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Q5P3C5 | MKSASTVVATRILGLDPGLRITGFGVIDKLGNQLRYVASGCIRTRDGELPGRLKTLLDGVREVVAAYTPDQVAVEKVFVNVNPQSTLLLGQARGAVICGAVSCDLPVHEYTALQVKQAVVGYGKAAKEQVQHMVQRLLALDGCPSPDAADALACAICHAHGGQGTAGAFAGRRRAGRILVAPDPG | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 19252
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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C1DRG0 | MTLILGIDPGSRITGFGVVRDGGRGCEYIASGCIRTGSGSLPERLQAVYRGVTEIIRSHGPVTMGIEQVFMARNADSALKLGQARGAAIVAAAEAGLEIAEYTATQVKQAIVGSGGADKRQVQMMVMHLLRLVQKPQIDASDALAIALCHAHHRQSLIPHGLDGARRRGGRLRL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18431
Sequence Length: 174
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q5LAS7 | MIQPVKEKIILGIDPGTTIMGYGVLRVCGTRPEMIAMGIIDLRKFGNHYLKLRHIHERVLSIIESYLPDELAIEAPFFGKNVQSMLKLGRAQGVAMAAALSRDIPITEYAPLKIKMAITGNGQASKEQVADMLQRMLHFAKEDMPVFMDATDGLAAAYCHFLQMGRPVMEKGYSGWKDFIAKNPERVK | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 20995
Sequence Length: 188
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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A9IYK9 | MAETIRIIGIDPGLRYTGWGVIDLAGNRLQFVAAGTVSSDVQCDLASRLCQIHKGLSEVVHQFMPHEAAVEHVFVNKDATATLKLGQARAIALLVPAQANCPVFEYAPNKVKKSVIGVGHGAKEQIHMMVKVLLPRAEFDSNDAADALALALCHSMHRKRIDQSYQARMAI | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18596
Sequence Length: 171
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q6MKB6 | MSLVILGVDPGSRITGFGVVRVANGKIEHINHGVIVMDGDDAFPRRMTELGSAFREVMEKYKPEQVVIEKIFLGKNADSAFKLGHARGVIMYEAGLGGAEVQEYATRSVKKGVTGNGGASKEDVQAILKVMLSLKTISRIDASDALAMACYHAFEMKKKALMQRAVSL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18158
Sequence Length: 168
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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B8DUE9 | MIVLGVDPGLTRCGVGVIEAGAYRRLSFIHVDVVRSDPHESQDLRLLKIYDGLCAKMDEFIPDTVSIERVFAQENRNTVLGTAQAAGMAMLAAAQRGIPVALHTPTESKMAITGNGKAEKIQMERMVARILNLNALPTPADAADALAIAICHALRPSGALEGGEREQHLTPAQRQWAQATQHATRRRGVRRGM | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 20896
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q2KVY8 | MRILGIDPGLRRTGFGVVDAEGSRLRYIASGTIVVPPDLALAQRLKVILDNLREVARETRPDVAALEIVFLNANPSSTLLLGHARGAALCALAESGLDVHEYTALQIKKSTVGTGRAAKEQVQMMVQHLLSLNGTPAPDSADALACAICHAHTGPLQERLSPLAATSRSGKSRIRKGRLLG | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 19173
Sequence Length: 181
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q5HCG1 | MNIIGIDPSLNSTGWAILSVHDNNYNEIRLVDNGSILTSNKKTIGERLNKIYSELLNILNSYKVDTASMEEIFINKNPKSSTLLCYARGVLLLTLNVACIPLFEYSANRVKKSITGNGHAKKEQVCFMIENILNIKCHGTYDISDAIAVAICHIYSIKAF | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17814
Sequence Length: 160
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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B1H0B2 | MIILGIDPGLSLTGWGVVEAFSRDKVNPLQYGCIKTMPSVPLIQRLQTINTKLQSVIDKYKPEVASIEELFFFKATKSIAAVGQTRGAIILTASLNKIPLFEYNPKSVKTALTGYGSADKYQMQRIVKTFLRLKEIPKPDDAADALAIAVCHVNTINWNANNNNNASVFLKNKVFKESAKPNLLKKLFSL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 21029
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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B0S1J5 | MRVLGIDPGIAIVGYSILDYDNNKIKCLEYGCITTSSKSALPDRLSFIYQEMNKIIDEFQPDDCAFEELFFNKNVKTAITVSQARGVEILSCINKDLRLYEYTPLQIKQAVVGYGRADKRQVQETVKTILKFNEIPKPDDAADAVAVALCHIFGSKFKYLNEMK | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18557
Sequence Length: 164
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q2JD96 | MRVLGVDPGLTRCGLGVVDGGLGIRAHLVEVGVVRTPATAEVAERLCAVSDGIDAWLDRTRPEAVAVEKVFSQANMRTVMGTAQAGAVAIVLAARRGLPVGLYTPSEVKAAVTGSGRADKAQVSFMITRLLGLTEAPRPADAADALALALCHLWRGPALARFRSAAPGGPTR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17761
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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B8H9D8 | MTLRVLGVDPGLTRCGIGVVDVERNRRATMVAVGVVGTSPDESLDQRLLVIATAIDEWLDRYEPQVLAVERVFSQLNVSTVMGVAQASGVVIAAAARRGIPVALHTPSEVKAAVTGSGSSNKDAVTKLVTKILRLDAPPRPADAADALALAITHAWRAGSGASVATTGPGSSSLTPAQRAWAEAEAKARRAR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 19910
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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A8F3S6 | MIIFGVDPGFGILGYGVLSVSGNSFQHVSHGTIQTEKQQNIALRLKVLYEELSNVIDNFKPSEIAMEKLFFSRNITTAISVGEARGIVLLLAAQRNIPVFEYTPHEIKKAVTGSGKASKKDVQQMIKILLNLKELPKPDDAADGLAIAWCHCAVRNITRRFS | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 17868
Sequence Length: 162
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q88NJ2 | MTLILGIDPGSRITGYGVVRQTARGCEYVASGCIRTGSGELHERLQIVFRGVSEIIAQHGPVTMGIERVFMARNADSALKLGQARGAAIVAAAEAGLEIAEYSATQVKQAVAGTGGANKEQVMMMVMHLLKLTQKPQIDASDALAIALCHAHTRSSLVPHGLTTARRRGGRLRL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 18428
Sequence Length: 174
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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Q4FTV0 | MAIIIGIDPGSRMTGYGILQQTGDKLTYIDSGTIRTDTKEMPERLKRIFNGLTRITQHHLKYADEPIYTAIEQVFMAENPDSALKLGQARGAAIAAMVALDLEVSEYTARQIKQAVCGYGAAAKEQVQDMVCRILTLDFVPQQDAADGLACAICHAHSSHSMNKLILNSAMRGRGASKKKGRWRLTEEDLGNLR | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 21324
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 3.1.21.10
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P79105 | MTKLEDHLEGIINIFHQYSVRVGHFDTLNKRELKQLITKELPKTLQNTKDQPTIDKIFQDLDADKDGAVSFEEFVVLVSRVLKTAHIDIHKE | Function: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10685
Sequence Length: 92
Domain: The hinge domain contributes significantly to its chemotactic properties.
Subcellular Location: Secreted
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P80511 | MTKLEEHLEGIVNIFHQYSVRKGHFDTLSKGELKQLLTKELANTIKNIKDKAVIDEIFQGLDANQDEQVDFQEFISLVAIALKAAHYHTHKE | Function: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites. Possesses filariacidal and filariastatic activity. Calcitermin possesses antifungal activity against C.albicans and is also active against E.coli and P.aeruginosa but not L.monocytogenes and S.aureus.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10575
Sequence Length: 92
Domain: The hinge domain contributes significantly to its chemotactic properties.
Subcellular Location: Secreted
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O77791 | MTKLEDHLEGIINIFHQYSVRTGHYDTLSKCELKKLITTELVNTIKNTKDQATVDRIFRDLDEDGDHQVDFKEFLSLLASVLVTAHENIHKE | Function: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10668
Sequence Length: 92
Domain: The hinge domain contributes significantly to its chemotactic properties.
Subcellular Location: Secreted
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Q0VCM0 | MADSYTELEKAVVVLVENFYKYVSKHSLVKNKISKSSFRKMLQKELNHMLTDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITSPIANLIRQQEQQSSS | Function: Calcium-binding protein. Binds one calcium ion per monomer (By similarity). Can promote differentiation of adipocytes (in vitro) (By similarity). Overexpression in preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake (By similarity).
Sequence Mass (Da): 11776
Sequence Length: 103
Domain: S100A16 proteins, but not other S100 proteins, have only one functional Ca(2+) binding site per monomer. Upon Ca(2+) binding, undergoes conformational changes leading to the exposure of hydrophobic patches which could be implicated in the Ca(2+)-dependent nuclear export. Binds Zn(2+). Ca(2+) and Zn(2+) do not bind to the same site. Does not bind Cu(2+).
Subcellular Location: Nucleus
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Q96FQ6 | MSDCYTELEKAVIVLVENFYKYVSKYSLVKNKISKSSFREMLQKELNHMLSDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITGPIAKLIHEQEQQSSS | Function: Calcium-binding protein. Binds one calcium ion per monomer . Can promote differentiation of adipocytes (in vitro) (By similarity). Overexpression in preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake (By similarity).
Sequence Mass (Da): 11801
Sequence Length: 103
Domain: S100A16 proteins, but not other S100 proteins, have only one functional Ca(2+) binding site per monomer. Upon Ca(2+) binding, undergoes conformational changes leading to the exposure of hydrophobic patches which could be implicated in the Ca(2+) -dependent nuclear export. Binds Zn(2+). Ca(2+) and Zn(2+) do not bind to the same site. Does not bind Cu(2+).
Subcellular Location: Nucleus
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Q975F9 | MKAFILAAGSGERLEPITHTRPKAFVPILSKPLIEYQIEYLRKCGIRDITVIVSSKNKEYFEKKLKEISIVTQKDDIKGTGAAILSAKFNDEALIIYGDLFFSNEKEICNIITLKENAIIGVKVSNPKDYGVLVLDNQNNLSKIIEKPEIPPSNLINAGIYKLNSDIFTYLDKISISERGELELTDAINLMAKDHRVKVIEYEGYWMDIGKPWNIIDVNKWALDNLVFSQNLGNVEDNVKIKGKVIIEEDAEIKSGTYIEGPVYIGKGSEIGPNSYLRPYTILVEKNKIGASVEVKESVIMEGSKIPHLSYVGDSVIAEDVNFGAGTLIANLRFDEKEVKVNVKGKRISSGRRKLGAFIGGHVRTGINVTILPGVKIGAYARIYPGAVVNRDVGYGEFFKV | Cofactor: Can also use Mg(2+) and Zn(2+), with lower efficiency. Important for nucleotidylyltransferase activity.
Function: Bifunctional enzyme involved in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc). It has multiple amino-sugar-1-phosphate acetyltransferase activities, including glucosamine-1-phosphate (GlcN-1-P) acetyltransferase and galactosamine-1-phosphate (GalN-1-P) acetyltransferase activities, and multiple sugar-1-phosphate nucleotidylyltransferase activities, including N-acetylglucosamine-1-phosphate (GlcNAc-1-P) uridyltransferase and N-acetylgalactosamine-1-phosphate (GalNAc-1-P) uridyltransferase activities . Also catalyzes the formation of dTDP-glucose from dTTP and glucose-1-phosphate (Glc-1-P), and the reverse reaction, which produces dTTP from dTDP-glucose and diphosphate . Can also catalyze the formation of UDP-glucose from UTP and glucose-1-phosphate .
Catalytic Activity: alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate + dTDP-alpha-D-glucose
Sequence Mass (Da): 44516
Sequence Length: 401
Domain: The C-terminal domain is essential for the formation of the trimer and the high thermostability of the entire protein. The C-terminal 11 residues are important for GalN-1-P AcTase activity, but they have an inhibitory effect on the GlcN-1-P AcTase activity.
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
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P21453 | MGPTSVPLVKAHRSSVSDYVNYDIIVRHYNYTGKLNISADKENSIKLTSVVFILICCFIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNNFRLFLLISACWVISLILGGLPIMGWNCISALSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNISKASRSSEKSLALLKTVIIVLSVFIACWAPLFILLLLDVGCKVKTCDILFRAEYFLVLAVLNSGTNPIIYTLTNKEMRRAFIRIMSCCKCPSGDSAGKFKRPIIAGMEFSRSKSDNSSHPQKDEGDNPETIMSSGNVNSSS | Function: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis (By similarity). Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.
PTM: S1P-induced endothelial cell migration requires the PKB/AKT1-mediated phosphorylation of the third intracellular loop at the Thr-236 residue.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42811
Sequence Length: 382
Subcellular Location: Cell membrane
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P48303 | MVSSTSIPVVKALRSQVSDYGNYDIIVRHYNYTGKLNIGVEKDHGIKLTSVVFILICCLIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNSSRSFLLISACWVISLILGGLPIMGWNCISSLSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNISKASRSSEKSLALLKTVIIVLSVFIACWAPLFILLLLDVGCKAKTCDILYKAEYFLVLAVLNSGTNPIIYTLTNKEMRRAFIRIISCCKCPNGDSAGKFKRPIIPGMEFSRSKSDNSSHPQKDDGDNPETIMSSGNVNSSS | Function: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury (By similarity).
PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for targeting to plasma membrane, enabling G(i) coupling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42746
Sequence Length: 383
Subcellular Location: Cell membrane
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Q9I8K8 | MTTCRLFAGFCQAVTMSKYSQYFNKTLIQVHYLTAKEMTAEELRDRIESKQSLSSLNILFVVICSIIILENLLVLIAVFRNKKFHSAMFFFIGNLAFSDLLAGSAYIANIFLSGPRTFHLTPVQWFIREGTAFIALSASVFSLLAIAIERYIAITKVKVYGSNKTCRMFLLIGACWVMSILLGGLPIIGWNCINNLDDCSAVLPLNTRYYIRFVVTIFSIILLSIVILYVRIYLIVRTSHQEATNSPAYALLKTVTIVLGVFIICWLPAFTILLLDTSCKMKQCPILNNAGIFFSFATLNSALNPLIYTLRSKDMRKEFLRVLCCWGLLNCGRPPHRCMVPLKSSSSMEHCTNKHEHQSIPIMQDCTTCV | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P) . S1P receptor is critical for cell migration and epithelial integrity during vertebrate embryogenesis . Receptor for the chemokine-like protein FAM19A5 (By similarity). Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41777
Sequence Length: 370
Subcellular Location: Cell membrane
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O95136 | MGSLYSEYLNPNKVQEHYNYTKETLETQETTSRQVASAFIVILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGSVTLRLTPVQWFAREGSAFITLSASVFSLLAIAIERHVAIAKVKLYGSDKSCRMLLLIGASWLISLVLGGLPILGWNCLGHLEACSTVLPLYAKHYVLCVVTIFSIILLAIVALYVRIYCVVRSSHADMAAPQTLALLKTVTIVLGVFIVCWLPAFSILLLDYACPVHSCPILYKAHYFFAVSTLNSLLNPVIYTWRSRDLRREVLRPLQCWRPGVGVQGRRRGGTPGHHLLPLRSSSSLERGMHMPTSPTFLEGNTVV | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P) . S1P is a bioactive lysophospholipid that elicits diverse physiological effects on most types of cells and tissues . When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis . Receptor for the chemokine-like protein FAM19A5 . Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38867
Sequence Length: 353
Subcellular Location: Cell membrane
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P52592 | MGGLYSEYLNPEKVLEHYNYTKETLDMQETTSRKVASAFIIILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGHVTLSLTPVQWFAREGSAFITLSASVFSLLAIAIERQVALAKVKLYGSDKSCRMLMLIGASWLISLILGGLPILGWNCLNQLEACSTVLPLYAKHYVLCVVTIFSVILLAIVALYVRIYFVVRSSHADVAGPQTLALLKTVTIVLGVFIICWLPAFSILLLDSTCPVRACPVLYKAHYFFAFATLNSLLNPVIYTWRSRDLRREVLRPLQCWRRGKGVTGRRGGNPGHRLLPLRSSSSLERGMHMPTSPTFLEGNTVV | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P) (By similarity). S1P is a bioactive lysophospholipid that elicits diverse physiological effects on most types of cells and tissues (By similarity). Receptor for the chemokine-like protein FAM19A5 (By similarity). Mediates the inhibitory effect of FAM19A5 on vascular smooth muscle cell proliferation and migration (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38829
Sequence Length: 352
Subcellular Location: Cell membrane
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Q99500 | MATALPPRLQPVRGNETLREHYQYVGKLAGRLKEASEGSTLTTVLFLVICSFIVLENLMVLIAIWKNNKFHNRMYFFIGNLALCDLLAGIAYKVNILMSGKKTFSLSPTVWFLREGSMFVALGASTCSLLAIAIERHLTMIKMRPYDANKRHRVFLLIGMCWLIAFTLGALPILGWNCLHNLPDCSTILPLYSKKYIAFCISIFTAILVTIVILYARIYFLVKSSSRKVANHNNSERSMALLRTVVIVVSVFIACWSPLFILFLIDVACRVQACPILFKAQWFIVLAVLNSAMNPVIYTLASKEMRRAFFRLVCNCLVRGRGARASPIQPALDPSRSKSSSSNNSSHSPKVKEDLPHTAPSSCIMDKNAALQNGIFCN | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42250
Sequence Length: 378
Subcellular Location: Cell membrane
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O95977 | MNATGTPVAPESCQQLAAGGHSRLIVLHYNHSGRLAGRGGPEDGGLGALRGLSVAASCLVVLENLLVLAAITSHMRSRRWVYYCLVNITLSDLLTGAAYLANVLLSGARTFRLAPAQWFLREGLLFTALAASTFSLLFTAGERFATMVRPVAESGATKTSRVYGFIGLCWLLAALLGMLPLLGWNCLCAFDRCSSLLPLYSKRYILFCLVIFAGVLATIMGLYGAIFRLVQASGQKAPRPAARRKARRLLKTVLMILLAFLVCWGPLFGLLLADVFGSNLWAQEYLRGMDWILALAVLNSAVNPIIYSFRSREVCRAVLSFLCCGCLRLGMRGPGDCLARAVEAHSGASTTDSSLRPRDSFRGSRSLSFRMREPLSSISSVRSI | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. May be involved in cell migration processes that are specific for lymphocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41623
Sequence Length: 384
Subcellular Location: Cell membrane
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Q9H228 | MESGLLRPAPVSEVIVLHYNYTGKLRGARYQPGAGLRADAVVCLAVCAFIVLENLAVLLVLGRHPRFHAPMFLLLGSLTLSDLLAGAAYAANILLSGPLTLKLSPALWFAREGGVFVALTASVLSLLAIALERSLTMARRGPAPVSSRGRTLAMAAAAWGVSLLLGLLPALGWNCLGRLDACSTVLPLYAKAYVLFCVLAFVGILAAICALYARIYCQVRANARRLPARPGTAGTTSTRARRKPRSLALLRTLSVVLLAFVACWGPLFLLLLLDVACPARTCPVLLQADPFLGLAMANSLLNPIIYTLTNRDLRHALLRLVCCGRHSCGRDPSGSQQSASAAEASGGLRRCLPPGLDGSFSGSERSSPQRDGLDTSGSTGSPGAPTAARTLVSEPAAD | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/0)alpha and G(12) subclass of heteromeric G-proteins (By similarity). May play a regulatory role in the transformation of radial glial cells into astrocytes and may affect proliferative activity of these cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41775
Sequence Length: 398
Subcellular Location: Cell membrane
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Q91X56 | MEPGLLRPAPVSEVIVLHYNYTGKLRGARYQPGAGLRADAAVCLAVCAFIVLENLAVLLVLVRHPRFHAPMFLLLGSLTLSDLLAGAAYATNILLSGPLTLRLSPALWFAREGGVFVALAASVLSLLAIALERHLTMARRGPAPAASRARTLAMAVAAWGASLLLGLLPALGWNCLGRLETCSTVLPLYAKAYVLFCVLAFLGILAAICALYARIYCQVRANARRLRAGPGSRRATSSSRSRHTPRSLALLRTLSVVLLAFVACWGPLFLLLLLDVACPARACPVLLQADPFLGLAMANSLLNPIIYTFTNRDLRHALLRLLCCGRGPCNQDSSNSLQRSPSAAGPSGGGLRRCLPPTLDRSSSPSEHLSPQQDGVDTSCSTGSPGVATANRSLVPTATD | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/0)alpha and G(12) subclass of heteromeric G-proteins (By similarity). S1P activation on oligodendroglial cells modulates two distinct functional pathways mediating either process retraction or cell survival. S1P activation on O4-positive pre-oligodendrocytes induces process retraction via a Rho kinase/collapsin response-mediated protein signaling pathway. The S1P-induced survival of mature oligodendrocytes is mediated through a pertussis toxin-sensitive, Akt-dependent pathway. S1P activation on oligodendroglial cells modulates two distinct functional pathways mediating either process retraction or cell survival. These effects depend on the developmental stage of the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42331
Sequence Length: 400
Subcellular Location: Cell membrane
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Q684M3 | MEPGLLRPAPVSEVIVLHYNYTGKLRGARYQPGAGLRADAVVCLAVCALIVLENLAVLVVLGRHPRFHAPMFLLLGSLTLSDLLAGAAYAANILLSGPLTLRLSPALWFAREGGVFVALAASVLSLLAIALERLLTMERRGPAPAARRGRTLALAAGAWGVSLLLGLLPALGWNCLGRLEACSTVLPLYAKAYVLFCVLAFVGILAAICGLYARIYCQVRAKAQRLRARPGAGEGTSARARGTPRSLALLRTLSVVLVAFVACWGPLFLLLLLDVACPARACPVLLQADPFLGLAMANSLLNPIIYTFTNRDLRHALLRLICCGRRPCWGGSGTSRSPGSTLGASGGLHRWLPPGMDRSSSRSERSSPQRDGLDTSGSTGSPAAPTAAQTLVPPPAAD | Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/O)alpha and G(12) subclass of heteromeric G-proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41861
Sequence Length: 398
Subcellular Location: Cell membrane
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Q9BZJ4 | MADQDPAGISPLQQMVASGTGAVVTSLFMTPLDVVKVRLQSQRPSMASELMPSSRLWSLSYTKLPSSLQSTGKCLLYCNGVLEPLYLCPNGARCATWFQDPTRFTGTMDAFVKIVRHEGTRTLWSGLPATLVMTVPATAIYFTAYDQLKAFLCGRALTSDLYAPMVAGALARLGTVTVISPLELMRTKLQAQHVSYRELGACVRTAVAQGGWRSLWLGWGPTALRDVPFSALYWFNYELVKSWLNGFRPKDQTSVGMSFVAGGISGTVAAVLTLPFDVVKTQRQVALGAMEAVRVNPLHVDSTWLLLRRIRAESGTKGLFAGFLPRIIKAAPSCAIMISTYEFGKSFFQRLNQDRLLGG | Function: Mitochondrial transporter required for glutathione import into mitochondria . Glutathione, which plays key roles in oxidative metabolism, is produced exclusively in the cytosol and is imported in many organelles . Mitochondrial glutathione is required for the activity and stability of proteins containing iron-sulfur clusters, as well as erythropoiesis .
