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MAGT1_DANRE
ID   MAGT1_DANRE             Reviewed;         328 AA.
AC   Q7ZV50;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Magnesium transporter protein 1 {ECO:0000250|UniProtKB:Q9H0U3};
DE            Short=MagT1;
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1;
DE            Short=Oligosaccharyl transferase subunit MAGT1;
DE   Flags: Precursor;
GN   Name=magt1 {ECO:0000250|UniProtKB:Q9H0U3}; ORFNames=zgc:56218;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TOPOLOGY.
RX   PubMed=19717468; DOI=10.1073/pnas.0908332106;
RA   Zhou H., Clapham D.E.;
RT   "Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and
RT   vertebrate embryonic development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15750-15755(2009).
CC   -!- FUNCTION: Cell surface magnesium transporter.
CC       {ECO:0000269|PubMed:19717468}.
CC   -!- FUNCTION: Accessory component of the STT3B-containing form of the N-
CC       oligosaccharyl transferase (OST) complex which catalyzes the transfer
CC       of a high mannose oligosaccharide from a lipid-linked oligosaccharide
CC       donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif
CC       in nascent polypeptide chains. May be involved in substrate-specific N-
CC       glycosylation. {ECO:0000250|UniProtKB:Q9H0U3}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9H0U3}.
CC   -!- SUBUNIT: Accessory component of the STT3B-containing form of the
CC       oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:Q9H0U3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H0U3};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:Q9H0U3}. Endoplasmic reticulum
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Early developmental arrest.
CC       {ECO:0000269|PubMed:19717468}.
CC   -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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DR   EMBL; BC046002; AAH46002.1; -; mRNA.
DR   RefSeq; NP_955994.1; NM_199700.1.
DR   AlphaFoldDB; Q7ZV50; -.
DR   SMR; Q7ZV50; -.
DR   STRING; 7955.ENSDARP00000075309; -.
DR   TCDB; 1.A.76.1.3; the magnesium transporter1 (magt1) family.
DR   PaxDb; Q7ZV50; -.
DR   Ensembl; ENSDART00000080864; ENSDARP00000075309; ENSDARG00000058062.
DR   GeneID; 324944; -.
DR   KEGG; dre:324944; -.
DR   CTD; 84061; -.
DR   ZFIN; ZDB-GENE-030131-3667; magt1.
DR   eggNOG; KOG2603; Eukaryota.
DR   GeneTree; ENSGT00390000012030; -.
DR   HOGENOM; CLU_052855_0_0_1; -.
DR   InParanoid; Q7ZV50; -.
DR   OMA; IFQQMNL; -.
DR   OrthoDB; 1460433at2759; -.
DR   PhylomeDB; Q7ZV50; -.
DR   TreeFam; TF314850; -.
DR   Reactome; R-DRE-5223345; Miscellaneous transport and binding events.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q7ZV50; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 14.
DR   Bgee; ENSDARG00000058062; Expressed in granulocyte and 27 other tissues.
DR   ExpressionAtlas; Q7ZV50; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015693; P:magnesium ion transport; IGI:ZFIN.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR   InterPro; IPR006844; Mg_transporter-1.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12692; PTHR12692; 1.
DR   PANTHER; PTHR12692:SF2; PTHR12692:SF2; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Magnesium; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..328
FT                   /note="Magnesium transporter protein 1"
FT                   /id="PRO_0000246061"
FT   TOPO_DOM        23..177
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        199..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..293
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..328
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          40..168
FT                   /note="Thioredoxin"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   328 AA;  37422 MW;  A68197BF2D7D6EE6 CRC64;
     MLHKLLIVVF LVVCLHDMRL NGQKKKETLL SEKVSQMMEW VSKRAVVRLN GEKFKRLVRA
     HPRNYSVIVM FTALQPQRQC GVCRQADEEY QILANSWRYS SAFTNRIFFA MVDFDEGSDV
     FQMLNMNSAP TFINFPAKGK PKRADTYELQ VRGFAAEQLA RWVADRTDVH IRVIRPPNYA
     GPLMLGLLLA FIGSLAYLRR NNLEFLFNKN VWAFSALCFV LIMTSGQMWN HIRGPPYAHK
     NPNTGQVSYI HGSSQAQFVA ETHIVLLFNA AVTIGMVLLH EAATSGLDIV KRKIMCVAGI
     GLVVLFFSWL LSVFRAKYHG YPYSFLFG
 
 
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