ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A2VE55 | MAEVHRRQHARVKGEAPAKSSTHRHEEELGMASAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKALRVVKFPDFDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGVLLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYVFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKALDFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNIS... | Function: Nucleotide sugar antiporter transporting UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-glucose (UDP-Glc) from the cytosol into the lumen of the Golgi in exchange of UMP. By supplying UDP-N-acetylglucosamine, a donor substrate to heparan sulfate synthases, probably takes part in the synthesis of these glycoconj... |
Q76EJ3 | MTAGGQAEAEGAGGEPGAARLPSRVARLLSALFYGTCSFLIVLVNKALLTTYGFPSPIFLGIGQMAATIMILYVSKLNKIIHFPDFDKKIPVKLFPLPLLYVGNHISGLSSTSKLSLPMFTVLRKFTIPLTLLLETIILGKQYSLNIILSVFAIILGAFIAAGSDLAFNLEGYIFVFLNDIFTAANGVYTKQKMDPKELGKYGVLFYNACFMIIPTLIISVSTGDLQQATEFNQWKNVVFILQFLLSCFLGFLLMYSTVLCSYYNSALTTAVVGAIKNVSVAYIGILIGGDYIFSLLNFVGLNICMAGGLRYSFLTLSSQ... | Function: Nucleotide sugar antiporter transporting UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-glucose (UDP-Glc) from the cytosol into the lumen of the Golgi in exchange of UMP. By supplying UDP-N-acetylglucosamine, a donor substrate to heparan sulfate synthases, probably takes part in the synthesis of these glycoconj... |
Q762D5 | MEEPNAAPLPSRLARLLSALFYGTCSFLIVLVNKALLTTYGFPSPIVLGIGQMATTIMILYVFKLNKIIHFPDFDKKIPGKLFPLPLLYVGNHISGLSSTSKLSLPMFTVLRKFTIPFTLLLEAIILGTQYSLNIILSVLAIVLGAFIAAGSDLTFNLEGYVFVFLNDIFTAANGVYTKQKMDPKELGKYGVLFYNACFMLIPTVIISVSTGDFQQATEFRHWKNVLFIIQFLLSCLLGFLLMYSTALCSYYNSALTTAVVGAIKNVSVAYIGMLVGGDYIFSLLNFIGLNICMAGGLRYSFLTLSSQLKPKQPVDEESI... | Function: Nucleotide sugar antiporter transporting UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-glucose (UDP-Glc) from the cytosol into the lumen of the Golgi in exchange of UMP. By supplying UDP-N-acetylglucosamine, a donor substrate to heparan sulfate synthases, probably takes part in the synthesis of these glycoconj... |
Q5M8T2 | MRQLCRGRVLGISVAIAHGVFSGSLNILLKFLISRYQFSFLTLVQCLTSSTAALSLELLRRLGLIAVPPFGLSLARSFAGVAVLSTLQSSLTLWSLRGLSLPMYVVFKRCLPLVTMLIGVLVLKNGAPSPGVLAAVLITTCGAALAGAGDLTGDPIGYVTGVLAVLVHAAYLVLIQKASADTEHGPLTAQYVIAVSATPLLVICSFASTDSIHAWTFPGWKDPAMVCIFVACILIGCAMNFTTLHCTYINSAVTTSFVGVVKSIATITVGMVAFSDVEPTSLFIAGVVVNTLGSIIYCVAKFMETRKQSNYEDLEAQPRG... | Function: Probable UDP-glucose transmembrane transporter involved in UDP-glucose transport from the cytosol to the lumen of synaptic vesicles . It is involved in platelet dense granules maturation (By similarity).
Catalytic Activity: UDP-alpha-D-glucose(in) = UDP-alpha-D-glucose(out)
Location Topology: Multi-pass membr... |
Q8BGF8 | MRQLCRGRVLGISVAIAHGVFSGSLNILLKFLISRYQFSFLTLVQCLTSSTAALSLELLRRLGLIAVPPFGLSLARSFAGVAVLSTLQSSLTLWSLRGLSLPMYVVFKRCLPLVTMLIGVLVLKNGAPSPGVLAAVLITTCGAALAGAGDLTGDPIGYVTGVLAVLVHAAYLVLIQKASADTEHGPLTAQYVIAVSATPLLVICSFASTDSIHAWTFPGWKDPAMVSIFVACILIGCAMNFTTLHCTYINSAVTTSFVGVVKSIATITVGMVAFSDVEPTSLFIAGVVVNTLGSIIYCVAKFLETRRQSNYEDLESQAEG... | Function: Probable UDP-glucose transmembrane transporter involved in UDP-glucose transport from the cytosol to the lumen of synaptic vesicles . It is involved in platelet dense granules maturation .
Catalytic Activity: UDP-alpha-D-glucose(in) = UDP-alpha-D-glucose(out)
Location Topology: Multi-pass membrane protein
Seq... |
Q9VR50 | MLGKRTGSRHIAVVLLMCLFWYVISSSNNVIGKMVLNEFPFPMTVTLVQLCSITLYSGPFFNLWRIRKYQDIPRPYYYRLIVPLALGKLLASVTSHISLWKVPVSYAHTVKATMPLFTVVLTRVFFGEKQPTLVYLSLLPIITGVGIATVTEISFDMMGLISALISTMGFSMQNIFSKKVLKDTNIHHLRLLHLLGKLSLFIFLPLWLYMDSFAVFRHTAIKNLDYRVIALLFADGVLNWLQNIIAFSVLSLVTPLTYAVASASKRIFVIAVSLLILGNPVTWVNCVGMTLAIVGVLCYNRAKQLTRGREQPTLPLSQTS... | Function: Putative transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41618
Sequence Length: 373
Subcellular Location: Membrane
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Q96K37 | MAAAAVGAGHGAGGPGAASSSGGAREGARVAALCLLWYALSAGGNVVNKVILSAFPFPVTVSLCHILALCAGLPPLLRAWRVPPAPPVSGPGPSPHPSSGPLLPPRFYPRYVLPLAFGKYFASVSAHVSIWKVPVSYAHTVKATMPIWVVLLSRIIMKEKQSTKVYLSLIPIISGVLLATVTELSFDMWGLVSALAATLCFSLQNIFSKKVLRDSRIHHLRLLNILGCHAVFFMIPTWVLVDLSAFLVSSDLTYVYQWPWTLLLLAVSGFCNFAQNVIAFSILNLVSPLSYSVANATKRIMVITVSLIMLRNPVTSTNVL... | Function: Putative transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44773
Sequence Length: 410
Subcellular Location: Membrane
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Q8CD26 | MAAAATAGPGAGAGVPGAGGGGGAREGARVAVLCLLWYALSAGGNVVNKVILSAFPFPVTVSLCHILALCAGLPPLLRAWRVPPAPPVSGPGPGPHPASGPLLPPRFYPRYVLPLAFGKYFASVSAHVSIWKVPVSYAHTVKATMPIWVVLLSRIIMKEKQSTKVYLSLVPIISGVLLATVTELSFDVWGLVSALAATLCFSLQNIFSKKVLRDSRIHHLRLLNILGCHAVFFMIPTWVLVDLSTFLVSSDLAYVSQWPWTLLLLAVSGFCNFAQNVIAFSILNLISPLSYSVANATKRIMVITVSLIMLRNPVTSTNVL... | Function: Putative transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44325
Sequence Length: 409
Subcellular Location: Membrane
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Q75N73 | MKRLHPALPSCLLLVLFGIWRTAPQTHASSAGLPPLSATSFLEDLMDRYGKNDSLTLTQLKSLLDHLHVGVGRDNVSQPKEGPRNLSTCFSSGDLFAAHNLSERSQIGASEFQEFCPTILQQLDSQACTSENQKSEENEQTEEGKPSAIEVWGYGFLCVTVISLCSLMGASVVPFMKKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFNPQDNYVSKSAVVFGGFYLFFFTEKILKMLLKQKNEHHHGHNHFTSETLPSKKDQEEGVTEKLQNGDLDHMIPQHCNSELDGKAPGTDEKVIVNSMSVQDLQASQSACY... | Function: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity . Functions as an energy-dependent symporter, transporting through the membranes an electroneut... |
P0AG05 | MREAVIAEVSTQLSEVVGVIERHLEPTLLAVHLYGSAVDGGLKPHSDIDLLVTVTVRLDETTRRALINDLLETSASPGESEILRAVEVTIVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPATIDIDLAILLTKAREHSVALVGPAAEELFDPVPEQDLFEALNETLTLWNSPPDWAGDERNVVLTLSRIWYSAVTGKIAPKDVAADWAMERLPAQYQPVILEARQAYLGQEEDRLASRADQLEEFVHYVKGEITKVVGK | Function: Mediates bacterial resistance to the antibiotics streptomycin and spectinomycin.
Catalytic Activity: ATP + streptomycin = 3''-O-adenylylstreptomycin + diphosphate
Sequence Mass (Da): 29332
Sequence Length: 263
EC: 2.7.7.47
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Q8ZPX9 | MTLSIPPSIQCQTEAACRLITRVTGDTLRAIHLYGSAVAGGLKPNSDIDLLVTICQPLTEAQRATLMQELLALSSPPGASAEKRALEVTVVLYSQLVPWCFPPSREMQFGEWLREDICQGIYEPAQQDWDMVLLITQILETSIPLKGERAERLFTPAPAAQLLKALRYPLDLWQSTADVQGDEYHIVLTLARIWYTLSTGRFTSKDAAADWLLPQLPEDYAATLRAAQREYLGLEQQDWHILLPAVVRFVDFAKAHIPTQFT | Function: Mediates bacterial resistance to the antibiotics streptomycin and spectinomycin, does not confer resistance to kanamycin . Binds ATP first, then antibiotic .
