lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore. Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases.
Subcellular Localization:
Mitochondrion outer membrane; Single-pass membrane protein.
Sequence:
MESGHAAYETEAEVEGEKGQKKILLANAGQDSLKSFFVKKKKKKKKKKNIYIYIYIYIYIYIYISSPSACPAGGPGTLLSPDKLLPKGNAEKTEEEQERKTTVGSDGVVPERVRPAAGATFDVSLFVAQTTYRFSRTASWIGTTCFTIPVLPVVFETEKLQVERQQQVQQRQIVWGPNTGVSAGMPVALPSKKGRKSWKNLDCYCYMTCLGGTSLKIQ
The following text describes a protein:
Function:
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Subcellular Localization:
Peroxisome.
Sequence:
MPDEIVVKEQCHGKARVRVARVWRGDGKDHEFVEWTISIILSSDCIPAYSAGDNSSIVATDSIKNTVYALAKLCHQPVSIETFGIKLASHFLDTYKEVTGACVSLVQNNWERVSIDGIPHQHGFKLGSQKRTAEITISRDKSSVDVVSGFTDLSLLKTTKSGFEGFIRDKFTLLPEVRERLLASTVTAKWRYARKPSCYTGTYDKVTRTLFETFFGPSKSGVYSPSVQNTLYLMAQEVLRSVPEVSSIELNMPNLHFLPVNMPTVGVKFDHDVYLPTSEPHGSIQACLARKTLTSKL
The following text describes a protein:
Function:
Subunit e, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MVPPVQVSPLIKLGRYSTLFLGMAYGAKRYNYLKPRAEEEKRLAAEEKRKRDEQKRIERELAEAQEDTILK
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MVYITTNLRITQKLSIVTQLADLIFSASANASGVATVFFCLFYQNKLIEVISKLHKLDNKLKHMLIWKSYKRTQIFITCELFFVILLWISFFLNFMLHCNNTTWRCLYRWIVLYTLSKMSQVMLIQFCAFVVVLKQKFCVVNQYIKQVCKLNNGHYKNFLSQVEIIHNEILVTHNEIQTIFSVPLLMKIASQFVGIFCSLYFCIFGYIYDDEMVVPQNFHDIFLPLLCILTNTLEILITVTVCELTILEYKRTKKLLYRIPVTKTDSMLIRNINLFSLQLAHQKLEFSACGFFLINGTLLHTIVGAVTVYLIMFIQFDIATTTKGG
The following text describes a protein:
Function:
Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MKIAILYREEREKEGEFLKEKISKEHEVIEFGEANAPGRVTADLIVVVGGDGTVLKAAKKAADGTPMVGFKAGRLGFLTSYTLDEIDRFLEDLRNWNFREETRWFIQIESELGNHLALNDVTLERDLSGKMVEIEVEVEHHSSMWFFADGVVISTPTGSTAYSLSIGGPIIFPECEVLEISPIAPQFFLTRSVVIPSNFKVVVESQRDINMLVDGVLTGKTKRIEVKKSRRYVRILRPPEYDYVTVIRDKLGYGRRIE
The following text describes a protein:
Function:
Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.
Subcellular Localization:
Nucleus.
Domain:
The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.
