lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Domain:
The RING-CH-type zinc finger domain is required for E3 ligase activity.
Sequence:
MLLAIGVIVWCWGLLSRRPMLRRQGKQKGRCCVLFSDLEVFLLRPPTPSASPPAFTPMNELNAEGNATSSATESHSLANGHYQPVTGEEALDTRGPDDWTHSVVDPPRTLDCCSSSEDCSKEKLDERLSLNSCTDSGVRTPLCRICFQGPEQGELLSPCRCSGSVRCTHEPCLIKWISERGSWSCELCYYKYQVIAISTKNPLQWQAISLTVIEKVQIAAAVLGSLFLIASISWLVWSSLSPSAKWQRQDLLFQICYAMYGFMDLVCIALIVHEGPSVFRIFNRWQAVNQQWKVLNYDKVKDNEDHQKTGATFRTLSLPLTHRMGQSGPEGEPSTSTSSLMAAAAAAAAGTVTPTTNSVPPAAGATTEPQDSSEPSNGQPSLPDHHCAYNILHLLSHLRQQEPRGQTSNSNRELVMRVTTV
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MANQTNSKAKALLGWVDARFPLSKMWKEHLSEYYAPKNFNFWYFFGSLSMLVLVIQIVSGIFLTMNYKPDGNLNAYHLPAAFTAVEYIMRDVSGGWIIRYMHSTGASFFFIVVYLHMFRGLIYGSYKKPRELVWIFGSLIFLALMAEAFMGYLLPWGQMSFWGAQVIINLFSAIPVIGPDLSTWIRGDFNVSDVTLNRFFALHVIAVPLVLLGLVVAHIIALHEVGSNNPDGVEIKKLKDENGVPLDGIPFFPYYVVHDILAVTIFLIVFCAVMFFAPEGGGYFLEAPNFDAANALKTPPHIAPVWYFTPFYAILRAIPSFAGTQVWGVIGMGAAVVLIALLPWLDKGEVKSVRYRGPIFKTALVLFIIAFIGLGILGAMVATDTRTLVARILSFVYFAFFLGMPFYTKLDTNKPVPERVTMSTTKQKIMFFVYVGITVVGAYLFATNI
The following text describes a protein:
Function:
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Plays an important role in sociosexual interactions since its enhances courtship in a pheromone-dependent manner.
Miscellaneous:
MISCELLANEOUS: The atypical heteromeric and topological design of the odorant receptors appears to be an insect-specific solution for odor recognition, making the OR/Orco complex an attractive target for the development of highly selective insect repellents to disrupt olfactory-mediated host-seeking behaviors of insect disease vectors. Odor-evoked OR currents are independent of known G-protein-coupled second messenger pathways.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNDSGYQSNLSLLRVFLDEFRSVLRQESPGLIPRLAFYYVRAFLSLLCQYPNKKLASLPLYRWINLFIMCNVMTIFWTMFVALPESKNVIEMGDDLVWISGMALVFTKIFYMHLRCDEIDELISDFEYYNRELRPHNIDEEVLGWQRLCYVIESGLYINCFCLVNFFSAAIFLQPLLGEGKLPFHSVYPFQWHRLDLHPYTFWFLYIWQSLTSQHNLMSILMVDMVGISTFLQTALNLKLLCIEIRKLGDMEVSDKRFHEEFCRVVRFHQHIIKLVGKANRAFNGAFNAQLMASFSLISISTFETMAAAAVDPKMAAKFVLLMLVAFIQLSLWCVSGTLVYTQSVEVAQAAFDINDWHTKSPGIQRDISFVILRAQKPLMYVAEPFLPFTLGTYMLVLKNCYRLLALMQESM
The following text describes a protein:
Function:
Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body (By similarity).
Subcellular Localization:
Bacterial flagellum basal body.
