ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q5QGT7 | MCTSLTTCEWKKVFYEKMEVAKPADSWELIIDPNLKPSELAPGWKQYLEQHASGRFHCSWCWHTWQSAHVVILFHMFLDRAQRAGSVRMRVFKQLCYECGTARLDESSMLEENIEGLVDNLITSLREQCYEEDGGQYRIHVASRPDSGPHRAEFCEACQEGIVHWKPSEKLLEEEVTTYTSEASKPRAQAGSGYNFLSLRWCLFWASLCLLVVYLQFSFLSPAFF | Function: Specifically promotes functional cell surface expression of olfactory receptors, but not of other GPCRs.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 26068
Sequence Length: 225
Subcellular Location: Cell membrane
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Q9BQQ7 | MAGDTEVWKQMFQELMREVKPWHRWTLRPDKGLLPNVLKPGWMQYQQWTFARFQCSSCSRNWASAQVLVLFHMNWSEEKSRGQVKMRVFTQRCKKCPQPLFEDPEFTQENISRILKNLVFRILKKCYRGRFQLIEEVPMIKDISLEGPHNSDNCEACLQGFCAGPIQVTSLPPSQTPRVHSIYKVEEVVKPWASGENVYSYACQNHICRNLSIFCCCVILIVIVVIVVKTAI | Function: Promotes functional cell surface expression of the bitter taste receptors TAS2R16 and TAS2R43.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 27031
Sequence Length: 232
Subcellular Location: Membrane
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Q5QGU6 | MMEEDIGDTEQWRHVFQELMQEVKPWHKWTLIPDKNLLPNVLKPGWTQYQQKTFARFHCPSCSRSWASGRVLIVFHMRWCEKKAKGWVKMRVFAQRCNQCPEPPFATPEVTWDNISRILNNLLFQILKKCYKEGFKQMGEIPLLGNTSLEGPHDSSNCEACLLGFCAQNDLGQASKPPAPPLSPTSSKSAREPKVTVTCSNISSSRPSSKVQMPQASKVNPQASNPTKNDPKVSCTSKPPAPPLSPTSLKSAREPKVTVTCSNISSSRPSSKVQMPQASKVNPQTSNPTKNDPKISCTSKPSTTPRLTIQQLSVVSPPAP... | Function: Promotes functional cell surface expression of the bitter taste receptors TAS2R16 and TAS2R43.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 52220
Sequence Length: 474
Subcellular Location: Membrane
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Q96DX8 | MVVDFWTWEQTFQELIQEAKPRATWTLKLDGNLQLDCLAQGWKQYQQRAFGWFRCSSCQRSWASAQVQILCHTYWEHWTSQGQVRMRLFGQRCQKCSWSQYEMPEFSSDSTMRILSNLVQHILKKYYGNGTRKSPEMPVILEVSLEGSHDTANCEACTLGICGQGLKSCMTKPSKSLLPHLKTGNSSPGIGAVYLANQAKNQSAEAKEAKGSGYEKLGPSRDPDPLNICVFILLLVFIVVKCFTSE | Function: Probable chaperone protein which facilitates trafficking and functional cell surface expression of some G-protein coupled receptors (GPCRs). Promotes functional expression of the bitter taste receptor TAS2R16 . Also promotes functional expression of the opioid receptor heterodimer OPRD1-OPRM1 (By similarity).... |
Q9ER80 | MLFPDDFSTWEQTFQELMQEEKPGAKWSLHLDKNIVPDGAALGWRQHQQTVLGRFQCSRCCRSWTSAQVMILCHMYPDTLKSQGQARMRIFGQKCQKCFGCQFETPKFSTEIIKRILNNLVNYILQRYYGHRKIALTSNASLGEKVTLDGPHDTRNCEACSLNSHGRCALAHKVKPPRSPSPLPKSSSPSKSCPPPPQTRNTDFGNKTFQDFGNRTFQGCREPPQREIEPPLFLFLSIAAFALFSLFTR | Function: Probable chaperone protein which facilitates trafficking and functional cell surface expression of some G-protein coupled receptors (GPCRs). Promotes functional expression of the bitter taste receptor TAS2R16 (By similarity). Also promotes functional expression of the opioid receptor heterodimer OPRD1-OPRM1 .... |
Q0VTA9 | MKKWECVVCGFIYDEAEGLPDEGIEPGTAWNNVPEDWVCPDCGVGKDDFEMVEI | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.
Sequence Mass (Da): 6067
Sequence Length: 54
Pathway: Hydrocarbon metabolism; alkane degradation.
Subce... |
P04170 | MQKYVCNVCGYEYDPAEHDNVPFDQLPDDWCCPVCGVSKDQFSPA | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Sequence Mass (Da): 5115
Sequence Length: 45
Subcellular Location: Cyt... |
P12692 | MSRYQCPDCQYIYDENKGEPHEGFHPNTSWNDIPKDWACPDCAVRDKVDFIFLADSPSKETQLGVNSQLANSESGISDATPTGMAVLAAELVIPLNQENKNEGCAAKTEVLDQASTPQVVRKSSTRKKMRNK | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Not known. Probably involved in an electron transport pathway, but not required for the hydrocarbon hydroxylating system. Seems to be non-functional.
Sequence Mass (Da): 14619
Sequence Length: 132
Pathway: Hydrocarbon metabolism; alkane degradation.
Subcellular Locati... |
C5CN80 | MSTPARNTTLTSNTPAGAPRLPGAPAPQVLPARPEPLALHASDSALIVVDMQNAYASMGGYVDSAGFDISGAQGTIANIARTIAAARTAGMLVVFLQNGWDAAYVEAGGPGSPNWHKSNALKTMRARPELAGKFLAKGGWDYELIAEMKPQPGDIVVPKTRYSGFFNSTLDSTLRARGIRHLVFTGIATNVCVESTLRDAFHLEYFAVMLEDATHELGGAAIQKASVYNVETFFGWVSTVDDFVRSFAPATA | Function: Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
Catalytic Activity: (Z)-3-ureidoacrylate + H(+) + H2O = (Z)-3-aminoacrylate + CO2 + NH4(+)
Se... |
A1JMX8 | MILNARPEPIAFPTSASALIVVDMQNAYASEGGYLDLAGFDVSATAPIITNIKRAITAARAAGIQVIFFQNGWDPQYVEAGGEGSPNWHKSNALKTMRKQPELMGKLLAKGDWDYALVDELQPQAGDIVIAKPRYSGFFNTQLDSILRAKGIHHLIFTGIATNVCVESTLRDGFFFEYFGVVLEDATHQAGPDFAQKAALYNIETFFGWVSDVETFCNCIAPSAQLSQSA | Function: Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
Catalytic Activity: (Z)-3-ureidoacrylate + H(+) + H2O = (Z)-3-aminoacrylate + CO2 + NH4(+)
Se... |
Q9A4N4 | MPKTVITPPGTQTPIAPFSPGTLADGIVYVSGTLAFDKDNNVAFPGDAEAQTRQVLETIKSVIETAGGTMEDVTMNHIFLTDWVHYAPMNKVYAEYFPGDKPARYCIQCGLVKPGFVVEIASVAHIGKT | Function: Involved in pyrimidine catabolism. Catalyzes the deamination of 3-aminoacrylate to malonic semialdehyde, a reaction that can also occur spontaneously. RutC may facilitate the reaction and modulate the metabolic fitness, rather than catalyzing essential functions.
Catalytic Activity: (Z)-3-aminoacrylate + H(+)... |
C8U5H2 | MPKSVIIPAGSSAPLAPFVPGTLADGVVYVSGTLAFDQHNNVLFADDPKAQTRHVLETIRKVIETAGGTMADVTFNSIFITDWKNYAAINEIYAEFFPGDKPARFCIQCGLVKPDALVEIATIAHIAK | Function: Involved in pyrimidine catabolism. Catalyzes the deamination of 3-aminoacrylate to malonic semialdehyde, a reaction that can also occur spontaneously. RutC may facilitate the reaction and modulate the metabolic fitness, rather than catalyzing essential functions.
Catalytic Activity: (Z)-3-aminoacrylate + H(+)... |
Q8XAV0 | MNIVDQQTFRDAMSCMGAAVNIITTDGPAGRAGFTASAVCSVTDTPPTLLVCLNRGASVWPVFNENRTLCVNTLSAGQEPLSNLFGGKTPMEHRFAAARWQNGVTGCPQLEEALVSFDCRISQVVSVGTHDILFCAIEAIHRHATPYGLVWFDRSYHALMRPAC | Function: Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway.
