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Protein

Protein 5NUC

Gene
N/A
Organism
Rhipicephalus microplus (Cattle tick) (Boophilus microplus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.

Catalytic activityi

UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.
A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Zinc 1By similarity
Metal bindingi28 – 281Zinc 1By similarity
Metal bindingi79 – 791Zinc 1By similarity
Metal bindingi79 – 791Zinc 2By similarity
Metal bindingi111 – 1111Zinc 2By similarity
Sitei112 – 1121Transition state stabilizerBy similarity
Sitei115 – 1151Transition state stabilizerBy similarity
Metal bindingi212 – 2121Zinc 2By similarity
Metal bindingi235 – 2351Zinc 2By similarity
Binding sitei350 – 3501SubstrateBy similarity
Binding sitei387 – 3871SubstrateBy similarity
Binding sitei392 – 3921SubstrateBy similarity
Binding sitei415 – 4151SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SABIO-RKP52307.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein 5NUC
Including the following 2 domains:
UDP-sugar hydrolase (EC:3.6.1.45)
Alternative name(s):
UDP-sugar diphosphatase
UDP-sugar pyrophosphatase
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
OrganismiRhipicephalus microplus (Cattle tick) (Boophilus microplus)
Taxonomic identifieri6941 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariParasitiformesIxodidaIxodoideaIxodidaeRhipicephalinaeRhipicephalusBoophilus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 14›141 PublicationAdd
BLAST
Chaini15 – 555541Protein 5NUCPRO_0000000021Add
BLAST
Propeptidei556 – 58025Removed in mature formSequence AnalysisPRO_0000000022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 51By similarity
Glycosylationi172 – 1721N-linked (GlcNAc...)Curated
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi349 ↔ 354By similarity
Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi478 ↔ 481By similarity
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Lipidationi555 – 5551GPI-anchor amidated asparagineSequence Analysis

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Tissue specificityi

Gut, ovaries and salivary glands.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP52307.
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

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.
PROSITEiPS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

P52307-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GRLLACLLLP GLAATDFTAT VLHTNDVHGR FEQITASGTR CTKQAAEAQQ
60 70 80 90 100
CVGGIARQKT VVSQAAASGA NVLFLNAGDY YQGSIWYYVL GAPIVAEAVN
110 120 130 140 150
YLAHDAMALG NHEFDRGAEG LVPLLTESRV PIVGCNVDFS EEPTLKPLQP
160 170 180 190 200
KPSVVVERAG IKIGLIGYTT MNTTYLSSPG KVRFTDEAEC IQREAQRLRR
210 220 230 240 250
EEGVQVIIAV GHSGVPRDLE ICERVPEVSL VVGGHTHTFL YSGPTENGRV
260 270 280 290 300
SGDKPQGPYP IVVDRAADSR CLVVQDFYMG KYMGNISITW NQRGEVVRWS
310 320 330 340 350
GQPVLLDRSI PEDPDGIALL DRYRDRVAQS QASVVAESKV LLDGDKNRCR
360 370 380 390 400
LDECNLGNLV MDAFLKKMAS LPSPQASWTR VAAVIANAGG IRASIDEQST
410 420 430 440 450
GGRITFEDVV NVLPFGNTLV EMNVTGAQLK GLLEHGVHRH DVKGYVPPAE
460 470 480 490 500
LVLAAGLRVV YDIQREPYDR VVEAHILCTE CRVPRYEPLE YARQYRIAAL
510 520 530 540 550
SYIVHGGDNF DFSFVKPKDM YDTGFQDAEI VMKYMNSTSP ITTALDGRVT
560 570 580
FLKTNQASDA CLNLASPFLV LLVLVVFYHL
Length:580
Mass (Da):63,460
Last modified:January 11, 2001 - v2
Checksum:i588EEF2014071AB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti15 – 151T → K AA sequence (PubMed:8387372).Curated
Sequence conflicti37 – 393SGT → HXG AA sequence (PubMed:8387372).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80634 mRNA. Translation: AAB38963.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80634 mRNA. Translation: AAB38963.1.

3D structure databases

ProteinModelPortaliP52307.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP52307.

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.
PROSITEiPS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of ecto 5-nucleotidase from the cattle tick Boophilus microplus."
    Liyou N., Hamilton S., Elvin C., Willadsen P.
    Insect Mol. Biol. 8:257-266(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The nucleotidase of Boophilus microplus and its relationship to enzymes from the rat and Escherichia coli."
    Willadsen P., Riding G.A., Jarmey J., Atkins A.
    Insect Biochem. Mol. Biol. 23:291-295(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-40 AND 162-180.

Entry informationi

Entry namei5NTD_RHIMP
AccessioniPrimary (citable) accession number: P52307
Secondary accession number(s): P90696
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2001
Last modified: January 7, 2015
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.