Sequence:
MVKLANPLYTEWILEAIQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNPGRFSSVKPGTFPKSAKGSRGSCNDLRNVDWNKLLRRAIEGLEEPNGSSLKNIEKYLRSQSDLTSTTNNPAFQQRLRLGAKRAVNNGRLLKDGPQYRVNYGSLDGKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTTNVKALRWQCIECKTCSACRVQGRNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDEGSMNAFTGRGSPGRGQKTKVCTTPSSGHAASGKDSSSRLAVTDPTRPGATTKITTTSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATGTTQKLKPPPSSLPPPTPISGQSPSSQKSSTATSSPSPQSSSSQCSVPSLSSLTTNSQLKALFDGLSHIYTTQGQSRKKGHPSYAPPKRMRRKTELSSTAKSKAHFFGKRDIRSRFISHSSSSSWGMARGSIFKAIAHFKRTTFLKKHRMLGRLKYKVTPQMGTPSPGKGSLTDGRIKPDQDDDTEIKINIKQESADVNVIGNKDVVTEEDLDVFKQAQELSWEKIECESGVEDCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYHHHERHISIKAISRATGMCPHDIATTLQHLHMIDKRDGRFVIIRREKLILSHMEKLKTCSRANELDPDSLRWTPILISNAAVSEEEREAEKEAERLMEQASCWEKEEQEILSTRANSRQSPAKVQSKNKYLHSPESRPVTGERGQLLELSKESSEEEEEEEDEEEEEEEEEEEEDEEEEEEEEEEEEEENIQSSPPRLTKPQSVAIKRKRPFVLKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIEVEEDGRKPVLRKAFQHQPGKKRQTEEEEGKDNHCFKNADPCRNNMNDDSSNLKEGSKDNPEPLKCKQVWPKGTKRGLSKWRQNKERKTGFKLNLYTPPETPMEPDEQVTVEEQKETSEGKTSPSPIRIEEEVKETGEALLPQEENRREETCAPVSPNTSPGEKPEDDLIKPEEEEEEEEEEEEEEEEEEGEEEEGGGNVEKDPDGAKSQEKEEPEISTEKEDSARLDDHEEEEEEDEEPSHNEDHDADDEDDSHMESAEVEKEELPRESFKEVLENQETFLDLNVQPGHSNPEVLMDCGVDLTASCNSEPKELAGDPEAVPESDEEPPPGEQAQKQDQKNSKEVDTEFKEGNPATMEIDSETVQAVQSLTQESSEQDDTFQDCAETQEACRSLQNYTRADQSPQIATTLDDCQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQSAISVPSLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSNLTSSSLTQSSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLAEIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHISMRTKSASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGTQPYAQQPMQTPPHGNMMYTAPGHHGYMNTGMSKQSLNGSYMRR
The following text describes a protein:
Function:
May be involved in vacuolar sorting and osmoregulation.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MQFGKSLLKHVYTRTFKSSLTCSIFAFTLLMIFFVLDWKRMNVYPRLDEIPGLNVLRAWDDLQEITKSPHPYNSHASDVVRNYILEELYKLKKQDEGNVEVIDDLSSTTTFIMPDTNIRSYFEGSNILVRFRGDNERLRPILLSSHFDSVSTGFGATDNGMGVASALELARYYAEHKPERDLIINFNNAEEDYLYGARAFTEHEWSKNVTAFLNLEGAGAGGKALLFRSTNNHVARSYFKSNRFAFASVLGIDAFKRGVIKSETDYVVYEKMNNGTAGLDLAFFRNRGIYHTERDDIQHTSIFSLNHMLVNAFISLRNLLDEKSQHFKGSSPLYFPVFGSYWQINLNLHLFLNVVFLIACPAILFMCLFRFPSLYAQLKKPCYLICFTLSSLFVLIFDYVVVQSLTKLNPYVIHSSPDAVLAFFFLTNLLGLVYSFRYVATHSRMSNEELSCIEIVLIWYVSMFWYISLLIATLTSIVRGLGSLYFVNFGFFCSFFCCILTLIRVRYFVDRMVTINRPANPEQMPLVQSTSGNAYGTSRYPQHRLKAVVSKSASVKLNDNLWSVLFFSCLVPLPLFTCYNLLSEVFIPAVHQSLIDGPYSNTCYKFAVILVFMAIINSSPFVFRALSKKSSAILLMLWVSLLFNILRAEPFNEKAPIKFRVFQHLNLDTSENLFHVQNIEPYTQKVLNDYPKIISDTSYQCVDRDCFYEAEEPTLGFDGPLQNAINITLHKSLNSSLAELRVDAFETKWCYFDFSVPVYVDSINGFEVQEEHQSLRLGVRNFGTPFVVKTVAKDEDSPTNVTVTCMWDEFDHDKIPSYTSLLNYIPAWSVLTKNSTGLLKMSKTHVM
The following text describes a protein:
Function:
Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells.