Catalytic Activity: ATP + streptomycin = 3''-O-adenylylstreptomycin + diphosphate
Sequence Mass (Da): 29348
Sequence Length: 262
Domain: Has an N-termin... |
P48065 | MDGKVAVQECGPPAVSWVPEEGEKLDQEDEDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFVCGIPVFFLEVALGQYTSQGSVTAWRKICPLFQGIGLASVVIESYLNVYYIIILAWALFYLFSSFTSELPWTTCNNFWNTEHCTDFLNHSGAGTVTPFENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWVICYFCIWKGVKSTGKVVYFTATFPYLMLVILLIRGVTLPGAYQGIIYYLKPDLFRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYKDCI... | Function: Transporter that mediates cellular uptake of betaine and GABA in a sodium- and chloride-dependent process . May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation. Probably also involved in renal and hepati... |
P31651 | MDRKVAVHEDGYPVVSWVPEEGEMMDQKGKDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFSCGIPVFFLEVALGQYSSQGSVTAWRKICPLLQGIGMASVVIESYLNIYYIIILAWALFYLFSSFTWELPWTTCTNSWNTEHCVDFLNHSSARGVSSSENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWIICYFCIWKGVKSTGKVVYFTATFPYLMLIILLIRGVTLPGAYQGIVFYLKPDLLRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYRDSI... | Function: Transporter that mediates cellular uptake of betaine and GABA in a sodium- and chloride-dependent process (By similarity). May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation (Probable). Probably also in... |
P48055 | MDTKLAVHEDAPPLVSWVPEEGEKLEQEGEDQAKDRGQWTNKMEFVLSVAGEIIGLSNVWRFPYLCYKNGGGAFFVPYFIFFFSCGIPVFFLEVALGQYTSQGSVTAWKKICPLFQGIGLASVVIESYLNVYYIIILAWALFYLFSSFTSELPWTTCTNSWNTEYCQHALNHSGAGIGSSTENFTSPVMEFWERRVLGITAGIHDLGALRWELALCLLLAWIVCYFCIWKGVKYTGKVVYFTATFPYLMLVILLIRGVTLPGAYQGIVYYLKPDLLRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYRDSI... | Function: Transporter that mediates cellular uptake of betaine and GABA in a sodium- and chloride-dependent process. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation (By similarity). Probably also involved in r... |
P48056 | MDRKVTVHEDGCPVVSWVPEEGEMMDQKDKDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFSCGIPVFFLEVALGQYSSQGSVTAWRKICPLLQGIGMASVVIESYLNIYYIIILAWALFYLFSSFTWELPWTTCTNSWNTEHCVDFLNYSSTRAASYSENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWIICYFCIWKGVKSTGKVVYFTATFPYLMLIILLIRGVTLPGAYQGIVFYLKPDLLRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYRDSI... | Function: Transporter that mediates cellular uptake of betaine and GABA in a sodium- and chloride-dependent process. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation (By similarity). Probably also involved in r... |
A5PJX7 | MDSRVSGTTSNGETKPVCPGLEKAAEDGALQREQWSNKMEFLLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYLIFLFTCGIPVFLLETALGQYTSQGGITAWRKICPIFEGIGYASQMIVTLLNIYYIIVLAWALFYLFSSFTIDLPWGSCRHDWNTERCVEFQRTNGSLNATAENATSPVIEFWERRVLKISEGIQHLGALRWELALCLLLAWVVCYFCIWKGVKSTGKVVYFTATFPYLMLVVLLIRGVTLPGAAQGIQFYLYPNLTRLWDPQVWMDAGTQIFFSFAICLGCLTALGSYNKYHNNCYRDSIALCFL... | Function: Mediates sodium- and chloride-dependent transport of gamma-aminobutyric acid (GABA) (By similarity). Can also mediate transport of beta-alanine, taurine and hypotaurine (By similarity).
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in)... |
Q9NSD5 | MDSRVSGTTSNGETKPVYPVMEKKEEDGTLERGHWNNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYLVFLFTCGIPVFLLETALGQYTSQGGVTAWRKICPIFEGIGYASQMIVILLNVYYIIVLAWALFYLFSSFTIDLPWGGCYHEWNTEHCMEFQKTNGSLNGTSENATSPVIEFWERRVLKISDGIQHLGALRWELALCLLLAWVICYFCIWKGVKSTGKVVYFTATFPYLMLVVLLIRGVTLPGAAQGIQFYLYPNLTRLWDPQVWMDAGTQIFFSFAICLGCLTALGSYNKYHNNCYRDCIALCFL... | Function: Mediates sodium- and chloride-dependent transport of gamma-aminobutyric acid (GABA) . Mediates transport of beta-alanine . Can also mediate transport of taurine and hypotaurine (By similarity).
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 N... |
Q2PG55 | MDSRASGTASNGETKPVYPVMEKEEEEGTLERGHWNNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYLVFLFTCGVPVFLLETALGQYTSQGGVTAWRKICPIFEGIGYASQMIVILLNVYYIIVLAWALFYLFSSFTIDLPWGGCHHEWNTEHCVEFQKTNGSLNGTSENATSPVIEFWERRVLKISDGIQHLGALRWELALCLLLAWVICYFCIWKGVKSTGKVVYFTATFPYLMLVVLLIRGVTLPGAAQGIQFYLYPNLTRLWDPQVWMDAGTQIFFSFAICLGCLTALGSYNKYHNNCYRDCLALCFL... | Function: Mediates sodium- and chloride-dependent transport of gamma-aminobutyric acid (GABA) (By similarity). Can also mediate transport of beta-alanine, taurine and hypotaurine (By similarity).
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in)... |
P31649 | MENRASGTTSNGETKPVCPAMEKVEEDGTLEREHWNNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYLIFLFTCGIPVFFLETALGQYTNQGGITAWRRICPIFEGIGYASQMIVSLLNVYYIVVLAWALFYLFSSFTTDLPWGSCSHEWNTENCVEFQKANDSMNVTSENATSPVIEFWERRVLKLSDGIQHLGSLRWELVLCLLLAWIICYFCIWKGVKSTGKVVYFTATFPYLMLVVLLIRGVTLPGAAQGIQFYLYPNITRLWDPQVWMDAGTQIFFSFAICLGCLTALGSYNKYHNNCYRDCIALCIL... | Function: Mediates sodium- and chloride-dependent transport of gamma-aminobutyric acid (GABA) . Can also mediate transport of beta-alanine, taurine and hypotaurine and is the major taurine transporter in hepatocytes .
