lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MAGWTNSTGSGSGSGGGRGSGGRGFMNLHYNNDMFHDSTNAGGGRGRFIGGRSRGRPPQQHHYRFRRVDAVHRDSPPASLSDQQAASSNSSRHARLTHPISTADKSSTSGTAAPPSNREPDDKAIRNAANFECNVCFDIAAEPVVTKCGHLFCWECLYQWLHVHSHHRECPVCKGQVADDAIIPIYGRGGSAASVNNAPPRPTGARVESSRQQQPTLRPFEFPSLNMNPRMTSLREAFLSLMTNSIVDVEMDNSDAMTYFDDGEFYPGVNELDMEVDRYGDPDDDEVYEYDYHFGGVPLFGSAGTEASNPSSSQAHADMINIRDYTVSTTTGGYHHQEFGYSGTRPNYNRGRRGRRNRSRASTDHLLSADEMMVMPGSSGFVHNNNGSSSNVSAGAAFQPNHGWTERRGRSNRNSNSGGGRGGMQDRRRQRTHYN
The following text describes a protein:
Function:
CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).
Sequence:
MEERVYERILRATKREFYEQASIDPTVLPLLEKADREGVETAWHRYLKQQPQCGFGLLGVCCRNCNMGPCRIDPFGYGPDKGICGADADTIVARNLMRALAAGAAAHSDHARDIVEVFRGIVDGWAKDYKIADEQKLLGIARALGVKTDGKSIMEVAKEVVEIAEMEFGKPDNSPLRFLNAYAPERRKELWRKLGITPRAIDREVTEIMHRTHMGVDADPLNLIAQGLRAALADGWSGSMMATLFSDVMFGTPKPIKVWANLGVLREDSVNVMVHGHNPLLSMQIAEVAKDPEMVELAKSVGAEGINVVGMCCTGNEVLMRLGIPIAGNFLQQELAIITGALEAVIVDYQCIMPALVDVASCYHTKIITTEPKTKIPGAIHIEFDKANARESAKKILKVAVENFKNRVKERVFIPKEKMEAVVGFSVEAILSALGGSLEPLADALKSGKIKGIAGVVGCTNPKVRHDSSHVAITKELIANDILVVGTGCWAIAMSKHGFFKPEAAEMAGPGLREVCKALGIPPALHMGSCVDCSRMLIALAALADHLGVDISDLPAAGSAPEWYSEKAVSIGSYFVASGLLVHLGTIPQVLGSKRVVELLTKDAESLVGGKFFVETDPVKAARVMIEHIREKRRKLGWPE
The following text describes a protein:
Function:
Converts proline to delta-1-pyrroline-5-carboxylate. Important for the use of proline as a sole carbon and energy source or a sole nitrogen source.
Sequence:
MITRDFFLFLSKSGFLNKMARNWGSRVAAGKIIGGNDFNSSIPTIRQLNSQGLSVTVDHLGEFVNSAEVARERTEECIQTIATIADQELNSHVSLKMTSLGLDIDMDLVYENMTKILQTAEKHKIMVTIDMEDEVRCQKTLDIFKDFRKKYEHVSTVLQAYLYRTEKDIDDLDSLNPFLRLVKGAYKESEKVAFPEKSDVDENYKKIIRKQLLNGHYTAIATHDDKMIDFTKQLAKEHGIANDKFEFQMLYGMRSQTQLSLVKEGYNMRVYLPYGEDWYGYFMRRLAERPSNIAFAFKGMTKK
The following text describes a protein:
Function:
Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell junction. Early endosome. Late endosome. Lysosome. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated (By similarity). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC) (By similarity).
Sequence:
MDGFRIYPSDNYTEDDLGSGDYDSMKEPCFREENAHFNRIFLPTVYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVLTLPFWAVDAVANWYFGKFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVREADGRYICDRFYPSDSWLVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGYQKRKALKTTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFESTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSVSRGSSLKILSKGKRGGHSSVSTESESSSFHSS
The following text describes a protein:
Function:
Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.
