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P52307

- 5NTD_RHIMP

UniProt

P52307 - 5NTD_RHIMP

Protein

Protein 5NUC

Gene
N/A
Organism
Rhipicephalus microplus (Cattle tick) (Boophilus microplus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    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

    Zinc.

    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

    1. 5'-nucleotidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. nucleotide binding Source: UniProtKB-KW
    4. UDP-sugar diphosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. nucleotide catabolic process Source: InterPro

    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

    1. anchored component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    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

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    GRLLACLLLP GLAATDFTAT VLHTNDVHGR FEQITASGTR CTKQAAEAQQ    50
    CVGGIARQKT VVSQAAASGA NVLFLNAGDY YQGSIWYYVL GAPIVAEAVN 100
    YLAHDAMALG NHEFDRGAEG LVPLLTESRV PIVGCNVDFS EEPTLKPLQP 150
    KPSVVVERAG IKIGLIGYTT MNTTYLSSPG KVRFTDEAEC IQREAQRLRR 200
    EEGVQVIIAV GHSGVPRDLE ICERVPEVSL VVGGHTHTFL YSGPTENGRV 250
    SGDKPQGPYP IVVDRAADSR CLVVQDFYMG KYMGNISITW NQRGEVVRWS 300
    GQPVLLDRSI PEDPDGIALL DRYRDRVAQS QASVVAESKV LLDGDKNRCR 350
    LDECNLGNLV MDAFLKKMAS LPSPQASWTR VAAVIANAGG IRASIDEQST 400
    GGRITFEDVV NVLPFGNTLV EMNVTGAQLK GLLEHGVHRH DVKGYVPPAE 450
    LVLAAGLRVV YDIQREPYDR VVEAHILCTE CRVPRYEPLE YARQYRIAAL 500
    SYIVHGGDNF DFSFVKPKDM YDTGFQDAEI VMKYMNSTSP ITTALDGRVT 550
    FLKTNQASDA CLNLASPFLV LLVLVVFYHL 580
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80634 mRNA. Translation: AAB38963.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80634 mRNA. Translation: AAB38963.1 .

    3D structure databases

    ProteinModelPortali P52307.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P52307.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    3.90.780.10. 1 hit.
    InterProi IPR008334. 5'-Nucleotdase_C.
    IPR006146. 5'-Nucleotdase_CS.
    IPR006179. 5_nucleotidase/apyrase.
    IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view ]
    PANTHERi PTHR11575. PTHR11575. 1 hit.
    Pfami PF02872. 5_nucleotid_C. 1 hit.
    PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR01607. APYRASEFAMLY.
    SUPFAMi SSF55816. SSF55816. 1 hit.
    SSF56300. SSF56300. 1 hit.
    PROSITEi PS00786. 5_NUCLEOTIDASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 91 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