Catalytic Activity: 4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chlo... |
Q9UN76 | MDKLKCPSFFKCREKEKVSASSENFHVGENDENQDRGNWSKKSDYLLSMIGYAVGLGNVWRFPYLTYSNGGGAFLIPYAIMLALAGLPLFFLECSLGQFASLGPVSVWRILPLFQGVGITMVLISIFVTIYYNVIIAYSLYYMFASFQSELPWKNCSSWSDKNCSRSPIVTHCNVSTVNKGIQEIIQMNKSWVDINNFTCINGSEIYQPGQLPSEQYWNKVALQRSSGMNETGVIVWYLALCLLLAWLIVGAALFKGIKSSGKVVYFTALFPYVVLLILLVRGATLEGASKGISYYIGAQSNFTKLKEAEVWKDAATQIF... | Function: Amino acid transporter that plays an important role in the absorption of amino acids in the intestinal tract. Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na(+)/Cl(-)-dependent manner . Transports non-alpha-amino acids such as beta-alanine with ... |
Q9H2J7 | MPKNSKVVKRELDDDVTESVKDLLSNEDAADDAFKTSELIVDGQEEKDTDVEEGSEVEDERPAWNSKLQYILAQVGFSVGLGNVWRFPYLCQKNGGGAYLLPYLILLMVIGIPLFFLELSVGQRIRRGSIGVWNYISPKLGGIGFASCVVCYFVALYYNVIIGWSLFYFSQSFQQPLPWDQCPLVKNASHTFVEPECEQSSATTYYWYREALNISSSISESGGLNWKMTICLLAAWVMVCLAMIKGIQSSGKIIYFSSLFPYVVLICFLIRAFLLNGSIDGIRHMFTPKLEIMLEPKVWREAATQVFFALGLGFGGVIAF... | Function: Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for the branched-chain amino acids, particularly leucine, valine and isoleucine and methionine. Can also transport low-affinity substrates such as alanine, phenylalanine, glutamine and pipecolic acid. Mediates the saturable, p... |
Q28001 | NVWRFPYLCQKNGGGAYLVPYLVLLIIIGIPLFFLELAVGQRIRRGSIGVWHYVCPRLGGIGFSSCIVCLFVGLYYNVIIGWSIFYFFKSFQYPLPWSECPVSRNGTVAVVEAECEKSSATTYFWYREALDISNSISESGGLNWKMTLCLLVAWRIVGMAVVKGIQSSGKVMYFSSLFPYVVLACFLVRGLLLRGAIDGILHMFTPKLDKMLDPQVWRDAATQIF | Function: Functions as a sodium-dependent vesicular transporter selective for proline, glycine, leucine and alanine. In contrast to other members of this neurotransmitter transporter family, does not appear to be chloride-dependent (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 2537... |
Q8I7T3 | MKSQKIGSMILLIGILLAIFNFAYSDDDIERFSINPEKPISFTSDQPGFPTSADFPIGSILANSFYSFGGDVNYFQLNISLMEEFSKDGNTGSQATWNQYTSVPVSPISSAVTANRVYTMSIGSLNRVKKGDITSMESTDFLNDEKYSSLVTTLNGGVSYGDDVFFLSSKSATGEAVLIHINDTATGTFGTSSYDEILLDAAINDPSSITVDSKLGLAFIGDSDGDILVFNMTLKAKIAIYSNSSIANLRSSGVVDEERQLLYICGQAGGMNSYITQVDIFHYSATDITLLHSFTILGSLCPSAGIDVKGGQLFFSTTTS... | Function: Involved in substrate adhesion, myosin-independent cytokinesis, organization of actin cytoskeleton, and phagocytosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104675
Sequence Length: 952
Subcellular Location: Cell membrane
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Q8ZL65 | MHKNGKFIPLLALGFTFFLSGCDYFADKHLVEEMKEQQKEQETKINLLEKQQKEQEAKINLLEKQQATIINTTKKVTEVVGRVERKQRLFDYTELDPSQTHYFIINNGNIGLAGRILSIEPIDNGSVIHLDLVNLLSIPVSNLAFNMTWGTKKPSEAKDLPRWKQLLLNTKMDSTIELLPGAWTNVTLTLKGVSPNNLKYLKIGIDMENVIFDSIQPINDTKKKPKK | Function: Required for proper surface expression of the autotransporter adhesin SadA. Could be directly involved in the biogenesis of functionally active SadA.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25906
Sequence Length: 227
Domain: The homotrimer is held together by an extended N-terminal coiled coil, wh... |
P76149 | MTITPATHAISINPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAEKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPIILAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIKDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH... | Function: Catalyzes the NAD(+)-dependent oxidation of succinate semialdehyde to succinate. It acts preferentially with NAD as cosubstrate but can also use NADP. Prevents the toxic accumulation of succinate semialdehyde (SSA) and plays an important role when arginine and putrescine are used as the sole nitrogen or carbo... |
Q8VY78 | MDGEELTEQETALYDRQIRVWGANAQRRLTKAHILVSGIKGTVAEFCKNIVLAGVGSVTLMDDRLANMEALNANFLIPPDENVYSGKTVAEICSDSLKDFNPMVRVSVEKGDLSMLGTDFFEQFDVVVIGYGSRATKKYVNEKCRKLKKRVAFYTVDCRDSCGEIFVDLQDYKYTKKKLEEMVECELNFPSFQEAISVPWKPIPRRTAKLYFAMRVIEVFEESEGRKHGECSLLDLARVLEIKKQLCEANSVSESHIPDILLERLITGTTEFPPVCAIVGGILAQEVIKAVSGKGDPLKNFFYYDGEDGKGVMEDISDSF... | Function: The dimeric enzyme acts as an E1 ligase for SUMO1 and SUMO2. It mediates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2. Functionally redundant with its paralog SAE1B.
Sequence Mass (Da): 36123
Sequence Length: 322
Pathway: Protein modification... |
A2VE14 | MVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASQVLLVGMKGLGAEIAKNLILAGVKGLTMLDHEQVSPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTENIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTKVAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCSVKEALEVDWSSDKAKAALKRTTPDYFLLQVLLKFRTDKGRDPSSDTFGEDSELLLQIRNDVLDALGVNPDLLPEDFVRYCFSEMAPVCAVVGGILAQEIVKALSQ... | Function: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2 (By similarity).
Sequence Mass (Da): 38306
Sequence... |
Q54WI4 | MTNPENTPMTTTNEGGKGLTEYEAKIYDRSIRLWGVDAQAKLRQSKVLFIGINGLMSEIIKNVVLAGVDSITLVDDHIITTSDLSAHLFINEDSVGKVISTESVFAISELNPLVTIDVYDKEIETMDDQFIKNYTMVVISDKNLNNVSKVNSLCRKNNVSFIFSHSFGLKGLFFSDLNEFKYFTKTTTEPPKTETHISIFKSFKESMGYDWSKTNSRTPLPFFALSTLYQFEEKHNRVPDNISDSDLSELKSIINSSIEKFNLKNTDSNKYFEETKDLLNKMNIEISPVCAIVGGIVGAEIIKIITQNMQVLNNFFFYDG... | Function: The dimeric enzyme acts as an E1 ligase for sumo. It mediates ATP-dependent activation of sumo and formation of a thioester with a conserved cysteine residue on sae2 (By similarity).
Sequence Mass (Da): 37227
Sequence Length: 330
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleu... |
Q9UBE0 | MVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTKVAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCPVKEALEVDWSSEKAKAALKRTTSDYFLLQVLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCFSEMAPVCAVVGGILAQEIVKALSQ... | Function: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.
Sequence Mass (Da): 38450
Sequence Length: 346
Pat... |
Q8JGT5 | MVEKEEAVISEEEAAQYDRQIRLWGLEAQKRLRTSRVLLVGMRGLGAEVAKNLILAGVKALTLLDHEQVSSEDSRAQFLIPSGSLGQNRAEASLNRARNLNPMVSVEADTENINQKSDDFFTQFDVVCLTSCPSDLLVRVNHICHKHNIKFFTGDVYGYHGSMFADLGEHEFVEEKAKVTKAKPLVEDGPEAKKAKIDPTETILVKKKVQFCPLKDALEIDWRSEKAKSALKKTPTDYFLLQVLMKFRTDKGRDPQPSSYQEDSELLLQICSDVLDSLGVSPDLLPKDFASYCFSEMAPVCAVVGGVLGQEIVKALSLRD... | Function: The heterodimer acts as an E1 ligase for sumo1, sumo2, and sumo3. It mediates ATP-dependent activation of sumo proteins followed by formation of a thioester bond between a sumo protein and a conserved active site cysteine residue on uba2/sae2 (By similarity).
Sequence Mass (Da): 38247
Sequence Length: 344
Pat... |
B1Y647 | MNAAVKALHENDYLVADLSLAAWGRKEIRIAETEMPGLMAIREEFAAKQPLKGARVTGSLHMTIQTAVLVETLQALGAQVRWASCNIFSTQDHAAAALAVQGTPVFAYKGETLADYWDYTHRIFEFGAAGTDGEGPNMILDDGGDATLLMHLGKRAEKDLSLLDNPKSEEETCLYAAIRAKLAVDPTWYSRKGAQIIGVTEETTTGVHRLKEMSAAGTLLFRAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVACVAGYGDVGKGSAQALRALSAQVWVTEIDPINALQAAMEGYKVVTMEYAADKADIFVT... | 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): 52057
Sequence Length: 477
Pathway: Amino-acid biosynthesis; L-homocystei... |
Q75FU8 | MSVTTQEKDLSYKVKDLSQAEWGRQEIILAEKEMPGLMALRQEYKGKKPLAGARIAGSLHMTIQTAVLIETLTELGAEVRWSSCNIFSTQDHAAAAIAKAGIPVFAWKGETEEEYWWCIEQTIFFGDKGPNMILDDGGDLTAYIHEKYPKLLSEIRGISEETTTGVKSLYKLLKKGELKVPAFNVNDSVTKSKFDNLYGCRESLADGIKRATDVMLAGKVALVCGFGDVGKGSAASLRNFGARVIVTEIDPICALQASMEGYQVLRVEDIIEQVDIVVTATGNDDIITLEHMKAMKDGAILCNIGHFDTEIQMSRLNNEK... | 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): 48233
Sequence Length: 436
Pathway: Amino-acid biosynthesis; L-homocystei... |
Q7TWW7 | MTGNLVTKNSLTPDVRNGIDFKIADLSLADFGRKELRIAEHEMPGLMSLRREYAEVQPLKGARISGSLHMTVQTAVLIETLTALGAEVRWASCNIFSTQDHAAAAVVVGPHGTPDEPKGVPVFAWKGETLEEYWWAAEQMLTWPDPDKPANMILDDGGDATMLVLRGMQYEKAGVVPPAEEDDPAEWKIFLNLLRTRFETDKDKWTKIAESVKGVTEETTTGVLRLYQFAAAGDLAFPAINVNDSVTKSKFDNKYGTRHSLIDGINRGTDALIGGKKVLICGYGDVGKGCAEAMKGQGARVSVTEIDPINALQAMMEGFD... | 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): 54338
Sequence Length: 495
Pathway: Amino-acid biosynthesis; L-homocystei... |
P50110 | MVKGSVHLWGKDGKASLISVDSIALVWFIKLCTSEEAKSMVAGLQIVFSNNTDLSSDGKLPVLILDNGTKVSGYVNIVQFLHKNICTSKYEKGTDYEEDLAIVRKKDRLLEYSLLNYVDVEISRLTDYQLFLNTKNYNEYTKKLFSKLLYFPMWYNTPLQLRSQARENCEEIIGSLTLEDDEEFVESKAMESASQLAQSKTFKIAHKNKIKGKQELQQVKYNLQFDNRLQSCVSNWLAARKKLDDSVILSSDLLFLANLYVQLGLPDGNRIRSKLEQTFGSELLNSMSNKIDDFVHRPSNNLEQRDPQFREQGNVVMSLY... | Function: Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.