Catalytic Activity: glutathione(in) = glutathione(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39249
Sequence Length: 359
Subcellular Location: Mitochondrion inner membrane
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Q6DHC3 | MSCQESSPGPPGDITPFQQMMASCSGAIITSLLVTPLDVVKIRLQAQKNPFPKGKCFVYCNGLMDHICVCENGNTKVWYKAPGHFSGTLDAFLKIIRMEGIRSLWSGLPPTLIMAVPATVIYFTCYDQLFALLKLKMGDRSDLAPLFAGAIARVGSATVISPLELIRTKMQSEKQSYREMSAVIRSALKNEGLRSLWRGWGPTLLRDVPFSAMYWFNYEKGKWWLCKRYSCSEPTVAITFTAGALSGSIASIITLPFDVVKTKRQVEMGELQTMKLSTQVSSSTCSVMKRIVAENGVSGLFAGFMPRLIKVAPACAIMISTYEFGKAFFRKYNHQKEGQATASQHIISHTEKH | Function: Probable mitochondrial transporter required for glutathione import into mitochondria. Glutathione, which plays key roles in oxidative metabolism, is produced exclusively in the cytosol and is imported in many organelles (By similarity). Mitochondrial glutathione is required for the activity and stability of proteins containing iron-sulfur clusters (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39100
Sequence Length: 353
Subcellular Location: Mitochondrion inner membrane
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Q552L9 | MLSNSVNNNNNNNNINNSNSNNNDSNIHKNVKKLMVASIFGGIMSSLIVTPLDVVKTRLQTQNTGSHINQKHVFKGTLDAFKKIYKNEGPLTFWRGVTPSLLMTIPSATIYFTSYEYLKEYLYQFNDTEAYNIYTVPLVAGTLARIFSASVTSPFELLRTNSQGIVLQNAYKNTVAMAASSSTATIGTIPLSSEQRFNSFKLYRDIVNNVGIKGLWRGLGPTLVRDVPFSAIYWAGYEVLKNKLMKSQIDPNFSRNSKSPFFINFIAGATSGTLAAVLTTPIDVIKTRIQMSAQQTLSPSLTPQQQLDFIKKNNSSIYHLKQILSQEGWKGLTKGLVPRVAKVSPACAIMISTFEYIKQSHIADDN | Function: Mitochondrial transporter required for glutathione import into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40633
Sequence Length: 366
Subcellular Location: Mitochondrion inner membrane
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Q8TBP6 | MDPETRGQEIIKVTPLQQMLASCTGAILTSVIVTPLDVVKIRLQAQNNPLPKGKCFVYSNGLMDHLCVCEEGGNKLWYKKPGNFQGTLDAFFKIIRNEGIKSLWSGLPPTLVMAVPATVIYFTCYDQLSALLRSKLGENETCIPIVAGIVARFGAVTVISPLELIRTKMQSKKFSYVELHRFVSKKVSEDGWISLWRGWAPTVLRDVPFSAMYWYNYEILKKWLCEKSGLYEPTFMINFTSGALSGSFAAVATLPFDVVKTQKQTQLWTYESHKISMPLHMSTWIIMKNIVAKNGFSGLFSGLIPRLIKIAPACAIMISTYEFGKAFFQKQNVRRQQY | Function: Probable mitochondrial transporter required for glutathione import into mitochondria . Glutathione, which plays key roles in oxidative metabolism, is produced exclusively in the cytosol and is imported in many organelles . Mitochondrial glutathione is required for the activity and stability of proteins containing iron-sulfur clusters, as well as erythropoiesis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38125
Sequence Length: 338
Subcellular Location: Mitochondrion inner membrane
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Q8BGP6 | MEPETEGPPPTIPVTPLQQMIASCTGAVLTSLMVTPLDVVKIRLQAQNNPFPKGKCFLYSNGLMDHMCVCEEESKKAWYKKPGNFRGTLDAFLKILRNEGIKSLWSGLPPTLVMAIPATVIYFTCYEQLSAFLKTKLGENETRIPIVAGVVARFGAVTVISPLELIRTKVQSKKFSYKELYQFVSMRVSEDGWISLWKGWAPTILRDVPFSAMYWYNYENLKRWLCEKSGLYEPTFMINFTSGALSGSFAAVATLPFDVVKTQKQTQLWTNEYCKFPAPLDMSTWTIMKNIVADKGFSGLFTGLIPRLVKIVPACAIMISSYELGKSFFQKQNVESR | Function: Probable mitochondrial transporter required for glutathione import into mitochondria. Glutathione, which plays key roles in oxidative metabolism, is produced exclusively in the cytosol and is imported in many organelles (By similarity). Mitochondrial glutathione is required for the activity and stability of proteins containing iron-sulfur clusters, as well as erythropoiesis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37964
Sequence Length: 337
Subcellular Location: Mitochondrion inner membrane
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Q6P316 | MQKNTEPVQEAINITPSQQMIASSMGALLTSFFVTPLDVVKIRLQAQSKPFIKGKCFVYCNGLMDHLCLCTNGNGKAWYRAPGHFRGTTDAFVQIIRNEGIKSLWSGLPPTLVMAVPATVIYFTCYDQLRDILIRSMPERAEIASLVAGATARLWSATLISPLELIRTKMQYRPLSYKELRQCIQSSVAKDGWLALWKGWGPTVLRDVPFSALYWHNYELVKQSLCQRYNTLQPTFAISFTAGAVSGSIAAIVTLPFDVVKTRRQVEVGELEMFTYSQKRSSSTWKLMRAIVIENGFGGLFAGLIPRLIKVAPACAIMISTYEFGKSFFRKLNNERQLKSL | Function: Probable mitochondrial transporter required for glutathione import into mitochondria. Glutathione, which plays key roles in oxidative metabolism, is produced exclusively in the cytosol and is imported in many organelles (By similarity). Mitochondrial glutathione is required for the activity and stability of proteins containing iron-sulfur clusters (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38259
Sequence Length: 341
Subcellular Location: Mitochondrion inner membrane
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Q0II44 | MGAQPEQTQKPSSRVQTLFKRVKAFFTKTGPPPPPPAPSRNLGCTHVYGYVFGHLGEREPEHSPSQQVLDTGEQLMVPVDVLEVDNEGALWKFLLSGAMAGAVSRTGTAPLDRAKVYMQVYSSKKNFMNLLGGLRSLIQEGGIRSLWRGNGINVLKIAPEYAIKFSVFEQCKNYFCGVHESPPFQERLLAGSLAVATSQTLINPMEVLKTRLTLRRTGQYKGLLDCARQILEQEGTRALYRGYLPNMLGIIPYACTDLAVYEMLNCLWLKSGRDMKDPSGLVSLSSVTLSTTCGQMASYPLTLVRTRMQAQGQLGPFSNLAYHDPLPLLSELSHDPPKHTQTDSQTLHI | Function: Calcium-independent ATP-Mg/Pi exchanger that catalyzes the electroneutral exchange of Mg-ATP or free ADP against an hydrogenphosphate and participates in the net transport of adenine nucleotides across the mitochondria inner membrane.
Catalytic Activity: ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38571
Sequence Length: 349
Subcellular Location: Mitochondrion inner membrane
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Q8N5S1 | MGAQPGEPQNTCSRIQTLFRRVKTLLIKAPPPPQPPPPPPSWNPGCTHVYGYAFGHMHDNNLEHLPSQQVLDTGEQLMVPVEVLEVDNKEALWKFLLSGAMAGAVSRTGTAPLDRAKVYMQVYSSKTNFTNLLGGLQSMVQEGGFRSLWRGNGINVLKIAPEYAIKFSVFEQCKNYFCGIQGSPPFQERLLAGSLAVAISQTLINPMEVLKTRLTLRRTGQYKGLLDCARQILQREGTRALYRGYLPNMLGIIPYACTDLAVYEMLQCFWVKSGRDMGDPSGLVSLSSVTLSTTCGQMASYPLTLVRTRMQAQDTVEGSNPTMRGVLQRILAQQGWLGLYRGMTPTLLKVLPAGGISYVVYEAMKKTLGI | Function: Calcium-independent ATP-Mg/Pi exchanger that catalyzes the electroneutral exchange of Mg-ATP or free ADP against an hydrogenphosphate and participates in the net transport of adenine nucleotides across the mitochondria inner membrane.
Catalytic Activity: ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40795
Sequence Length: 370
Subcellular Location: Mitochondrion inner membrane
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Q8BVN7 | MGVHLEVLDTGEQLMVPVDVLEEENKGTLWKFLLSGAMAGAVSRTGTAPLDRARVYMQVYSSKSNFRNLLSGLRSLVQEGGVRSLWRGNGINVLKIAPEYAIKFSVCEQSKNFFYGVHSSQLFQERVVAGSLAVAVSQTLINPMEVLKTRLTLRFTGQYKGLLDCARQILERDGTRALYRGYLPNMLGIIPYACTDLAVYELLQCLWQKLGRDMKDPSGLVSLSSVTLSTTCGQMASYPLTLVRTRMQAQDTVEGSNPTMQGVFKRILSQQGWPGLYRGMTPTLLKVLPAGGISYLVYEAMKKTLGVQVLSR | Function: Calcium-independent ATP-Mg/Pi exchanger that catalyzes the electroneutral exchange of Mg-ATP or free ADP against an hydrogenphosphate and participates in the net transport of adenine nucleotides across the mitochondria inner membrane.
Catalytic Activity: ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34505
Sequence Length: 312
Subcellular Location: Mitochondrion inner membrane
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Q0P483 | MGNVVQERQGALAQGEVLPRPAASQSEGFKQGRSVLNSLVSGAFAGAVAKTAVAPLDRTKIIFQVSSNRFSAKEAYRLIYRTYLKDGFFSLWRGNSATMVRVIPYAAIQFCAHEQYKGILGKYYGFQGKALPPVPRLLAGSLAGTTAAIITYPLDMVRARMAVTPKEMYSNIMDVFVRISREEGLKTLYRGFTPTILGVVPYAGLSFFTYETLKKTHAEKTGRAHPFPYERLVFGACAGLIGQSASYPLDVVRRRMQTAGVTGHTYSTVLGTMREIVAEEGIVRGLYKGLSMNWVKGPIAVGISFMTFDLTQILLRKFQLL | Function: Mitochondrial carrier mediating the transport of coenzyme A (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine nucleotides and adenosine 3',5'-diphosphate.
Catalytic Activity: ADP(out) + CoA(in) = ADP(in) + CoA(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35336
Sequence Length: 321
Subcellular Location: Mitochondrion inner membrane
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Q86VD7 | MGNGVKEGPVRLHEDAEAVLSSSVSSKRDHRQVLSSLLSGALAGALAKTAVAPLDRTKIIFQVSSKRFSAKEAFRVLYYTYLNEGFLSLWRGNSATMVRVVPYAAIQFSAHEEYKRILGSYYGFRGEALPPWPRLFAGALAGTTAASLTYPLDLVRARMAVTPKEMYSNIFHVFIRISREEGLKTLYHGFMPTVLGVIPYAGLSFFTYETLKSLHREYSGRRQPYPFERMIFGACAGLIGQSASYPLDVVRRRMQTAGVTGYPRASIARTLRTIVREEGAVRGLYKGLSMNWVKGPIAVGISFTTFDLMQILLRHLQS | Function: Mitochondrial carrier mediating the transport of coenzyme A (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine nucleotides and adenosine 3',5'-diphosphate.
Catalytic Activity: ADP(out) + CoA(in) = ADP(in) + CoA(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35409
Sequence Length: 318
Subcellular Location: Mitochondrion inner membrane
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P0CK96 | MSSSVKTPALEELVPGSEEKPKGRSPLSWGSLFGHRSEKIVFAKSDGGTDENVLTVTITETTVIESDLGVWSSRALLYLTLWFFFSFCTLFLNKYILSLLGGEPSMLGAVQMLSTTVIGCVKTLVPCCLYQHKARLSYPPNFLMTMLFVGLMRFATVVLGLVSLKNVAVSFAETVKSSAPIFTVIMSRMILGEYTGLLVNLSLIPVMGGLALCTATEISFNVLGFSAALSTNIMDCLQNVFSKKLLSGDKYRFSAPELQFYTSAAAVAMLVPARVFFTDVPVIGRSGKSFSYNQDVVLLLLTDGVLFHLQSVTAYALMGKISPVTFSVASTVKHALSIWLSVIVFGNKITSLSAVGTALVTVGVLLYNKARQHQQEALQSLAAATGRAPDDTVEPLLPQDPRQHP | Function: Putative transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43777
Sequence Length: 405
Subcellular Location: Membrane
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P78382 | MAAPRDNVTLLFKLYCLAVMTLMAAVYTIALRYTRTSDKELYFSTTAVCITEVIKLLLSVGILAKETGSLGRFKASLRENVLGSPKELLKLSVPSLVYAVQNNMAFLALSNLDAAVYQVTYQLKIPCTALCTVLMLNRTLSKLQWVSVFMLCAGVTLVQWKPAQATKVVVEQNPLLGFGAIAIAVLCSGFAGVYFEKVLKSSDTSLWVRNIQMYLSGIIVTLAGVYLSDGAEIKEKGFFYGYTYYVWFVIFLASVGGLYTSVVVKYTDNIMKGFSAAAAIVLSTIASVMLFGLQITLTFALGTLLVCVSIYLYGLPRQDTTSIQQGETASKERVIGV | Function: Transports CMP-sialic acid from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges CMP-sialic acid for CMP . Binds both CMP-sialic acid and free CMP, but has higher affinity for free CMP (By similarity). Also able to exchange CMP-sialic acid for AMP and UMP . Also mediates the transport of CDP-ribitol (By similarity).
Catalytic Activity: CMP(out) + CMP-N-acetyl-beta-neuraminate(in) = CMP(in) + CMP-N-acetyl-beta-neuraminate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36779
Sequence Length: 337
Subcellular Location: Golgi apparatus membrane
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Q61420 | MAPARENVSLFFKLYCLTVMTLVAAAYTVALRYTRTTAEELYFSTTAVCITEVIKLLISVGLLAKETGSLGRFKASLSENVLGSPKELAKLSVPSLVYAVQNNMAFLALSNLDAAVYQVTYQLKIPCTALCTVLMLNRTLSKLQWISVFMLCGGVTLVQWKPAQATKVVVAQNPLLGFGAIAIAVLCSGFAGVYFEKVLKSSDTSLWVRNIQMYLSGIVVTLAGTYLSDGAEIQEKGFFYGYTYYVWFVIFLASVGGLYTSVVVKYTDNIMKGFSAAAAIVLSTIASVLLFGLQITLSFALGALLVCVSIYLYGLPRQDTTSIQQEATSKERIIGV | Function: Transports CMP-sialic acid from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges CMP-sialic acid for CMP . Binds both CMP-sialic acid and free CMP, but has higher affinity for free CMP . Also able to exchange CMP-sialic acid for AMP and UMP (By similarity). Also mediates the transport of CDP-ribitol (By similarity).