Catalytic Activity: FMNH2 + NAD(+) = FMN + 2 H(+) + NADH
Sequence Mass (Da): 17760
Sequence Length: 164
EC: 1.5.1.42
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B9KKV6 | MIGKVAGILDFRGPDHVLIDVRGVGYIVYVSDRTLASMPGLGEAVALYTELVVREDLLQLFGFPTMIEKEWHRLLMTVQGVGAKAGMAILGALGAEGTARAITLGDARSIQAAPGIGPKIAQRVVLELKSKAPALMAMGGGTAALAPSEPPEPQPGTSSGSRRKTRAPEPPRPSHTADALSALANLGYQPTDAAQAVAQAAGESPDADTAALIRAALKLLAPKS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A9WA87 | MIASIRGIIQSIGIDHLIVETGGVGLLIYAPRSTLNAVGQIGSETFLYTLLIVREDALTLYGFSDPAQRNLFEQLIGVSGVGPKIALNLLSSGSPDEIQKSIAGGDIARLARVPGIGKKTAERIVLELRGKIDLRQLSGTTPGNVSTLDRELTDILISLGYSATEAAAAIAALPGDAPPTLEERLRLALRYFGSA | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q5L6Z3 | MYDYIRGVLTYISSSTMVIESQGLGFSIFAPERWLIELSSQLHRELIVYTYTVVRETEHVLYGFHTRGERECFRMLISFSGVGPKTGLAILNTFSLSQLCSIARAEDIKAIASVPGIGKKTAEKLMVDLKQKLADLLPLDAQILASWEPAKPSCMEEGIQALAALGYPKSSAERMIAEAMSELPDHASVAEILPIALKKNLQGLNKI | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
B3QVA9 | MLSYLSGTLIEKFSTEIVVEVNGVGYLLNISATTHEKLPAIGNQIKILTYLYVREDALQLYGFITTEDREVFKLLIAISGVGPKLAQTILSGMSTAQLRESVIAGDTKALTAIAGVGKKTAERIILELKDKLVKLDLKIDIKETAFRSDKQQVRNDAYSALISLGFTKSIAEKAMRAAIAEVPDGSVDDLIRVALRHVQS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
P66745 | MIASVRGEVLEVALDHVVIEAAGVGYRVNATPATLATLRQGTEARLITAMIVREDSMTLYGFPDGETRDLFLTLLSVSGVGPRLAMAALAVHDAPALRQVLADGNVAALTRVPGIGKRGAERMVLELRDKVGVAATGGALSTNGHAVRSPVVEALVGLGFAAKQAEEATDTVLAANHDATTSSALRSALSLLGKAR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q7NAN2 | MITSVYAKIEYVTNTKMLFVANNWGYWVNVKPNSGFSRTDNNVLVFLHELTFLAQNNAINKELYAFKSLKEKEWFKALLTINGIGPKTAMNVMVNKQEEVLTLIKNNDLNGLLRLENINKKVATMLLASDIASKHYLKNQIVVSDKVEPQIDDDEKIDDSKDLNDDELLSEIVIEAIDCLISLGYKQEQIKTALAEIDLKNESINDSADLVAVIIKQIGLRTSEVS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q49424 | MITSIFGKVTFVGKRKIIVEHNWISYWFNTKENHKFEKNLEKNKQIFCHIIKKIVANQIIEEAFAFNTLEEKEWFCRLIELNGIGSKTALNLLNNDLEEIKQYILENNYSALCGINGVNNKIARALLSLEIFEKSENNKNIKGVQVADGYDELFETLKSLGYKQQEIQDALKMIEVKPDFDISQLVAEVIKLMSFKNNEITNKTA | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q6MT68 | MNDYINGLLHKIDDKYLYIELNNSGYRFLYLKTDLKDLKLNQNNQVYVAINVIDNVFKYYGFKNQLIRDLFELLININTIGEKTAFLILENYNYNELIDIFKNGRTDKILQLKGIGNYTARLIINSVQKELFNNKISDKKNKVITSLEKLGYKTKDIYKIIINIDEDMNIEDLTKYVLEQLSYLHN | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q98PR2 | MLLYRLGKIIHVNKKYIIFESDSAGYTINITRAENFEKDRTLKLYIYELSNEYQKTLYGFTHFKERVLFEDLISINGIGPRIALILLNDGWEKIASLIANGNWETLSRYPYINVKNCHQIIFELQNKWAKFLEKDEKVPSANIQNISDATETLKMLGFKREQIKYALESANLQDDVETLVENAIKKISTVNGKEARN | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q4A6N7 | MTLYKIGEIVYKNNNNIILESKGEGNLVTICDNSRYSKGEKLKLYLYEVKNDYIQQTYGFKTFKERLLFTDLISIDKIGPKTAMLILDQNWELVANLIAEGDWKEISKINYISDKSAKLICVELKDKWAKIIQNKEVKKFDDITNIKELKQTLNKLGFKASDIDYAVNNISSTKELDLMVEESINLITTQMHANNQTT | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q4L6Y7 | MYAYIRGKLTQLFPTHVVVESINGVGYEIQTPNSYRFQKYLEKELVIYTSLIVREDAQLLYGFINEEEKDMFLSLIKVTGIGPKSALAILATSTPNEVKMAIENENDAYLTKFPGIGKKTARQIVLDLKGKVQITRETTETLLSMNEENSNSENLVKEALLALEALGYSKREISKVEKVLNKSTFDSVDEAVKLGLKTLVS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q46IJ6 | MAIVSSITNHSSLPNDKGEERLVGPSLLKEELKLSQQDSLRPKSFDDFVGQSELKKVLEISVKASLKRGEALDHLMLYGPPGLGKTTMALVIAEELGVKARVTSAPALERPRDIVGLLINIQPRELIFVDEIHRLNRISQELLYPAMEDRRLDLTVGKGTSSRMRSIEIPPFTLVGATTKPAALSSPMRDRFGITQRLDFYNYLDLENIIKRSAKLINLVISEEASQQLAKRCRGTPRIANRLIRRVRDYAEVYSHSKKIDVEVVNDALDLHRVDQRGLDATDRSYIGLLVNQYQGGPVGLETLAAGLGEDSTTLETVVE... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0LGY6 | MTERIVEPKPHEDDLPVENSLRPRRLDEYVGQQTVKENLAVFIEAARQRAEPLDHVLFHGFPGLGKTSLATVISNELGVNMRSTSGPVIERAGDLAAILTNLEQGDVLFIDEIHRLNHVVEEILYPAMEDFQLDIIIGQGPSARTIKLDLPPFTLVGATTRAGLLSPPLRDRFGVTLRLEFYKVDELKLIVTRSARILGIRVDAEGALEIAKRSRGTPRIANRLLRRVRDYAEVRADGRITREVADLALRMLDVDEKGFDGMDRKILSTIIEKYDGGPVGIETLSAAVSEERDTLEDVYEPYLIQEGFLNKTPRGRLATR... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A5GI46 | MAIVSSNAASQRPRPDRGPDRVPNRVVDGARQAEDDRDPGRVGAKEDSLRPKRLADYIGQRELKQVLGIAVQAAVGRGEALDHVLLYGPPGLGKTTMAMVLAEELGVTCRITSAPALERPRDIVGLLVTLQPKDLLFIDEIHRLSRVAEELLYPAMEDRRLDLTVGKGSTARTRALDLPPFTLVGATTRAGALSSPLRDRFGLIQRLEFYGLEDLQAIVERAAGLLDLDLSAAACTEIARRCRGTPRIANRLLRRVRDVACVRACAGRIDQALVDEALTLHRVDGRGLDASDRRLMELLLQSHGGGPAGLDTLAAALGED... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q57396 | MAIKRSGNNNLSPNVKSDLLSPEVIPQERSTSPELEQQEASLRPQRLADYIGQRDLKEVLRIAIQAAQGRQEAIDHLLLYGPPGLGKTTLALILAEEMQVRCKITAAPALERPRDITGLLLALQPGDILFIDEIHRLNRLTEELLYPAMEDFRLDITMGKGQSAKVRSLKLAHFTLVGATTKVGSLTSPLRDRFGLIQRLRFYEVDELQQIILRTAGILSVSISPTGAEAIAMRARGTPRIANRLLKRVRDYAQVKQQPEIDPALASEALDLYQVDKRGLDWTDRLVLQTLIEQFQGGPTGLEAIAAATGEDAKTIEEVY... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q47N43 | MSEHDRELVSPEAALDDHAVESALRPRTLDEFVGQDRVREQLSLVLRSAQQRGTAPDHILMSGGPGLGKTTLAMIIAAELGAPLRITSGPAIERSGDLAAVLSTLREGEVLFLDEIHRMARPAEEMLYVAMEDFRVDVMVGKGPGATAIPLEIAPFTLVGATTRAGMLPAPLRDRFGFVAHMDFYSPEELELILHRSARLLGIELLDDAAAEIARRSRGTPRIANRLLRRVRDYAQVRGDGRLTLECARAALSLYEVDDEGLDRLDRAVLDALLRRFRGGPVGLSTLAVSVGEEPETVEIVAEPFLVRAGFIARTPRGRV... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q56313 | MSEFLTPERTVYDSGVQFLRPKSLDEFIGQENVKKKLSLALEAAKMRGEVLDHVLLAGPPGLGKTTLAHIIASELQTNIHVTSGPVLVKQGDMAAILTSLERGDVLFIDEIHRLNKAVEELLYSAIEDFQIDIMIGKGPSAKSIRIDIQPFTLVGATTRSGLLSSPLRSRFGIILELDFYTVKELKEIIKRAASLMDVEIEDAAAEMIAKRSRGTPRIAIRLTKRVRDMLTVVKADRINTDIVLKTMEVLNIDDEGLDEFDRKILKTIIEIYRGGPVGLNALAASLGVEADTLSEVYEPYLLQAGFLARTPRGRIVTEKA... | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
Q3Z9B2 | MRILGIDPGTMVVGYGVIEAADDELSLIGFSSLTPPASAPIPQRLAYIYKGLVEVIELYQPDEVAVESPFADKNIKSALAIGKAQAVALLAAANHSLSVTEYSPACIKSRVSGSGTASKEQIQEMVRLLLNLAEIPQPNDAADALAVAICHHSHRAFANITSQGD | 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... |
Q9RX75 | MRVLGIDPGLANLGLGLVEGDVRRAKHLYHVCLTTESAWLMPRRLQYLHEELTRLLTEYRPDAVAIEDQILRRQADVAFKVGQAFGVVQLACAQAGVPIHAYGPMQVKKSLVGTGRADKEQVIYMVKASLGIRELFNNHAADALALALTHLAHAPMQERSERLAAAGRAARTGDAPLRR | Cofactor: In vitro only Mn(2+) supports endonuclease activity; Mg(2+) inhibits binding to HJ DNA . Another study shows Mn(2+) is the preferred cofactor but Mg(2+) does support cleavage . Binds 2 Mn(2+) ion per subunit (By similarity).
