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Database: UniProt
Entry: M3ZZF8_XIPMA
LinkDB: M3ZZF8_XIPMA
Original site: M3ZZF8_XIPMA 
ID   M3ZZF8_XIPMA            Unreviewed;       612 AA.
AC   M3ZZF8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE            EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
DE   AltName: Full=Ecto-5'-nucleotidase {ECO:0000256|ARBA:ARBA00029793};
GN   Name=NT5E {ECO:0000313|Ensembl:ENSXMAP00000007602.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000007602.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000007602.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000007602.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00000815};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-
CC       anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
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DR   AlphaFoldDB; M3ZZF8; -.
DR   Ensembl; ENSXMAT00000007610.2; ENSXMAP00000007602.2; ENSXMAG00000007577.2.
DR   eggNOG; KOG4419; Eukaryota.
DR   GeneTree; ENSGT00530000063775; -.
DR   HOGENOM; CLU_005854_7_1_1; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   CDD; cd07409; MPP_CD73_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 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:SF24; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362119};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT   DOMAIN          70..283
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          377..552
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
SQ   SEQUENCE   612 AA;  67374 MW;  F14C2A1E1179CB13 CRC64;
     MFRVAVRFDR GKRKRRRRKR RRSSSGCKQL RFFSGSVLRS AQMEHTIFLL LLILLLGTAV
     PSAADWTLVL LHTNDVHARV EETSVHSIKC GREEKCYGGV ARRATEIRRI RSEEPNVLLL
     DAGDQFQGTV WFTLYKGAEA AHFMNRLGYD AMVFGNHEFD NGVDGLMKPF LRDINCSILS
     ANIRPDSTLA STFGAAFQPY KIFEVGGQRV GVVGYTSRET PALSQPGPHL DFLEEVSTLQ
     PIVDKLKTLG VNKIIALGHS GIAVDRLIAR KVRGVDVVIG GHTNTFLYTG QPPSLERLEG
     DYPIMEVSDD GRRVPVVQAY AFGKYLGFLK VTFDDGGNVV RSTGNPILLD NSIKQDAAVL
     AEVEAWKQNL TSFTAQVVGK TLVFLNASQS ACRFHECNLG NLICDAMVDN YTRSFDGQRW
     SNVSACIMNG GGIRSSIDER IYNGSVTLED LLTVLPFAGT FDRVLLKGST LRAAFEHGAH
     RYGSKAGEFL QVSGLRVVLD VSRPAGRRVR SLSILCTQCR VPRYDPVRDA AVYAVVLPSY
     LVTGGDGFNV IKNGILEHSI GHLDVLVLSN YMKKKGWLYP AVEGRITVLS RAPAPQATLA
     SLGLLVLFVL SC
//
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