Sequence:
MAASAKKKNKKGKTISLTDFLAEDGGTGGGSTYVSKPVSWADETDDLEGDVSTTWHSNDDDVYRAPPIDRSILPTAPRAAQEPNIDRSHLPKSPPYTAFLGNLPYDVTEESIKEFFRGLNISAVRLPREPSNPERLKGFGYAEFEDLDSLLSALSLNEESLGNRRIRVDVADQAQDKDRDDCSFGRDRNRDSDKTDTDWRARPATDTFDDYPPRRGDDSFGDKNGFMLLPCS
The following text describes a protein:
Function:
Intake of glucose and galactose.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MVSLSTQSNVPSGNKAPVNNGVALSVATTIFFMWGFLTCLNDILIPHLKAVFELNFAQAMLVQFTFFGAYFLMSLPAGWLVARLGYKQGIVAGLAVAAVGALGFWPAAELRVYGAFLGALFVLATGITILQVAANPYVALLGPERSASSRLTLAQALNSLGTAIAPLFGGWLILSNTVMTGDQLKVLPDAEQLAYRVQEAQAVQGPYIGLAVVLFLLAIFVFLFRLPALTDASAQKDESAHSLLDALRHPHVRFGVLAIFFYVGAEVAIGSLMVNYFSLPQIGGFTERQATNYVSAYWTLAMIGRFIGSALLAKLSPRVLLSVFAGINALLLGLTMASGGMLAVYALVAIGLFNSIMFPTIFTLGIERLGPLTGRASSLLIMAIVGGAIVPYLQGLLADRIGLHESFVLPLLCYLYIVFYGIWGSRLRGALAEARA
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MDLFVINRHGDSKPEVTAEEETAKLATVLKRIERKKQQRIRQREREREKRQTPKKNPKQKTTVPKRPPKTPEADEFIEPQPKIKRPPDLKSFTILGASTAAKKPKADRVLPQWLANPTVISSDLQELTCKVSKLKELDKGLREQLKANGVKYLFPVQAEVIPWVLQSRQNADIMFPRDVCVSAPTGSGKTLAFVLPVVQTLKQFTVRKIRALVILPTQDLAEQVFKSFKLYTQGTRIEVGLVSGKQMFQAEQKQLVYFNECFGFVSKIDILVCTAGRLVNHLKSTNGFNLQALEFLIIDEADRVLESVQDDWLYHLEKHIYTIQNRKVLNVCTLQRQRAPQKLLFSATLTQDPEKIEKLSLFQPKLFTSSVVENSNESEEKPMILTGKYTTPKELTEKYIVCSKDVKPLVLYAFLKRENLTKTLVFTHSVESAHRLKILLKSLFKKRLKIEEISSNLKGKSRDEFISSFTKGEVDLLICTDFLARGIDLPGVNCVISYSAPKYLKTYIHRAGRTARAGESGLAVTLLHEEQVPAFKTLLKKEIEEVEVGVEELEGLSEKYKKALGKLKEAVNEEQKVGMESVLSKKKAFKKLKKKVINSVK
The following text describes a protein:
Function:
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Sequence:
MIYSRSKLPSEGEILIATVKQVFDYGSYVSLDEYGGLQAFLPWSEVSSKWVKNIRDVLKENRKVIVKVIRVDRRKGTVDVSLKKVTDDERRKKNLQWKKIQRLDKILELVSQKLKLSEKDAWEQVAWKLEAKYGDPITAIEKAVKEGEKILIDAGVPEIWVKPLLEEASKHAEERKVKMSGLITVRTNEPLGVEKIKEVISKALENIEQDYESLLNIKIYTIGAPRYRVDVVGTNPKEASEALNQIISNLIKIGKEENVDISVVKK
The following text describes a protein:
Function:
Possesses DNA-binding and endonuclease activities. Binds DNA cooperatively in sequence-independent manner at the DNA minor groove. Exhibits apurinic/apyrimidinic site-driven endonuclease activity. Binds RNA; shows high affinity for poly(A) and a lower affinity for poly(U) templates. In vitro, prevents transcription after DNA binding. Associates with the telomeric region, the subtelomeric TARE6 repeat sequence and the var gene promoters.
Subcellular Localization:
Nucleus. Chromosome. Chromosome, telomere. Cytoplasm.