Sequence:
MEKSMQPIQLFELASRQAEWLSVRQEVVATNIANANTPKFHAKDVSPFEAVMQATSQQVGMARTNPAHLGESTLSENIAVRDNPVNNEIGMQESGNSVGLAEEMTKTGEIKRQYDLNASLVKSFHRMMLMTVKR
The following text describes a protein:
Function:
Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.
Subcellular Localization:
Cytoplasm.
Sequence:
MTVENNLPKVSVLFVCLGNYCRSPMAHAVFQEEVRKQGLEHLFDTIDSAGTGHWHVGSTPDSRTMQTLHSHGVKFHHIGRKLRKIDFDQFDYIFGMDHSNIRNIEKVRPKDSKARVLLFGEYRSPGVQRIVDDPYYGGDQGFEICYQQLIDFSKNFLESLK
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MHRKQKMGPVTFEDVAVNFSLGEWALLDSYQKKLYRDVMMETFMNLISIGKTEEESMDVNYPQLQRNSRIQVVEKFCDYEHSSQCGKTHQQMTEHIVNGESHPAVKVYESSVNVKDINGHSSSDVLLRGQNEEKPYRCQELVEKAIKREKCWKDVTYSESFHTLESVPATENSCENTQTYESYRTLTPHQDSKRAHAGDELHECKQFEKTLKGESDIQIYERIHTGEKPLEYKQCGEAFVNSSHRTKHQRIHTREKTYSCRHCGETFLYSMARRNHEKTHKRDHTREKTYSCRHCGETFLYSKACRDHEKTHKKERSFICKYCGKACIHSYQLLQHERRHTREKRYTCAQCGKAFRRSSNLHKHERIHSERKLYACKHCGKAFISEGNCSNHERIHTAGKTYVCKQCGKGFTRSLSLQKHERRHTQEKQYTCAQCGKAFRRSSNLHRHERIHSEKKLYACKHCGKAFNIASYCYNHERIHTAEKTYVCNQCGKGFTLSSYLQKHKRIHTGEKPYTCKYCGKAFTHPGAHHKHEKIHTREKPYVCV
The following text describes a protein:
Function:
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. LAGE3 functions as a dimerization module for the complex.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MQDPSGDKVCRAGGEEDGEDGQHTSRVHDTEADPHHTEASSHRTEGSSHLTETSSRPSEAENGHDNSPHVNRAQDVGTQASPQGSLNSRVPVEARVVVEEAAIAPQGEQAPIIPGPSGDAATTAGSRLLEFSVTVPFRTAVEANIACRTLASNIQQQQVMVQQEFTVNDTILTVRWTTEDPVLFRTSINAFLDQLSLVVRNIPRPVFMAVFKQGRGRNN
The following text describes a protein:
Function:
Inositol polyphosphate sensor that associates with transcription factors to regulate inorganic phosphate (Pi) starvation responses. Probably acts by binding inositol polyphosphate via its SPX domain. Acts as a Pi exporter, mediating efflux of Pi out of cells. Transfers Pi from the epidermal and cortical cells to the root xylem vessels. Involved in the transfer of Pi from roots to shoots. Involved in abscisic acid (ABA) induction of stomatal closure and ABA repression of stomatal opening.
Miscellaneous:
MISCELLANEOUS: Pi content in shoot of pho1 mutant can be restored to wild-type levels after treatment with cytokinins.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=In transgenic plants, relocates partially to the plasma membrane in the presence of high extracellular Pi.
Domain:
The EXS domain is essential for Pi efflux out of cells and is necessary for the endomembrane localization; The SPX domain provides a basic binding surface for inositol polyphosphate signaling molecules.
