
    Tissue: Liver.

Entry informationi

Entry namei5NTD_RAT
AccessioniPrimary (citable) accession number: P21588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 11, 2015
This is version 129 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.