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during gene... |
B8FQV7 | MLILGIDPGTAIMGYGLIEKKGNRLFPVDYACWRTPAHTPMPERLLMLYHEIEAYIKEKQPHHVAVEELFFNRNTTTAISVGQARGVVLLAAAQCGLPVYEYTPLQVKQAVAGYGRADKQQIQQMVRALLGLQEIPKPDDTADALAIAICHAHSVNLLNRMGGAL | 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... |
Q729U1 | MAASVTVIGIDPGSQCTGWGIVREASGVLTLVDCGAIRPKGGDFAARLGDLYRQLADVVRAHTPDEAAVEDVHAAQNVATALKLGQARGVVVAACAAHGVPVIDYRPSVIKKALVGTGRAEKEQVGYMVGQVLGVRPDWKLDTGDALAAAICHLNQRRLTRLAGLA | 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... |
B8E2P3 | MVVIGFDPGTAITGYGILNKGEDGISIIEYGALTTPSGWGIGRRLNYLFDQVSSLLDLYNPDVVVMENIFFNKNIKTAINIGQAQGVIILAAEQHQKEISILTPLEVKLSVVGYGRATKNQIQYMVKEILKLKDIPKPDDVADALALCISYIYKQEGC | 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... |
B7USP0 | MAIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQMSESRLNLARGRLR | 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... |
Q2RZ65 | MIILGVDPGSRATGYGLVDPSGGDEHLVAADTIRLADTDDHPTRLKQIYDALVDVIDAHGPDEFAVEMPVYGQNPQSMLKLGRAQAAAMMAALNRDLPVAQYTPKEVKKSVTGNGNASKKQVGFMIESILSAREQTFAHDTADALAIALCHGNRDAHDDGDSYTGWASFVDANPDRVSE | 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... |
Q91ZZ5 | MWLLLHVILLTEVKDFALADSSMVAPLCPKGYFPCGNLTKCLPRAFHCDGVDDCGNGADEDNCGDTSGWTTIFGTVHGNVNKVTLTQECFLSQYPQHCYCRENELECVKADLKAVPKVSSNVTLLSLKKNKIHRLPVKVFSRYTELRKIYLQHNCITHISRRAFLGLHNLQILYLSHNCITSLRPGIFKDLHQLAWLILDDNPITRISQKSFMGLNSLFFLSMVGNRLEALPETLCAQMPQLNWVDLANNGIKYITNSTFLTCDSLTVLFLPRNQIGFVPEKTFSSLKNLGELDLSSNMITKLPVHLFSDLHLLQKLNLS... | Function: Receptor for relaxin. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. May also be a receptor for Leydig insulin-like peptide (INSL3) (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82934
Sequence L... |
M4BMH6 | MQSILWFALIASVVFLVLVDLASGLNGLETLSSGADVDELTTATRLLRAAHLDRKLSEERAFISGESIGSWWTKVTEWLRVKFELIIAYIKQLRVKSNDVKDDAATNDAAHAKDDAAANKAARAKDDASRATYEAARANYEAARAYDDATRAQDVAALEAARAIEATDIAAYTGANAEYEQSMFLNGFVKTIDLHNEKNAPIMTRLNKSLDEAKKSSTFREIADGVNESKVALVVHEKQDGYLLWILHLKWAVEAKSPKDVVERILKDLGTHDVPHLQERAEQVKKAYTIFLLYVERMSRATHPK | Function: Secreted effector that confers enhanced plant susceptibility during both compatible and incompatible interactions between the pathogen and its host . Promotes the sexual reproduction of the pathogen in the plant host .
Sequence Mass (Da): 33946
Sequence Length: 305
Domain: The RxLR-dEER motif is required for ... |
M4C319 | MRLDILLFTLSSSTSLALSYSLPMDPAHSSVHTLSAADRHIGERVTRQRHLREEPANEARNYSDLAVEIKRLVEELDSRVLEQADISLLDRHYAGDYKAFRSDLMTYGYQTRFAEQYKLFKKLGIDFKHNY | Function: Secreted effector that suppresses callose deposition, a hallmark of pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) and renders host plants more susceptible to bacterial infection . Reduces host plant responsiveness to salicylic acid (SA) in haustoriated cells into which host-translocate... |
Q69KL9 | MARVYVGNLDPRVTARELEDEFRVFGVLRSVWVARKPPGFAFIDFDDRRDAQDAIRDIDGKNGWRVELSRNASSGRGGRDRYGSSESKCYECGETGHFARECRLRIGSGGLGSGRRRSRSRSRSRSPRYRRSPSYGRRSYSPAGRSPRRRSVSPARARSYSRSPQYNRGRDESPAYDNGYRRSRS | Function: Involved in pre-mRNA splicing.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 21183
Sequence Length: 185
Subcellular Location: Nucleus
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Q9SJA6 | MSRVYVGNLDPRVTERELEDEFRSFGVIRSVWVARRPPGYAFLDFEDSRDARDAIREVDGKNGWRVEQSHNRGGGGGRGGGRGGGDGGRGRGGSDLKCYECGESGHFARECRSRGGSGGRRRSRSRSRSPPRYRKSPTYGGRRSYSPRARSPPPPRRRSPSPRGRNYSRSPPPYRARDEVPYANGNGLKDVRRSRS | Function: Probably involved in intron recognition and spliceosome assembly.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 21915
Sequence Length: 196
Subcellular Location: Nucleus
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Q94AK4 | MSSIRNTHWCHRCQRAVWLRARDAVCSYCGGGFVEEIDIGPSRAHRDVERDPTFDLMEAFSAFMRSRLAERSYDREISGRLGSAGSESFSNLAPLLIFGGQAPFRLAGGDNSSVEAFVNGAAPGIGIARGTNAGDYFFGPGLEELIEQLSSGTHHRGPPPAPKSSIDALPTIKITQKHLKSSDSHCPVCKDEFELKSEAKQMPCHHIYHSDCIVPWLVQHNSCPVCRKELPSRGSSSSTQSSQNRSTNGRENSRRRNIFSNLWPFRSSSSSSTQNRRDTNNTATAEEGHYHHHQQQQQQHQHQHQQQQSHMGYSGWPFDY | Function: E3 ubiquitin-protein ligase that promotes osmotic stress and abscisic acid (ABA) responses . Regulates negatively drought-mediated control of early seedling development, probably by influencing proline content, water loss, membrane ion leakage and the expression of dehydration stress-related genes (e.g. RAB18... |
Q6K9C3 | MARVYVGNLDPRVTAREIEDEFRVFGVLRSVWVARKPPGFAFIDFDDRRDAEDAIRDLDGKNGWRVELSTKAGSGRGRDRSGGSDMKCYECGEPGHFARECRLRIGSGGLGSGRRRSRSRSRSPRYRGRSRSRSPRYRRSPSYGRSPRDRSPKRRSYSRSPPPARARSYSRSPPPPRERSYSRSPAQPANREESPYANNA | Function: Involved in pre-mRNA splicing. In protoplast assay, enhances splicing efficiency of WAXY intron 1 and alters the selection of the 5'-splice sites by stimulating site 1 (proximal site).