Sequence:
MVKFSKELEAQLIPEWKEAFVNYCLLKKQIKKIKTSRKPKPASHYPIGHHSDFGRSLFDPVRKLARTFSDKLFSNSEKPEILQVRRRRGSSETGDDVDEIYQTELVQLFSEEDEVKVFFARLDEELNKVNQFHKPKETEFLERGEILKKQLETLAELKQILSDRKKRNLSGSNSHRSFSSSVRNSDFSAGSPGELSEIQSETSRTDEIIEALERNGVSFINSATRSKTKGGKPKMSLRVDIPDAVAGAEGGIARSIATAMSVLWEELVNNPRSDFTNWKNIQSAEKKIRSAFVELYRGLGLLKTYSSLNMIAFTKIMKKFDKVAGQNASSTYLKVVKRSQFISSDKVVRLMDEVESIFTKHFANNDRKKAMKFLKPHQTKDSHMVTFFVGLFTGCFISLFVIYIILAHLSGIFTSSDQVSYLETVYPVFSVFALLSLHMFMYGCNLYMWKNTRINYTFIFEFAPNTALRYRDAFLMGTTFMTSVVAAMVIHLILRASGFSASQVDTIPGILLLIFICVLICPFNTFYRPTRFCFIRILRKIVCSPFYKVLMVDFFMGDQLTSQIPLLRHLETTGCYFLAQSFKTHEYNTCKNGRYYREFAYLISFLPYFWRAMQCVRRWWDESNPDHLINMGKYVSAMVAAGVRITYARENNDLWLTMVLVSSVVATIYQLYWDFVKDWGLLNPKSKNPWLRDNLVLRNKNFYYLSIALNLVLRVAWIETIMRFRVSPVQSHLLDFFLASLEVIRRGHWNFYRVENEHLNNVGQFRAVKTVPLPFLDRDSDG
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MPPTGVASSMAGQEERRLKLQDTLRTVGMLFKRLHRVYNICSDCGPSAGSQYTPIEPDVTLQSLVPMKDEAKTSEEKKPSEVTRSLQEERARLTEALAVQPPGIIPESTQVTPQERHNKTWVKNLIRVSVLLTLMGNGTRL
The following text describes a protein:
Function:
Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. Requires the other members of the gamma-secretase complex to have a protease activity; Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Domain:
The PAL motif is required for normal active site conformation.
Sequence:
MSNNKKFEDGEFDSSSSKISNNDNIILDNNSSINNSNNNDDNIFSINDNDEEFNEKTSLINNKSETNKIEEEVEIEGLDEEYEQEMTLQDFSKMIVMILIPVSITMAAVVYFVKLLNSQTVYASTIYIDYSQLSTGDSGGSEFVQSLIAASIVLGMIIITTVCFVLLYKYRCLKILYGWLFLSVGMMLGSFGSTFFQSLLIAGNMALDYVTFAFLIYNFTVCGIVAVFWYSHQYVNQLYLVIISILMAISLTRLPQWTIFTLLVIVAIYDLFAVLCPRGPLKVLVELSQERKESIPALVYETGKGSDNNLKLGLGDFIFYSLLISRAALVHMSTVFTVFISIITGLFLTLLCLAIFNRALPALPISIFLGILVYYLSTTFLYPFIEALTIAQVFV
The following text describes a protein:
Function:
Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Subcellular Localization:
Nucleus.
Sequence:
MLNPNKIIKEGDRVVMYNGKDNMAVLTMESNNVYNSKFGSYRHKNIIGKEYGSKLSSDNGNGFCHVIAMTPELWSITLDHRTQILFNLDISTIIFNLELKNGSRAVESGTGSGSLSSSIARTIAPKGHLFTFEFHEERVKFARKDFKDNGLDQYITVTHRDACGKEGFLRQDINNDIDAVFLDLPSPWDAIENAIAVMHDGSMLCSFSPCIEQVQNTCLKLADSKFQEIKTIEVLIRTFDTRLQEYEELNLTNPYIDNNNNNNNNNNIEENRGKFEIGGIEGLKKDKLLSKPFTEARGHTGYLTFARYLPNA
The following text describes a protein:
Function:
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Subcellular Localization:
Cytoplasm.