Subcellular Localization:
Nucleus inner membrane; Single-pass membrane protein; Nucleoplasmic side. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity).
Sequence:
MDDYAVLSDTELAAVLRQYNIPHGPILGSTRKLYEKKIFEYETQRRRLSPPSSSSSSFSYRFSDLDSASVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTRTYGEPESVGMSKSFRRPGTSLVDADDTFHHQVRDDIFSSSEEEGKDRERPIYGRDSAYQSIAEYRPISNVSRSSLGLSYYPRSSTSSVSSSSSSPSSWLTRRAIRPEKQAPTAALGQDRQVPLWGQLLLFLAFATFLLFVYYSIQAQEGNPFWMDP
The following text describes a protein:
Function:
[GLV7p]: Signaling peptide (root growth factor) that maintains the postembryonic root stem cell niche. Regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells (By similarity).
Miscellaneous:
MISCELLANEOUS: 'Golven' means irregular waves in Dutch.
Subcellular Localization:
[GLV7p]: Secreted.
Sequence:
MTTLSKILCVLIILLLCFSFRYSLHEDGNQQSSRDFVSTAKAIKYGDVMKKMIRGRKLMMASGEKEEAETKMKRGNRETERNSSKSVEEDGLVAYTADYWRAKHHPPKNN
The following text describes a protein:
Function:
Glycosyltransferase that catalyzes the synthesis of dodecaprenyl-phosphate galacturonate (Dod-P-GalA), likely from UDP-GalA and dodecaprenyl-phosphate. Dod-P-GalA is the lipid donor required for GalA transfer to lipopolysaccharide (LPS) specific residues catalyzed by the GalA transferases RgtA, RgtB, RgtC and RgtD.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MQTTVEPIRGTNDPVQSLELSLVVPIFNEEQSVGPLVERVAAAMVSYPHRWELILVDDGSTDATLVNARKYVGREGLALRIVELQRNFGQTAAMQAGIDTARGRLIATMDGDLQNDPKDIPSMVSELERRELDLLVGWRKNRKDGLFLRKIPSWCANYLIGRITGVKLHDYGCSLKIYRASIIKQVKLMGEMHRFIPAWVAGVVPSSRIGEMAVTHHAREHGVSKYGISRTFRVILDLLSVMFFMRYKARPGHFFGSLGLGLGALAMLILLYLGFDKFILGNDIGTRPMLMVGVVLLLSSVQMITTGILAEMIARTYYRDDASPNYIVRQIFDDQSQA
The following text describes a protein:
Function:
Tegument protein that plays different roles during the time course of infection (By similarity). Participates in both the accumulation of viral mRNAs and viral protein translation at late time of infection (By similarity). Modulates the RNase activity of the virion host shutoff protein ORF17 probably to ensure necessary levels of key cellular mRNAs and proteins (By similarity). Plays a role in microtubule reorganization that occurs after viral infection by stabilizing microtubule network (By similarity). Plays a role in the inhibition of host innate immune system by targeting the CGAS enzymatic activity which is the principal cytosolic DNA sensor that detects invading viral DNA. Acts by mediating disruption of liquid-like droplets in which CGAS is activated, thereby preventing CGAS activity.
Subcellular Localization:
Virion tegument. Host cytoplasm. Host nucleus. Host Golgi apparatus. Note=One of the most abundant tegument protein (about 2000 copies per virion). Localizes in the cytoplasm at 8 hours postinfection and in the nucleus at 16 hours postinfection. During virion morphogenesis, this protein probably accumulates at the trans-Golgi where secondary envelopment occurs.