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 22797
Sequence Length: 200
Subcellul... |
Q3KQ35 | MSSPDGGYASDDQNQGKCSVPIMMTGLGQCQWAEPMTSLGEGKLKSDAGSANSRSKAEARIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKSLTLAEKRPFVEEAERLRVQHMQDHPNYKYRPRRRKQVKRMKRAENGFMHMAEAQESAVLGADGRMCLENFSLGYHEQTYPHGQVPQSSHYREPQAVAPHYDGYSLPTPESSPLDLAEADPVFFTSPAQDECQMMPYSYNGSYPHQQNSMLVRQMPQTEQMGQVSPVQGMMACQSSPHMYYGQMYLPGSARHHQLHQAGQPSPPPEAQQMGRADHIQPAD... | Function: Transcriptional activator. Binds to the DNA sequence 5'-AACAAT-3' (By similarity). All of the sox17 proteins are required for embryonic endoderm development and gastrulation movements, and show some redundancy in function. In addition, the sox17 proteins have distinct but overlapping roles in later gut develo... |
O42601 | MSSPDCGYSSDDQIQGSCSVPMMMGQYQWTEPLTVFQDLKPKRDEGSADSRSKAEGRIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKSLTLATKRPFVEEAERLRVQHIQDYPDYKYRPRRKKQVKRMKREEDGFLPSANFPGSQIMDNNVMVGENYRMQYSAQNHQQNQLPPAGYFEGHNSMGYYYRDYSVPNYHISQNSSGYDSPPAQDEYQALSYSFNSSYMPYQQNATTPVMAKQMAVTQNIPQESPEHGMMASPQMYNRQMYVSECAKTHPMAQTEQHFPSYQSQKTVRQNYLQSQQDGHLESDI... | Function: Transcription activator. Doesn't appear to bind to the consensus 5'-AACAAT-3' DNA binding site, but binds 5'-ATTGTT-3'. All of the sox17 proteins are required for embryonic endoderm development and gastrulation movements, and show some redundancy in function. In addition, the sox17 proteins have distinct but ... |
P46283 | METSIACYSRGILPPSVSSQRSSTLVSPPSYSTSSSFKRLKSSSIFGDSLRLAPKSQLKATKAKSNGASTVTKCEIGQSLEEFLAQATPDKGLRTLLMCMGEALRTIAFKVRTASCGGTACVNSFGDEQLAVDMLADKLLFEALQYSHVCKYACSEEVPELQDMGGPVEGGFSVAFDPLDGSSIVDTNFTVGTIFGVWPGDKLTGITGGDQVAAAMGIYGPRTTYVLAVKGFPGTHEFLLLDEGKWQHVKETTEIAEGKMFSPGNLRATFDNSEYSKLIDYYVKEKYTLRYTGGMVPDVNQIIVKEKGIFTNVTSPTAKA... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-phosphate + phosphate
Sequence Mass (Da): 42414
Sequence Length: 393
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 3.1.3.37
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P46284 | MAAMMMRQKVAGAIAGERRSAVAPKMGRAATAPVVVASANASAFKGAAVTARVKASTRAARVQSRRTAVLTQAKIGDSLAEFLVEATPDPKLRHVMMSMAEATRTIAHKVRTASCAGTACVNSFGDEQLAVDMVADKLLFEALKYSHVCKLACSEEVPEPVDMGGEGFCVAFDPLDGSSSSDTNFAVGTIFGVWPGDKLTNITGREQVAAGMGIYGPRTVFCIALKDAPGCHEFLLMDDGKWMHVKETTHIGEGKMFAPGNLRATFDNPAYERLINFYLGEKYTLRYTGGIVPDLFQIIVKEKGVFTNLTSPTTKAKLRI... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-phosphate + phosphate
Sequence Mass (Da): 41760
Sequence Length: 389
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 3.1.3.37
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O20252 | METSMACCSRSIVLPRVSPQHSSALVPSSINLKSLKSSSLFGESLRMTTKSSVRVNKAKNSSLVTKCELGDSLEEFLAKATTDKGLIRLMMCMGEALRTIGFKVRTASCGGTQCVNTFGDEQLAIDVLADKLLFEALNYSHFCKYACSEELPELQDMGGPVDGGFSVAFDPLDGSSIVDTNFSVGTIFGVWPGDKLTGVTGRDQVAAAMGIYGPRTTYVLALKDYPGTHEFLLLDEGKWQHVKETTEINEGKLFCPGNLRATSDNADYAKLIQYYIKEKYTLRYTGGMVPDVNQIIVKEKGIFTNVISPTAKAKLRLLFE... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-phosphate + phosphate
Sequence Mass (Da): 42081
Sequence Length: 387
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 3.1.3.37
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P46285 | METVAAAGYAHGAATRSPACCAAMSFSQSYRPKAARPATSFYGESLRANTARTSFPAGRQSKAASRAALTTRCAIGDSLEEFLTKATPDKNLIRLLICMGEAMRTIAFKVRTASCGGTACVNSFGDEQLAVDMLADKLLFEALEYSHVCKYACSEEVPELQDMGGPVEGGFSVAFDPLDGSSIVDTNFTVGTIFGVWPGDKLTGVTGGDQVAAAMGIYGPRTTFVVALKDCPGTHEFLLLDEGKWQHVKDTTSIGEGKMFSPGNLRATFDNPDYDKLVNYYVKEKYTLRYTGGMVPDVNQIIVKEKGIFTNVTSPTAKAK... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-phosphate + phosphate
Sequence Mass (Da): 42061
Sequence Length: 393
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 3.1.3.37
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Q6NT16 | MEALGDLEGPRAPGGDDPAGSAGETPGWLSREQVFVLISAASVNLGSMMCYSILGPFFPKEAEKKGASNTIIGMIFGCFALFELLASLVFGNYLVHIGAKFMFVAGMFVSGGVTILFGVLDRVPDGPVFIAMCFLVRVMDAVSFAAAMTASSSILAKAFPNNVATVLGSLETFSGLGLILGPPVGGFLYQSFGYEVPFIVLGCVVLLMVPLNMYILPNYESDPGEHSFWKLIALPKVGLIAFVINSLSSCFGFLDPTLSLFVLEKFNLPAGYVGLVFLGMALSYAISSPLFGLLSDKRPPLRKWLLVFGNLITAGCYMLL... | Function: Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecu... |
D3Z5L6 | MDEAGSPAPAGTGGGDDPGGSTRETSRRLSREQIFVLVSAASMNLGCMMTYSILGPFFPKEAEKKGASNTMIGMIFGCYALFELLASLVFGKYLVHIGAKFMFIAGMFVSGGVTILFGVLDQLPEGPIFIAMCFLVRIVDAIGFGAAITASSSILAKAFPNNVATVMGSLEVFSGLGLVAGPPLGGLLYQSFGYEVPFIFLGCIVLLMIPLNLYILPSYAQESDPGKQSFWKLVTLPKMGLLAFVIISLSSCFGFLDPTLSLFVMEKFSLSTGYVGLVFLGLSLSYAISSPLFGLLSDKMPTLRKWLLVFGNLITAGCYM... | Function: Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecu... |
D4A9K4 | MDTAGPPAPAGTEGDGPGGSTGETSRRLSKEQIFVLVSAASMNLGCMMTYSILGPFFPKEAEKKGASNTTIGMIFGCYALFELLASLVFGKYLVHIGAKFMFIAGMFVSGGVTILFGVLDQLPEGPIFIAMCFLVRIVDAIGFGAAITASSSILAKAFPNNVATVMGSLEVFSGLGLVAGPPLGGLLYQSFGYEVPFIFLGCIVLLMIPLNLCILPSYESDAGKQSFWKLVTLPKIGLIAFVIISLSSCFGFLDPTLSLFVMKKFSLSTGYVGLVFLGLSLSYAISSPLFGLLSDKMPNLRKWFLVFGNLITAGCYMLLG... | Function: Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecu... |
P41440 | MVPSSPAVEKQVPVEPGPDPELRSWRHLVCYLCFYGFMAQIRPGESFITPYLLGPDKNFTREQVTNEITPVLSYSYLAVLVPVFLLTDYLRYTPVLLLQGLSFVSVWLLLLLGHSVAHMQLMELFYSVTMAARIAYSSYIFSLVRPARYQRVAGYSRAAVLLGVFTSSVLGQLLVTVGRVSFSTLNYISLAFLTFSVVLALFLKRPKRSLFFNRDDRGRCETSASELERMNPGPGGKLGHALRVACGDSVLARMLRELGDSLRRPQLRLWSLWWVFNSAGYYLVVYYVHILWNEVDPTTNSARVYNGAADAASTLLGAIT... | Function: Antiporter that mediates the import of reduced folates or a subset of cyclic dinucleotides, driven by the export of organic anions . Mechanistically, acts as a secondary active transporter, which exports intracellular organic anions down their concentration gradients to facilitate the uptake of its substrates... |
P41438 | MVPTGQVAEKQAYEEPRQDHELKSWRCLVFYLCFFGFMAQLRPGESFITPFLLERKFTKEQVTNEIIPMLPYSHLAVLVPVFLLTDYLRYKPVLVLQCLSFVCVWLLLLLGTSVVHMQLMEVFYSVTMAARIAYSSYIFSLVHPSRYQRMASYSRAAVLLGVFISSVLGQALVTVGHISTYTLNCVSLGFILFSLVLSLFLKRPKRSLFFNRSTLARGALPCELDQMHPGPDRPETRKLDRMLGTCRDSFLVRMLSELVENARQPQLRLWCLWWVFNSSGYYLITYYVHVLWRSTDSSLSYNGAVDAASTLLSAITSFSA... | Function: Antiporter that mediates the import of reduced folates . Mechanistically, acts as a secondary active transporter, which exports intracellular organic anions down their concentration gradients to facilitate the uptake of its substrates (By similarity). Has high affinity for N5-methyltetrahydrofolate, the predo... |