Location Topology: Multi-pass membrane prot... |
Q08986 | MDILKRGNESDKFTKIETESTTIPNDSDRSGSLIRRMKDSFKQSNLHVIPEDLENSEQTEQEKIQWKLASQPYQKVLSQRHLTMIAIGGTLGTGLFIGLGYSLASGPAALLIGFLLVGTSMFCVVQSAAELSCQFPVSGSYATHVSRFIDESVGFTVATNYALAWLISFPSELIGCALTISYWNQTVNPAVWVAIFYVFIMVLNLFGVRGFAETEFALSIIKVIAIFIFIIIGIVLIAGGGPNSTGYIGAKYWHDPGAFAKPVFKNLCNTFVSAAFSFGGSELVLLTSTESKNISAISRAAKGTFWRIAIFYITTVVIIG... | Function: High-affinity S-adenosylmethionine permease, required for utilization of S-adenosylmethionine as a sulfur source.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64354
Sequence Length: 587
Subcellular Location: Membrane
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Q08985 | MARLPLKQFLADNPKKVLVLDGGQGTELENRGIKVANPVWSTIPFISESFWSDESSANRKIVKEMFNDFLNAGAEILMTTTYQTSYKSVSENTPIRTLSEYNNLLNRIVDFSRNCIGEDKYLIGCIGPWGAHICREFTGDYGAEPENIDFYQYFKPQLENFNKNDKLDLIGFETIPNIHELKAILSWDESILSRPFYIGLSVHEHGVLRDGTTMEEIAQVIKDLGDKINPNFSFLGINCVSFNQSPDILESLHQALPNMALLAYPNSGEVYDTEKKIWLPNSDKLNSWDTVVKQYISSGARIIGGCCRTSPKDIQEISAA... | Function: Homocysteine S-methyltransferase involved in the conversion of S-adenosylmethionine (AdoMet) to methionine to control the methionine/AdoMet ratio. Converts also S-methylmethionine (SMM) to methionine.
Catalytic Activity: L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-methionine
Sequence Mass (Da): 36669
... |
Q2HJ55 | MGTVHARSLEPLPASGPDFGALGEEAEFVEVEPEAKQEILENKDVVVQHVHFDGLGRTKDDIIMYEIRDVFKAKNLIEVMRKSHEAREKLLRLGIFRQVDVLIDTCQGDDALPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKLPNLLGRAEKVTFQFSYGTKETSYGLSFFKPQPGNFDRNFSVNLYKVTGQFPWSSLRETDRGVSAEYSFPTWKTSHTVKWEGVWRELGCLSRVASFAVRKESGHSLKSSLSHSMVIDSRNSSILPKRGALLKVNQELAGYTGGDVSFLKEDFELQLNKQLILDTVFSASLWG... | Function: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes. Required for the assembly of TOMM40 into the TOM complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52042
Sequence Length: 469
Do... |
P46576 | MSEKTFHKAQTIRAKASGVPSIVEAVQFHGVRITKNDALVKEVSELYRSKNLDELVHNSHLAARHLQEVGLMDNAVALIDTSPSSNEGYVVNFLVREPKSFTAGVKAGVSTNGDADVSLNAGKQSVGGRGEAINTQYTYTVKGDHCFNISAIKPFLGWQKYSNVSATLYRSLAHMPWNQSDVDENAAVLAYNGQLWNQKLLHQVKLNAIWRTLRATRDAAFSVREQAGHTLKFSLENAVAVDTRDRPILASRGILARFAQEYAGVFGDASFVKNTLDLQAAAPLPLGFILAASFQAKHLKGLGDREVHILDRCYLGGQQD... | Function: May play a role in the maintenance of the structure of mitochondrial cristae.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47127
Sequence Length: 434
Domain: Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane be... |
Q9V784 | MPKSGRDGGASKDSKYDLSKISARVDRVNVSGLLRTHNDYVMRAADGLFKASNFQDLMLEAMSTKSYLHELGIFKDVSVHIDVSRGADASPQGYEVTFKGNEMSRMMGSAGTEIGQNEGSLRTELTIPNILGRGENISLQGSYSSTRANDLQLKFWKPFFHTRFKENRPEMSFSIFRQTDRFDISSFQTTNIGYLVDFSAHTMVGVDLTHSLQYENAIRDVGLLNKSVPFAIRDHCGPKLASLLRYSVVYDNRDGNVFPTRGIYLKSVNEYCGLGGNVAYTSSTAHGELNVPLFAGLVAQFCARVGVVKETKNTTQLPIS... | Function: May play a role in the maintenance of the structure of mitochondrial cristae.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49059
Sequence Length: 443
Domain: Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane be... |
Q9Y512 | MGTVHARSLEPLPSSGPDFGGLGEEAEFVEVEPEAKQEILENKDVVVQHVHFDGLGRTKDDIIICEIGDVFKAKNLIEVMRKSHEAREKLLRLGIFRQVDVLIDTCQGDDALPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKLPNLLGRAEKVTFQFSYGTKETSYGLSFFKPRPGNFERNFSVNLYKVTGQFPWSSLRETDRGMSAEYSFPIWKTSHTVKWEGVWRELGCLSRTASFAVRKESGHSLKSSLSHAMVIDSRNSSILPRRGALLKVNQELAGYTGGDVSFIKEDFELQLNKQLIFDSVFSASFWG... | Function: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes . Required for the assembly of TOMM40 into the TOM complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51976
Sequence Length: 469
... |
Q8BGH2 | MGTVHARSLEPLPSSGTDFGALGEEAEFVEVEPEAKQEILENKDVVVQHVHFDGLGRTKDDIIICEIGEVFKAKNLIEVMRRSHEAREKLLRLGIFRQVDVLIDTCHGEDALPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKLPNLLGRAEKVTFQFSYGTKETSYGLSFFKPQPGNFERNFSVNLYKVTGQFPWSSLRETDRGVSAEYSFPLWKTSHTVKWEGVWRELGCLSRTASFAVRKESGHSLKSSLSHAMVIDSRNSSILPRRGALFKVNQELAGYTGGDVSFIKEDFELQLNKPLALDSVFSTSLWG... | Function: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes. Required for the assembly of TOMM40 into the TOM complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51864
Sequence Length: 469
Do... |
Q6AXV4 | MGTVHARSLEPLPSSGTDFGALGEEAEFVEVEPEAKQEILENKDVVVQHVHFDGLERTKDDIIICEIGEVFKAKNLIEVMRRSHEAREKLLRLGIFRQVDVLIDTCHGEDALPNGLDVTFEVTELRRLTGSYNTMVGNNEGSMVLGLKLPNLLGRAEKVTFQFSYGTKETSYGLSFFKPQPGNFEKNFSVNLYKVTGQFPWSSLRETDRGVSAEYSFPLCKTSHTVKWEGVWRELGCLARTASFAVRKESGHSLKSSLSHAMVIDSRNSSILPRRGALLKVNQELAGYTGGDVSFIKEDFELQLNKPLVLDSVFSTSLWG... | Function: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes. Required for the assembly of TOMM40 into the TOM complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51960
Sequence Length: 469
Do... |
Q10478 | MTEQFESTSFPSDIPAVNEESKLSAEETFKSLSEILAENSTLPVGISSIRVTGAHHTRPSFIRKVLKTCLDTSKPAKSRSLLETLNAIQETTGNLMAFNVYETANIKIDRASSSVSGDDDLDVTIQVKEKPRLYVETGTDVGNVEGNVHANVLARNVFGGAELLSGNVSYGTRNRSTMSVNFETPVNADPKTRLRFNGHSNLRDNKSISSHDLLTKGITLSLQHQDLWSGEHLLSQNLLWRQVTHLTEYASPSVRLEAGDSLKQSLSYTYTRDTRDHLMIPTKGDYVRQTLELAGFGFLPGDASFLKSEFWGQKAVALNS... | Function: May be required for the assembly pathway of mitochondrial outer membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51763
Sequence Length: 475
Domain: Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembra... |
P53969 | MTSSSGVDNEISLDSPMPIFNESSTLKPIRVAGVVTTGTDHIDPSVLQAYLDDTIMKSITLGQLVKNADVLNKRLCQHHIALNAKQSFHFQGNTYISDEKETHDVVPLMEVVSQLDILPPKTFTAKTGTNFGNDNDAEAYLQFEKLIDKKYLKLPTRVNLEILRGTKIHSSFLFNSYSSLSPQSILNLKVFSQFYNWNTNKGLDIGQRGARLSLRYEPLFLHKLLHNPHSNESPTLFHEWFLETCWRSTKICSQGTSAPYMYSGTMLSQAGDQLRTILGHTFVLDKRDHIMCPTKGSMLKWSNELSPGKHLKTQLELNSV... | Function: Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.
Location Topology: Multi-pass membrane prot... |
Q54Y14 | MFLVDWFYNMFLWLGFFKKEAKIVIIGLGNAGKTTLLHLLVTGSLKSHIPTLRPNAESFTYGNVNFKAYDLGGQQNLRFLWKQYVPDSKTIIVFMVDSSDYNSIIESKSEIHDILGDEHLSQSPLLILGSKCDAKGHHNRENLIDLLDIRRFELGLNNSNNVPFDLIMTSSITRYGITDMLNWLDKCTDIIKNN | Function: 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 (By similarity).