Catalytic Activity: CMP(out) + CMP-N-acetyl-beta-neuraminate(in) = CMP(in) + CMP-N-acetyl-beta-neuraminate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36453
Sequence Length: 336
Subcellular Location: Golgi apparatus membrane
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P78381 | MAAVGAGGSTAAPGPGAVSAGALEPGTASAAHRRLKYISLAVLVVQNASLILSIRYARTLPGDRFFATTAVVMAEVLKGLTCLLLLFAQKRGNVKHLVLFLHEAVLVQYVDTLKLAVPSLIYTLQNNLQYVAISNLPAATFQVTYQLKILTTALFSVLMLNRSLSRLQWASLLLLFTGVAIVQAQQAGGGGPRPLDQNPGAGLAAVVASCLSSGFAGVYFEKILKGSSGSVWLRNLQLGLFGTALGLVGLWWAEGTAVATRGFFFGYTPAVWGVVLNQAFGGLLVAVVVKYADNILKGFATSLSIVLSTVASIRLFGFHVDPLFALGAGLVIGAVYLYSLPRGAAKAIASASASASGPCVHQQPPGQPPPPQLSSHRGDLITEPFLPKLLTKVKGS | Function: Transports uridine diphosphate galactose (UDP-galactose) from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges UDP-galactose for UMP . It is also able to exchange UDP-galactose for AMP and CMP, and to transport UDP-N-acetylgalactosamine (UDP-GalNAc) and other nucleotide sugars . As a provider of UDP-galactose to galactosyltransferases present in the Golgi apparatus, it is necessary for globotriaosylceramide/globoside (Gb3Cer) synthesis from lactosylceramide .
Catalytic Activity: UDP-alpha-D-galactose(in) + UMP(out) = UDP-alpha-D-galactose(out) + UMP(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41307
Sequence Length: 396
Subcellular Location: Endoplasmic reticulum membrane
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Q9R0M8 | MAAVGVGGSTAAAGAGAVSSGALEPGSTTAAHRRLKYISLAVLVVQNASLILSIRYARTLPGDRFFATTAVVMAEVLKGLTCLLLLFAQKRGNVKHLVLFLHEAVLVQYVDTLKLAVPSLIYTLQNNLQYVAISNLPAATFQVTYQLKILTTALFSVLMLNRSLSRLQWASLLLLFTGVAIVQAQQAGGSGPRPLDQNPGAGLAAVVASCLSSGFAGVYFEKILKGSSGSVWLRNLQLGLFGTALGLVGLWWAEGTAVASQGFFFGYTPAVWGVVLNQAFGGLLVAVVVKYADNILKGFATSLSIVLSTVASIRLFGFHLDPLFALGAGLVIGAVYLYSLPRGAVKAIASASASGPCIHQQPPGQPPPPQLSSRGDLTTEPFLPKSVLVK | Function: Transports uridine diphosphate galactose (UDP-galactose) from the cytosol into the Golgi apparatus . It functions as an antiporter that exchanges UDP-galactose for UMP (By similarity). It is also able to exchange UDP-galactose for AMP and CMP, and to transport UDP-N-acetylgalactosamine (UDP-GalNAc) and other nucleotide sugars (By similarity). As a provider of UDP-galactose to galactosyltransferases present in the Golgi apparatus, it is necessary for globotriaosylceramide/globoside (Gb3Cer) synthesis from lactosylceramide (By similarity).
Catalytic Activity: UDP-alpha-D-galactose(in) + UMP(out) = UDP-alpha-D-galactose(out) + UMP(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40766
Sequence Length: 390
Subcellular Location: Golgi apparatus membrane
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O16658 | MNRANDTSSNLKLISLVVLIVQTTALVLTLRYSQTQKSEGPRYLSSTAVVCAEIIKLITCFFVIYRNNGYRFSGMLNELNREIFASPQTRADSLKVAVPAIMYVIQNNLLFFALKKLDAATYQVTYQLKILTTAIFSVTMLGKSLHRYNWMALILLTAGVALVQYPSGDSTTSKSTAAEHDASDNILGLGAVLAACFSSGFAGVYFEKILKTSKVSLWIRNIQLAFFSVFGALLVCWLYDWQAISDDGFLRGYNGVIWIVVLLQAYGGLVIALVVKYADNILKGFAVSLSIILSSFTSWLVLGDLTITTTFAIGATVVIFATFLYGHEPKSTPAEAHNA | Function: Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) transporter in the Golgi apparatus . UDP-N-acetylgalactosamine (UDP-GalNAc) transporter in the Golgi apparatus . Apparently transports UDP-GlcNAc and UDP-GalNAc simultaneously, and independently, by an unknown mechanism . Functions redundantly with nucleotide sugar transporter srf-3 . May be involved in gonadal development .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37175
Sequence Length: 339
Subcellular Location: Golgi apparatus membrane
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O77592 | MSTNLKYLSLGILVFQTTSLVLTMRYSRTLKEEGPRYLSSTAVVVAELLKIMACILLVYKDSKCSLRALNRILHDEILNKPMETLKLAIPSGIYTLQNNLLYVALSNLDAATYQVTYQLKILTTALFSVSMLSKKLGVYQWLSLVILMTGVAFVQWPSDSQELDSKELSAGSQFVGLMAVLTACFSSGFAGVYFEKILKETKQSVWIRNIQLGFFGSIFGLMGVYIYDGELVSKNGFFQGYNRLTWIVVILQALGGLVIAAVIKYADNILKGFATSLSIILSTLISYFWLQDFVPTSVFFLGAILVITATFLYGYDPKPTGNPTKA | Function: Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) transporter in the Golgi apparatus. May supply UDP-GlcNAc as substrate for Golgi-resident glycosyltransferases that generate branching of diantennary oligosaccharides (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36156
Sequence Length: 326
Subcellular Location: Golgi apparatus membrane
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Q9Y2D2 | MFANLKYVSLGILVFQTTSLVLTMRYSRTLKEEGPRYLSSTAVVVAELLKIMACILLVYKDSKCSLRALNRVLHDEILNKPMETLKLAIPSGIYTLQNNLLYVALSNLDAATYQVTYQLKILTTALFSVSMLSKKLGVYQWLSLVILMTGVAFVQWPSDSQLDSKELSAGSQFVGLMAVLTACFSSGFAGVYFEKILKETKQSVWIRNIQLGFFGSIFGLMGVYIYDGELVSKNGFFQGYNRLTWIVVVLQALGGLVIAAVIKYADNILKGFATSLSIILSTLISYFWLQDFVPTSVFFLGAILVITATFLYGYDPKPAGNPTKA | Function: Transports diphosphate-N-acetylglucosamine (UDP-GlcNAc) from the cytosol into the lumen of the Golgi apparatus, functioning as an antiporter that exchanges UDP-N-acetyl-alpha-D-glucosamine for UMP . May supply UDP-GlcNAc as substrate for Golgi-resident glycosyltransferases that generate highly branched, multiantennary complex N-glycans and keratan sulfate . However, the exact role of SLC35A3 still needs to be elucidated, it could be a member of a catalytically more efficient multiprotein complex rather than function independently as a single transporter .
PTM: O-Glcnacylation regulates the stability of SLC35A3 and the specific complex formation with MGAT4B.
Location Topology: Multi-pass membrane protein
Catalytic Activity: UDP-N-acetyl-alpha-D-glucosamine(in) + UMP(out) = UDP-N-acetyl-alpha-D-glucosamine(out) + UMP(in)
Sequence Mass (Da): 35985
Sequence Length: 325
Subcellular Location: Golgi apparatus membrane
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Q8R1T4 | MSANLKYLSLGILVFQTTSLVLTMRYSRTLKEEGPRYLSSTAVVVAEFLKIMACIFLVYKDSKCSVRALNRVLHDEILNKPMETLKLAIPSGIYTLQNNLLYVALSNLDAATYQVTYQLKILTTALFSVSMLGKKLGVYQWLSLVILMAGVAFVQWPSDSQELNSKDLSTGSQFVGLMAVLTACFSSGFAGVYFEKILKETKQSVWIRNIQLGFFGSIFGLMGVYVYDGELVSKNGFFQGYNQLTWIVVALQALGGLVIAAVIKYADNILKGFATSLSIILSTIISYFWLQDFVPTSVFFLGAILVIAATFLYGYDPKPAGNPTKA | Function: Transports diphosphate-N-acetylglucosamine (UDP-GlcNAc) from the cytosol into the lumen of the Golgi apparatus, functioning as an antiporter that exchanges UDP-N-acetyl-alpha-D-glucosamine for UMP . May supply UDP-GlcNAc as substrate for Golgi-resident glycosyltransferases that generate highly branched, multiantennary complex N-glycans and keratan sulfate (By similarity). However, the exact role of SLC35A3 still needs to be elucidated, it could be a member of a catalytically more efficient multiprotein complex rather than function independently as a single transporter (By similarity).
PTM: O-Glcnacylation regulates the stability of SLC35A3 and the specific complex formation with MGAT4B.
Location Topology: Multi-pass membrane protein
Catalytic Activity: UDP-N-acetyl-alpha-D-glucosamine(in) + UMP(out) = UDP-N-acetyl-alpha-D-glucosamine(out) + UMP(in)
Sequence Mass (Da): 35976
Sequence Length: 326
Subcellular Location: Golgi apparatus membrane
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Q9NP94 | MEQLLGIKLGCLFALLALTLGCGLTPICFKWFQIDAARGHHRLVLRLLGCISAGVFLGAGFMHMTAEALEEIESQIQKFMVQNRSASERNSSGDADSAHMEYPYGELIISLGFFFVFFLESLALQCCPGAAGGSTVQDEEWGGAHIFELHSHGHLPSPSKGPLRALVLLLSLSFHSVFEGLAVGLQPTVAATVQLCLAVLAHKGLVVFGVGMRLVHLGTSSRWAVFSILLLALMSPLGLAVGLAVTGGDSEGGRGLAQAVLEGVAAGTFLYVTFLEILPRELASPEAPLAKWSCVAAGFAFMAFIALWA | Function: Transporter for the divalent cation Zn(2+) . Mediates the influx of Zn(2+) into cells from extracellular space. The Zn(2+) uniporter activity is independent of H(+)-driving force, but is modulated by extracellular pH and membrane potential. Transports also other divalent cations Zn(2+), Cd2(+), Cu2(+), Co2(+) in the order of decreasing affinity, respectively . In the skin, aids in the differentiation of keratinocytes in the epidermis (By similarity).
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32742
Sequence Length: 309
Subcellular Location: Cell membrane
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Q5E960 | MVKLLVAKILCMVGMFFFMLLGSLLPVKIIEMDFEKAHRSKKILSLCNTFGGGVFLATCFNALLPAVREKLKEVLTLAHISTDYPLAETIMLLGFFMTVFLEQLVLTFRKERPAFIDLETFNASSDAGSDSEYESPFMGGPRGHALYAEPHGHSHGLSVQELSRSSPLRLLSLVFALSAHSVFEGLALGLQEEGEKVVSLFVGVAIHETLVAVALGINMARSAMALRDAAKLAVTVSAMIPLGISLGLGIDSAQGMPSSVASVLLQGLAGGTFLFVTFFEILAKELEEKSDRLLKVLFLVLGYTVLAGMVFIKW | Function: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space. Controls Zn(2+) accumulation into dentate gyrus granule cells in the hippocampus. Mediates Zn(2+) reuptake from the secreted milk within the alveolar lumen.
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33991
Sequence Length: 314
Subcellular Location: Cell membrane
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Q9BRY0 | MVKLLVAKILCMVGVFFFMLLGSLLPVKIIETDFEKAHRSKKILSLCNTFGGGVFLATCFNALLPAVREKLQKVLSLGHISTDYPLAETILLLGFFMTVFLEQLILTFRKEKPSFIDLETFNAGSDVGSDSEYESPFMGGARGHALYVEPHGHGPSLSVQGLSRASPVRLLSLAFALSAHSVFEGLALGLQEEGEKVVSLFVGVAVHETLVAVALGISMARSAMPLRDAAKLAVTVSAMIPLGIGLGLGIESAQGVPGSVASVLLQGLAGGTFLFITFLEILAKELEEKSDRLLKVLFLVLGYTVLAGMVFLKW | Function: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space. Controls Zn(2+) accumulation into dentate gyrus granule cells in the hippocampus. Mediates Zn(2+) reuptake from the secreted milk within the alveolar lumen.
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33601
Sequence Length: 314
Subcellular Location: Cell membrane
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Q99K24 | MTKLLVAKVLCMVGVFFFMLLGSLLPVKVIEADLEKAHRSKKVLSLCNTFGGGVFLATCFNALLPAVRDKLQQVLSLGHISTDYPLAETLMMVGFFLTVFVEQLVLTFRRERPPFIDLETFNAGSDAGSDSEYESPFVGVGNRSHSLYPEPTAHTHGAGLRLRELGRPGPLRLLSLVFALSAHSVFEGLALGLQEEGERVVSLFVGVAIHETLVAVALGISMARSAVPLRDAAKLAVTVSAMIPVGIGLGLGIESARSVASSVASALLQGLAGGTFLFVTFLEILAKELEERSEQLLKVLFLVLGYAVLAGMVFLKW | Function: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space . Controls Zn(2+) accumulation into dentate gyrus granule cells in the hippocampus . Mediates Zn(2+) reuptake from the secreted milk within the alveolar lumen .