Sequence:
MASTEEVSQERSENSIQVSMTKKPTFYARIGKRMFTGNEEKNPFDEVIITGLGNATKIAIGAASIMEKEDIGQIVKVQTAYFSSDRINRRIPKITIVLKKHPDFVAN
The following text describes a protein:
Function:
Involved in the transport of siderophore iron and so has a role in iron homeostasis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MTENYGSMEHRKKSFRNNENLEQQFHPLREELDNAGPINDRTSELSLEGVSKAEAIASTWSKRSIIVAYLGLYLLSFASSLEQQTTYSLQRYATSNFSAHSNLATINLVGNILLAVVRAPMVKAADVFGRSESLSLALGMTVLGYLSLAFSRNIQMFTVAYILYICGQTGLGLLSQLIIADTSSLLNRGILSAIPELPYLATVWIGPVLAQAFHPEKNYGWRLGYGIWAFILPTVSLPLLASLFLNQRKAKAAGLYREHHNLINHSTPEKLRLFYLFWQELDGLGIVLFVSGFTLLLLPFSHSSQVVSPDSTILTLFTITLSIALLVTLCFYDVKYARYPVFALKSLKDRTILGSCVLIFTYFMSYYIFSNFLTSFLQVSYGLSIDMSSLTLNVFVFSMTTTAILSGFLMKRFGRFKMLLMISVPMYVLGILGIILFGINDNHYTRPLVLVLILAGMGGGLLTLSAQIAVQSVSSHAKLGMNLTLYLTFSSVGGAFGSAIAGGVWSKRLSSRLLHDLKDHLPVPEIESIFRDLRTALSYPQGTQIRNIINVAYTATEKDLFHISLVASLFMFAGLVIIRDVPLSTENHDTAVETPSE
The following text describes a protein:
Function:
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Subcellular Localization:
Cytoplasm. Mitochondrion inner membrane. Mitochondrion matrix.
Sequence:
MARNYEAAISALNLLQSNFAAIQQVNKDRKNMNLRSIPETIEWLRRIGYKPSDLDQLNLVHIAGTKGKGSTSAFVSSILSQYTVSQSPELESSSPKITKVGLYTSPHLRFARERIKIDNAPLSEEKFAQYFFEVWDRLEEAARVAGENPSDPQTKPQYFRYLTLMAFHTYISEGVDAAVIECGIGGEYDCTNVIDRPVSTAITSLGIDHTALLGNTIEEIAWHKGGIIKPGVKVFSSPQPPSAEEVLHKRAQEKGTQLQIVSGHRELHGGSELKLGLAGDFQYTNASLAVATAAEFLAKLGLEDIPPDFMERPLPPKFRKGLESARLGGRCETRREKDITWYIDGGHTLESIKLAGQWFASQIQNNSSSSAAAKRKLRLLIFNQQTRDSNALAQALHETLSSALGSESPFTHAIFCTNVTYKDAGYRPDLVSMNTNASDVERLRVQNGLAEKWTSIDPKAEVKVFGTIEEAVDFARELARQERGPIAHDEAPIMTFVTGSLHLVGGFLDVIETKPCSQ
The following text describes a protein:
Function:
Acyltransferase that mediates the acylation of lysophospholipids to produce phospholipids (glycerophospholipids). Highest activity with lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) producing phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity), but also converts lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) to phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Has a preference for unsaturated fatty acids of at least 16 carbons such as oleoyl-CoA ((9Z)-octadecenoyl-CoA) and palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA). Glycerophospholipids are important structural and functional components of cellular membrane, acyl-chain remodeling regulates the molecular species distribution of glycerophospholipids which can affect membrane fluidity and curvature. Essential for fertility and viability together with Oysgedart (Oys). Required for germ cells to migrate into the mesoderm.
Subcellular Localization:
Endoplasmic reticulum. Membrane; Multi-pass membrane protein.