Q4U2R8 | MAFNDLLQQVGGVGRFQQIQVTLVVLPLLLMASHNTLQNFTAAIPTHHCRPPADANLSKNGGLEVWLPRDRQGQPESCLRFTSPQWGLPFLNGTEANGTGATEPCTDGWIYDNSTFPSTIVTEWDLVCSHRALRQLAQSLYMVGVLLGAMVFGYLADRLGRRKVLILNYLQTAVSGTCAAFAPNFPIYCAFRLLSGMALAGISLNCMTLNVEWMPIHTRACVGTLIGYVYSLGQFLLAGVAYAVPHWRHLQLLVSAPFFAFFIYSWFFIESARWHSSSGRLDLTLRALQRVARINGKREEGAKLSMEVLRASLQKELTMG... | Function: Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as 2-oxoglutarate or glutarate . Mediates the uptake of OA across th... |
Q8VC69 | MAFNDLLKQVGGVGRFQLIQVTMVVAPLLLMASHNTLQNFTAAIPAHHCRPPANANLSKDGGLEAWLPLDKQGRPESCLRFPFPHNGTEANGTGVTEPCLDGWVYDNSTFPSTIVTEWNLVCSHRAFRQLAQSLFMVGVLLGAMMFGYLADRLGRRKVLILNYLQTAVSGTCAAYAPNYTVYCIFRLLSGMSLASIAINCMTLNMEWMPIHTRAYVGTLIGYVYSLGQFLLAGIAYAVPHWRHLQLAVSVPFFVAFIYSWFFIESARWYSSSGRLDLTLRALQRVARINGKQEEGAKLSIEVLQTSLQKELTLNKGQASA... | Function: Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as 2-oxoglutarate or glutarate . Mediates the uptake of OA across th... |
O57379 | MPFSELLEQVGSTGRFQVLHVTLLCIPVLMMASHNLLQNFVATVPSHYCNAHANLSQARLSLEESLLITVPLDGAGKPQRCQRYAAPQWHLLGKNGTSGSGDLADATESMDAALQECSDGWSYNSTVRSSTIISEWHLVCDMHSFKQMGQTIYMGGVLVGALLFGGLSDRYGRRILLLISNLLMAVSGTCAAFSSSFSLFCVFRFGCGLALSGLGLNTFSLIVEWIPTRIRTAVGTTTGYCYTLGQLILVLLAYFIRDWRWLTLAVSLPFYVFFLIAWWFHESSRWLALSNRTEHALKNLKSVARFNGRHEEAEKLDIKM... | Function: Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). Mediates the sodium-independent uptake ... |
Q9TSY7 | MAFNDLLKQVGGVGRFQRIQVTLVVLPLLLMASHNTLQNFTAAIPPHHCRPPAHANLSKDGGLQAWLPQDTQGRPKSCLRFTSPQERPPFLNGTEANGTGTTEPCTDGWIYDNSTFPSTIVTEWDLVCSHRALRQLGQSLYMAGVLIGAMVFGYLADRLGRRKVLILNYLQTAVSGTCAAFSPNFTVYCTFRLLSGMSLAGIALNCMTLNVEWMPIHTRAYVGTLAGYVYSTGQFLLAGVAYAVPHWRYLQLLVSVPFFAFFVYSWFFIESARWYSTPGRLDLTLKALQKVARINGKQEEGAKLSMEVLRTNLQKELTMS... | Function: Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as 2-oxoglutarate or glutarate . Mediates the uptake of OA across th... |
Q9Y694 | MGFEELLEQVGGFGPFQLRNVALLALPRVLLPLHFLLPIFLAAVPAHRCALPGAPANFSHQDVWLEAHLPREPDGTLSSCLRFAYPQALPNTTLGEERQSRGELEDEPATVPCSQGWEYDHSEFSSTIATESQWDLVCEQKGLNRAASTFFFAGVLVGAVAFGYLSDRFGRRRLLLVAYVSTLVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRTVAGVLSSTFWTGGVMLLALVGYLIRDWRWLLLAVTLPCAPGILSLWWVPESARWLLTQGHVKEAHRYLLHCARLNGRPVCEDSFSQEAVS... | Function: Functions as a Na(+)-independent bidirectional multispecific transporter . Contributes to the renal and hepatic elimination of endogenous organic compounds from the systemic circulation into the urine and bile, respectively . Capable of transporting a wide range of purine and pyrimidine nucleobases, nucleosid... |
Q3YAW7 | MGFEELLEQVGGFGPFQLRNLALLALPRILLPLHFLLPVFLAAVPAHRCALPGTPANLSFQDAWLEAYLPREADGTFSSCLRFTHPQAVPNITLGREGRSPGDLQGNRSSMPCTQGWEYDRSEFSSTIATEWDLVCEQKDLSRAASTFFFVGVLVGAVAFGYLSDRFGRRRLLLVAYVSALVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRIVAGVLSSTFWTGGVMLLALVGYLIRDWRWLLLAVTLPLAPGILSLWWVPESARWLLTQGRVEEAQRYLLRCARLNGRPVPQDGLSREALSEV... | Function: Functions as a Na(+)-independent bidirectional multispecific transporter. Contributes to the renal and hepatic elimination of endogenous organic compounds from the systemic circulation into the urine and bile, respectively. Capable of transporting a wide range of purine and pyrimidine nucleobases, nucleosides... |
Q8TCC7 | MTFSEILDRVGSMGHFQFLHVAILGLPILNMANHNLLQIFTAATPVHHCRPPHNASTGPWVLPMGPNGKPERCLRFVHPPNASLPNDTQRAMEPCLDGWVYNSTKDSIVTEWDLVCNSNKLKEMAQSIFMAGILIGGLVLGDLSDRFGRRPILTCSYLLLAASGSGAAFSPTFPIYMVFRFLCGFGISGITLSTVILNVEWVPTRMRAIMSTALGYCYTFGQFILPGLAYAIPQWRWLQLTVSIPFFVFFLSSWWTPESIRWLVLSGKSSKALKILRRVAVFNGKKEEGERLSLEELKLNLQKEISLAKAKYTASDLFRI... | Function: Functions as an organic anion/dicarboxylate exchanger that couples organic anion uptake indirectly to the sodium gradient . Transports organic anions such as estrone 3-sulfate (E1S) and urate in exchange for dicarboxylates such as glutarate or ketoglutarate (2-oxoglutarate) . Plays an important role in the ex... |
Q9HAS3 | MELRSTAAPRAEGYSNVGFQNEENFLENENTSGNNSIRSRAVQSREHTNTKQDEEQVTVEQDSPRNREHMEDDDEEMQQKGCLERRYDTVCGFCRKHKTTLRHIIWGILLAGYLVMVISACVLNFHRALPLFVITVAAIFFVVWDHLMAKYEHRIDEMLSPGRRLLNSHWFWLKWVIWSSLVLAVIFWLAFDTAKLGQQQLVSFGGLIMYIVLLFLFSKYPTRVYWRPVLWGIGLQFLLGLLILRTDPGFIAFDWLGRQVQTFLEYTDAGASFVFGEKYKDHFFAFKVLPIVVFFSTVMSMLYYLGLMQWIIRKVGWIML... | Function: Sodium-dependent, pyrimidine- and purine-selective . Involved in the homeostasis of endogenous nucleosides . Exhibits the transport characteristics of the nucleoside transport system cib or N3 subtype (N3/cib) (with marked transport of both thymidine and inosine) . Employs a 2:1 sodium/nucleoside ratio . Tran... |
Q9ERH8 | MSRADPGKNSEPSESKMSLELRPTAPSDLGRSNEAFQDEDLERQNTPGNSTVRNRVVQSGEQGHAKQDDRQITIEQEPLGNKEDPEDDSEDEHQKGFLERKYDTICEFCRKHRVVLRSTIWAVLLTGFLALVIAACAINFHRALPLFVITLVTIFFVIWDHLMAKYEQRIDDFLSPGRRLLDRHWFWLKWVVWSSLILAIILWLSLDTAKLGQQNLVSFGGLIMYLILLFLFSKHPTRVYWRPVFWGIGLQFLLGLLILRTRPGFVAFDWMGRQVQTFLGYTDTGARFVFGEKYTDHFFAFKILPIVVFFSTVMSMLYYL... | Function: Sodium-dependent, pyrimidine- and purine-selective . Involved in the homeostasis of endogenous nucleosides . Exhibits the transport characteristics of the nucleoside transport system cib or N3 subtype (N3/cib) (with marked transport of both thymidine and inosine) . Employs a 2:1 sodium/nucleoside ratio . Also... |
Q99808 | MTTSHQPQDRYKAVWLIFFMLGLGTLLPWNFFMTATQYFTNRLDMSQNVSLVTAELSKDAQASAAPAAPLPERNSLSAIFNNVMTLCAMLPLLLFTYLNSFLHQRIPQSVRILGSLVAILLVFLITAILVKVQLDALPFFVITMIKIVLINSFGAILQGSLFGLAGLLPASYTAPIMSGQGLAGFFASVAMICAIASGSELSESAFGYFITACAVIILTIICYLGLPRLEFYRYYQQLKLEGPGEQETKLDLISKGEEPRAGKEESGVSVSNSQPTNESHSIKAILKNISVLAFSVCFIFTITIGMFPAVTVEVKSSIAG... | Function: Uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis . Functions as a Na(+)-independent transporter . Involved in the transport of nucleosides such as adenosine, guanosine, inosine, uridine, thymidine and cytidine . Also tra... |
Q9JIM1 | MTTSHQPQDRYKAVWLIFFVLGLGTLLPWNFFMTATKYFTNRLDVSQNVSSDTDQSCESTKALADPTVALPARSSLSAIFNNVMTLCAMLPLLVFTCLNSFLHQRISQSVRILGSLLAILLVFLVTAALVKVEMDALIFFVITMIKIVLINSFGAILQASLFGLAGVLPANYTAPIMSGQGLAGFFTSVAMICAIASGSELSESAFGYFITACAVVILAILCYLALPRTEFYRHYLQLNLAGPAEQETKLDLISKGEEPKGRREESGVPGPNSPPTNRNQSIKAILKSICVPALSVCFIFTVTIGLFPAVTAEVESSIAG... | Function: Uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis . Functions as a Na(+)-independent transporter (By similarity). Involved in the transport of nucleosides such as adenosine, guanosine, inosine, uridine, thymidine and cyti... |
Q14542 | MARGDAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQARLAGAGNSTARILSTNHTGPEDAFNFNNWVTLLSQLPLLLFTLLNSFLYQCVPETVRILGSLLAILLLFALTAALVKVDMSPGPFFSITMASVCFINSFSAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLLSMASGVDAETSALGYFITPCVGILMSIVCYLSLPHLKFARYYLANKSSQAQAQELETKAELLQSDENGIPSSPQKVALTLDLDLEKEPESEPDEPQKPGKPSVFTVFQKIWLTALCLVLVFTVTLSVFPAITAMVTSSTS... | Function: Bidirectional uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis . Functions as a Na(+)-independent, passive transporter . Involved in the transport of nucleosides such as inosine, adenosine, uridine, thymidine, cytidine a... |
