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Protein

Protein 5NUC

Gene
N/A
Organism
Rhipicephalus microplus (Cattle tick) (Boophilus microplus)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi26Zinc 1By similarity1
Metal bindingi28Zinc 1By similarity1
Metal bindingi79Zinc 1By similarity1
Metal bindingi79Zinc 2By similarity1
Metal bindingi111Zinc 2By similarity1
Sitei112Transition state stabilizerBy similarity1
Sitei115Transition state stabilizerBy similarity1
Metal bindingi212Zinc 2By similarity1
Metal bindingi235Zinc 2By similarity1
Binding sitei350SubstrateBy similarity1
Binding sitei387SubstrateBy similarity1
Binding sitei392SubstrateBy similarity1
Binding sitei415SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SABIO-RKiP52307

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 141 PublicationAdd BLAST›14
ChainiPRO_000000002115 – 555Protein 5NUCAdd BLAST541
PropeptideiPRO_0000000022556 – 580Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 51By similarity
Glycosylationi172N-linked (GlcNAc...) asparagineCurated1
Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi349 ↔ 354By similarity
Glycosylationi423N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi478 ↔ 481By similarity
Glycosylationi536N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi555GPI-anchor amidated asparagineSequence analysis1

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
SMRiP52307
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni502 – 508Substrate bindingBy similarity7

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
InterProiView protein in InterPro
IPR008334 5'-Nucleotdase_C
IPR036907 5'-Nucleotdase_C_sf
IPR006146 5'-Nucleotdase_CS
IPR006179 5_nucleotidase/apyrase
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
PANTHERiPTHR11575 PTHR11575, 1 hit
PfamiView protein in Pfam
PF02872 5_nucleotid_C, 1 hit
PF00149 Metallophos, 1 hit
PRINTSiPR01607 APYRASEFAMLY
SUPFAMiSSF55816 SSF55816, 1 hit
PROSITEiView protein in PROSITE
PS00786 5_NUCLEOTIDASE_2, 1 hit

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)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti15T → K AA sequence (PubMed:8387372).Curated1
Sequence conflicti37 – 39SGT → HXG AA sequence (PubMed:8387372).Curated3

Sequence databases

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

Similar proteinsi

Entry informationi

Entry namei5NTD_RHIMP
AccessioniPrimary (citable) accession number: P52307
Secondary accession number(s): P90696
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2001
Last modified: March 28, 2018
This is version 101 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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