Sequence:
MAEFEEDLPHNGLMDGIASGVGVPVEALRLLLTILAGYPVAALYQKFISVIADKTVHHMFFAGCGAGLCYFNYGLDTYHSLIAILTTYFLVLLLRKKTQIFLAINFVFHMSYLLLGYFYTSSNDYDILWTMPHCILVLRMIGYGFDITDGLKEESELSKDQKETALKKPPSLLELLAFSYFPSGFLVGPQFPFRRYKAFVDGEFRQHEGNVEAGVRRFGAGAFYLIVCQVGLRYLPDSYFLTPEFAQVSFVKRIYLLGFWAKFSLYKYISCWLLTEGALICIGLTYKGEDKNGQPDWSGCSNVKLKLLETGNTMEHYVQSFNVNTNQWVGQYIYKRLKFLNNRTISYGAALGFLAVWHGYHSGYYMTFLMEYMVVSTEKQITRFYTKVVLPQWGHILNNSDIYKLLYFITLKSYNVVYMGWCLTAFVFLKYERWIVVYGAVSYYGFTFLVLWAAFYHTFNHFFRSSSRKLAGEDQKLQDSNTDKLVEEKKPEDKKSE
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MAVSLLLRGGRIRALKAALLEAKVFRGELASTVPLSTESENNKKAAGPTSKTESVFKEPTLVPESSDTTTYKNLQHHEYNAFTFLDLNLDLSKFRLPQPSSGRESPRH
The following text describes a protein:
Function:
Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MEKSNEKLILLTGIFVSALTISNVIAGKLVNIGPFLVPVAVLCYPITFAVTDIVSEVYGKRTAQKMVWTGFFTSLILVIYSQIAVFYPPASIFANNEAFVKVFGSTPRIVLASILAYILSQTHDVWAFHFWKKITRGSHLWLRNNLSTMVSQFIDTLTFITVAFAGTIPGNVLVQMIFSQYVVKLIMALIDTPFVYLGVKLVSGQWTVKEGS
The following text describes a protein:
Function:
Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKNPEAQQDVSVSQGFRMLFYTMKPNETSFQTLEEVPDYVKKATPFFISLMLLELVVSWIRKGKPPGRLDDALTSISAGVLSRLPSLFFRSIELTSYIYIWENYRVFNLPWDSPWTWYSTFLGVDFGYYWFHRMAHIFYSPLALFIPPSVYAVHLQFNLLYQFWIHTEVINNLGPLELILNTPSHHRLHHGRNRYCIDKNYAGVLIIWDKIFGTFEAENEKLVYGLTHPINTFEPIKVQFHHLFSIWTTFWATPGFFNKFSVIFKGPGWGPGKPRLGLSEEIPEVTGKEVPFSSSSSRLLKIYTVVHFALMLAFYEETFADTAALSQVTLLLRVCFIILTLTSIGFLLDQRPKAAIMETLRCLMFLMLYRFGHLKPLVPSLSSAFEIVFSICIAFWGVRSMKQLTTRPWK
The following text describes a protein:
Function:
RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Involved in poly(A) site recognition. May be involved in coupling transcription termination and mRNA 3'-end formation (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MQAYTEIAPPTAVSHAITLPFLSSRSNNLIVAKNSLLQVFELKSTVTEVASGGEGEADNAAANFDTEAADVPLQRIENTAKLVLVGEFPLAGTVISLARVKALNTKSRAEALLVAFRDAKLSLVEWDPETYNLHTISIHYYENPDVPGLAPWDAELKDTYNFLTADPSSRCAALKFGTHNLAILPFRQRDLAEDEYDSDNEAAQEGKAERANGANGDDAVKTPYSSSFVLPLTNLDPTLTHPVHLAFLHEYREPTFGVISSSKATAASLLTHRKDILTYTVFTLDLEQKASTTLLSVPGLPYDLTQVVPLPHPIGGALLVGSNEIIHVDQAGKTNGVAVNELAKACTSFALSDQADLALRLEGCTLELLSQDTGDVMIVLNDGSIFILTFSLDGRNVSAMTIQPVPADNGGNILKTRASCSTNLGRGRLFIGSEDGESVLMGWTSTSNQLRRKQSNTAQSGDDEDMSDVEEEEVDDLDDDLYNDTATTVKKITAAAAEPTAPGTYTFRVHDVLPSIAPIRDTVLHPGKDTESLTKGEIMLSTGRGAAGAITALNRELHPTMLAQTELPSSNGVWAVHAKKQAPAGIVADFGQDAEANASSDVDYDQYLVVSKAWEDGTESTVVYEVHGNELSETEKGDFERDEGLTLSVGVLARGTKVVQVLRSEVRTYDSELGMEQIIPMEDEETGNELNIINASFADPYLLIQREDSSVKIYKATGDGEVEDVEATGLSGTEWLSASLFQSSSFTEVFAFLLTPEGGLRIFAMSQLEKPSYVAEALGFLPPLLTMDYMPKRSSAKATITEILAADLGDATSRSPHLIVRTSNDDLVIYKAIHSPSRSSSDLWTHNLRWVKLSQQHVPRYMEDGAQEEAADEPGFESTLLALDNINGYSTVIQRGRSPAFILKESSSAPRVIGLSGNPVKSLTRFHTSSCQRGFAYLDSTDTLRISQLPPSTHYGHLGWAARRMPMDAEVHALAYHPSGLYVIGTGQPEEYTLDPNDTFHYELPKEETSFKPKVEHGIIKVMDEKTWTVIDTHVLDPQEVILCIKTLNLEVSETTHQRKDVIAVGTAIVLGEDLATKGNIRIFEVITVVPEPDHPETNKRLKLIVKDEVKGTVSAISDLGTQGFLIMAQGQKSMVRGLKEDGTLLPVAFMDMQCYVTTLKTLPNTGMLLMGDAYKGAWFTGYTEEPYKMMLFGRSKHHLECITADFLPFEEQLHIIVADADMNLQVLQFDPDHPKSMGGTRLLQKSTFHTGHFPSTMHLLQSRLHMPTASEFTTSTTSSLPLHQILCTSQSGTLALITPLSESSYRRLSGLATHLQQFLDSPCGLNGKAFRAADVMEGGWDAGTQRAMLDGGLLMRWGELGEQRRREGLGKVGW
The following text describes a protein:
Function:
Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position.
Subcellular Localization:
Secreted.
Sequence:
MKKSIALVLSIVLLAALFAVPASAGEQNTIRVIVSVDKAKFNPHEVLGIGGHIVYQFKLIPAVVVDVPANAVGKLKKMPGVEKVEFDHQAVLLGKPSWLGGGSTQPAQTIPWGIERVKAPSVWSITDGSVSVIQVAVLDTGVDYDHPDLAANIAWCVSTLRGKVSTKLRDCADQNGHGTHVIGTIAALNNDIGVVGVAPGVQIYSVRVLDARGSGSYSDIAIGIEQAILGPDGVADKDGDGIIAGDPDDDAAEVISMSLGGPADDSYLYDMIIQAYNAGIVIVAASGNEGAPSPSYPAAYPEVIAVGAIDSNDNIASFSNRQPEVSAPGVDILSTYPDDSYETLMGTSMATPHVSGVVALIQAAYYQKYGKILPVGTFDDISKNTVRGILHITADDLGPTGWDADYGYGVVRAALAVQAALG
The following text describes a protein:
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.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MNIDEVEQRDGIRFTWNTWVSTSQEARKNLHIPIGCLYSPLLPKPLVADRAPIKCSHCGAVINPYCSVDYNSNLWTCCFCLTRNQLQYQNLPELQVTTFEYRDVQENIRYIPTYIFVIDTTCTEHELEELKTNLTTVISLLPPTTRIGLITFGQCVTVHNLMCESDCLISVAFANKVNSPIAIQCGLLLSPNSNQYIIPIEQCELTFMSIIESLQVDGFDVPQTERPKRATGAALDIAQNMLKAVNMSGHIIAFVAGPCTEGPGKIIGTSLNETLRCHQDIVNENTPYMAAAKQFYDGVADKLIQNESACTILACSMDQTGLMEMRKLYEGTGGIAYYFEDYTHEALRETLLRLFDGQVWKSNVAIEVQTCKEMKVCGALGPLTSGNKKTSSVSPTSVAVGGTSLWKASAALKNTSYAFIFDVTNPQTNPKRTNEVGFIQFITTYYDELGRKCTRATTSSRMWTNPSQEGFEKLAAGFDQEAATTLMARYAAYKAETEDSREAIRWLDRSLIKMCQRFGDFRKDDPNSFKLSPNFSIYPQFMFHLRRSHFLKVFNCTPDETSVFRATLNRETVNNTLTMIQPTLDSYKYGQQPVPVLLSLQSVKPDEILLLDTYFYLVVFRGNAVAEWMKQKLEEKPEYAGLKDYYALPEEDAKELSKTRIPAPRIYVCNQYSGNQRFLMTILDPAVAPGQNKNDLVFTEDVNLDTFLTHLRQLAVKDTLN
The following text describes a protein:
Function:
Probable coreceptor of Wnt proteins. Involved in neuronal pathway recognition and ventral muscle attachment site selection. Non-vital for development. May be part of a signal transduction cascade involved in learning and possibly memory.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Domain:
The extracellular WIF domain is responsible for Wnt binding.