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34002
Sequence Length: 317
Subcellular Location: Cell membrane
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A4IIC5 | MNLIFAKVLCLLAILVLMMLGSLIPVKISEADFDKSSRSRKILSLSNSFAGGVFLATCFNALLPAVREKFFDLLKIGNISTDYPLAETIMMVGFFLTVFVEQTVMTFRKEKPSFIDMETFNAGSDIGSDSEFESPFISANHGHNLYEGGHSHHSHSLNIKELSSSSPIRLFSLVFALSAHSVFEGLALGLQEDGNKLLSLFIGVVIHETLVAMALGVSMAKVNTHLKDAIKMAVLVSTMIPIGIVVGMAIQSAQNMASSIASALLQGIAGGTFIFVTFFEILVKELEEKNDRLLKVLFLVLGYTVLAVLVLFKW | Function: Transporter for the divalent cation Zn(2+). Mediates the influx of Zn(2+) into cells from extracellular space.
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34231
Sequence Length: 314
Subcellular Location: Cell membrane
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Q6P5W5 | MASLVSLELGLLLAVLVVTATASPPAGLLSLLTSGQGALDQEALGGLLNTLADRVHCANGPCGKCLSVEDALGLGEPEGSGLPPGPVLEARYVARLSAAAVLYLSNPEGTCEDARAGLWASHADHLLALLESPKALTPGLSWLLQRMQARAAGQTPKMACVDIPQLLEEAVGAGAPGSAGGVLAALLDHVRSGSCFHALPSPQYFVDFVFQQHSSEVPMTLAELSALMQRLGVGREAHSDHSHRHRGASSRDPVPLISSSNSSSVWDTVCLSARDVMAAYGLSEQAGVTPEAWAQLSPALLQQQLSGACTSQSRPPVQDQLSQSERYLYGSLATLLICLCAVFGLLLLTCTGCRGVTHYILQTFLSLAVGAVTGDAVLHLTPKVLGLHTHSEEGLSPQPTWRLLAMLAGLYAFFLFENLFNLLLPRDPEDLEDGPCGHSSHSHGGHSHGVSLQLAPSELRQPKPPHEGSRADLVAEESPELLNPEPRRLSPELRLLPYMITLGDAVHNFADGLAVGAAFASSWKTGLATSLAVFCHELPHELGDFAALLHAGLSVRQALLLNLASALTAFAGLYVALAVGVSEESEAWILAVATGLFLYVALCDMLPAMLKVRDPRPWLLFLLHNVGLLGGWTVLLLLSLYEDDITF | Function: Selective transporter that mediates the uptake of Zn(2+) . Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability . Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher concentrations .
PTM: The extracellular N-terminal ectodomain is cleaved when cells are Zn(2+) deficient, N-terminally cleaved SLC39A4 is internalized at a faster rate.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Sequence Mass (Da): 68408
Sequence Length: 647
Domain: The N-terminal extracellular domain is required for high efficient zinc transport.
Subcellular Location: Cell membrane
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P0DX17 | MGGQTVWMTLSFKLLLYYCMISLLMPAIFILATRAQVDKFRKFNESTQTKSSQELFEEAFEEQGYYLQRLFLQYGDNGTLTYEGLQKLLGSLGLGEVSVLEIRHGEAKHPSQSISHSHSHEDHHPSQGTTNSPPLRESLDAKSALSGSPAELGRSDYFLHPALRNKQEESVSLLSDHPTEKHLHGNCLNVTQLLWNFGLGQASHITPAHFTFLCPALLYQIESGVCLRHTEDHSQASKTSEGFLIALGWASLALLVISLPSLVALGMAPLLQPSVLQVFLCPMAGMAVGTLCGDALLHLMPHAIFSQHTDHQNAVFKGLSVLGGLYLLFIFESLLGLKQHFKNLKRRKHDAECGRELDALQGTSSANQNESSGHGHSHGQAEPGQTGIRSMAWMVVMGDGIHNLTDGLAIGVAFSQSLTGGFSTAIAVFCHELPHELGDLAVLLSAGWPVRRLLVFSGLSALLGFVGVLAGSALGNHWASHSPWILTLTAGVFLYVALADMMPEMLHGACGSVSPLKRFLLQALGLLTGGAIMLCIALFEDHIAVSLGENSLGEN | Function: Uniporter that transports zinc(2+) into polarized cells of enterocytes, pancreatic acinar and endoderm cells across the basolateral membrane and participates, notably, in zinc excretion from the intestine by the uptake of zinc from the blood into the intestine. The transport mechanism is temperature- and concentration-dependent and saturable (By similarity). Mediates zinc homeostasis that is essential for venous angiogenesis .
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60009
Sequence Length: 555
Subcellular Location: Basolateral cell membrane
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Q6ZMH5 | MMGSPVSHLLAGFCVWVVLGWVGGSVPNLGPAEQEQNHYLAQLFGLYGENGTLTAGGLARLLHSLGLGRVQGLRLGQHGPLTGRAASPAADNSTHRPQNPELSVDVWAGMPLGPSGWGDLEESKAPHLPRGPAPSGLDLLHRLLLLDHSLADHLNEDCLNGSQLLVNFGLSPAAPLTPRQFALLCPALLYQIDSRVCIGAPAPAPPGDLLSALLQSALAVLLLSLPSPLSLLLLRLLGPRLLRPLLGFLGALAVGTLCGDALLHLLPHAQEGRHAGPGGLPEKDLGPGLSVLGGLFLLFVLENMLGLLRHRGLRPRCCRRKRRNLETRNLDPENGSGMALQPLQAAPEPGAQGQREKNSQHPPALAPPGHQGHSHGHQGGTDITWMVLLGDGLHNLTDGLAIGAAFSDGFSSGLSTTLAVFCHELPHELGDFAMLLQSGLSFRRLLLLSLVSGALGLGGAVLGVGLSLGPVPLTPWVFGVTAGVFLYVALVDMLPALLRPPEPLPTPHVLLQGLGLLLGGGLMLAITLLEERLLPVTTEG | Function: Uniporter that transports zinc(2+) into polarized cells of enterocytes, pancreatic acinar and endoderm cells across the basolateral membrane and participates, notably, in zinc excretion from the intestine by the uptake of zinc from the blood into the intestine (By similarity). The transport mechanism is temperature- and concentration-dependent and saturable (By similarity). In addition, is also a high affinity copper transporter in vitro . Also may regulate glucose-stimulated insulin secretion (GSIS) in islets primarily through the zinc-activated SIRT1-PPARGC1A axis (By similarity). Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera . Plays a role in eye development .
PTM: Methylated at His-375 by METTL9.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Sequence Mass (Da): 56461
Sequence Length: 540
Subcellular Location: Basolateral cell membrane
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Q9D856 | MGPPVHHLLTGLCVGVALGWVGGSVPNLGPAEQEQNHYLAQLFGLYGENGTLTAGGLARLLHSLGLGRVQGLRLGHHEPPTGRAAPTSGDNFTHRLQEPELSVDIWAGMPLGPSGWGDQEESKAPDLHGSGPSSLDLFQRLLLLDHSLADHLNEDCLNGSQLLVNFGLSPVAPLTPRQFALLCPALLYQIDSRVCIKTPAPAPPGDVLSALLHSGLAVLFLSLPAPLSLLLLRLLGPRLLRPVLGFLGALAVGTLCGDALLHLLPHAQGGRHTGPSEQSEEDLGPGLSVLGGLFLLFMLENTLGLVRHRGLRPRCCRNKRDLGEPNPDPEDGSGMVLRPLQAASEPEVQGQRENRQSSPSLAPPGHQGHSHEHRGGSIAWMVLLGDCLHNLTDGLALGAAFSDGFSSGLSTTLAVFCHELPHELGDFAMLLQEGLSFRKLLLLSLVSGALGLGGAALGVGLSLGPVPLTPWVFGTTAGVFLYVALVDMLPTLLRPPEPLPVFHVLLQGLGLLLGGSLMFTIALLEEQLVPTVPDG | Function: Uniporter that transports zinc(2+) into polarized cells of enterocytes, pancreatic acinar and endoderm cells across the basolateral membrane and participates, notably, in zinc excretion from the intestine by the uptake of zinc from the blood into the intestine . The transport mechanism is temperature- and concentration-dependent and saturable . In addition, is also a high affinity copper transporter in vitro (By similarity). Also may regulate glucose-stimulated insulin secretion (GSIS) in islets primarily through the zinc-activated SIRT1-PPARGC1A axis . Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (By similarity). Plays a role in eye development (By similarity).
PTM: N-Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Sequence Mass (Da): 56275
Sequence Length: 535
Subcellular Location: Basolateral cell membrane
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Q6L8F3 | MMTFLCTRSGRRASGVECRIAAERAYFRVRGLPVANMIGWWPRLCPVMSLALLWACSVGAGSDCKSVAIETDSRIAEQTQQRHLQALFDKYGQNGSISLEGLFNLLKGVGLDRIRKVMVHHPGNAHNHTHTHDHTHTHVDKLTAHTHPVTTKKGDMDHSVEKSDPVPKAQPDPASGKKSQSDAHHNLYMKMNQESTTALTTPSYVTRSRRTNRSADYDFTQDHASFSPSQPNVTHSNHTHHDEDTPTHQHDDHDEHEHARASLGCQNASTILQTHGMRKEASLSVKDFSFLCPALLMQIDSKSCIVHEDEDEHSDHSHHHKHHHHHHDHQHLQHPHNHTNGRGQRNTPVYIAWLGGFLSITLISLLALVGVVLIPLMNRVCFNFLLSFLVALAVGTLSGDALLHLIPHSQGHHHHGHSEEHAEEEDSLRPVWTGLTALSGVYIMFLIEHFLTLGKMYKDKNQKVQKRVDLTTEVLESEKLPSLEENDVKIEAAETNGGRALAEEEEVMLGAELYNDIDCENKCHSHFHDTVGQSDEQHHHHHDYHHILHHHHSQNHHPHTHTHRHTHSYSQQHFEQAGVATLAWMVIMGDGLHNFSDGLAIGAAFTEGLSSGLSTSVAVFCHELPHELGDFAVLLKAGMSVRQAMLYNLLSALMGYLGMIIGILIGHYAENVATWIFALTAGLFMYVALVDMVPEMLHNDASEAGFSHYGFFLLQNAGILLGFGIMLIIAVFEDRIQLDLGY | Function: Acts as a zinc-influx transporter which plays a role in zinc homeostasis and in the induction of epithelial-to-mesenchymal transition (EMT).
PTM: Cleaved on the N-terminus before locating to the plasma membrane.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Sequence Mass (Da): 83030
Sequence Length: 742
Subcellular Location: Cell membrane
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Q13433 | MARKLSVILILTFALSVTNPLHELKAAAFPQTTEKISPNWESGINVDLAISTRQYHLQQLFYRYGENNSLSVEGFRKLLQNIGIDKIKRIHIHHDHDHHSDHEHHSDHERHSDHEHHSEHEHHSDHDHHSHHNHAASGKNKRKALCPDHDSDSSGKDPRNSQGKGAHRPEHASGRRNVKDSVSASEVTSTVYNTVSEGTHFLETIETPRPGKLFPKDVSSSTPPSVTSKSRVSRLAGRKTNESVSEPRKGFMYSRNTNENPQECFNASKLLTSHGMGIQVPLNATEFNYLCPAIINQIDARSCLIHTSEKKAEIPPKTYSLQIAWVGGFIAISIISFLSLLGVILVPLMNRVFFKFLLSFLVALAVGTLSGDAFLHLLPHSHASHHHSHSHEEPAMEMKRGPLFSHLSSQNIEESAYFDSTWKGLTALGGLYFMFLVEHVLTLIKQFKDKKKKNQKKPENDDDVEIKKQLSKYESQLSTNEEKVDTDDRTEGYLRADSQEPSHFDSQQPAVLEEEEVMIAHAHPQEVYNEYVPRGCKNKCHSHFHDTLGQSDDLIHHHHDYHHILHHHHHQNHHPHSHSQRYSREELKDAGVATLAWMVIMGDGLHNFSDGLAIGAAFTEGLSSGLSTSVAVFCHELPHELGDFAVLLKAGMTVKQAVLYNALSAMLAYLGMATGIFIGHYAENVSMWIFALTAGLFMYVALVDMVPEMLHNDASDHGCSRWGYFFLQNAGMLLGFGIMLLISIFEHKIVFRINF | Function: Zinc-influx transporter which plays a role in zinc homeostasis and in the induction of epithelial-to-mesenchymal transition (EMT) . When associated with SLC39A10, the heterodimer formed by SLC39A10 and SLC39A6 mediates cellular zinc uptake to trigger cells to undergo epithelial- to-mesenchymal transition (EMT) . The SLC39A10-SLC39A6 heterodimer also controls NCAM1 phosphorylation and its integration into focal adhesion complexes during EMT (By similarity). Zinc influx inactivates GSK3B, enabling unphosphorylated SNAI1 in the nucleus to down-regulate adherence genes such as CDH1, causing loss of cell adherence . In addition, the SLC39A10-SLC39A6 heterodimer plays an essentiel role in initiating mitosis by importing zinc into cells to initiate a pathway resulting in the onset of mitosis . Participates in the T-cell receptor signaling regulation by mediating cellular zinc uptake into activated lymphocytes . Regulates the zinc influx necessary for proper meiotic progression to metaphase II (MII) that allows the oocyte-to-egg transition .
PTM: Cleaved on the N-terminus before locating to the plasma membrane.
