5NTD_DIPOM
ID 5NTD_DIPOM Reviewed; 577 AA.
AC P29240;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=5'-nucleotidase;
DE EC=3.1.3.5;
DE AltName: Full=Ecto-nucleotidase;
DE Flags: Precursor;
OS Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX NCBI_TaxID=1870830;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electric lobe;
RX PubMed=1765099; DOI=10.1111/j.1432-1033.1991.tb16443.x;
RA Volknandt W., Vogel M., Pevsner J., Misumi Y., Ikehara Y., Zimmermann H.;
RT "5'-nucleotidase from the electric ray electric lobe. Primary structure and
RT relation to mammalian and procaryotic enzymes.";
RL Eur. J. Biochem. 202:855-861(1991).
CC -!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane permeable
CC nucleosides.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; X62278; CAA44168.1; -; mRNA.
DR PIR; S19564; S19564.
DR AlphaFoldDB; P29240; -.
DR SMR; P29240; -.
DR PRIDE; P29240; -.
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: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; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; Signal; Zinc.
FT SIGNAL 1..30
FT CHAIN 31..552
FT /note="5'-nucleotidase"
FT /id="PRO_0000000024"
FT PROPEP 553..577
FT /note="Removed in mature form"
FT /id="PRO_0000000025"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 500..506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 122
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 552
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 353..358
FT /evidence="ECO:0000250"
FT DISULFID 365..387
FT /evidence="ECO:0000250"
FT DISULFID 476..479
FT /evidence="ECO:0000250"
SQ SEQUENCE 577 AA; 63613 MW; 3B52535C2F70C0DB CRC64;
MPRVPSASAT GSSALLSLLC AFSLGRAAPF QLTILHTNDV HARVEETNQD SGKCFTQSFA
GVARRWTKIE ELRARDKNVL LLDAGDQYQG TIWFNYYKGA EAAHFIEAVG YNAMALGNHE
FDNGAEGLLD PFLLNVSFPV LSANLEQGED QVPSLIGYYK PSTVLDVNGE KIGVVGYTSK
ETPTLSSPGP HLIFKDEIQA VQHEVDILVS QGIDKIIALG HSGFETDKLI AQKVRGVDVV
VGGHSNTFLY TGKAPSNDVP VGPYPFLVNS DDQRTIPVVQ AYAYGKYLGY LKLTFDKGEV
IKREGNPILL NSSIIQDPVL LAEVNKWKES LANFGKEVIG RTVVYLNGTT EECRNRECNM
GNLICDAMIQ QNIRNPDEKF WNHVSICIFQ GGGIRAPINE QNNGTIQVDS LLAVLPFGST
IDLLEVYGST LRAAFDHSVR RYGQNTGEFL QVSGIQVQFN LKRPPGSRVV KIDVLCADCR
VPHYQPLLDN KIYKIVTNSY IAEGGDGFTM LKNERLRYDT GSTDISVVSS YIKQMKVVYP
AVEGRILFVE NSATLPIINL KIGLSLFAFL TWFLHCS