Sequence:
MAPNLLTIGLLLTLIASGQAHLNIFLNLHEVLRLIGVSAELYYVREGAINDYALNFAVPVPANISDVTFTWQSLVDHPLPYSINIATSDTEVLPRPILNISRIGDVPVEPQTWGIALKCSGTRNAEVTVTINVEVILDRATNNNTNLIFKRKKICLREEQDSAHEEYDDDDLDLLQTARKGHGGDIHYVDRNDEHVVANGHQAPEKQRPVVTESPVGRGNSGGSKRDFDPMLRENLVPPASGLVTLIVGGILALVLVSTLILIAYCAKGPSKRHPSNGVHLIKTSSFQRLPTISSTAHNSIYVCPSTITPTYATLTRPFREYEHEPEEFNRRLQELTVQKCRVRLSCLVQEGNFGRIYRGTYNDCQEVLVKTVAQHASQLQVNLLLQESMMLYEASHPNVLSVLGISIEDYATPFVLYAATGSVRNLKSFLQDPSYARSVTTIQTVLMGSQLAMAMEHLHNHGVIHKDIAARNCVIDDQLRVKLTDSALSRDLFPGDYNSLGDGEYRPIKWLSLEALQKSHYNEGSDVWSFGVLMWEMCTLGKLPYAEIDPYEMEHYLKDGYRLAQPFNCPDELFTIMAYCWASMPAERPSFSQLQICLSEFHTQITRYV
The following text describes a protein:
Function:
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Sequence:
MVSMLRKYLLECPRKFGNKYDNKVRSDLRRALFLAASDDGKYFNLFFPDRPEAKDDQESESEDEEEYIMADNRDDPAHPGRPCVRRFSKGEPTYRCLTCGLDETCVLCSYCFNPEDHQDHQVTVSISPTSNGGVCDCGDPEAWVKQFSCKYHEIDNFTASDLPQDLYDALLETVETAMDYLIDVLSHSDVAIYKFTEAEQVLANFVNSQLSPSVYGARDDHDDSRFTLSMWNDQRYSFTHAEILIKKATGKNDNFCKMVSQHIDSHGRATVRVSSSLGDLMDAKRQMAHTMLIPTSTAGMNEMATSVRSSRDSFREEMCDTIIHWLDDISKCPIQGNYFAIRDIVCKAFCRPWRVGSAKFLGEVPFNLDADVAHYKDRMEKRAALTPEGDIPEYEDYQENMAEFDVPEQETNPIGNAGNGIGRDPDTPLTTGNPDYWVRGRTNPDWSAPEVLELLGCPMSKRARVCYLLFFDIRLWKSIRNVLQNLYISVMVAHPGFKSILGIYYAEIYRQIVEMHILLDREHEVSVITHLSTQLLTAPSIATQISKYKYLTDYMGALFLFFTRGAFGPADAVNVGYHKVEMLVLRAQHTRFRRIFHDMNYILNRTTEKENTCGAPDRIRQVSDLFLLFQGAQTMKRQVGTHIEFEIDTWVYFFYPTACLLQLGQMIASGSRSCRLEDNEAAIRIVSNALTLWGSGRLNYRSMSNEANVPEFVSVNWGMEQYLTLKFDVASQDVSLYHPLHAFCSWLIECGQVMQSRRLREILTDVQLADGPNPMDQAVHPRSLALSVLFEYPIRVLVLLSQIKVGLWVRNGVNVVSQLTHYRDQSLRDTAFARDLFMVQTALAVHDPALVFVSIVHRFGLSQLSTPDTKHPVYEDKEKYMIEELLHTLLVLVLERTHLYGYDEKETKRAHILKQIVHSLCFRPNSFTEICKQISEDLTSEELFETILLDVAEIQQPTGNSESRKYKLKDEYFDMVDPYFAHFSSNQRNDCLRVLQTRLAKKQGCSESEVVVMPPMDPPLEGVFKNIGAFTKTRPFAYFCKSVLEFLVGQPDGDITGLLLHLILVAVTDKSQVDIDPQEFATTASGPLPDYRLGANELGSMLVEPLCKLYEQEHPKNGAVIRYLVDKLAGDDIALRELSDKLASSVASTAVSGSSGAMSPTSTKREQAKQRQARIMEEFKQQQQAFEQNHADNSGEDEDMEGGESNEDVCILCMQSKSNAPGAVFGVSGLFTSSNVYRRFPADHSDLVEECLNWNGNLDQSRSDVMMQLKFTCDPEWQKLQDERVARNRIGPGFPNENHGTVATSCGHGMHHECYLELRKTILKQTQVTRNKAENPEAGEFLCPLCKSFNDVFLPVFHSSNERNWDTVLSSPSEAGGSGSLAGENKIFLDYLDGRFEVREPLTASVILGNQLADATQAGDEGEDHDDFWLDQLIVQWENRFEPGLAAIMTRIENPADLIKILSNTVQQLEISLRGVATQPTGLFFEQLSSNNVATLRNMCEIVFVALTQIRTAQNHTLSRQFMTVNQSAGIERLAVFLCYDRFVGLQFNHMLRYFVSQKLALNLDYFIKTWAKGELDWTRGPVFEHMPRFFGHEQGIEAVKAIAERLLQHQEGVPEVTEAVAATVYTLAVKATTVCLREACLLVYGLYASGETPEISEDDDIDDCENDWYEAQKLTRFLKIPHLDDILQGVLGTSEVFSIEARAFNTINAASKPIVPFYFAPQRLLHLPERLDDLYTPGYHASPSVKQQSKSMSTDPAVCLFCGESVNTQYNDPWDADKSGECNKHMRKHHRDKCIFLLPKKTSILLLSKDQGSFHPAPYFDLHGERDEVMKRGRPQFLNEGRYEKFMREMWLQPGIPNYIARQLDSSHDPGGWETL
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNKCRKQPLGSSPETFSPDVLADIFELFAKNFSYGKPLNNEWQLPDPSEIFTCDHTEFSAFLDLKNSLNEVKNLLSDKKLDEWHEHTAFTNKAGKIISHVRKSVNAELCTQAWCKFHEILCSFPLIPQEAFQNGKLNSLHLCEAPGAFIASLNHYLKSHRFPCDWNWVANTLNPYHEANDNLTMIMDDRLIANTLHCWYFGPDNTGDIMTLKYLTGLQNFINSMGTIHLITADGSFDCQGNPGEQEALVSCLHYCEAVTALMTLGNGGSFVLKMFTLFEHCSINLMYLLNCSFDQVHIFKPATSKAGNSEVYVVCLYYKGRETIYPILSKMVLNFGSEMTKKALFPHHMIPESFLRKHEECCTFFHKYQLETISENIRLFECMGKREQAKLNSLRDYAVQYFMQKFQLKPLSRNNWLVKKSNIGCSTNTKWFGQRSRYFKTYNERKMLETLSWKDKVAKGYFNSWAEEHATYHPGQSSLLEGTAFNLECHLWQVLQGKKLPKVKCSPFCDGEILKALNESVEKSLGGALNFDLKFRPKQKHCCSCHVFSEELIFSELFSLTKCLQDHQDKEPSTQIKCLLVGFPALHNIKMPIPLEVRLLESAALMTFSCSLLHDGDPTYQQLFLDCVLHSLQQLHTGDVMILPILSCFTRFMAGLIFVLHSCFRFITFSCPISSEPLKTCAVLLCVGYQDLPNPVFQYLQNVNELLRDLVNTEAPQQVLQFVPMEVLLKGALLDFLWDLNAAIAKRYLHLIIQGEREEIIGSL
The following text describes a protein:
Function:
Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MGFRFQNLNPMYRSYLSRLSSPKNPHPNPVIVQSLNPHFHIYSPPLFSDNPNYSIPRRWHFGHSHDHHDHHHNITKEGEKIFRLGLGADIGLATTKALTGYLSGSTAIIADAAHSISDVVLSGVALWSFKAAKAPKDEEHPYGHGKFETLGALGISCMLLATAGGIAWHALDLLIGLLSTVPEVVNNHLLAHGHIDHHGGNHHGIDMDHPILALNVTIVAICVKEGLYWITKRAGERQGSGLMKANAWHHRADAISSVVALIGVGGSILGVKFLDPLAGLVVSGMILKAGLETGYQRHVSFKMIVAILQFKSYHAHVFLIEWIYTSPVFAVFLDFSVLELVDAAIPAEQLEPINQTILQVEGVKGCHRLRGRRAGSNLYLDVHIVVDPFSSISAAHGIGENVRHQIHKSHPEVTEVFIHIDPAYVEFSPDVMDQKESLKRIMEQKSNISAREEDVEAIVCGTFSSKFPEKFVVERITRHMLRGKLLLEVEVGMPPDIMICDAMEAAKEAEKEILNAASNIVHVNVQLRLGRPIPEFRYI
The following text describes a protein:
Function:
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs.