Sequence:
MAQFKYGSSTPSEVLTDLAAKNNVSVLDREFQVFLDANDELSNLRDDFLIPKKSTFPGVDCDDEDQNGNCAYLCGNSLGLQPKSAQQDAQKKKQVLQNWELNAIECHKVGYLPAIFCDNFARDGMAKLVGCHRDEVVIMNGLTVNLHLMMVSFYQPTQTRHKILIEEHAFPSDYYVVRSQIQQRGFDDSSMLFLKPRKGEEIFRMEDVLEVIKKEGDSIALVMLPGVHYFTGQVFDIKTITHTAHAKGCYVGFDLAHAVGNIELELHEWDVDFSCWCTYKYLNSGPGNLGAAFVHKKFNDAKLPKFLGWWGHRESTRFEMSNDLDFASGAESYRLSNPPPLLVACVLASLKVFGKTSIRKLREKSFLLTGYLEFMLKHYFSKQPGSSKPSVEILTPTNFNERGCQVSLRFSCSLLEVSNKLKKEGMIFDTRQPNVMRVSPVPLYNTFHDVYRFVQALRKSLSNYNQN
The following text describes a protein:
Function:
Involved in vesicular protein trafficking.
Miscellaneous:
MISCELLANEOUS: Present with 20700 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MLLTSLLQVFACCLVLPAQVTAFYYYTSGAERKCFHKELSKGTLFQATYKAQIYDDQLQNYRDAGAQDFGVLIDIEETFDDNHLVVHQKGSASGDLTFLASDSGEHKICIQPEAGGWLIKAKTKIDVEFQVGSDEKLDSKGKATIDILHAKVNVLNSKIGEIRREQKLMRDREATFRDASEAVNSRAMWWIVIQLIVLAVTCGWQMKHLGKFFVKQKIL
The following text describes a protein:
Function:
Activates the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Ex acts synergistically along with Mer and Kibra to regulate the Hippo signaling pathway. Involved in the control of cell proliferation in imaginal disks. May bind to certain proteins of signal transduction pathways by interaction with their SH3 domains. Required for apical localization of Schip1.
Subcellular Localization:
Apical cell membrane. Note=Apical surface of disk cells.
Sequence:
MRAFCTVSAPLEVCASSAEQLSPGSRFLALRLLGQQQPKTLYFLVDAKSRVREVYTQTCLHFATQGMLDTELFGLAVLIDGEYMFADPESKLSKYGPKSWRSSHTHGLDANGRPLLELHFRVQFYIESPFMLKDETSRHNYYLQLRHNILQRDLPREQAEQALVFLAGLALQADLGDAPPGTSNSKDDSGEETSASPSNGGRGLSATTTLPKISKRANERMLRLSTYVASTSKRETIPLPPSLPPNGADYYRIEDYLPSGLHTPWARSAMRACHREHLGMATAEAELLYIQQACSLHETINAHTYRMRLAKSEQGSGSAWFVVYAKGIKILGGESTNSSSNPETTTFLWPNITKLSFERKKFEIRSGESRITLYAASDEKNKLLLTLCKDTHQWSMKLAARLKEVSKREEEEAAESQRLHASYACSRSLLLPYKSKNEQRISVISSTSSNTTSGIVSDRVHSEDELEIMINTPPAPLAAPSTESLALAHLLDRPSVSRQTSSVGQMSLKDLEEQLAALSVRPQDASSNGATIVTNSSVQRNSMGTTANDSSTATDSPSSQHNIGSQCSSTCSTVVVTSPVNGAGASSSGAPIPVHSTSSSLELGFSHTAQNSALSETSPDDFLSTSAREETESVSGASGVYTLAHGAPPTETSGVYTMHSSELTGQSSEIAESEKSSHYGMFQPQKLEETHVQHSDSVDGKKKEDFRPRSDSNVSTGSSFRGDGSDPTDNKHSLLSAEELTNLIVGRGTYPSRKTVSSSLHSDCDYVTLPLGDQGEEEVDQPPAPPPPYSARHEKTGLCGPPIAKPIPKPIAVVAPKPDSPPCSPPVPPAPIPAPPPAIRRRDPPPYSISSKPRPTSLISVSSSAHPAPSAAGSMSSLKSEEVTARFITTRPQISILKAHTSLIPDGAKPSYAAPHHCSSVASSNGSVCSHQLSQQSLHNSNYAGGSQASLHHHHVPSHHRHSGSAAIGIVPYGLHKSTASLHHQQSCVLLPVIKPRQFLAPPPPSLPRQPPPPPPPNHPHLASHLYEREMARKQLELYQQQLYSDVDYVIYPIQDPAVSQQEYLDAKQGSLLAAMAQAAPPPPHHPYLAMQVSPAIYRSTPYLPLTLSTHSRYASTQNLSDTYVQLPGPGYSPLYSPSMASLCSSYEPPPPPPLHPAALAAAAAAGAGSSSSSMFARSRSDDNILNSLDLLPKGKRLPPPPPPPYVNRRLKKPPMPAPSEKPPPIPSKPIPSRMSPIPPRKPPTLNPHHANSPLTKTSSGAQWAGERPRPDLGLGLGLNRGNNSILAQLQASMVAQSHAQAQAQALDIALLREKSKHLDLPLISALCNDRSLLKQTKVVINPKTGQEMPTSSAQPSGATTNGVANSSAGAGTLSKARKGSTVSHRHPQDKLPPLPVQQLAEANNYVIDPAVMMKQQQQQQQHNKTS
The following text describes a protein:
Function:
Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. May inhibit NF-kappa-B transcription, and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). Has a negative regulation effect on G1 to S transition of mitotic cell cycle. Involved in growth regulation. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Translocates from the cytoplasm to the nucleus, after hormone exposure.
Sequence:
MEAPGEGPCSESQVIPVLEEDPVDYGCEMQLLQDGAQLQLQLQPEEFVAIADYTATDETQLSFLRGEKILILRQTTADWWWGERAGCCGYIPANHLGKQLEEYDPEDTWQDEEYFDSYGTLKLHLEMLADQPRTTKYHSVILQNKESLKDKVILDVGCGTGIISLFCAHHARPKAVYAVEASDMAQHTSQLVLQNGFADTITVFQQKVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDTWLKGDGIIWPTTAALHLVPCSAEKDYHSKVLFWDNAYEFNLSALKSLAIKEFFSRPKSNHILKPEDCLSEPCTILQLDMRTVQVPDLETMRGELRFDIQKAGTLHGFTAWFSVYFQSLEEGQPQQVVSTGPLHPTTHWKQTLFMMDDPVPVHTGDVVHGFCCVTKKSGMEKAHVCLSELGCHVRTRSHVSTELETGSFRSGGDS
The following text describes a protein:
Function:
Auxiliary spliceosomal protein involved in splicing of specific pre-mRNAs that affect multiple aspects of development.
Subcellular Localization:
Nucleus.