Location ... |
Q9Y6B6 | MSFIFDWIYSGFSSVLQFLGLYKKTGKLVFLGLDNAGKTTLLHMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHVQARRVWKNYLPAINGIVFLVDCADHERLLESKEELDSLMTDETIANVPILILGNKIDRPEAISEERLREMFGLYGQTTGKGSISLKELNARPLEVFMCSVLKRQGYGEGFRWMAQYID | Function: GTP-binding protein involved in transport from the endoplasmic reticulum to the Golgi apparatus (By similarity). Activated by the guanine nucleotide exchange factor PREB (By similarity). Involved in the selection of the protein cargo and the assembly of the COPII coat complex (By similarity). Synergizes with ... |
Q4WJS7 | MWIINWFYDILASLGLLNKHAKLLFLGLDNAGKTTLLHMLKNDRVATLQPTAHPTSEELAIGNNRFTTFDLGGHQQARRLWKDYFPEVSGIVFLVDAKDHERFPESKAELDALLAMEELAKVPFLILGNKIDHPDAVSEDELRHQLGLYQTTGKGKVPLEGIRPIEVFMCSVVMRQGYGEGIRWLSQYV | 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 control... |
P0C950 | MWLINWFYDLLASLGLLNKHAKLLFLGLDNAGKTTLLHMLKNDRVAILQPTAHPTSEELAIGNNRFTTFDLGGHQQARRLWKDYFPEVSGIVFLVDAKDHECFPESKAELDALLAMEELAKVPFLILGNKIDHPDAVSEDDVRHQLGLYQTTGKGKVPLEGIRPIEVFMCSVVMRQGYGEGIRWLSQYV | 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 control... |
Q59S78 | MWIFDWFQDILSSLGLWNKHAKLLFLGLDNAGKTTLLHMLKNDRLATLQPTLHPTSEELAIGSVRFTTFDLGGHQQARRLWKDYFPEVNGIVFLVDAADTERFAESKAELESLFRIEELSQVPFVILGNKIDVPTAVGEMELKNALGLYNTTGKDTGKLPEGTRPIEVFMVSVVMRSGYGEAFKWLSQYI | 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 control... |
Q55630 | MSSSSELGNASSVPLQFLLFIDDRPNSQDSVQEIGQCLTNLLDGHSHDLQILQISKHPHLVEHFRLVATPSLIKLQPEPRQVLAGSNIIQQLQKWWPRWQQELAMDPNPEDTGQSPSCPREISSVGYSGELMKMSDELFLLKKDKEELLQQIQFKDQILAMLAHDLRSPLTAASIAVDTLELLQHKPIEEQKPALRSQLLYQARKQFKIMDRLIEDILQASKNLNSQFQVHGRPLAIADLCQEVLELYQAKFSKKNLTITYDIPKDLPNVFADEELIRQVIANLLDNAIKYTPAHGSITVGALHRTTQKVQVSITDNGPG... | Function: Member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression. One of several clock output pathways. Participates in the Kai clock protein complex, the main circadian regulator in cyanobacteria, via its interaction with KaiC. KaiC enhances the autophosphorylation ac... |
Q8DMT2 | MKASADASSPQETTPPLSLLLFVANRPGDEEETAAIQAHIQQLPSNFSFELKVVPIGEQPYLLEEYKLVATPALIKVRPEPRQTLAGRKLLQKVDYWWPRWQREVALGLQADMQKSAAEQSDCSMELSRLKDELFQLRQERDRLAEQLQFKDRIISLLAHELRNPLTAGGIALETLESNLQEESSQQLPIEDIQRLFHHARSQTQTMGQLITDLLLAARGPQDKLQIMARQLDLRQLCQETVEDVRLNFERKKQHFTTDIPLDLPLVYGDGDRIRQVLVNLLDNACKYTPEGGKIHLSAFHRMTQKVQVTVSDTGPGIPI... | Function: Member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression. One of several clock output pathways. Participates in the Kai clock protein complex, the main circadian regulator in cyanobacteria, via its interaction with KaiC. KaiC enhances the autophosphorylation ac... |
P00633 | MDKVIARPYKRPNALCRLICFPWAGGNCSFFIRWCEAFSSIIVVSVIRLAGRECRDTEPFPEDMAEVVNEITNALLKDLQEKPFALFGHSFGSFVSYALAVHLKEKHGLEPVHMFFSGSYGPHSEYFHLMYKLPEVEDSRLLELIHTLGGTPPEFLQNEQITKHLLRVLKEDQKVLVTYPWHDVRKKYFSCDLTCFNGSDEKNHGSEAWIAITSGDTSIYSLPGNHFYLMEPSNETFLIKYITKCIENSDI | Function: In fatty acid biosynthesis chain termination and release of the free fatty acid product is achieved by hydrolysis of the thio ester by a thioesterase I, a component of the fatty acid synthetase complex. The chain length of the released fatty acid is usually C16. However, in the mammary glands of non-ruminant ... |
Q9NV23 | MERGDQPKRTRNENIFNCLYKNPEATFKLICFPWMGGGSTHFAKWGQDTHDLLEVHSLRLPGRESRVEEPLENDISQLVDEVVCALQPVIQDKPFAFFGHSMGSYIAFRTALGLKENNQPEPLHLFLSSATPVHSKAWHRIPKDDELSEEQISHYLMEFGGTPKHFAEAKEFVKQCSPIIRADLNIVRSCTSNVPSKAVLSCDLTCFVGSEDIAKDMEAWKDVTSGNAKIYQLPGGHFYLLDPANEKLIKNYIIKCLEVSSISNF | Function: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16).
Catalytic Activity: (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]
... |
Q9AST3 | MMSFVISDEFLGTFVPILVYWVYSGMYICLGSLDKYRLHSKIDEDEKNLVSKSAVVKGVLLQQTLQAIISVILFKITGSDADAATTQQFSILLLARQFIIAMLVIDTWQYFIHRYMHLNKFLYKHIHSQHHRLIVPYSYGALYNHPLEGLLLDTIGGALSFLFSGMSPRTAIFFFSFATIKTVDDHCGLWLPGNPFHIFFSNNSAYHDVHHQLYGTKYNFSQPFFVMWDRILGTYLPYSLEKRANGGFETRPIKVSKDE | Function: Involved in sphingolipid trihydroxy long-chain base (4-hydroxysphinganine) biosynthesis. Can use C18- and C20-sphinganine as substrates to produce C18- and C20-phytosphinganines (D-ribo-2-amino-1,3,4-trihydroxyoctadecane and -eicosane).
Catalytic Activity: a dihydroceramide + 2 Fe(II)-[cytochrome b5] + 2 H(+)... |
Q9SKB2 | MAVPTGSANLFLRPLILAVLSFLLLSSFVSSVEWLDIDSSDLKALQVIETELGVNSQRSSASDVNPCGRRGVFCERRHSATTGEYVLRVTRLVYRSRSLTGTISPVIGMLSELKELTLSNNQLVNAVPVDILSCKQLEVLDLRKNRFSGQIPGNFSSLSRLRILDLSSNKLSGNLNFLKNLRNLENLSVANNLFSGKIPEQIVSFHNLRFFDFSGNRYLEGPAPVMSSIKLQTSPHQTRHILAETPTSSPTNKPNNSTTSKAPKGAPKPGKLKKKKKKSKKKKVAAWILGFVVGAIGGTISGFVFSVLFKLIIQAIRGSE... | Function: Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Acting as a counterplayer of BIR1, promotes the activation of plant defense and cell death . Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity . Functions as an inhibitor/regulator of abs... |
Q2FE79 | MKNKYISKLLVGAATITLATMISNGEAKASENTQQTSTKHQTTQNNYVTDQQKAFYQVLHLKGITEEQRNQYIKTLREHPERAQEVFSESLKDSKNPDRRVAQQNAFYNVLKNDNLTEQEKNNYIAQIKENPDRSQQVWVESVQSSKAKERQNIENADKAIKDFQDNKAPHDKSAAYEANSKLPKDLRDKNNRFVEKVSIEKAIVRHDERVKSANDAISKLNEKDSIENRRLAQREVNKAPMDVKEHLQKQLDALVAQKDAEKKVAPKVEAPQIQSPQIEKPKVESPKVEVPQIQSPKVEVPQSKLLGYYQSLKDSFNYG... | Function: Plays a role in the inhibition of both the innate and adaptive immune responses. Possesses two N-terminal domains that bind the Fc region of IgG and two domains that form a tripartite complex with complement factors C3b and CFH. By recruiting CFH and C3b, the secreted form acts as a potent complement inhibito... |
Q84WV4 | MANLPKSSVNYPGTLTPLEPNRPSPQPDRTPVPHSPPVVASPIPPRFPQPSFRPDQMSSPSMKSPSLLSPANGIRTGSPIPRLSTPPGPPVFNTPVKPAAVPFRTSPATPQPMAYSSANSSLPVSTPSFYSNGSSVGSQRDLPDVVRMEEPIAADSPYVLFSANKVLKQKKLANVASLGFGAIVSAGREISPGPQIIQRDPHRCLNCGAYSNPYSSILIGSGQWQCVICENMNGSKGEYVASSKNELQNFPELSLPLVDYVQTGNKRPGFVPASDSRTSAPVVLVIDECLDEPHLQHLQSSLHAFVDSLPQTTRLGIILY... | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (By similarity). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By simila... |