Location Topology: Multi-pass membrane protein
Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Sequence Mass (Da): 85047
Sequence Length: 755
Subcellular Location: Cell membrane
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G4SDH4 | MGCSAATFILVALFGSSSWMGTNSVWMQLPLLTSELPEQWNLPSYLAGVVQIACIVPLIYTILHKGVKSFTIPTAPLIIALLSLACCCQLGLSFFWSDYSEIFGAPRSWPLYSLLFGLAIVNAMSNVLFMPFMAQFHPAYLNAYFVGMGLSSLAPSLLSLAQGTSMFKCDEKGVAERFPPNFSVSIFFFVIFSFTCVALFAFIALYRSGAHTHFATPNKKEPNEGTPLKKDLNNTSSSRKGDDEDESPIEIHETGAPAIDAIVSELDVTFREELQKSFRDANYLERSAMINDDSEPHPVDYITGVKFTFLLFTTALVNAQMNGIITSVQSYAALPYSQATYHFAVTLSNVVSPLSSFLPFFISVRSIPVLAILTACSTAMTAFIVYLAALSPNLIFNSVTIGSALSIGGSLIAAGLHSYLRVVFASLLREGHQSESRLFWCGVFIQIGSFIGSAVMFPLVNIAHLFTSAPQCKSIS | Function: Riboflavin transporter.
Catalytic Activity: riboflavin(in) = riboflavin(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51842
Sequence Length: 476
Subcellular Location: Cell membrane
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Q9VRR2 | MKFAEHLTAHITPEWRKQYINYEEMKAMLYAAIEQSPSAELVEREMVTRYFAKFDEEFFHYCDKELAKINTFYSEKMAEATRKYGSLRSELTEALEMGHPKKLPAWKRRTPLGKKNVPARKIQDLKLAFSEFYLGLILLQNYQNLNFTGFRKILKKHDKLLSVDYGARWRTDHVEAAHFYTNKDIDRLIQETEQAVTQDIEGGDRQRAMKRLRVPPLGEQQSPWTTFKVGLFSGAFVVLFITVVIAAMFYGFGENWRAGMRMFRAPFLIIECLFLWGVNVYGWRSSGVNHVLIFELDPRNHLSEQNIMEVASVFGVIWACCVLSYIFCDPLGIPQYAAPLCLYTLMAAFLLNPTKTFHHEARFWAIRILIRVIMAPFCFVNFADFWLADQLNSMVPAFLDIPFLICFFGRSPTWHKAGKAASHCVEYVSLLHPIVAIMPAYFRFAQCIRRYRDTKESFPHLVNAAKYATSFFVVIFAHKYHTTTDTYPLSKENPWFYCWITAAIFSSCYAYTWDIKMDWGLFDSKAGDNRFLREEIVYSSTWFYYFGIIEDLILRFSWTLSMSLIEAGYIEGDVMMTILSPLEVFRRFIWNYFRLENEHLNNVGKFRAVRDISVAPMDCSDQTTILRMMDETDGVLNRRRGKAAGGKSATKKNKQEQRLLLQGESIEDLCS | Function: Inorganic ion transporter that mediates phosphate ion export across the cell membrane . Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling . The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (By similarity). In enterocytes and differentiating progenitors of the gut, promotes the biogenesis and maintenance of organelles called PXo bodies that store intracellular inorganic phosphate (Pi), and also regulates Cka-JNK mediated tissue homeostasis in response to Pi availability in these tissues . Under conditions of adequate Pi, transports Pi into PXo bodies which convert and store the Pi in the form of phospholipids . It also inhibits Cka at the post-transcriptional level to prevent Cka-bsk/JNK mediated cell proliferation . Upon Pi starvation, Pxo expression is down-regulated resulting in the PXo bodies decreasing in phospholipid content until they undergo lysosomal/autophagosomal degradation and release the stored Pi back into the cytosol for use by the cell . Decrease in Pxo expression also activates the Cka protein, which moves to the nucleus to activate bsk/JNK which then induces nearby progenitor cells to proliferate and form new absorptive cells, probably helping the organism to cope with the nutrient deficiency by maximizing absorption of dietary Pi .
Catalytic Activity: phosphate(in) = phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78202
Sequence Length: 671
Domain: The SPX domain has high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7) (By similarity). Its affinity for inorganic phosphate is two to three orders of magnitude lower (By similarity).
Subcellular Location: Membrane
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Q9UBH6 | MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQKESTGVTTLRQRRKPVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSRGADWRVAHVEVAPFYTCKKINQLISETEAVVTNELEDGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLFCGIFIVLNITLVLAAVFKLETDRSIWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRSNLSHQHLFEIAGFLGILWCLSLLACFFAPISVIPTYVYPLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSLELKWDESKGLLPNNSEESGICHKYTYGVRAIVQCIPAWLRFIQCLRRYRDTKRAFPHLVNAGKYSTTFFMVTFAALYSTHKERGHSDTMVFFYLWIVFYIISSCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITSTTLLPHSGDIIATVFAPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQDDGVRNRQKNRSWKYNQSISLRRPRLASQSKARDTKVLIEDTDDEANT | Function: Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux .
Catalytic Activity: phosphate(in) = phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81535
Sequence Length: 696
Domain: The SPX domain has high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is tow to three orders of magnitude lower.
Subcellular Location: Cell membrane
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Q9Z0U0 | MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDVQKESSGVTTLRQRRKPVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSRGADWRVIHVEVAPFYTCKKINQLISETEAVVTNELEDGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLFCGIFIVLNITLVFAAVFKLETDRTVWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRNNLSHQHLFEIAGFLGILWCLSLLACFFAPISIIPIYVYPLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSFELKWDESKGLLPNDPQEPEFCHKYSYGVRAIVQCIPAWLRFIQCLRRYRDTRRAFPHLVNAGKYSTTFFTVTFAALYSTHEEQNHSDTVVFFYLWVFFCIISSCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITATFKPHVGNIIATVFAPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQEDGVRNRQKNRSWKYNQSISLRRPRLASQSKARDTKVLIEDTDDEANT | Function: Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (By similarity).
Catalytic Activity: phosphate(in) = phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81751
Sequence Length: 695
Domain: The SPX domain has high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is tow to three orders of magnitude lower.
Subcellular Location: Cell membrane
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Q9QZ71 | MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDVQKESSGVTTLRQRRKPVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSRGADWRVIHVEVAPFYTCKKINQLISETEAVVTNELEDGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLFCGIFIVLNITLVFAAVFKLETDRTVWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRNNLSHQHLFEIAGFLGILWCLSLLACFFAPISVIPIYVYPLALYGLMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSFELKWDESKGLLPNDPQEPEFCHKYSYGVRAIVQCIPAWLRFIQCLRRYRDTRRAFPHLVNAGKYSTTFFTVTFAALYSTHKEQNHSDTVVFFYLWVFFCIISSCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITATTFKPHVGDIIATVFAPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQEDGVRNRQKNRSWKYNQSISLRRPRLASQSKARDTKVLIEDTDDEANT | Function: Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (By similarity).
Catalytic Activity: phosphate(in) = phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81804
Sequence Length: 696
Domain: The SPX domain has high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is tow to three orders of magnitude lower.
Subcellular Location: Cell membrane
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A5PJS2 | MELAERFLLDALAYLECALGVVCYVLLKLVGSPYGRYASSGSAFGLPARAAWTVQELPSLALPLLACAGAGAPAERLNRWPNCILLAMFLVHYAQRSLVFPFLIRGGKPMPLYAFLLAFIFCTYNGYLQSRYLSQYAVYADDWLSDPRFLTGSALWLIGMLINIHSDHVLRNLRKPGETGYKIPRGGLFEYISAANYFGEVVEWCGYALASWSIQGWAFAVFTFCVLFTRAQQHHKWYHEKFEDYPKFRKIMIPFLV | Function: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Catalytic Activity: a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29186
Sequence Length: 257
Subcellular Location: Microsome membrane
EC: 1.3.1.22
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P18405 | MATATGVAEERLLAALAYLQCAVGCAVFARNRQTNSVYGRHALPSHRLRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTCNGYLQSRYLSHCAVYADDWVTDPRFLIGFGLWLTGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHEWYLRKFEEYPKFRKIIIPFLF | Function: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Catalytic Activity: a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29459
Sequence Length: 259
Subcellular Location: Microsome membrane
EC: 1.3.1.22
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P24008 | MVPLMELDELCLLDMLVYLEGFMAFVSIVGLRSVGSPYGRYSPQWPGIRVPARPAWFIQELPSMAWPLYEYIRPAAARLGNLPNRVLLAMFLIHYVQRTLVFPVLIRGGKPTLLVTFVLAFLFCTFNGYVQSRYLSQFAVYAEDWVTHPCFLTGFALWLVGMVINIHSDHILRNLRKPGETGYKIPRGGLFEYVSAANYFGELVEWCGFALASWSLQGVVFALFTLSTLLTRAKQHHQWYHEKFEDYPKSRKILIPFVL | Function: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Catalytic Activity: a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29780
Sequence Length: 259
Subcellular Location: Microsome membrane
EC: 1.3.1.22
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P31213 | MQVQCQQSPVLAGSATLVALGALALYVAKPSGYGKHTESLKPAATRLPARAAWFLQELPSFAVPAGILARQPLSLFGPPGTVLLGLFCLHYFHRTFVYSLLNRGRPYPAILILRGTAFCTGNGVLQGYYLIYCAEYPDGWYTDIRFSLGVFLFILGMGINIHSDYILRQLRKPGEISYRIPQGGLFTYVSGANFLGEIIEWIGYALATWSLPALAFAFFSLCFLGLRAFHHHRFYLKMFEDYPKSRKALIPFIF | Function: Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Catalytic Activity: a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28407
Sequence Length: 254
Subcellular Location: Microsome membrane
EC: 1.3.1.22
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Q8RW97 | MGSEPRFEPRPELIDLPVLQKFKLYATPSNFYLIGRDENKSFRRILKIDRRDQNELNLFEDPTRYTKDEMRELKRRMIVGNEESGGFKAITTCYGIIGFVRFLEPYYMLLITKRKKVGEICGHTVYGIAESQMIAIPHPSIQSKVAKSEAELRYKKLLSVVDLSKNFYFSYTYHLMYSLQKNIGNTERGNPHDNTMFVWNSFLTREIRKILQNSIWTVALIYGFFQQTKCSVSGEKFVFTIIARRSRHYAGTRYLRRGVNDIGRVANDVETEQIVSKVVPAGQKIPITSVVQVRGSIPLFWSQEASVFNPQPEIILNKKDANYEATQHHFQNLRQRYGNRIIILNLLKTVTGEKKHRETILRGEFAKTIRFINKGMDREHRLKAIHFDLSKHYKKGADGAFNHLCIFSRKSLELTDLFYCKAPSGVGAEEVIYDSFFNNPIPSQDEEASSPEKEDMKADIFLLQNGVLRTNCIDCLDRTNFAQYAHGLVSLGHQLRTLGISGPPVVDLNNPLAIELMDAYQKMGNTLAMQYGGSEAHSKMFCDLRGNWNMVMRQRDIFTAVRRYYSNAYQDSDKQNAINVFLGHFRPRLGRPALWELDSDQHNIGRSGSNLDIENMRPLIRRSFSDNIIMDCDLNLEELVRENSQPTYEGLNGGVSGTNLEFPFYETEPASLSFLSVMRNEELMRETGSGQMFQGSSSNSDSHRPNDIPGFSHSYVTKFTPAEDIFERGSSKSVSSDNLFTDRDESVTSLTNTNSSFEFPIMGGSDLLPGFSNAFARWVFSARAW | Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89837
Sequence Length: 785
Domain: The phosphatase catalytic core motif (or RXNCXDCLDRTN motif) from the SAC domain is found in metal-independent protein phosphatases and inositol polyphosphate phosphatases.