Sequence:
MKPSKSHHKEKTARRREEKLEESDNPKYRDRAKERRENQNPDYDPSELSSFHAVAPPGAVDIRAADALKISIENSKYLGGDVEHTHLVKGLDYALLNKVRSEIVKKPDGEDGDGGKTSAPKEDQRVTFRTIAAKSVYQWIVKPQTIIKSNEMFLPGRMTFVYDMEGGYTHDIPTTLYRSKADCPVPEEFVTVNVDGSVLDRIAKIMSYLRLGSSGKVLKKKKKEKDGKGKMSTIANDYDEDDNKSKIENGSSVNISDREVLPPPPPLPPGINHLDLSTKQEEPPVARTDDDDIFVGEGVDYTVPGKDVTQSPISEDMEESPRDKEKVSYFDEPAYGPVQEKVPYFAEPAYGPVQPSAGQEWQDMSAYGAMQTQGLAPGYPGEWQEYQYAEQTGYQEQYLQPGMEGYEVQPETDVLLDPQLMSQEEKDRGLGSVFKRDDQRLQQLRESDAREKDPTFVSESYSECYPGYQEYNHEIVGSDEEPDLSKMDMGGKAKGGLHRWDFETEEEWEKYNEQKEAMPKAAFQFGVKMQDGRKTRKQNRDRDQKLNNELHQINKILTRKKMEKEGGDVASLDAAEAQTPKRSKH
The following text describes a protein:
Function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular Localization:
Cytoplasm.
Sequence:
MERLLMNVEEVVTREEFLRLKGGSAYLGFEPLWPIHIGWLIWAYKLAELKEAGFDVIVLVATWHAWINDKGSIEELRAHGERVRAVLDRIGKFKYVYGDDVAKDPKYWELVVKIAKETSLARVKRATPVMGRRAEEVELDFSKLMYPLMQVADIFYLGVDVAVGGMDQRRAHMLARDVAEKLGLKKPIALHTPIITSLSGTGRMEGTHREIDEVYAMYKMSKSKPQSAILITDSEEDVRKKIWAAYCPPRETKFNPVFEIAAYLLIPYHGPLEIKGRRYEEGNALERDYREGVVTPQELKEAVASALVGLLSKLKL
The following text describes a protein:
Function:
Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.
Sequence:
MISYCPICAKPVYFAERKRSLGKDYHPLCLKCFQCKRQLTAGQHAEYDDKPYCNRCYLLHFGPRGKGARGSTSRASTHATTVSSSAIPAAENKDRC
The following text describes a protein:
Function:
Forms chloride channels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MTVSYALSVSSARYSAFLKLLQKWKGSVLKAVWAELLVWIGLYTAIALIINLSFSPETKTAISIEAARLDDQLGILDIKFMLGFFVTIVVDRWKTILQNIGFIETVALSVSTIIRGSDDNVRLARRSIIRYLVLSQAMVYRDISMRVRRRFPTMKSLMEAGFIFENELHELEQTETGYNKYWVPINWCNSIVWRMQEQKYIEAPVSTNNVLNNIRDFRTQLENLCKFDWVPIPISYPQIVFLAVRIHFFFTLFTRQYIPMETEEYLWYRHIPLIPATSFFLYLGWMKVAEALLNPFGEDDDDFEGNWVIDKNIKTGMQIVDESHAECPILNIDQFSDPKFGPMYPSVLAEHPHILQGSAADVVIPDSDKSKMVHVDSKTSVASGASGSNDQRRESSIRRRFRRLSTRLKLGRSISHPKGQTVKSPGGESTQSAFSNLEFVTEENEDPRADMRIDMEEEKPNKK
The following text describes a protein:
Function:
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit Sdhb of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF3. Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MSRPSRLQRQVLSLYRELLRAGRGTPGAEARVRAEFRQHASLPRTDVLRIEYLYRRGRRQLQLLRSGHATAMGTFVRPRGPAEEPGDATAPGTRLDDGGAPKNSCEDTGARETRSDGR
The following text describes a protein:
Function:
Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. A protease cascade involving ndl, gd, snk and ea results in activation of the spz Toll receptor ligand; acts downstream of ndl but upstream of snk and ea. Activation of ea requires activation of the ndl-gd-snk protease cascade and sulfation of a vitelline membrane component by pip. Localized activation of the Toll receptor in the ventral region of the embryo defines cell identities along the dorsal-ventral continuum.
Subcellular Localization:
Secreted.