Q7SZE5 | MATFQEFIQQNEDRDGVRFSWNVWPSSRLEATRMVVPVASLFTPLKERPDLPPIQYEPVLCSRATCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPTYAGISEVNQPAELLPQFSTIEYVVQRGPQMPLNFLYVVDTCMEDDDLQALKESLQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLNAKQLQEMLGLTKPAAAQAGRGPQQPQVPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVTQGKRPLRSLGVALSIAVGLLECTFPNTGARIMAFIGGPATQGPGMVVGDELKTPIRSWHDIEKDN... | Function: 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 for their transport to the... |
Q15436 | MTTYLEFIQQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCSRTTCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPSYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPLTQATRGPQVQQPPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDN... | Function: 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 for their transport to the... |
Q8H0S3 | MSEMASMDPEGIDGVRMTWNVWPRTKVEASKCVIPVAACISPIRYHRDIPSVEYAPLRCRICTAALNPFARVDFLAKIWICPICFQRNHFPPHYHVMSETNVPCELYPQYTTVEYTLPNPSQPTGVGNFDQTGAVSGQPSPSVFVFVLDTCMIEEEFGYAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSDLTKVYVFRGDKEISKDQVLEQLGLGASGRRNPVGGFPMGRDNSANFGYSGVNRFLLPASDCEFTIDLLLEELQTDQWPVQAGRRQSRCTGVAISVATGLLGACFPGTGARIVALIGGPCSEGPGT... | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (By similarity). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By simila... |
Q9SIJ7 | MAEFGELEAQDGVRMPWNIIPVATKKEQSIDSEVPVSAIYTPLKPLRSQSLLLPYSPLRCRTCRSVLNPYSVVDFSACNWGCPFCFNRNPFPLNYSSVADNNLPPELFPHSTTVEYLCDSFSSPSPPVFLFVVDTCLISEELDFLKSSLFQALDLLPDTSILGLITFDSLVRVYELGFPHCTKSYFFHGNKDCTKDQLLDQLSFFVKNPKPSSGVIAGARDGLSSDDIARFLLPASDCHFTLHSVLEELGNSPWPVAADHRPARCTGVALRIAASLLGACFPGSAARIMAFIGGPSTQGPGAIVSRELSDPIRSHKDIDK... | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (By similarity). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By simila... |
Q9ZQH3 | MAVRATVSRFPIDSDAQEASGLPWGLTVTPFAAKDENGIGPACGSNGHLLPRCENCYAYFNTYCELDQWAWNCSLCGTLNGLPSDAIARYSNPHSIPEMTSSFIDLEMPLDGSEEEMTQARPVYVAAIDISSSEEFLELTKSALLAALEALSPGALFGLVTFSHKIGLYDVQGPIPVVKNVFIPPDGESSLSLELEDVMPLLQFLAPVETCKDRIAAALETLRPITSWERSAGAGQGMDSVLMGGRGFGTAMEALFNYLGSEFGNTFALARVFAFLSGPPDYGRGQLDTSRYGEQYASKRVDADRALLPEQTPFYKDLAT... | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (By similarity). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By simila... |
Q9LUG1 | MAETANTDLEGIDGVRMTWNVWPHSKAEASKCVIPLAACISPIRRHADIPTLPYAPLRCRTCSAALNAYAQVDFTAKLWICPFCYQRNHFPPHYHVISETNLPGELYPQYTTVEYTLPPPVANGEGLVDPPVFVFVLDTCMIEEELDFAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSEMSKVFVFKGDKEISKDQILDQLGLGGSSRRGGSKGPQNGFPSSGLNRFLLPASECEFTLNSLLDELQSDQWPVKPGHRSQRCTGVALSVAAGLLGACLPGTGARIVALIGGPCTEGPGTIVSKDLSDPVRSHKDLD... | Function: 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 .
Location Topology: Peri... |
Q8VXX0 | MAEMADKAKVEEMDWEGIDGVRMTWNLWPRTKVEASKCVIPLAASISPIRRHPLILDLPYAPLDCKTCKALLNAFARVDFAAMNWVCPFCYHRNHFPSHYHSISEINLPGELYPQYTTVEYTLPPDPSRVPPPPVFVFVLDTCMIEEELGYAKSALKQAIGLLPENALVGFVSFGTQAHVHELGFSEMSKVFVFKGNKEVTKDQILDQLGLGSSSRRAPTSGFSKGAQNGFQSSGVDRFLLPASECEYTLDLLLDELQSDQWPVQPGHRPQRCTGVALSVAAGLLGACLPGTGARIVALVGGPCTEGPGTIISKDLSDPV... | Function: 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 .
Location Topology: Peri... |
Q84WI4 | MDFLELEAIEGLRWSWNSWPTTKSDCESLVVPLSIMYTPLMHFSELPTIPYDPLICSRCGAVLNPYARVDYQSRIWSCPFCFHKNLFPRSYSGITETNLPAELFPTYSAVEYSPLPSRQSGSNTTTPTAAASWSNGFNQGVRSMPSNSSFSSLASSTVGGGGGVISELGPAFVFVVDASMVEDELRAVRSDVLFVIEQLPENCLVALITFDSMVRVYDLGFSECSKVVVFHGERDLSPDQIQQFLGLGYSKQFHHGKMSAIRKQSFLLPLVECEFNLTSAFEEIIPLVDVKPGHRPHRSTGAAISTALGLLEGCSVTTGS... | Function: 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 .
Location Topology: Peri... |
Q38036 | MQESINGNLSEERISGAQQPEAWNGAPVNGSPEQQSASGAESNQLRFQSSLSDSERERQKATDLEHRRAAFARHFGCAPGSEKHVESYSSFDEKDTRVQLAEFYRFNDGHLKKWGYF | Function: Participates in the assembly of the viral procapsid in the cytoplasm. Forms first a 12S pre-assembly complex with protein H, and F and G pentamers, then twelve 12S complexes are joined by the D protein to form the procapsid. Internal scaffold protein B is released from the procapsid upon genome packaging. Aut... |
P03633 | MEQLTKNQAVATSQEAVQNQNEPQLRDENAHNDKSVHGVLNPTYQAGLRRDAVQPDIEAERKKRDEIEAGKSYCSRRFGGATCDDKSAQIYARFDKNDWRIQPAEFYRFHDAEVNTFGYF | Function: Participates in the assembly of the viral procapsid in the cytoplasm. Forms first a 12S pre-assembly complex with protein H, and F and G pentamers, then twelve 12S complexes are joined by the D protein to form the procapsid. Internal scaffold protein B is released from the procapsid upon genome packaging . Au... |
O36367 | MSRDSLFVAGFVDISTCPKEDPSLNLDAQTWSRYLPLSTSIPLTVEHFSEAQVGWVTGLFSVAQGLFCTAVITAGEFLELLDSLYLECTVAQHSPKADLPRNPRAEVLHSWLPELSLSSVHPDLLGTKDEPGQVFHHISLCALGRRRGTVAVYGDSLAWVLSRFQSLSRDDVAMIATNALTPPSQAPEFTVKLGLLFAKAIDAGFISNRISTLKLDRQAAGISPATYLKASAVPQKLETAAPLNQPEGADTLIDSTMSGPGAPPAPQDDLIPVPRSAFLNMLESTVSRTHPANGDAPALLPFGRYNMVQVPKGLTPYVRP... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
P54817 | MADAPDGGSADARVDAEPSALARASMPVYVGGYLALYGMGDEGELVLTREQVARALPPAAPLPINIDHASACEVGAVLALADDDAGLFFVGVINCPQLADTLAGVAHPAFFGADAPSLTPRERFLYLVSNYLPSVSLSSRRLAPDEEADGTLFAHVALCVLGRRVGTIVTYDATPDACVAPFRRLSPRARAALLANAEAARAALGDRAWPVPREALAQTLLSTAVNNMLVRDKWDTVSRRRREAGIAGHTYLQASAVFPLPTGGEGPERTGGRERAQKSAVAGGVCIALPVAGGRARQPELPPAPPPPPPPPAMSAAHQA... | Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interact... |
Q6AWX6 | MPLVRLQVRNVYGLGQKELHTKVDREDPKAILDDVAVSGLVGILRQLGDLTEFAAEIFHGIQEEVMITASRSNKLKMRLKQIEAKVPTIQKTVLAQTNHIHFAYTGGLEWHPRIPNVQNHFMYDELPPFIMTPYEDCREPPRLHLLDKFDINGPGSCLKRYSDPTHFKRASRASKPSEIKKKKSIQRGRDISRLASVANQSDRKTCTSLSFSGRTSTSKTASTIEIESKSDLQEHRSFSFDSRSGGEKPKRVSSSSRFTPGSRTIASVLSESESESDSPSQDLTARGSSSVSWHEKAEIVECNVLQCATDEAPEVMETNF... | Function: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. Regulates trichome branch positioning and expansion.