Subcellular Location: Vacuole membrane
EC: 3.1.3.-
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Q7X911 | MVSRLKIHSGLRLWEFPDQYVIEPTDGSSASCLDISRLDGSMKLIDQVAECNSLRVPKIRSIFGVVGMLKLLAGSYLVVVTESESVGSFLGHPIYKINSLKFLPCDHSLENPHEEQKKMETDDYSRLLSVAERTTGLYFSYEINLTLTAQRLHDLGDESKLLPLWRQAEPRFLWNNYMLEVLIDNKLDQFLLPVIQGSFHSFQTAIGRDIVDITLIARRCSRRNGTRMWRRGADPDGYVANFVETEQIVRMNGYTSSFVQIRGSMPFMWEQIVDLTYKPKFEIVQPEEAARIAERHFLDLRKKYGSVLAVDLVNKHGGEGRLSERFAGAMQHITGDDVRYLHFDFHHICGHIHFERLAILYEQMEDFLEKNGYFLLNEKGEKMKEQLGIVRTNCIDCLDRTNVTQSMIGRKLLELQLKRIGVFGAEETIRSHQNFDECYKILWANHGDDISIQYSGTPALKGDFVRYGQRTIQGVLQDGWNALARYYLNNFADGTKQDAIDLVQGHYIVAVSRDMAPVPRKRGLEAVANFPVALTVILISFWFATMSVKQVGSGYKHLLFSLVWAGISVAVAALVRANGRIFCNRPSLHKPRS | Function: Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Involved in priming for different defense responses.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67626
Sequence Length: 593
Domain: The phosphatase catalytic core motif (or RXNCXDCLDRTN motif) from the SAC domain is found in metal-independent protein phosphatases and inositol polyphosphate phosphatases.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.3.-
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Q9C5G5 | METVDSRNKLHSRLRLWEFPDQYIIEPADGSGSSCLDISRVDASMKLIDQVPESNSVRVPKIRSIFGVVGMLKLLAGSYLVVVTESERVGSFLGHPIFKVTTLKVLPCDHSLKNSPEEQKKMETEFSKLLSVAEKTTGLYFSYEVNLTLSSQRLHEMGDESKSLPLWRQAEPRFLWNNYMLEVLIDNKLDQFLLPVIQGSFNSFETAIGRDIVDITLIARRCTRRNGTRMWRRGADLDGYVANFVETEQIVQMNGYTSSFVQVRGSMPFMWEQVVDLTYKPKFEIVQPEEAKRIAERHFLDLRKKYGSVLAVDLVNKQGGEGRLCEKYATVMQHITGDDIRYLHFDFHQICGHIHFERLSILYEQIEGFLEKNGYFLLNEKGEKMKEQLGVVRSNCIDCLDRTNVTQSMIGRKMLEVQLKRIGVFGAEETISSHLNFDEHYKILWANHGDEISIQYSGTPALKGDFVRYGHRTAHGVLKDGWSSLRRYYLNNFADGTKQDAIDLLQGHYIVAVSRDMAPVPQKGGLEAVANFPVALFVVLMSFWFATMSLKQTGSDYKHKHLFFSLLWTGICVGMAALVRANGRIFCNRPRLHKPRG | Function: Phosphoinositide phosphatase that preferentially hydrolyzes PtdIns(4)P. Regulates the accumulation of PtdIns(4)P on membrane compartments at the tips of growing root hairs leading to proper root hair development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68237
Sequence Length: 597
Domain: The phosphatase catalytic core motif (or RXNCXDCLDRTN motif) from the SAC domain is found in metal-independent protein phosphatases and inositol polyphosphate phosphatases.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.3.-
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Q96328 | MEIAPSTSRFKLYDQFELLEFPDKYVVKPIESPEEGFSVNRRDGNIKPLDENASSGSPTRVSTIYGVGGTIRLLAGTYLLVITSREEVGNFLGLPIFRVTAMKFLPCNEALRFATAQEKKDETYFRTLLQALETTPGLYFSYETDLTLNLQRRCKLAEGWNRKPMWKQADPRYVWNWHLLEDLIECKLDGFIIPILQGSYQVAELKLKNSPAVVSIMSRRCTRRLGTRMWRRGANLEGDAANFVESEQIVEINGFKFSLLQVRGSIPLLWEQIVDLSYKPRLKINKHEETPKVVQRHFHDLCQRYGEIMAVDLTDQHGDEGALSKAYATEMEKLPDVRYVSFDFHQVCGTTNFDNLGVLYEQIGDEFEKQGYFLVDADENILEEQKGVIRSNCIDCLDRTNVTQSFMGQKSLNLQLQRIGVCDSTECISTFEDDYTKFRTIWAEQGDEVSLQYAGTYALKGDLVRYGKQTMTGAIKDGLSAMSRYYLNNFQDGVRQDALDLISGRYTVGTHSPSQLQPIGSQPSFLPVASALLIGGVTVTSFTIHQAGRNTQQYLASALWAGVTAGVVAMIKANGRHLTSRPRLCHLI | Function: Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66464
Sequence Length: 588
Domain: The phosphatase catalytic core motif (or RXNCXDCLDRTN motif) from the SAC domain is found in metal-independent protein phosphatases and inositol polyphosphate phosphatases.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.3.-
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Q9HBV2 | MSPRGTGCSAGLLMTVGWLLLAGLQSARGTNVTAAVQDAGLAHEGEGEEETENNDSETAENYAPPETEDVSNRNVVKEVEFGMCTVTCGIGVREVILTNGCPGGESKCVVRVEECRGPTDCGWGKPISESLESVRLACIHTSPLNRFKYMWKLLRQDQQSIILVNDSAILEVRKESHPLAFECDTLDNNEIVATIKFTVYTSSELQMRRSSLPATDAALIFVLTIGVIICVFIIFLLIFIIINWAAVKAFWGAKASTPEVQSEQSSVRYKDSTSLDQLPTEMPGEDDALSEWNE | Function: Plays a role in acrosome expansion and establishment of normal sperm morphology during spermatogenesis (By similarity). Important for male fertility .
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 32143
Sequence Length: 294
Subcellular Location: Cytoplasmic vesicle
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Q9DA48 | MRARGAGCPAGLLAVGWLILVGLQASQASNVTSSGGGVQEPAVAREGESESESESEEEAENEGEVPESETTAEADAEEEVQNRTIVKEVEFGMCTVTCGVGIREVILTNGCPGGESKCVVRVEECRGPVDCGWGKPISENLDSARLSCVHISPENRFKYVWKLLKPDQQPVILTNDSAVLEITREIRPLAFECDTLDNNEMVASVKFTVYTTNELQMRRSSRPDTDAVLVFVLTIGVIICIFVIFVLIFIIINWAAVKSFWGSKTSATEIQSELSSMRYKDSTSLDQSPTDIPVHEDDALSEWNE | Function: Plays a role in acrosome expansion and establishment of normal sperm morphology during spermatogenesis. Important for male fertility.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 33343
Sequence Length: 305
Subcellular Location: Cytoplasmic vesicle
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D5K8A9 | MSPGGAGCSAGLLLTVGWLLLAGLQSTCGINVTAVQDPSLVSEGENEGEEEAENDSEVENEPQAEAEQDVSNKTVVKEVEFGMCTVTCGVGIREVLLTNGCPGGESKCIVRVEECRGPVDCGWGKPISENLESVRLSCVHTSPVNRFKYVWRLLRPNQQAVILANDSAILEVQRETHPMAFQCETLDNNEIVATVKFTVYTTAELQMKRSSRPDTDAVLVFVLTIGVIICIFVIFVLIFIIVNWATVKDFWASKASTTEIQSELSSMKYKDSTSLDQSPTEIPGHEDDALSEWNE | Function: Plays a role in acrosome expansion and establishment of normal sperm morphology during spermatogenesis. Important for male fertility.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 32239
Sequence Length: 295
Subcellular Location: Cytoplasmic vesicle
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Q8IXA5 | MVSALRGAPLIRVHSSPVSSPSVSGPRRLVSCLSSQSSALSQSGGGSTSAAGIEARSRALRRRWCPAGIMLLALVCLLSCLLPSSEAKLYGRCELARVLHDFGLDGYRGYSLADWVCLAYFTSGFNAAALDYEADGSTNNGIFQINSRRWCSNLTPNVPNVCRMYCSDLLNPNLKDTVICAMKITQEPQGLGYWEAWRHHCQGKDLTEWVDGCDF | Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro.
PTM: The processed form derives from the membrane form by proteolytic processing.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 23431
Sequence Length: 215
Subcellular Location: Cytoplasmic vesicle
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Q9D9X8 | MGICMSMYTQVLVPVDADGDHHILWSRFYERWGSCFNPCAGLVNCLPPHSSALYLCHRMEARSRAPRRQLCPPGITWLALAYLLSCLLASSKAKVFSRCELAKEMHDFGLDGYRGYNLADWVCLAYYTSGFNTNAVDHEADGSTNNGIFQISSRRWCRTLASNGPNLCRIYCTDLLNNDLKDSIVCAMKIVQEPLGLGYWEAWRHHCQGRDLSDWVDGCDF | Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 25020
Sequence Length: 221
Subcellular Location: Cytoplasmic vesicle
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B6VH79 | MISALWGALLIRVHSSPVSSPSVSGPPRLVSCGSSQSSALSQSGGSTSTTGTEARSRALGRRWCPAAIMLLALVSLLSCLLPSSEAKVYSRCELARVLQDFGLDGYRGYSLADWVCLAYFTSGFNAAALDYEADGSTNNGIFQINSRRWCSNLTPNVPNVCRMYCS | Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro (By similarity).
PTM: The processed form derives from the membrane form by proteolytic processing.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 17714
Sequence Length: 166
Subcellular Location: Cytoplasmic vesicle
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B6VH77 | MVSALREAPLIRVHSSPVSSPSVSGSRRPVSCLSSQSSALSQSGGGSTSAAGIEARSRALRRRWCPAGIILLALISLLSCLLPASEAKVYGRCELARVLHDFGLDGYRGYSLADWVCLAYFTSGFNTAAVDHEADGSTNNGIFQINSRRWCRNLTPNVPNVCQMYCS | Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro (By similarity).
PTM: The processed form derives from the membrane form by proteolytic processing.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 17899
Sequence Length: 167
Subcellular Location: Cytoplasmic vesicle
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Q32PB3 | MVLGWLPLLVMVLAPGTTGVKDCVFCELTDSTSCPGTSMRCGDDEDCFTGHGVAPGVGPIINKGCVHATSCGHEEPINYMGVTYSLTTNCCTGHMCNGAPDPTRGRLAGAAASLALGVLLLLQHVL | Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12964
Sequence Length: 126
Subcellular Location: Cell membrane
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Q7VUL8 | MNAVTDKSVADYIVADMALAGWGRRELAIAETEMPGLMAIRDEYAASQPLKGARIAGSLHMTIQTGVLIETLVALGAEVRWASCNIFSTQDHAAAAIAATGTPVFAIKGETLEEYWQYTHKIFEWPEGRHANMILDDGGDATLLLHLGARAEQDISVLAKPGSEEERVLFAAIKETLGRDPKWYSTRLAQIKGVTEETTTGVHRLYQMSQKGELAFAAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMVAGKIAVVAGYGDVGKGCAQALVALRAQVWVTEIDPICALQAAMEGFKVVTMEEAAAHADIFVTATGNYHVITRQHMEAMKDQAIVCNIGHFDNEIDVAGLENCQWEEIKPQVDHVIFPDGKRIILLAKGRLVNLGCATGHPSFVMSSSFANQTIAQIELFTRNEAYTTGQVYVLPKHLDEKVARLHLKKLGVKLSTLSKQQADYIGVPVEGPFKPDHYRY | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 51631
Sequence Length: 472
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
|
A0A087WNH6 | MNAKPGFTDYIVKDIALADFGRKEISLAETEMPGLMATREEYGPKQPLKGARIAGSLHMTIQTAVLIETLAALGADIRWVSCNIYSTQDHAAAAIAAAGIPVFAVKGETLTEYWDYTAKLFDWHGGGTPNMILDDGGDATMLVHAGYRAEQGDTAFLDKPGSEEEEIFYALVKRLLKEKPKGWFAEIAKNIKGVSEETTTGVHRLYEMANKGTLLFPAINVNDSVTKSKFDNLYGCRESLVDGIRRGTDVMLSGKVAMVAGFGDVGKGSAASLRQAGCRVMVSEVDPICALQAAMEGYEVVTMEDAAPRADIFVTATGNKDIITIEHMRAMKDRAIVCNIGHFDNEIQIASLRNLKWTNIKPQVDEIEFPDKHRIIMLSEGRLVNLGNAMGHPSFVMSASFTNQTLAQIELFANNKDSKYAKKVYVLPKTLDEKVARLHLAKIGVKLTELRKDQADYIGVKQEGPYKSDHYRY | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine, which is a strong inhibitor of SAM-dependent methyltransferases. Catalyzes the hydrolysis of S-adenosyl-L-homocysteine into L-homocysteine and adenosine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 52040
Sequence Length: 473
Domain: Each protomer consists of two large domains, the substrate-binding domain and the cofactor-binding domain, which are separated by a deep crevice forming the substrate-access channel to the active site, and a small C-terminal oligomerization domain.
