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UniProtKB/Swiss-Prot entry P29240

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 5NTD_DISOM
Primary accession number P29240
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 61)
Name and origin of the protein
Protein name 5'-nucleotidase [Precursor]
Synonyms EC 3.1.3.5
Ecto-nucleotidase
Gene name None
From
Discopyge ommata (Electric ray) [TaxID: 7785] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; Elasmobranchii; Squalea; Hypnosqualea; Pristiorajea; Batoidea; Torpediniformes; Narcinoidei; Narcinidae; Discopyge.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Electric lobe;
DOI=10.1111/j.1432-1033.1991.tb16443.x; PubMed=1765099 [NCBI, ExPASy, EBI, Israel, Japan]
Volknandt W., Vogel M., Pevsner J., Misumi Y., Ikehara Y., Zimmermann H.;
"5'-nucleotidase from the electric ray electric lobe. Primary structure and relation to mammalian and procaryotic enzymes.";
Eur. J. Biochem. 202:855-861(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X62278; CAA44168.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S19564; S19564.
3D structure databases
HSSP P07024; 2USH. [HSSP ENTRY / PDB]
ModBase P29240.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008253; Molecular function: 5'-nucleotidase activity (inferred from electronic annotation from EC).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009166; Biological process: nucleotide catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR008334; 5'-Nucleotdase_C.
IPR006146; 5'-Nucleotdase_CS.
IPR006179; 5_nucleotidase.
IPR004843; M-pesterase.
Graphical view of domain structure.
Gene3D G3DSA:3.90.780.10; 5'-Nucleotdase_C; 1.
PANTHER PTHR11575; 5_nucleotidase; 1.
Pfam PF02872; 5_nucleotid_C; 1.
PF00149; Metallophos; 1.
Pfam graphical view of domain structure.
PRINTS PR01607; APYRASEFAMLY.
PROSITE PS00785; 5_NUCLEOTIDASE_1; 1.
PS00786; 5_NUCLEOTIDASE_2; 1.
BLOCKS P29240.
ProtoNet P29240.
Phylogenomic databases
HOVERGEN P29240; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding; Nucleotide-binding; Signal; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    30  30      
CHAIN   31   552  522     5'-nucleotidase. PRO_0000000024
PROPEP   553   577  25     Removed in mature form. PRO_0000000025
REGION   500   506  7     Substrate binding (By similarity). 
METAL   39    39        Zinc 1 (By similarity). 
METAL   41    41        Zinc 1 (By similarity). 
METAL   86    86        Zinc 1 (By similarity). 
METAL   86    86        Zinc 2 (By similarity). 
METAL   118   118        Zinc 2 (By similarity). 
METAL   221   221        Zinc 2 (By similarity). 
METAL   244   244        Zinc 2 (By similarity). 
BINDING   417   417        Substrate (By similarity). 
SITE   119   119  1     Transition state stabilizer (By similarity). 
SITE   122   122  1     Transition state stabilizer (By similarity). 
LIPID   552   552        GPI-anchor amidated serine (By similarity). 
CARBOHYD   135   135        N-linked (GlcNAc...) (Potential). 
CARBOHYD   311   311        N-linked (GlcNAc...) (Potential). 
CARBOHYD   347   347        N-linked (GlcNAc...) (Potential). 
CARBOHYD   403   403        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 577 AA [This is the length of the unprocessed precursor] Molecular weight: 63613 Da [This is the MW of the unprocessed precursor] CRC64: 3B52535C2F70C0DB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPRVPSASAT GSSALLSLLC AFSLGRAAPF QLTILHTNDV HARVEETNQD SGKCFTQSFA 

        70         80         90        100        110        120 
GVARRWTKIE ELRARDKNVL LLDAGDQYQG TIWFNYYKGA EAAHFIEAVG YNAMALGNHE 

       130        140        150        160        170        180 
FDNGAEGLLD PFLLNVSFPV LSANLEQGED QVPSLIGYYK PSTVLDVNGE KIGVVGYTSK 

       190        200        210        220        230        240 
ETPTLSSPGP HLIFKDEIQA VQHEVDILVS QGIDKIIALG HSGFETDKLI AQKVRGVDVV 

       250        260        270        280        290        300 
VGGHSNTFLY TGKAPSNDVP VGPYPFLVNS DDQRTIPVVQ AYAYGKYLGY LKLTFDKGEV 

       310        320        330        340        350        360 
IKREGNPILL NSSIIQDPVL LAEVNKWKES LANFGKEVIG RTVVYLNGTT EECRNRECNM 

       370        380        390        400        410        420 
GNLICDAMIQ QNIRNPDEKF WNHVSICIFQ GGGIRAPINE QNNGTIQVDS LLAVLPFGST 

       430        440        450        460        470        480 
IDLLEVYGST LRAAFDHSVR RYGQNTGEFL QVSGIQVQFN LKRPPGSRVV KIDVLCADCR 

       490        500        510        520        530        540 
VPHYQPLLDN KIYKIVTNSY IAEGGDGFTM LKNERLRYDT GSTDISVVSS YIKQMKVVYP 

       550        560        570 
AVEGRILFVE NSATLPIINL KIGLSLFAFL TWFLHCS
P29240 in FASTA format

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