Sequence Mass (Da): 92090
Sequence Length: 821
Domain: Activates the Arp2/3 complex and binds actin through the C-terminal VCA (verprolin... |
Q6AZY7 | MKVRSAGGDGDALCVTEEDLAGDDEDMPTFPCTQKGRPGPRCSRCQKNLSLHTSVRILYLFLALLLVAVAVLASLVFRKVDSLSEDISLTQSIYDKKLVLMQKNLQGLDPKALNNCSFCHEAGQLGPEIRKLQEELEGIQKLLLAQEVQLDQTLQAQEVLSTTSRQISQEMGSCSFSIHQVNQSLGLFLAQVRGWQATTAGLDLSLKDLTQECYDVKAAVHQINFTVGQTSEWIHGIQRKTDEETLTLQKIVTDWQNYTRLFSGLRTTSTKTGEAVKNIQATLGASSQRISQNSESMHDLVLQVMGLQLQLDNISSFLDD... | Function: Seems to protect cells by scavenging oxidative molecules or harmful products of oxidation.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 65137
Sequence Length: 606
Subcellular Location: Endoplasmic reticulum membrane
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A5PJQ2 | MENKAMYLHATVSDRDSSSIFEEPFDGRSLSKLNLCEDGPCHKGRAGGCCTQLGSLSALKHAVLGLYLLVFLILVGIFILAVSRPRSSPDDLKALTRNVNRLNESFRDLQLRLLQAPLQGELSEQVWKAHDALQNQSDSLLALAGAVQRLEGALWGLQAQAAQSEQAVVLLRERAAQQSDAAQLELYQLQVDSNRSQLLLRRHAGLLDGLARRVGALSDELADVGGALRGLNLSLSYDVALQGTRLRDLRVLVSNASEDARRLRLAHRGLELQLKQELAVLNGVTEDLRLKDWEHSIALRNITLAKGPPGPKGDPGDAGK... | Function: Ferritin receptor that mediates non-transferrin-dependent delivery of iron. Mediates cellular uptake of ferritin-bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific... |
Q5RFW0 | MENRAMYLTTTHEDRENSSFYEESYDGMNLSKLNLCEEVNSTKYRRKTDNRCGQLDSLTSIKYAIVSLYILVLLTIFGLCIAVSKSHASWRREEALLENVTRLGEQSETLQMSLSQIPSQSDLLENIWKLESLFHNHTEQLRLLGLLTQGLERDIKDLQAFAEHTTDSVAQLWDHLSMISHSSQRNSTHLGDELASTAGSIREQDALLKTMVGNVETLQERLEDMGWTLQTLNHSLGGDVSLHQIKIYELQEKIVNVTHDTLGMKITQTHLEDQLRNEIQVLNVVTADLRLKEWEHSMALKNLTIFQGPPGPKGEKGDVG... | Function: Ferritin receptor that mediates non-transferrin-dependent delivery of iron. Mediates cellular uptake of ferritin-bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific... |
Q6ZMJ2 | MENKAMYLHTVSDCDTSSICEDSFDGRSLSKLNLCEDGPCHKRRASICCTQLGSLSALKHAVLGLYLLVFLILVGIFILAVSRPRSSPDDLKALTRNVNRLNESFRDLQLRLLQAPLQADLTEQVWKVQDALQNQSDSLLALAGAVQRLEGALWGLQAQAVQTEQAVALLRDRTGQQSDTAQLELYQLQVESNSSQLLLRRHAGLLDGLARRVGILGEELADVGGVLRGLNHSLSYDVALHRTRLQDLRVLVSNASEDTRRLRLAHVGMELQLKQELAMLNAVTEDLRLKDWEHSIALRNISLAKGPPGPKGDQGDEGKE... | Function: Ferritin receptor that mediates non-transferrin-dependent delivery of iron. Mediates cellular uptake of ferritin-bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific... |
Q7K5M0 | MSASHFREQLALCITLAVLAAASGDYRANMFLNGQYQNGIKDQKENNLLVNPSTNVFLNHAIISRQASPFQGPTYLPPKEFLKCAPGQQCVRSGQCLNGYFAQQLPKIQNCDPETTVCCTYRPPPTTTTTTTTSVPVANCAYDSDCVTPDNCRNGEISAINYVKKQGPNRCPAPNICCRIPSTTLTEDGYIFNLPEKTFPLPTKPAVLAMPSTQAPFRPQPTTAVPASRPTIEYLPPSTTQHPSYEKVQTSRRPVYLPPSPATESASSLIPKIRPRPEPRPQPTRRPTNEYLPPAAANEIPRFEPDRAPQPSNQKPIYRG... | Function: Inactive serine protease that plays a role in germ-band retraction and dorsal closure morphogenesis in embryogenesis; contributes to amnioserosa attachment and epithelial apico-basal polarity by regulating the localization of laminin LanA on the apical side of the amnioserosa epithelium . Contributes to epith... |
Q9L1E4 | MITTSLRRRTAAAVLSLSAVLATTAATAPGAAPAPSAAPAKAAPACPQFDDRTKAAADRGVDVDRITPEPVWRTTCGTLYRSDSRGPQVVFEEGFHAKDVQNGQYDVEKYVLVNQPSPYVSTSYDHDLYKTWYKSGYNYYVDAPGGIDVNKTIGDTHKWADQVEVAFPGGIQRKYIIGVCPVDRQTKTEIMSDCESNPHYQPWH | Function: ADP-ribosylates the N2 amino group of guanosine, deoxyguanosine, GMP, dGMP, cGMP, GTP and dGTP; oligo-guanosine, oligo-deoxyguanosine and tRNA are ADP-ribosylated less efficiently, while dsDNA is a very poor substrate . Also acts on GDP .
Catalytic Activity: guanosine + NAD(+) = H(+) + N(2)-(ADP-D-ribosyl)-gu... |
Q9UAC9 | MKTVIFLIVSSLLLIGVKTDNGYLLDKYTGCKVWCVINNESCNSECKIRGGYYGYCYFWKLACFCQGARKSELWNYNTNKCNGKL | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. It binds to distinct receptor sites of mammal and insect voltage-gated sodi... |
Q96I15 | MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGNPSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTSKGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDILAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAAELVTQNCEAYE... | Function: Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.
Catalytic Activity: AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine
Sequence Mass (Da): 48149
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 4.4.1.16
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Q68FT9 | MDVARNGARGSVESPPNRKVYMDYNATTPLEPEVIQAVTEAMKEAWGNPSSSYVAGRKAKDIINTARASLAKMIGGKPQDIIFTSGGTESNNLVIHSTVRCFHEQQTLQGRTVDQISPEEGTRPHFITCTVEHDSIRLPLEHLVEDQVAEVTFVPVSKVNGQVEVEDILAAVRPTTCLVTIMLANNETGVIMPISEISRRIKALNQIRAASGLPRVLVHTDAAQALGKRRVDVEDLGVDFLTIVGHKFYGPRIGALYVRGVGKLTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAADLVSENCETYEAHMRDIRDYLEE... | Function: Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.
Catalytic Activity: AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine
Sequence Mass (Da): 47256
Sequence Length: 432
Subcellular Location: Cytoplasm
EC: 4.4.1.16
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Q5U4Q9 | MADAESQNGENHLPHKIYLDYNATTPPATEVVKAVEEALREAWGNPSSSYTAGCKAKELIDTARAHVAKMVGGKPEDIIFTSGGTEANNMVLFSTVENFNSTSKERQNNRVALALPHIITSNVEHDSVALPLLHLQKTHRAEITFVPVSTVTGRIEVEDIISAVRPNTCLVSIMLANNETGVIMPVGELSQCLASMSKERSAQGLPKILLHTDAAQALGKVEVDVQELGVNYLTIVGHKFYGPRIGALYVRGLGQHSSLLPMLYGGGQERNFRPGTENTPMIAGLGKAAELVFLHCAVYEAHMRRIRDYLEERLEAVFED... | Function: Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.
Catalytic Activity: AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine
Sequence Mass (Da): 46993
Sequence Length: 431
Subcellular Location: Cytoplasm
EC: 4.4.1.16
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P45697 | MNYLVMISFALLLMTGVESVRDAYIAKPHNCVYECARNEYCNDLCTKNGAKSGYCQWVGKYGNGCWCIELPDNVPIRVPGKCHR | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels thereby blocking neuronal transmission. This toxin is active against both mammals and insects, and is classified as an alpha-like toxin. It is active on Nav1.2/SCN2A (EC(50)=139-25... |
Q6GPA8 | MSDKPNNFPPLPRFIPLKPCFYQDFDTDIPDLHRTTAKRLYYLWMLNSITLGVNLIGCLAWLIGGGSATNFGLAFLWLILFTPCSYVCWFRPIYKAFKTDSSFNFMAFFFTFTAQLVISIIQAVGIPGWGVCGWIASISFFGTNVGSAVVMLIPTIMFTAVAVLSFVALTKVHRFYRGAGGSLSKAQEEWTTGAWKNPHVQQAAQNAAFGATQGAMTQNEPQYSATPNYGYSNEM | Function: Required for the calcium-dependent exocytosis of signal sequence-containing cytokines. Probably acts in cooperation with the SNARE machinery (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26073
Sequence Length: 235
Subcellular Location: Cell membrane
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Q6NUK1 | MLRWLRDFVLPTAACQDAEQPTRYETLFQALDRNGDGVVDIGELQEGLRNLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDVDGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKIMMQVHGSKSDKMNIFGGFRQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGK... | Function: Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleo... |
O43819 | MLLLTRSPTAWHRLSQLKPRVLPGTLGGQALHLRSWLLSRQGPAETGGQGQPQGPGLRTRLLITGLFGAGLGGAWLALRAEKERLQQQKRTEALRQAAVGQGDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGLPPVQPVFITVDPERDDVEAMARYVQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQISDSVRRHMAAFRSVLS | Function: Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 . Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2... |
Q8VCL2 | MLLALGPKAWPKLSQFKPLLRISGGETLHRNSRHWAGQGQRQGPGLRTRLLITALFGAGLGWAWLAARAEKEQWRQQQRTEALRQAAVGQGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRKLEAEPDLPLVQPVFITVDPERDDVAAMARYVQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQIVESIRRHIAAFHSVLP | Function: Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/... |
P0C7I7 | MNQVARGAGAKRYADAKAALAGVVADGQTLAVGGFGLCGIPEALIAALRDSAVSGLTVISNNAGVDGFGLGQLLATRQIRKMISSYVGENKEFERQYLAGELELEFNPQGTLAERLRAGGAGIPAFYTATGYGTIVAYGKETREFDGKHYVLETALQADVALIKAWRADTAGNLVFRKTARNFNPACAMAGRVCIAEVEEIVELGAIDPDQVHLPGIYIDRLVLNATPEKRIEQRTVRQGDK | Catalytic Activity: a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate
Sequence Mass (Da): 25814
Sequence Length: 242
Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
EC: 2.8.3.5
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Q54JD9 | MLSRNLKTLVKNKNILYFTTSTSKSNKIYENAKEAVKDIPNGSKLLVGGFGLCGIPENLISAVRDTGVKDLTVVSNNAGVDDFGLGVLLKSRQIKRMISSYVGENATFESQYLKGELEVELTPQGNLAERLRAGGAGIPAFYTSTGVGTVLVEEGGFPIKYANDGSGKVEIKSEPRPTQLYNGRKYCLEESITGDYALIKAWKADTRGNLVFRNTARNFNPPMATAAKITIAEVEEIVDAGEIKPDEVHVPGIYIQRIVKGPSFEKRIERLTVQKEKTGEAAAKPKDEAAAKRERIVRRAALEFEDGMYCNLGIGMPTLA... | Function: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.