Sequence:
MRLHLAAILILCIEHVTKAVAQGMPISPCPKVFQYRFDGSEWFGLMAVRSPDGHQPLHIRVTLSMRGKPTTYTQNYLGEIELLTRGKFTHNAPVLYKIRFPKHHFPPKLLLMSANNHVICFGSGEHSIFMTQIQLEHIRKLSFIPDKKSSLLLDPEEEEVRKTDDKPPSTPHIQFKKKPFAQAPKEICGRIDRDLDFHLSQRTESLHVAIGEPKSSDGITSPVFVDDDEDDVLEHQFVDESEAEAIESDSADSLPSITRGSWPWLAAIYVNNLTSLDFQCGGSLVSARVVISSAHCFKLFNKRYTSNEVLVFLGRHNLKNWNEEGSLAAPVDGIYIHPDFNSQLSSYDADIAVIILKDEVRFNTFIRPACLWSGSSKTEYIVGERGIVIGWSFDRTNRTRDQKLSSELPGKKSTDASAPKVVKAPIVGNAECFRANAHFRSLSSNRTFCAGIQAEERDTHQSGASIYTGISGAGLFIRRNNRWMLRGTVSAALPAVETPDAESSHKLCCKNQYIIYADVAKFLDWITAFVI
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MMSSIPPLLPKLDAILVLDGDGNRLAGKYYGDFMKTPTAADANDKTTTAQSVEQLRNSFERQLQSKIGGIAARPDAAEVVTVLGKTAVFCGGSSTQGGQGGGDVRVVHIGPPGESELVLAHLAEGMYEALSHLMGGATDRNMILDNLELVFLLIDEHCDGGIILETDGHKLASSVLLRDEHDNREGDEQGRQGQGGGGQQGGMSMGGGFGGMGGGDMTIAQALRQAREQIISNLSQN
The following text describes a protein:
Function:
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPWVLSALVLTVAFWVLAFCGFDNYPSSRLLALCFAPFGALLRWYLSLYNSKPMCKRFPFFTFLPNVAASCLSCAMEIVGSVVYQDSASAYRHFVMYGQGAVMVGFLGSLSTVSTWVNELDGLSSRRLFWAYRYGLASVIISQLASVFILGMYDAYGSDPLIG
The following text describes a protein:
Function:
Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Not involved in the GTP-dependent ribosomal translocation step during translation elongation.
Subcellular Localization:
Mitochondrion.
Sequence:
MPWCNTRLRTCGASPKIFLRRVRCPVLLHNWTIGRVSSVSKMILRFLRSYSKRVDITRVRNIGIIAHIDAGKTTTTERMLYYSGKIKRIGDVDHGDTITDFLPQERSRGITIQSAAISFNWRDNYTVNLIDTPGHADFTFEVIRSLRVLDGCVTILDAVAGVEAQTEKVWKQAAEIPKVCFINKMDRVGAGYSRAVKELIVKLKTRVLLLNTPLFAARDSSADPVFVGVLDAVNGQLLEWDPEDPDKISAKAVDKECAHYEELVSAREALVETLSEVDEKLVEYFLGEADGDYMKVPVEVLNESIRRATLSQYAVPVLCGASFKNIGVQPLLDAVVDYLPSPAEARLPELSNKDLPVQHHLKNGLLVNKNANLCLALAFKVTTDPIRGAMVFIRVYSGVLNSGHTVYNSSTGVKFKLGKLIKMHANVAEDIKSLHPGDIGVLAGANVADHVRTGDTIVAHCTSKDGIRSFKKAELALRIHPIDIPPPVFSAAVEPRTLGNKKAMDESLTQLTREDPSLVIVRDEETGQTVMNGMGELHLEIAADRLLNEFKAPVRVGKVAVSYKETINTATETKHSETDDGYSFELEVRQYNEEDKVLFSNGWYPLGSDNNYLVIDPNPRFNEDNWPFPLKYEAFVNSIISCCIVALQRGGKTAGFPLHSCVIHVKRWRLPLDCAAAASILLTVRPLIISALTSLPTSAFSILEPIMNVEVTVQQQDLGSVVQDLTGARKANILSIDDEHHWADAAVTDKDVHLFHDIAEKQYLPPDSTVFQAKLNKEGQTGKIVKAHVPLKEMVSYMNKLRMLTKGRGSFHMSYLGMERASSDRVDGILEDADL
The following text describes a protein:
Function:
Major capsid protein that self assembles to form an icosahedral capsid with a T=147 symmetry. Represents around 50% of the total virion protein mass.