Sequence:
MDSHSQKAWKWWKKFGEKPICLAPMAEISDLSWRMLIRNHGVKVCWTGMLNAHQWSQGSGYQNKFFNTCPEDHPLIAQIAGSNEDQDLIVAAAKDLAKYADGVDVNLGCTQKIASRSEYGYFMVDNCQKREKTLELFRRLCKEVNCPICAKIRIFIDDSGEVSEKITIDFAKKLEEAGVSLLQVHGRAEHRNKQADVYNEIIKHIVQAVNIPVVANGGINTVEDAHKFMEETGAAGVSVAQALLKDPTAFDPTGKKPRKDYALEYLNLSKEKGVRFFGPKKHIFIFYEKEIRENKELAKQIEQSTTIEQLIEFVNAHP
The following text describes a protein:
Function:
RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to bind to an RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, Stress granule.
Sequence:
MSSDEEDFNDIYGDDKPTTTEEVKKEEEQNKAGSGTSQLDQLAALQALSSSLNKLNNPNSNNSSSNNSNQDTSSSKQDGTANDKEGSNEDTKNEKKQESATSANANANASSAGPSGLPWEQLQQTMSQFQQPSSQSPPQQQVTQTKEERSKADLSKESCKMFIGGLNWDTTEDNLREYFGKYGTVTDLKIMKDPATGRSRGFGFLSFEKPSSVDEVVKTQHILDGKVIDPKRAIPRDEQDKTGKIFVGGIGPDVRPKEFEEFFSQWGTIIDAQLMLDKDTGQSRGFGFVTYDSADAVDRVCQNKFIDFKDRKIEIKRAEPRHMQQKSSNNGGNNGGNNMNRRGGNFGNQGDFNQMYQNPMMGGYNPMMNPQAMTDYYQKMQEYYQQMQKQTGMDYTQMYQQQMQQMAMMMPGFAMPPNAMTLNQPQQDSNATQGSPAPSDSDNNKSNDVQTIGNTSNTDSGSPPLNLPNGPKGPSQYNDDHNSGYGYNRDRGDRDRNDRDRDYNHRSGGNHRRNGRGGRGGYNRRNNGYHPYNR
The following text describes a protein:
Function:
Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins; Probable hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
Sequence:
MPIENKVIENLASSLIREYLSRKGLKETLKTMDAELPRQELSINNRITLAREMHLEGLLKKNKVYFCYMGEFLKDLSNNIIDVLCQEQPLSTMIEVIVKHIKETSRPRTRSSGRSLSFSEDKNEVFTKVTKPVIDDSTSNNGNVDNDIETIELEDQLEHSSPTLSPRIQQQHDSTRQTPITLNIATALKEIIFGKGTGLFNYEWRIQSFLFSDVEGIQYGIVQKKGGPCGILAALQAFFLKHLLFTNPENQNIAKSQIANVTESMQQESLVLAIAETLWKAGNCRRSVVALLQSSVHFKGNSQFRLDQLTEKFQNPKGNGCILYLYSLILSRTVEGVKEDMDDPNCKLMGAYNYCSQEIVNLIVTGKATSNTFDGIIELTGNEGDKCQLTGLKSQSQIGLLSLLEHYESCKVGNYFKSPEYPIWVVYSESHYSVVFSLNRKILDLSDVPKTFDLYYYDGLGNQDEEIRLTVDPYQQVTVNEKDLIPPLDLCIRTSLYTLNA