Catalytic Activity: a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-C... |
Q9W058 | MLCRLVGNRSLGARYTASIKAIACYSTSGKQRNGKIYESAIDAVADVQDGAQILFGGFGICGIPEKMINALKQKGVKNITGVSNNGGVDDTGLGVLIKQKQVSKVIGSYVGENTELVRQYLEGELAVELTPQGTLAEKIRAGGAGIPAFYTPTGYATLVQEGGAPIKYSKDGKVEISSEKKPVKEFNGKNYVMEESIFADFAFVKAQKADPLGNLVFNKAARNFNAPMCRAAKITVAEVEEIVPIGALSPDEIHVPGIYINRIFKGTNYNKRVERLRITEPKDPSKPAPPPNPAQVLRERIARRVALEFHDGMYANLGIG... | Function: Key enzyme for ketone body catabolism . Transfers the CoA moiety from succinate to acetoacetate . Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity).
Catalytic Activity: a 3-oxo acid + succinyl-C... |
Q8H780 | MSLTLEFLLLLIVLILSHHAHSGSIVKFLPGFEGPLPFELETGYIGIGEEEEVQLFYYFIKSEKNPEEDPLLLWLSGGPGCSSLTGLLFENGPVALKFEVYNGSVPSLVSTTYSWTKMANIIFLDQPVGSGFSYSRTPLVDKISDTGEVKRIYEFLQKWLSKHQQFFSNPFYVGGDSYSGMIVPPLVQEIGKGNYQINLQGYILGNPITDTESEQNYQIPYAHGMALISDELYKSMERICKGNYVKVDSLNTKCYKLIKDYQKCIHKLNKYHILLPDCDITSPDCFLYRYTLITFWANNKSVREALQVNKGSIGKWVQCN... | Function: Catalyzes the formation of 1,2-bis-O-sinapoyl beta-D-glucoside.
Catalytic Activity: 2 1-O-(trans-sinapoyl)-beta-D-glucose = 1,2-di-O-sinapoyl beta-D-glucose + D-glucose
Sequence Mass (Da): 49150
Sequence Length: 430
Subcellular Location: Secreted
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Q9C7D4 | MGSWIPKLLLLQLVLLLTKHADSSSIIKYLPGFEGPLPFELETGYIGVGEEDEDQMFYYFIKSESNPKTDPLLLWLSGGPGCSSFTGLIYENGPLGFKVEAYNGSIPTLVSTTYSWTKVANIIYLDQPVGTGFSYSRNPLADIPSDTGSAKRVDEFLRKWLTKHPEYFSNPFYAGGNSYSGKMVPVIVQEISNGNCIYGKPQIRLQGYVLGSPVTDYDLDRNSRIQFAHGMALISNELYESMKRTCGGNYIFVDPLNTECLELIKDYDNCVSGIYENLILVPKCDLTSPDCHSYRSMLSDYWANNESVRRALKVVEGTTG... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 49237
Sequence Length: 435
Subcellular Location: Secreted
EC: 3.4.16.-
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Q9C7D6 | MGKECYYLSWILKFHLLLVLIQLVDSGSTIRFLPGFQGPLPFELETGYIGVGEAEKDQMFYYFIKSESNPEKDPLLLWLSGGPFCSSFTALIYENGPIAFKAEEYNGSIPSLVSTTYAWTKVASILYLDQPVGTGFSYSRNPLADIPSDTGVAKPVNEFLHKWLDKHPEFLSNPLYVAGNSYSGIVIPTIVQEISNGNHLDSKPQINLQGFVLGNPATDTDIDLNSRIPFAHGKALISDEHYESLKRSCQGNYISVNPRNTKCLKLLEDFKKCVSGISEEYILKPDCMWLYSCMANLHSLSEYWANEKSVRKALLVNEGT... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 49505
Sequence Length: 437
Subcellular Location: Secreted
EC: 3.4.16.-
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Q9C7Z9 | MSKAWKLKLLLLLQLLLLSQHDVDSASVISYLPGFEGLLPFHLETGYIGVGEGEKVQLFYYFIKSENNPEEDPLIIWLTGGPACTALSALAFEIGPLTFKTEGYNGGLPSLVSTSYSWTKVASIIFLDQPVGTGYSYSTTPLSYKPSDTGEAKQTYEFLQKWLVENPQFVSNPIYVGGDSYAGIVVPAIVQQISIGNEHGYKPQINLKGYILGNPSTDLDSDHNSKIPYAHRMGLISDELYESLKRTCQGNYVKVDPTNTKCLKLMEDYGKCVSRINEGLILIALCDLASPNPYSGEHGGRSYLQTLVQSDLSLPTPDCY... | Function: Probable carboxypeptidase.
Sequence Mass (Da): 52300
Sequence Length: 464
Subcellular Location: Secreted
EC: 3.4.16.-
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Q8VZU3 | MRNLSFIVLFLLTLFFIHHLVDASLLVKSLPGFEGPLPFELETGYVSIGESGDVELFYYFVKSERNPENDPLMIWLTGGPGCSSICGLLFANGPLAFKGDEYNGTVPPLELTSFSWTKVANILYLEAPAGSGYSYAKTRRAFESSDTKQMHQIDQFLRSWFVKHPEFISNPFYVGGDSYSGKIVPGAVQQISLGNEKGLTPLINIQGYVLGNPVTDKNIETNYRVPFAHGMGLISDELFESLERSCGGKFFNVDPSNARCSNNLQAYDHCMSEIYSEHILLRNCKVDYVLADTPNIRTDRRRVMKEFSVNDSSSLPPPSC... | Function: Involved in plants secondary metabolism. Functions as acyltransferase to form the sinapate ester sinapoylcholine also known as sinapine. Able to convert in vitro benzoylglucose into benzoylcholine.
PTM: N-glycosylated.
Catalytic Activity: 1-O-(trans-sinapoyl)-beta-D-glucose + choline = D-glucose + O-sinapoylc... |
A0A0C3VJP4 | MEKVSLYACLILNLSLLVIFPYSKASQADKLNEFILSRKSQNPPKTLSWEEGDALKTLFSSAAYVAPPQEELRLADKIVTLPGQPYGVNFDQYSGYVTVDPETGRELFYYFVESPCNSSTKPLVLWLNGGPGCSSLGYGAFQELGPFRVNSDGKTLYRNPYAWNEVANVLFLESPAGIGFSYSNTTSDYDKSGDKSTAKDSYVFLINWLERFPQYKTRDFYISGESYAGHYVPQLASTILHNNKLYKNTIINLKGISLGNAWIDDATSLKGLYDNLWTHALNSDQTHELIEKYCDFTKQNYSAICTNAMNMSMIEKGKID... | Function: Carboxypeptidase that, together with KPI106, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis).
Sequence Mass (Da): 55297
Sequence Length: 495
Subcellular Location: Secreted
EC: 3.4.16.-
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P63019 | RDGYPLASNGCKFGCSGLGENNPTCNHVCEKKAGSDYGYCYAWTCYCEHVAEGTVLWGDSGTGPCRS | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin binds, in vitro, to sodium channels and inhibits the inactivation of the activated channels. Seems not toxic to mice, crickets a... |
H1ZZI2 | MKTLFLIITSFILLEVEGIKNGYPRDSKGCTFECGQDAKHGDDYCDKMCKTTLKGEGGDCDFEYAECWCDNIPDTVVTWKNKEPKCKQI | Function: Inhibits voltage-gated sodium channels (Nav).
Sequence Mass (Da): 10112
Sequence Length: 89
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0DUI1 | MNYFILLFVATFLLLDVNCKKDGYPVDANNCKFECWKNEYCDELCKAKRAESGYCYKLKLSCWCEGLPDDEPTKTSDRCYGTGR | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Is possibly toxic to mice .
Sequence Mass (Da): 9746
Sequence Length: 84
Domain: Has the structural arrangement of an alpha... |
A0A7S8MV32 | MKTLNFCLFLVIISSLTVRVFCLNDRFLTVNDNYVICLYINKSFVNCENLCKAYMNAKDGFCRQPHCFCTDVE | Function: Putative sodium channel toxin.
Sequence Mass (Da): 8517
Sequence Length: 73
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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P0C910 | GRDGYIVDTKNCVYHCYPPCDGLCKKNQAKSGSCGFLYPSGLACWCVALPENVPIKDPNDDCHK | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission.
Sequence Mass (Da): 7009
Sequence Length: 64
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets... |
P13488 | GRDGYIAQPENCVYHCFPGSSGCDTLCKEKGATSGHCGFLPGSGVACWCDNLPNKVPIVVGGEKCH | Function: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. As it competes neither with the classical alpha-toxin AaH2 nor the beta-toxin Css2, this toxin is an alpha-like toxin.
Sequence Mass (Da): ... |
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