O54699 | MAHGNAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQGRLAGTNSSAETPSTNHTSPTDTFNFNNWVTLLSQLPLLLFTLLNSFLYQCIPESVRILGSLLAILLLFALTAALVKVDLSPGLFFSITMASVWFINSFCAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLTSLASGVDPQTSALGYFITPCVGILLSIICYLSLPHLKFARYYLTKKPQAPVQELETKAELLGADEKNGIPVSPQQAGPTLDLDPEKELELGLEEPQKPGKPSVFVVFRKIWLTALCLVLVFTVTLSVFPAITAMVTTSSNS... | Function: Bidirectional uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis . Functions as a Na(+)-independent, passive transporter (By similarity). Involved in the transport of nucleosides such as inosine, adenosine, uridine, thymid... |
Q9BZD2 | MAVVSEDDFQHSSNSTYRTTSSSLRADQEALLEKLLDRPPPGLQRPEDRFCGTYIIFFSLGIGSLLPWNFFITAKEYWMFKLRNSSSPATGEDPEGSDILNYFESYLAVASTVPSMLCLVANFLLVNRVAVHIRVLASLTVILAIFMVITALVKVDTSSWTRGFFAVTIVCMVILSGASTVFSSSIYGMTGSFPMRNSQALISGGAMGGTVSAVASLVDLAASSDVRNSALAFFLTATVFLVLCMGLYLLLSRLEYARYYMRPVLAAHVFSGEEELPQDSLSAPSVASRFIDSHTPPLRPILKKTASLGFCVTYVFFITS... | Function: Uniporter that mediates the facilitative transport of nucleoside across lysosomal and mitochondrial membranes . Functions as a non-electrogenic Na(+)-independent transporter . Substrate transport is pH-dependent and enhanced under acidic condition, probably reflecting the location of the transporter in acidic... |
Q99P65 | MAFASEDNVYHSSNAVYRAPSNHQEADQEALLGKLLDYPAPGLQRPEDRFNGAYIIFFCLGIGGLLPWNFFVTAKEYWAYKLRNCSSPASGEDPEDMDILNYFESYLAVASTVPSLLFLVANFLLVNRVQVHVRVLASLSVSLAIFVVMIVLVKVDTSSWTRGFFSLTIACMAIISSSSTIFNSSVYGLTGSFPMRNAQALISGGAMGGTVSAVALLVDLAASSDVRDSTLAFFLMAAVFLGLCMGLYLLLSQLEYARYYMRPVAPVRVFSGEDNPSQDAPSASSVAPASRVMHTPPLGPILKKTASLGFCAVSLYFVTA... | Function: Uniporter that mediates the facilitative transport of nucleoside across lysosomal and mitochondrial membranes . Functions as a non-electrogenic Na(+)-independent transporter . Substrate transport is pH-dependent and enhanced under acidic condition, probably reflecting the location of the transporter in acidic... |
Q7RTT9 | MGSVGSQRLEEPSVAGTPDPGVVMSFTFDSHQLEEAAEAAQGQGLRARGVPAFTDTTLDEPVPDDRYHAIYFAMLLAGVGFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVALAAVLLNNVLVERLTLHTRITAGYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTVQQSSFYGYTGMLPKRYTQGVMTGESTAGVMISLSRILTKLLLPDERASTLIFFLVSVALELLCFLLHLLVRRSRFVLFYTTRPRDSHRGRPGLGRGYGYRVHHDVVAGDVHFEHPAPALAPNESPKDSPAHEVTGSGG... | Function: Electrogenic voltage-dependent transporter that mediates the transport of a variety of endogenous bioactive amines, cationic xenobiotics and drugs . Utilizes the physiologic inside-negative membrane potential as a driving force to facilitate cellular uptake of organic cations . Functions as a Na(+)- and Cl(-)... |
Q9I9R3 | MDSPASKKPRCERFREFFKSAKFLIYVGHALSTWGDRMWNFAVAVFLVELYGNSLLLTAVYGLVVAGSVLLLGAIIGDWVDKNPRLKVAQTSLVVQNSAVILCGALLMAVFQFKQQLSSMYDGWLLTTCYIMVISIANIANLASTAMSITIQRDWVVVVAGDDRSKLADMNATVRIIDQLTNILAPMLVGQIMAFGSHFIGCGFISGWNLFSMCLEYFLLWKVYQKTPALAFKAGQKDSDDQELKHLNIQKEIGNTESPVEASQLMTESSETKKDTGCCYQMAEPIRTFKDGWVAYYNQSIFFAGMSLAFLYMTVLGFDC... | Function: Transports Fe(2+) from the inside of a cell to the outside of the cell, playing a key role for maintaining systemic iron homeostasis . May be involved in transfer of Fe(2+) between maternal and fetal circulation .
Catalytic Activity: Fe(2+)(in) = Fe(2+)(out)
Location Topology: Multi-pass membrane protein
Sequ... |
Q9NP59 | MTRAGDHNRQRGCCGSLADYLTSAKFLLYLGHSLSTWGDRMWHFAVSVFLVELYGNSLLLTAVYGLVVAGSVLVLGAIIGDWVDKNARLKVAQTSLVVQNVSVILCGIILMMVFLHKHELLTMYHGWVLTSCYILIITIANIANLASTATAITIQRDWIVVVAGEDRSKLANMNATIRRIDQLTNILAPMAVGQIMTFGSPVIGCGFISGWNLVSMCVEYVLLWKVYQKTPALAVKAGLKEEETELKQLNLHKDTEPKPLEGTHLMGVKDSNIHELEHEQEPTCASQMAEPFRTFRDGWVSYYNQPVFLAGMGLAFLYMT... | Function: Transports Fe(2+) from the inside of a cell to the outside of the cell, playing a key role for maintaining systemic iron homeostasis . Transports iron from intestinal, splenic, hepatic cells, macrophages and erythrocytes into the blood to provide iron to other tissues (By similarity). Controls therefore dieta... |
Q5Z922 | MASDGHLAAPLLDGGGGVDDAALLRRLYVGHFLARWGARMWEFSVGLYMIRIWPGSLLLTAVYGVVEASAVAALGPIVGAVVDRLAYLQVLRLWLLLQGASFVAAGVSVTALLVYGARLAAAGFPAFVALVVVTNVSGALAALSTLAGTILIEREWVVVIAGGQPAAVLTGINSVIRRIDLSCKLLAPVLSGFFISFVSMEASAAALAAWNLAAVWVQYWLFVSVYAGFPALSETSQISRRRADDDEAAAAAQPQKVERLWMTMLPCWESWAVYARQEVVLPGVALAFLYFTVLSFGTLMTATLDWEGIPAYVISLARGV... | Function: May be involved in iron transport and iron homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52015
Sequence Length: 484
Subcellular Location: Membrane
|
F4KGN5 | MEEETETRVFLSNEQHQEEEEEEEEEPSLPRSMVISLYLGYFLARWGARTWEFSVALYMIYLWPNSLFLTAMYGVVESGSATLFGPIVGQMIDGMSYVKVLRLWLVTQNLSFIVAGGAVVALLVVPDLKSQNFPVFATLVVLTNLSGAIGVLSTLAGTVLIERDWVVVMSEGHSPAVLTRMNSVIRGIDLSSKLLSPVITGLIISFVSLRASAITFAAWATITVWIEYWLFISVYNGVPAIVQSDERRSLRSSQSQAEETDSASSFYVPLLHEEESYRNTQSRSRILRILERISESSFVSAWRNYLNQEIVLPGVSLALL... | Function: Vacuolar transporter that is involved in the transport of excess nickel into the vacuole under iron deficiency, increasing cellular tolerance to nickel under iron deficiency stress response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57094
Sequence Length: 512
Subcellular Location: Vac... |
Q2QNK7 | MGMVTATAAAALLASPPQGHLGRRCHLVVPGLRLRPPASSSPPHAAPPLRLSNFVPRCYITNVEVDVSHTSEQEALDDHPPLLPACAIPVVHLRDVPDASPFPLHESASHSTDFEELPVLSEGELHTIAATPAHPAGLYALYASYLFGNLVEQLWNFAWPAALAILHPSLLPVAIVGFFTKLSVFIGAPIVGKLMDHFPRIPMYTGLNAVQVATQLISAAMVIYAMKNVTHASTSAVVLKPWFIALVAAGAIERLAGLALGVAMERDWVVLLAGTNRPVALAQANAVLNRLDLVCETVGASVFGLLLSKYHPVTCLKIAC... | Function: May be involved in iron transport and iron homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62776
Sequence Length: 591
Subcellular Location: Membrane
|
Q8W4E7 | MVVSMALVRHSPSFDFLFHFPVDRSRFLSPVAFSSVRYHRFHSCRWLSLRSSPSCSRRLNSFSSRCSITNTDVCHEFVTTDDEIHEDLLTPIEDHSIPIVHLDTNISVTESLTLLTECTYVDTVLTALPVLSEEEQTVIAATPAHPEGLYVLYASCLVGNLVEQLWNFAWPSAIAMLYPSLLPVAVMGFVTKLAIIAGGPVVGKFMDYSPRVPTYISLNVIQAAAQVLSAGMIIHAYTVPSTSASSILLQPWFFALLFAGAIDSLCGIASGVAIERDWVVLLAGINRPIALAQANAVLHRIDLLCEIAGTMLFGILLSKY... | Function: Probable plastid transporter that may play a role in iron chelation, storage or sequestration under limiting iron conditions. In presence of exogenous antibiotics, may allow opportunistic entry of multiple aminoglycoside antibiotics into the chloroplast.