Subcellular Localization:
Virion.
Sequence:
MSISSSNVTSGFIDIATKDEIEKYMYGGKTSTAYFVRETRKATWFTQVPVSLTRANGSANFGSEWSASISRAGDYLLYTWLRVRIPSVTLLSTNQFGANGRIRWCRNFMHNLIRECSITFNDLVAARFDHYHLDFWAAFTTPASKAVGYDNMIGNVSALIQPQPVPVAPATVSLPEADLNLPLPFFFSRDSGVALPTAALPYNEMRINFQFHDWQRLLILDNIAAVASQTVVPVVGATSDIATAPVLHHGTVWGNYAIVSNEERRRMGCSVRDILVEQVQTAPRHVWNPTTNDAPNYDIRFSHAIKALFFAVRNTTFSNQPSNYTTASPVITSTTVILEPSTGAFDPIHHTTLIYENTNRLNHMGSDYFSLVNPWYHAPTIPGLTGFHEYSYSLAFNEIDPMGSTNYGKLTNISIVPTASPAAKVGAAGTGPAGSGQNFPQTFEFIVTALNNNIIRISGGALGFPVL
The following text describes a protein:
Function:
Energy-dependent efflux transporter responsible for decreased drug accumulation in multidrug-resistant cells. Specifically present in limbal stem cells, where it plays a key role in corneal development and repair.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
LLFSRTAEQPRLRKEAVGSIEIFRFADGLDITLMILGILASLVNGACLPLMSLVLGEMSDNLISGCLVQTNTTNYRNCTQSQEKLNEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSALAEDIGWFDSCDIGELNTRMTADIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSNELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEPGYTIGTVLAVFFSVIHSSYCIGAAVPHFETFTIARGAAFNVFQVIDKKPSIDNFSTAGYKPEFIEGTVEFKNVSFNYPSRPSIKILEGLNLRIKSGETVALVGPNGSGKSTVVQLLQRLYDPDDGFVSAASKTMHNHIGVVSQEPVLFGTTISNNIKYGRDDATDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGEQKQRIAIVRALVRNPKILILDEATSALDSESESAVQAALEKVSEQKLFLFPYSWLIIIVTLKDGMVAEKGAHAELMAKRGLYYSLVMSQDIKKADEQMESMTYSTERKTNSLPLRSVNSIKSDFIDKAEESTQSKEISLPEVSLLKILKLNKPEWPFVVLGTLASVLNGTVHPVFSIIFAKIITMFGNNDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKENSTGGLTTILAVDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEAVKNIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAIGETLVLAPEYSKAKSGAAHLFALLEKKPNIDSRSQEGKKPDTCEGNLEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRFYDPVQGQVLFDGVDAKELNVQWLRSQIAIIPQEPVLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGTQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQSVQ
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:
MALQQIFQDQIPETTFDQRDISFEKWNTIDLDKLEENSPEGFECNICLDVVHDPVVTLCGHLYCWPCIYKWIHFKTISSKNIDNQQPNCPVCKAEVSQKTLIPLYAHGQASKTSGKALNLGIVIPQRPPTPRCRSHGLIPNNNMPPLSQQSHDHHRNYTNTEHMLSPGGTTTGEIVYARMFGNSLNTNLYTYSSSYNLAGSNSPRLRRQLSHADQSLSRICFFLCCCLVTCLLLF