Sequence:
MASSDGDRLCRSNAVRRKTTPSYSGQYRTARRSVVVGPPDDSDDSLGYITTVGADSPSPVYADLYFEHKNTTPRVHQPNDSSGSEDDFEDIDEVVAAFREARLRHELVEDAVYENPLSVEKPSRSFTKNAAVKPKLEDSPKRAPPGAGAIASGRPISFSTAPKTATSSWCGPTPSYNKRVFCEAVRRVAAMQAQKAAEAAWNSNPPRNNAELDRLLTGAVIRITVHEGLNLIQAANEADLGEGASVSKRGHNRKTGDLQGGMGNEPMYAQVRKPKSRTDTQTTGRITNRSRARSASRTDARK
The following text describes a protein:
Function:
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
Subcellular Localization:
Late endosome membrane; Peripheral membrane protein.
Sequence:
MMTNQASLESSFSFLTQLTADELESLENDWERIKKLVDDSDVIKKQQMEKENLSASIKSLAEYNLSLEPKLNQAKVQLAQTHEQAVETFKSYDKNRLLMEGTPSKTQPDVQLALLQAETAKSEEECEKLVDNLMNKTVDVDTFITDYLTTRTLSHIRRIKCDKMTELLRQQQRRRESAPLPKTSNVQHEQYSAYSPTHPLNYSSRPMQSSYPNPMPSSSNYYPGPTSLIGYNNQVPGYMPAAGPPYPINNFAQPPPIASAIFSPGAPSYPQSSLY
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Domain:
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation; The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters; The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Sequence:
MNSLNLEINKEQEVLVISDIDNSSSILDEIKSQCKALTDSLQKSQQQNQYDSIVIISNKDFNKSLISMYSGLLKKGGKLSIYQTGENKDLINSSLDFMMAGLVDFESKPSVNQFKTIIQISKPSWDTNESESINIPTDSVNPWASIEQSSSERINENDLVNETDKNSKPATTLDDCEVGKTKKACKNCTCGRAEEEEKESKPKLTKEMIENPGVNSSCGNCSLGDAFRCGGCPYRGLPTFKVGEKIALPDDFLVDDI
The following text describes a protein:
Function:
Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100.
Domain:
The strongly acidic region might serve as a transcriptional activation domain.
Sequence:
MAPPAAAPELGSCCICLDAITGAARALPCLHAFCLACIRRWLEGRPTCPLCKAPVQSLIHSVASDECFEEIPVGGGPGADGALEPDAAVIWGEDYDAGPIDLTAADGEASGAGGEAGAADGSEAGGGAGGAEEAGEARGAGAGRAAGAAGGRAGRGADAAQEFIDRVARGPRLPLLPNTPEHGPGAPYLRRVVEWVEGALVGSFAVTARELAAMTDYVMAMLAECGFDDDGLADAMEPLIGEDDAPAFVRSLLFVAARCVTVGPSHLIPQQSAPPGGRGVVFLDTSDSDSEGSEDDSWSESEESSSGLSTSDLTAIDDTETEPETDAEVESRRTRGASGAARARRPAERQYVSTRGRQTPAVQPAPRSLARRPCGRAAAVSAPPSSRSRGGRRDPRLPAAPRAAPAAQARACSPEPREEGRGAGLGVAAGETAGWGAGSEEGRGERRARLLGEAGPPRVQARRRRRTELDRAPTPAPAPAPAPAPISTVIDLTANAPARPADPAPAAAPGPASAGAQIGTPAAAAAVTAAAAAPSVARSSAPSPAVTAAATSTAAAISTRAPTPSPAGRAPAADPRRAGAPALAGAARAEVGRNGNPGRERRPASAMARGDLDPGPESSAQKRRRTEMEVAAWVRESLLGTPRRSSAALAPQPGGRQGPSLAGLLGRCSGGSAWRQ
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MAPPAARLLVLLWAFAAARDASDSALFNEEVKRTVDLSSHLAKVTADVTLAHPGGAAPAAASFLVALEPELEAQMAHLGVQVKGEEEEENTLEVRETKIKGKSGTFFTVKLPSPLTAGAKIRVSIETVFTHALQPYPTQITQAEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNIESYTKLGNPTRSEDMLEYGPFKDIPAFSQDPFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEETVDLKHTGAVLKGPFSRYDYQRQPDSGISSVKSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIIGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVTDALTVKIILPEGAKNIHVDSPYEINRAPDELHYTYLDTFGRTVLVAHKNNLVEQHIQDIVVHYTFNKILMLQEPLLVVAAFYILFFTVILYVRLDFSITKDPAAEARMKVACITEQVLTLVNKRLGLYRHFDEAINKYKQSRDISTLNSGKKTLETEHKALTNEIASLQARLKTEGSDLCDKVSEIQKFDSQVKDLVLKSSGEAERLVAGKLKKESGMPAG