Location Topology: Multi-pass membrane protein
Sequence... |
B9FGV7 | MSMSKLLSPPPTSPPGPALSRLPCRRVAPPPVLPFPFPLRRLTSRRVFATSCSSSDSEHAPSASSTALAGAGDDLSAGVTQEREGALPFVQLSSGIVLRTEEQSLLGDHAPAPAPASAASSFALLDELNGGCREDDHLGETPAYPAAMNALYAACLAGNATEQLWNFTWPAAVAVLHPASILPVAVLGFFTKLVVFAAGPLVGELISSLPRIPAYRSLAAIQTAAHLVSVATITYAFAVHRAAAASLLLRPWFAVLVASTAVDRLACVALGIIAERDFVVQLAGAGRPVALAKANATLSRVDLLCETVGASIFALLLSKN... | Function: May be involved in iron transport and iron homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61214
Sequence Length: 593
Subcellular Location: Membrane
|
Q8IVJ1 | MSSKPEPKDVHQLNGTGPSASPCSSDGPGREPLAGTSEFLGPDGAGVEVVIESRANAKGVREEDALLENGSQSNESDDVSTDRGPAPPSPLKETSFSIGLQVLFPFLLAGFGTVAAGMVLDIVQHWEVFQKVTEVFILVPALLGLKGNLEMTLASRLSTAANIGHMDTPKELWRMITGNMALIQVQATVVGFLASIAAVVFGWIPDGHFSIPHAFLLCASSVATAFIASLVLGMIMIGVIIGSRKIGINPDNVATPIAASLGDLITLALLSGISWGLYLELNHWRYIYPLVCAFFVALLPVWVVLARRSPATREVLYSGW... | Function: Na(+)/Mg(2+) ion exchanger that acts as a predominant Mg(2+) efflux system at the plasma membrane . Transporter activity is driven by the inwardly directed electrochemical gradient for Na(+) ions, thus directly depends on the extracellular Na(+) ion concentration set by Na(+)/K(+) pump . Generates circadian c... |
Q91WN3 | MAMDSKKEIRLKRELGYFWGTNFLIINIIGAGIFVSPKGVLQHSSMNVGVSLCVWAVCAVLTLTSALCSAEIGITFPYSGAHYYFLKRCFGPLVAFLRLWTSLFLGPGLIASQALLLAEYGVQPFYPSCSAPILPRKCLALAMLWIVGILNSRGVKELSWLQTVSSVLKVGILGVISLSGLFLLVRGKKENVQRLQNAFDAEFPEVSQLIEAIFQGYFAFSGGGCFTCIAGELKKPSKTIPRCIFTGLPLVTVVYLLANISYLTVLTPQEMLSSDAVALTWTDRVIPQFTWTVPFAISASLFINLVINVLETSRVLYIAS... | Function: Associates with SLC3A1/rBAT to form a functional heterodimeric complex that transports anionic and neutral amino acids across the apical plasma membrane of renal epithelium. Preferentially mediates exchange transport, but can also operate via facilitated diffusion. May act as a major transporter for L-cystine... |
Q8TBB6 | MSGFFTSLDPRRVQWGAAWYAMHSRILRTKPVESMLEGTGTTTAHGTKLAQVLTTVDLISLGVGSCVGTGMYVVSGLVAKEMAGPGVIVSFIIAAVASILSGVCYAEFGVRVPKTTGSAYTYSYVTVGEFVAFFIGWNLILEYLIGTAAGASALSSMFDSLANHTISRWMADSVGTLNGLGKGEESYPDLLALLIAVIVTIIVALGVKNSIGFNNVLNVLNLAVWVFIMIAGLFFINGKYWAEGQFLPHGWSGVLQGAATCFYAFIGFDIIATTGEEAKNPNTSIPYAITASLVICLTAYVSVSVILTLMVPYYTIDTES... | Function: May be involved in arginine transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84052
Sequence Length: 771
Subcellular Location: Lysosome membrane
|
Q9LE86 | MGINFEDQTTLFNFVVREGNGVKGMIDSGLSSVPRPFVQPLSERIPTQKALTCEATQPIDLSNLDGPQHKEVAKQIVEAAETLGFFQVVNHGVSVELLELLKSSAHEFFAQAPEEKSMYLKEVSPSKLVKYGTSFVPDKEKAIEWKDYVSMLYTNDSEALQHWPQPCREVALEFLNSSMEMVKNVVNILMENVGVTLEEEKMNGLMGTKMVNMNYYPTCPSPELTVGVGRHSDMGMLTVLLQDGIGGLYVKLDNGEWAEIPPVHGALVINIGDTLQILSNGKYKSAEHRVRTTNIGSRVSVPIFTAPNPSQKVGPLPEVV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Involved in the pathway of sideretin biosynthesis from feruloyl CoA, a redox-active catecholic metabolite exuded by roots in response to iron deficiency in order to facilitate the uptake of iron; this pathway consists in the successive conversion from feruloyl CoA to ... |
P11701 | METKVRKKMYKKGKFWVVATITTAMLTGIGLSSVQADEANSTQVSSELAERSQVQENTTASSSAAENQDKTEVKETPSTNPAAATVENTDQTTKVITDNAAVESKASKTKDQAATVTKTSASTPEVGQTNEKAKATKEADITTPKNTIDEYGLTEQARKIATEAGINLSSLTQKQVEALNKVKLTSDAQTGHQMTYQEFDKIAQTLIAQDERYAIPYFNAKAIKNMKAATTRDAQTGQIADLDVWDSWPVQDAKTGEVINWNGYQLVVAMMGIPNTNDNHIYLLYNKYGDNNFDHWKNAGSIFGYNETPLTQEWSGSATV... | Catalytic Activity: [6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose
Sequence Mass (Da): 87385
Sequence Length: 795
Subcellular Location: Secreted
EC: 2.4.1.10
|
Q55242 | MDITVNSQSNTVAPKQAECKKMRYSIRKVATVGATSALVGTLAFLGATQVKADQVTETAPAVATATATPETSTASLTVASETATSVATSEAVESSVAHSEVATKPVTETQPSNTTPSVVEEKASSTVVTSSSDATTPSATVAAVSAPAHTSEAAVEAPTSTASSEAADTHTEVDLKVSENSAANANLSKLNGRIKSIVEENMTSDQIVALTEEEIKALNKVDFSDDAIKGTGTSLTYRNLKDIVASFLKQDSKLAVPYFKADTIINMPAFNTVDAQTMKKEEIDVWDSWPVQDAKSGVVSNWNGYQLVISMAGAPNKNSN... | Catalytic Activity: [6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose
Sequence Mass (Da): 103984
Sequence Length: 969
Subcellular Location: Secreted
EC: 2.4.1.10
|
O31411 | MMKWFAKLILSLSLAVVMAASSAAISFGASNSSLDTHASLVTQLDSAASEAAEGKSAMINESAINSNVTGWKLHGKGRMEVTGEGLRLTSDPQENVMAISETVADDFIYEADVMVTDPQADATLLFRSGEDGWSSYMLQLALGAGVIRLKDASGGEGVLNVERKVEAKPGDIYHLRVKAEGTRLQVYWGQQYEPVIDTEAAAHRTGRLGLHVWNGSALFQNIRVSDMSGNTLEPISSQGLWQPDLKGLKGTGEDGLEAKKVFRNHEADVVLEGDLILNGQGSAGLLFRSNAQGTEGYAAVLQGEGERVRVYLKKADGTIL... | Function: Catalyzes the hydrolysis of levan with endo-type specificity. The products of levan hydrolysis are a mixture of fructose and a series of fructooligosaccharides up to 12-mer, with levantriose being the major oligosaccharide obtained. Is not active towards sucrose.
Catalytic Activity: Random hydrolysis of (2->6... |
P05656 | MKKRLIQVMIMFTLLLTMAFSADAADSSYYDEDYRPQYHFTPEANWMNDPNGMVYYAGEYHLFYQYHPYGLQWGPMHWGHAVSKDLVTWEHLPVALYPDEKGTIFSGSAVVDKNNTSGFQTGKEKPLVAIYTQDREGHQVQSIAYSNDKGRTWTKYAGNPVIPNPGKKDFRDPKVFWYEKEKKWVMVLAAGDRILIYTSKNLKQWTYASEFGQDQGSHGGVWECPDLFELPVDGNPNQKKWVMQVSVGNGAVSGGSGMQYFVGDFDGTHFKNENPPNKVLWTDYGRDFYAAVSWSDIPSTDSRRLWLGWMSNWQYANDVP... | Function: Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose. Is also able to hydrolyze sucrose and to a small extent raffinose, but not melezitose, stachylose, cellobiose, maltose, and lactose.
Catalytic Activity: Hydrolysis of terminal, non-reducing (2->1)- and (2->6... |
P15400 | MHKEIAKELLLLAGGKNNIISISHCTTRLRFDVKDETKIDIHAIENLQGVQGTFFRYGLFQIIFGAGVVNKIYKEVVHVWETAPSEEPVHQKKASRKLNPAAAFAKTLSDIFVPIIPAITASGLLMGLIGMIKVFHWFAAGSPWIKMLDLVSSTAFILLPILVGFSAARQFGSNPYLGAVIAGLLTHPDLLDPSMLGSKTPSSLDIWGLHIPMMGYQGSMIPILLSVFVMSKIEKLLKSIVPKSLDVVIIPFITVMVTGCLALIVMNPAASIIGQIMTQSIVYIYDHAGIAAGALFGGIYSTIVLSGLHHSFYAIEATLL... | Function: Negatively regulates SacY activity by catalyzing its phosphorylation on 'His-99'.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49024
Sequence Length: 459
Domain: The PTS EIIB type-2 domain may serve a regulatory function, through its phosphorylation activity.