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
|
A6WX40 | MTASQDFVVKDLSLADWGRKELDIAETEMPGLMAAREEFGKSQPLKGARISGSLHMTIQTAVLIETLQALGAEVRWASCNIFSTQDHAAAAIAATGTPVFAIKGETLEEYWTYTDQIFQWPDGEPSNMILDDGGDATMYILIGARAEAGEDVLSNPGSEEEEVLFAQIKKRMAATPGFFTRQRDAIKGVTEETTTGVNRLYQLQKKGLLPFPAINVNDSVTKSKFDNKYGCKESLVDGIRRGTDVMMAGKVAVVCGYGDVGKGSAQSLAGAGARVKVTEVDPICALQAAMDGFEVVTLDDAASTADIIVTTTGNKDVITIDHMRKFKDMAIVGNIGHFDNEIQVAALRNLKWTNVKPQVDLIEFPDGKRIILLSEGRLLNLGNATGHPSFVMSASFTNQVLGQIELFTRTDAYKNEVYVLPKHLDEKVARLHLDKLGAKLTVLSEEQAAYIGVTPQGPFKSEHYRY | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 50776
Sequence Length: 466
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
|
Q7V926 | MVAVPTSTASLQALPQYVVADIDLADFGRKELSIAETEMPGLIALRIKYGSEKPLKGARIAGSLHMTIQTGVLIETLVALGADVRWASCNIFSTQDHAAAAIAASGVPVFATKGETLDEYWAYTHRILEWGDGGTPNMILDDGGDATGLVMLGSKAESDSSVLDNPGNEEETALFASIRTKLAEDSSFYSRIKSSIQGVTEETTTGVARLYQMQKSGELPFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMVAGKVALVMGYGDVGKGSAQSLRGLGATVMIAEIDPICALQAAMEGYRVVRLDEVVQDVDIFVTSTGNFQVIRHEHLIRMKDEAIVCNIGHFDNEIDVASLKDYPWENIKPQVDHITLPSGNKIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFSKGDQYADQVYVLPKHLDEMVARLHLEKIGARLTELTKQQADYISVPVEGPYKPDHYRY | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 51748
Sequence Length: 476
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
|
O58275 | MDCGRDYCVKDLSLADEGWKKIDWVSRFMPVLQHIRREFEEKKPFKGVRIAATLHLEMKTAFLLLTLKAGGAEVSAAASNPLSTQDDVVAALAKAGVKVYAIRGESKEQYYEFMHKALDIRPNIIIDDGADMISLVHKERQELLDEIWGGSEETTTGVIRLRAMERDGVLRFSVIAVNDSYMKYLFDNRYGTGQSTWDGVMRATNLLIAGKNVVVVGYGWCGRGIAMRARGLGATVIVVEVDPIKALEARMDGFLVMNMKEAAKIGDIFITATGDIKCIRREHFELMKDGAIMANAGHFDVEIWKPDLEELAVEISNPRPNVTEYKLKDGRRLYLLADGRLVNLVAADGHPAEIMDMSFALQAKAAEYIKDNHGKLEPRVYILPREIDEMVARIKLASMGIEIEELTEEQKKYLESWEHGT | Cofactor: Binds 1 NAD(+) per subunit.
Function: May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalytic Activity: H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine
Sequence Mass (Da): 47274
Sequence Length: 421
Pathway: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.13.2.1
|
Q55CW2 | METTTITSILDDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYNYKEWDNEMVCKWLHDTKRIQKVSIEIFKANEITGNYLESLTDKMLLKMGLTIRDLLSFRSEFDDLKNIFNETNLYNNIQKNSIDYSIDNNNLNNLNNNNNNNNNNNNNNNNNNNNNNNNNNKTIKAPTIDISQYVFIKQMKGSVNCSLEKYINKKTKERILIKRIGKSNINEETIINEISILCSIDHPNIIKTYGYYKDENYYYVASKFYPKGSIKTKSKSTPYNEINAKKVFGKVLKAIDYLHSLDPPIIHRDINSDNILFDENDEPILIDFGLSYKELKDDNNNDDDNYDNHNHNHNHNHNHNHDNDNDNDTNVKIKTQCMEPRWPSPEIHREPPHFSKESDIFSFGCTLFEILGYIITTPIIILPSIPSGMSLECQILFNETTKIDSCFRPTSKQLLNFSWFKETALLTSSEPQPLEPQPQPKPQTSQSKPKPSSSLSSSELPPQPPLESQSKPKPSQSKTQPTQPQSKLNPSSPPSSSSSSLSEPPKPQPSQSKPKPSSSLSSEPPPLEPQPKPQTSQSKPKPSSSLSSSEPPPLEPQPTQSSKPQPSQSKPQPIQSQPTQPQPTQPKSSKQQPQSKQQQQQQQQQQQQQQQQQQQQQQQQKSKPEQSKSKPEQSQSKPQPGQPLQSPSKPQPIPSTTKTTTTTTTTTTPNNNNNNNNNNNNNNNNNNNNIITSINLIECFKKNNSKIIISKDMEFDNPYEKTLHEKHLLKLGISDCKQININHKYFKKVLSFLNSHLTSALQMKMGPYQVDIAPEFDNIFKTLFISLVLEKIDKDTLLKGGKDLGDTSSTLILYTFYYFLSNTLIYQIILHKPTSFKLVGKLK | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 99725
Sequence Length: 875
Subcellular Location: Membrane
EC: 2.7.11.1
|
P02743 | MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV | Cofactor: Binds 2 calcium ions per subunit.
Function: Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
PTM: N-glycosylated with a complex biantennary oligosaccharide chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as asioalo-SAP are also detected .
Sequence Mass (Da): 25387
Sequence Length: 223
Subcellular Location: Secreted
|
Q8SS09 | MLDNIQEYLGVVKAKLTEFYEKVFQNFVKSLFGKPSSILFLGIDNAGKTTLVNKLKSDSTDVYMPTHHPSTSYIEIGNLKAQVIDLGGHTAARLAWRDYFYDCHGIVFIVDVHDVERFQEVREAYETVLSLEKRAPVVVLMNKIDLEGHTPETAEADYQWKSWLSQETGIENQEDPERGQVVKIFYVTITSGSANSITGPLARAFKWLEAMITYNNKKESL | Function: Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25103
Sequence Length: 221
Subcellular Location: Cytoplasmic vesicle
EC: 3.6.5.-
|
P0C583 | MWLWSWFYDILSNLGLLNKHGKLLFLGLDNAGKTTLLHMLKNDRVAILQPTLHPTSEELSVGNVKFTTFDLGGHQQARRLWKDYFPEVNGIVFLVDAKDHERLPEAKAEIDALLSMEELAKVPFVVLGNKIDHPEAVSEDELRQRLGLWQTTGKGRVPLEGIRPIEVFMCSVVMRQGYGEAIRWLSQYV | Function: Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. Vtr-7/sar1 controls the coat assembly in a stepwise manner. Activated sar1-GTP binds to membranes first and recruits the sec23/24 complex. These sec23/24-sar1 prebudding intermediates are then collected by the sec13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to sar1-GDP triggers coat release and recycles COPII subunits (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21583
Sequence Length: 189
Subcellular Location: Cytoplasmic vesicle
EC: 3.6.5.-
|
Q0UKC0 | MTVWDVLSSLGLMNKHAKLLFLGLDNAGKTTLLHMLKNDRVAVLQPTLHPTSEELSIGNVKFTTFDLGGHAQARRLWRDYFPEVSGIVFLVDAKDHERLNESKAELDALLAMEELKNTPFVILGNKIDHPEAVSEDQLRATLGLYQTTGKGKVPLEGIRPIEVFMCSVVMRQGYGEGIRWLSQYV | Function: Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20733
Sequence Length: 185
Subcellular Location: Cytoplasmic vesicle
EC: 3.6.5.-
|
Q01475 | MFIINWFYDALAMLGLVNKHAKMLFLGLDNAGKTTLLHMLKNDRLAVMQPTLHPTSEELAIGNVRFTTFDLGGHQQARRLWRDYFPEVNGIVYLVDCCDFERLSESKAELDALLAMEELARVPFLILGNKIDAPGAISEDELKAALGLYQTTGKGVSKPVPGIRPIEVFMCSVVLRQGYGEGFKWLAQYV | Function: Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. Sar1 controls the coat assembly in a stepwise manner. Activated sar1-GTP binds to membranes first and recruits the SEC23/24 complex. These sec23/24-sar1 prebudding intermediates are then collected by the sec13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to sar1-GDP triggers coat release and recycles COPII subunits (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21280
Sequence Length: 190
Subcellular Location: Cytoplasmic vesicle
EC: 3.6.5.-
|
Q9NQZ2 | MVGRSRRRGAAKWAAVRAKAGPTLTDENGDDLGLPPSPGDTSYYQDQVDDFHEARSRAALAKGWNEVQSGDEEDGEEEEEEVLALDMDDEDDEDGGNAGEEEEEENADDDGGSSVQSEAEASVDPSLSWGQRKKLYYDTDYGSKSRGRQSQQEAEEEEREEEEEAQIIQRRLAQALQEDDFGVAWVEAFAKPVPQVDEAETRVVKDLAKVSVKEKLKMLRKESPELLELIEDLKVKLTEVKDELEPLLELVEQGIIPPGKGSQYLRTKYNLYLNYCSNISFYLILKARRVPAHGHPVIERLVTYRNLINKLSVVDQKLSSEIRHLLTLKDDAVKKELIPKAKSTKPKPKSVSKTSAAACAVTDLSDDSDFDEKAKLKYYKEIEDRQKLKRKKEENSTEEQALEDQNAKRAITYQIAKNRGLTPRRKKIDRNPRVKHREKFRRAKIRRRGQVREVRKEEQRYSGELSGIRAGVKKSIKLK | Function: Essential for gene silencing: has a role in the structure of silenced chromatin. Plays a role in the developing brain (By similarity). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome .
PTM: Citrullinated by PADI4.
Sequence Mass (Da): 54558
Sequence Length: 479
Subcellular Location: Nucleus
|
A0A084B9Z1 | MSEALIGGGAKKVYILSRRRDVLESAAAKHEGILIPIQCDVTSKASLQSAVDIVTKDSGYVNLLIANSGTLGPTNRLDHDLSIHELRKNVFDNVSFEDFNNTLSVNTTGAYFTMLAFLELLDAGNKNALKGGFGGPSTEGGAPSIQSQVIFTSSLGAYSRDRLSPPAYSASKSALSHLAKHASTNLAKYGIRVNVLAPGLFPSEIATLMTANRDPATENLGDRMFIPARKFGGAEEMGGTVLYLASRAGSYCNGLILVNDGGRLSVMLSEY | Function: Short-chain dehydrogenase/reductase; part of the satratoxin SC1 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton . SC1 encodes 10 proteins, SAT1 to SAT10 . The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding . The putative short-chain reductase SAT3 may assist the PKS in some capacity . SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase . SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity . The probable transcription factor SAT9 may regulate the expression of the SC1 cluster . SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 . SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases . The SC2 cluster may be regulated by the transcription factor SAT15 . SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 . SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites . The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression .
Sequence Mass (Da): 28739
Sequence Length: 271
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
|
Q8W2B8 | MACINGENRDFSSSSSLSSLPMIVSRNFSARDDGETGDEFPFERIFPVYARGTLNPVADPVLLDFTNSSYDPIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSMTMEHDATREFFQNVAVAYRETIPNGSSVSGSCRERRH | Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Mass (Da): 38424
Sequence Length: 355
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.30
|
Q10QH1 | MAACVDKWPPAAYLCRLPEKFYCVLPDCTATDRPVVTASAAPAPAASGSSGDYVWDVLRAEAQDDADDEPLLRKFYHDLVLSRPSLESALASLLAAKLCIPGALPQDQLRDLLAGALAAHPEAGRAARADLVAARDRDPACAKMVHCFLYYKGFLALQAHRAAHALWSDNRRAPALLLQSRASEVFGVDIHPGARIGCGILLDHATGVVIGETAVVGYDVSILHGVTLGGTGKESGDRHPKVGDGVLIGAGASVLGNVHIGDGAKIGAGAVVLRDVADGTTAVGNPAKPIIGKKAAPQRRPEELPGVTMEQRWSD | Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Mass (Da): 32921
Sequence Length: 315
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
EC: 2.3.1.30
|
A0A084B9Z2 | MNGIYALQQTFVKFSLLALYHRLFWVNRHFVRSVWLVGIVQGCWGIAILLVHIFLCTPMEKIWTPWMVEGTCVDVNTLFAIYEALNSVLDFIVAGLAIWMLPSLQIRKSTRWHLAGLFVLGAFSGFIGIIKIVEAYDSAQRNFQAVIWNVVQMSISIICCCAPIYRSILPKMGMSSIPSWASWSLRGSSRRSKAVASTADGTSKFSMRSYQGEGKAGGTSVSGNWINLDGSSQRALAWVDAESHGKDQSTYQDIPMGRMKVERSVEVI | Function: Part of the satratoxin SC1 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings . Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton . SC1 encodes 10 proteins, SAT1 to SAT10 . The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding . The putative short-chain reductase SAT3 may assist the PKS in some capacity . SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase . SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity . The probable transcription factor SAT9 may regulate the expression of the SC1 cluster . SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 . SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases . The SC2 cluster may be regulated by the transcription factor SAT15 . SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 . SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites . The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29914
Sequence Length: 268
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
|
Q42538 | MPPAGELRHQSPSKEKLSSVTQSDEAEAASAAISAAAADAEAAGLWTQIKAEARRDAEAEPALASYLYSTILSHSSLERSISFHLGNKLCSSTLLSTLLYDLFLNTFSSDPSLRNATVADLRAARVRDPACISFSHCLLNYKGFLAIQAHRVSHKLWTQSRKPLALALHSRISDVFAVDIHPAAKIGKGILLDHATGVVVGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGCLIGAGATILGNVKIGAGAKVGAGSVVLIDVPCRGTAVGNPARLVGGKEKPTIHDEECPGESMDHTSFISEWSDYII | Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Mass (Da): 32770
Sequence Length: 312
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.30
|
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