5NTD_RHIMP
ID 5NTD_RHIMP Reviewed; 580 AA.
AC P52307; P90696;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein 5NUC;
DE Includes:
DE RecName: Full=UDP-sugar hydrolase;
DE EC=3.6.1.45;
DE AltName: Full=UDP-sugar diphosphatase;
DE AltName: Full=UDP-sugar pyrophosphatase;
DE Includes:
DE RecName: Full=5'-nucleotidase;
DE Short=5'-NT;
DE EC=3.1.3.5;
DE Flags: Precursor; Fragment;
OS Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Boophilus.
OX NCBI_TaxID=6941;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10380109; DOI=10.1046/j.1365-2583.1999.820257.x;
RA Liyou N., Hamilton S., Elvin C., Willadsen P.;
RT "Cloning and expression of ecto 5-nucleotidase from the cattle tick
RT Boophilus microplus.";
RL Insect Mol. Biol. 8:257-266(1999).
RN [2]
RP PROTEIN SEQUENCE OF 15-40 AND 162-180.
RX PubMed=8387372; DOI=10.1016/0965-1748(93)90010-p;
RA Willadsen P., Riding G.A., Jarmey J., Atkins A.;
RT "The nucleotidase of Boophilus microplus and its relationship to enzymes
RT from the rat and Escherichia coli.";
RL Insect Biochem. Mol. Biol. 23:291-295(1993).
CC -!- FUNCTION: Degradation of external UDP-glucose to uridine monophosphate
CC and glucose-1-phosphate, which can then be used by the cell.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC EC=3.6.1.45;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Gut, ovaries and salivary glands.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; U80634; AAB38963.1; -; mRNA.
DR AlphaFoldDB; P52307; -.
DR SMR; P52307; -.
DR VEuPathDB; VectorBase:LOC119174065; -.
DR SABIO-RK; P52307; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Nucleotide-binding; Signal; Zinc.
FT SIGNAL <1..14
FT /evidence="ECO:0000269|PubMed:8387372"
FT CHAIN 15..555
FT /note="Protein 5NUC"
FT /id="PRO_0000000021"
FT PROPEP 556..580
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000000022"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 502..508
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 115
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 555
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..51
FT /evidence="ECO:0000250"
FT DISULFID 349..354
FT /evidence="ECO:0000250"
FT DISULFID 478..481
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="T -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37..39
FT /note="SGT -> HXG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 580 AA; 63460 MW; 588EEF2014071AB7 CRC64;
GRLLACLLLP GLAATDFTAT VLHTNDVHGR FEQITASGTR CTKQAAEAQQ CVGGIARQKT
VVSQAAASGA NVLFLNAGDY YQGSIWYYVL GAPIVAEAVN YLAHDAMALG NHEFDRGAEG
LVPLLTESRV PIVGCNVDFS EEPTLKPLQP KPSVVVERAG IKIGLIGYTT MNTTYLSSPG
KVRFTDEAEC IQREAQRLRR EEGVQVIIAV GHSGVPRDLE ICERVPEVSL VVGGHTHTFL
YSGPTENGRV SGDKPQGPYP IVVDRAADSR CLVVQDFYMG KYMGNISITW NQRGEVVRWS
GQPVLLDRSI PEDPDGIALL DRYRDRVAQS QASVVAESKV LLDGDKNRCR LDECNLGNLV
MDAFLKKMAS LPSPQASWTR VAAVIANAGG IRASIDEQST GGRITFEDVV NVLPFGNTLV
EMNVTGAQLK GLLEHGVHRH DVKGYVPPAE LVLAAGLRVV YDIQREPYDR VVEAHILCTE
CRVPRYEPLE YARQYRIAAL SYIVHGGDNF DFSFVKPKDM YDTGFQDAEI VMKYMNSTSP
ITTALDGRVT FLKTNQASDA CLNLASPFLV LLVLVVFYHL