Subcellular Location: Cell m... |
Q19469 | MFEALKEVLGEINSKLAAVNNELSSKIMSENIVSTRPVAQAQYCGPYKLEKTLGKGQTGLVKTGTHCITGRKVAIKIVNKEKLSESVLQKVEREIAIMKLIEHPHVLHLYDVYENKKYLYLLLEHVSGGELFDYLVRKGRLMSKEARKFFRQIISALDFCHAHNICHRDLKPENLLLDERNNIKVADFGMASLQVEGSMLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILYALLVGALPFDDDNLRNLLEKVKRGVFHIPHFVPADVQSLLRAMIEVDPGKRYSLADVFKHPWVSGTTKADPELELPMSQVVQTHV... | Function: Regulates both neuronal polarity and synaptic organization when bound to strd-1. Kinase activity is required for the establishment, but not the maintenance, of both processes. Binding to nab-1 is essential for role in restricting axonal fate during neuronal polarization but is not required for regulating syna... |
Q09825 | MFTNTPVGGKRERQNGAHPAWSTLGANSAQIHQNTADLASKMHKLRYTKIRSPPTRVSIESITPKQRFPAPNFEQAYHSNIRYEQEESDNEEFENVVKNGHEASTNVFYESDGDDEEFVNEEYENSIDEESDDEGYSLNEDTTATNASFRYPMNQRSTRKSQFYSSKFKPLLWFGITLFSTLLIITLLHKGQEFYSRSFSSDNSQPSNSPVPNIPPASNDTKTSLKPDIIKDFTDSPSKVGGNEEFDYSTGDLITKKEFDKILQQKVEQLKQSLKEEMSNYKSSVPFEVELNDDWKFFIESTVRKYLTDPVSMPNFALLS... | Function: Associates with the spindle pole body and maintains a functional interface between the nuclear membrane and the microtubule motor proteins. Involved in chromosome segregation during meiosis where it associates with the telomeres.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58077
Sequen... |
Q73UK6 | MTTTENALTPDVRNGIEFKVADLSLADYGRRDIELSEQEMPGLMSLRREYHDVQPLKGARISGSLHMTVQTAVLIETLVALGAEVRWASCNIFSTQDHAAAAVVVGPHGTPEEPRGVPVFAWKGETLEEYWWAAEQALTWPPLADGTEAPANMILDDGGDATMLVLRGAQYEKAGVVPPDDEDDSAEHRVFLNLLRARFETDKTKWTKISESIKGVTEETTTGVLRLYQFAAAGDLAFPAINVNDSVTKSKFDNKYGCRHSLIDGINRGTDVLIGGKNVLVCGYGDVGKGSVESLAGQGARVTVTEIDPINALQALMEGY... | 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): 54435
Sequence Length: 496
Pathway: Amino-acid biosynthesis; L-homocystei... |
Q82WL1 | MSATINPVVDNSVFTDCKVADLSLADWGRKEIAIAETEMPGLMALREQYADKKPLAGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAAAAIAARNIPVFAYKGESLEEYWDYAHQIFEWASDGSHTANMILDDGGDATLLLILGSKAERDPSVIANPTNEEEQVLFASIRSRLASHPGWYSRNLAAIRGVTEETTTGVHRLYEMEKKGELPFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKIAVVCGYGDVGKGCAQSLRGLGATVWITEIDPICALQAAMEGYRVVTMDDACDKADIF... | 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): 52786
Sequence Length: 478
Pathway: Amino-acid biosynthesis; L-homocystei... |
Q94AG6 | MAPLTLSVDVKSSSATSHDVSKRVMQSSQLKINKGFFASVNTQEDKPFDFFRTLFEGFIAGGTAGVVVETALYPIDTIKTRLQAARGGGKIVLKGLYSGLAGNIAGVLPASALFVGVYEPTKQKLLKTFPDHLSAVAHLTAGAIGGLAASLIRVPTEVVKQRMQTGQFTSAPSAVRMIASKEGFRGLYAGYRSFLLRDLPFDAIQFCIYEQLCLGYKKAARRELSDPENALIGAFAGALTGAVTTPLDVIKTRLMVQGSAKQYQGIVDCVQTIVREEGAPALLKGIGPRVLWIGIGGSIFFGVLESTKRTLAQRRPNTVK... | Function: Transporter involved in exchange reactions through membranes. Has a low uniporter activity. Specifically mediates the transport of S-adenosylmethionine (SAM) and its closest analogs. Probably involved in the uptake of SAM in exchange for S-adenosylhomocysteine (SAHC), which is produced from SAM in the mitocho... |
F4HT41 | MTKALSGFCCSLSLSTLVRSSSSHMDSDIVSSSIDRSQTAMPDALAFKSINDPIKNQINSCAAICVKQDDPCHFLRVLYESLITGGLAGVVVEAALYPIDTIKTRIQVARDGGKIIWKGLYSGLGGNLVGVLPASALFFGVYEPTKQKLLKVLPDNLSAVAHLAAGALGGAVSSIVRVPTEVVKQRMQTGQFVSAPDAVRLIIAKEGFGGMYAGYGSFLLRDLPFDALQFCVYEQLRIGYKLAARRDLNDPENAMIGAFAGAVTGVLTTPLDVIKTRLMVQGSGTQYKGVSDCIKTIIREEGSSALWKGMGPRVLWIGIG... | Function: Probable S-adenosylmethionine (SAM) transporter able to catalyze both uniport and exchange reactions through membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36883
Sequence Length: 345
Subcellular Location: Plastid
|
A6QR09 | MDRPGFTASLVAGGVAGVSVDLILFPLDTIKTRLQSPQGFYKAGGFYGVYAGVPSTAIGSFPNAAAFFVTYEYVKWILHTDSSSYLMPVTHMLAASVGEVVACLIRVPSEVVKQRAQVSASSGTFHIFSNILCQEGIQGLYRGYKSTVLREIPFSLVQFPLWESLKALWSWRQDRVVDSWQAAVCGAFAGGFAAAVTTPLDVAKTRIMLAKAGSSTASGNILSALHAVWRTQGLSGLFAGVFPRMAAISLGGFIFLGVYDQTRSFLLELGRESP | Function: Mitochondrial S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter. Mediates the exchange of cytosolic S-adenosyl-L-methionine, the predominant methyl-group donor for macromolecule methylation processes, for mitochondrial S-adenosylhomocysteine(SAH), a by-product of methylation reactions.
Catalytic Ac... |
Q9VBN7 | MHLLQEPVNKLKFFHALVAGGVAGMVVDIALFPIDTVKTRLQSELGFWRAGGFRGIYKGLAPAAAGSAPTAALFFCTYECGKQFLSSVTQTKDSPYVHMAAASAAEVLACLIRVPVEIAKQRSQTLQGNKQSGLQILLRAYRTEGLKRGLYRGFGSTIMREIPFSLIQFPLWEYFKLQWTPLTGFDSTPFSVALCGAVAGGISAGLTTPLDVVKTRIMLAERESLNRRRSARRILHGIYLERGFSGLFAGFVPRVLWITLGGAFFFGFYDLTTRILGATSTDH | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May mediate the transport of S-adenosylmethionine (SAM) into the mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31038
Sequence Length: 283
S... |
Q70HW3 | MDRPGFVAALVAGGVAGVSVDLILFPLDTIKTRLQSPQGFSKAGGFHGIYAGVPSAAIGSFPNAAAFFITYEYVKWFLHADSSSYLTPMKHMLAASAGEVVACLIRVPSEVVKQRAQVSASTRTFQIFSNILYEEGIQGLYRGYKSTVLREIPFSLVQFPLWESLKALWSWRQDHVVDSWQSAVCGAFAGGFAAAVTTPLDVAKTRITLAKAGSSTADGNVLSVLHGVWRSQGLAGLFAGVFPRMAAISLGGFIFLGAYDRTHSLLLEVGRKSP | Function: Mitochondrial S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter. Mediates the exchange of cytosolic S-adenosyl-L-methionine, the predominant methyl-group donor for macromolecule methylation processes, for mitochondrial S-adenosylhomocysteine(SAH), a by-product of methylation reactions.
Catalytic Ac... |
Q6GLA2 | MERREFCASLLAGGTAGMCVDLILFPLDTIKTRLQSPLGFSKSGGFRGIYAGVPSTAVGSFPNAAAFFVTYESAKQLLRSDSSYLSPIIHMAAASLGEVVACLIRVPSEVIKQRAQVSPSSTTYQMLSATLRQEGIKGLYRGYKSTVLREIPFSLVQFPLWESLKDLWSWKQGRAVDSWQSAVCGAFAGGFAAALTTPLDVAKTRIMLAKAGSGVASGNVLFALHEIWRTQGIMGLFAGVIPRMTAISLGGFIFLGAYDKVRTLMLREQ | Function: Mitochondrial S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter. Mediates the exchange of cytosolic S-adenosyl-L-methionine, the predominant methyl-group donor for macromolecule methylation processes, for mitochondrial S-adenosylhomocysteine(SAH), a by-product of methylation reactions.
Catalytic Ac... |
Q6SPF0 | MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRAPRGAPAAAAAAAPPPTPAPPPPPAPVAAAAPARAPRAAAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAVAPPAGPRRAPPPAVAAREPPLPPPPQPPAPPQQQQPPPPQPQPPPEGGAVRAGGAARPVSLREVVRYLGGSGGAGGRLTRGRVQGLLEEEAAARGRLERTRLGALALPRGDRPGRAPPAASARPSRSKRG... | Function: Unmethylated CpG islands (CGIs)-binding protein which localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional repressor . Tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs . Plays a role in atherogenesis by bind... |
D3YXK1 | MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRVPRGGPAAPPPTPAPPPAPVAAPTRAPRAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAAAPPAGPRRAPPPAVAAREPPAPPQQQQPPPPQPQPPPEGGAARAGGPARPVSLREVVRYLGGSGGASGRLTRGRVQGLLEEEAARGRLERTRLGALALPRGDRPGRAPPAASARAARSKRGGEERVFEKEEEDEDEDEEEE... | Function: Unmethylated CpG islands (CGIs)-binding protein which localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional repressor . Tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs . Plays a role in atherogenesis by bind... |
O13035 | MARRLLTLLGLLAAAVASPVLWQKDCAKGPEVWCQSLRTASQCGAVKHCQQNVWSKPAVNSIPCDLCKELVTVVGKVLKDNGTEDEIRSYLEKRCEFLPDQGLASECKEIVDSYLPVIMDMIKEEFDKPEVVCSALSLCQSLQKHLAAMKLQKQLQSNKIPELDFSELTSPFMANVPLLLYPQDKPKQKSKATEDVCQDCIRLVTDVQEAVRTNATFVKSLVAHAKEECDRLGPGMSDMCKSYISEYSDLAIQMMMHMKDQQPKDICAMVGFCPSVKSVPLQTLVPAQVVHEVKMETVEKATVQEKTFSVCEICETMVKE... | Function: The lysosomal degradation of sphingolipids takes place by the sequential action of specific hydrolases. Some of these enzymes require specific low-molecular mass, non-enzymatic proteins: the sphingolipids activator proteins (coproteins).
PTM: This precursor is proteolytically processed to 4 small peptides, wh... |
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