The following text describes a protein:
Function:
Putative transcription regulator that controls rice tillering by initiating axillary buds and promoting their outgrowth. Rice tiller is a specialized grain-bearing branch that is formed on the unelongated basal internode and grows independently of the mother stem (culm) by means of its own adventitious roots.
Subcellular Localization:
Nucleus.
Domain:
The C-terminal part of the protein is important for tillering. Mutant moc1, in which the last 124 amino acids are missing, is mono culm.
Sequence:
MLRSLHSSSSSDTDNNSGGCKNNGGGGGEAAAAVEGGGDQRAVAAAAPSTRDLLLACADLLQRGDLPAARRAAEIVLAAAASPRGDAADRLAYHFARALALRVDAKAGHGHVVVGGGAARPASSGAYLAFNQIAPFLRFAHLTANQAILEAVDGARRVHILDLDAVHGVQWPPLLQAIAERADPALGPPEVRVTGAGADRDTLLRTGNRLRAFARSIHLPFHFTPLLLSCATTAPHHVAGTSTGAAAAASTAAAATGLEFHPDETLAVNCVMFLHNLAGHDELAAFLKWVKAMSPAVVTIAEREAGGGGGGGDHIDDLPRRVGVAMDHYSAVFEALEATVPPGSRERLAVEQEVLGREIEAAVGPSGGRWWRGIERWGGAARAAGFAARPLSAFAVSQARLLLRLHYPSEGYLVQEARGACFLGWQTRPLLSVSAWQPSSS
The following text describes a protein:
Function:
Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis. Moreover, through a functional complex formed of ABCB7, FECH and ABCB10, also plays a role in the cellular iron homeostasis, mitochondrial function and heme biosynthesis. In cardiomyocytes, regulates cellular iron homeostasis and cellular reactive oxygen species (ROS) levels through its interaction with COX4I1. May also play a role in hematopoiesis.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MALLAIHSWRWAAAAAAFEKRRHGVILIRPFVSIGGPGAQCRSSQLGGSGTARTSQISESLRHTTWQRLGKGNSRQLLDATRAVQAWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLAFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVTLVSGVLYYRCGAQFALVTLGTLGAYTTFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNENYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKDKAMASPLHITPQTATVAFENVHFEYIEGQKVLNGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGNIYLAGQNIQDVSLESLRRAVGVVPQDSVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILSAMRDAVKHRTSIFIAHRLSTVVDADEIIVLEQGKVAERGTHHGLLANPGSIYSEMWHTQSSRVQNHENPKWDAKKENVSKEEERKKLQEEIVNSVKGCGNCSC
The following text describes a protein:
Function:
Microtubule-associated protein that is essential for cortical microtubules organization and function.
Subcellular Localization:
Cytoplasm, cytoskeleton. Note=Associated to microtubules.
Sequence:
MSTEDEKLLKEAKKLPWDERLQHKNWKVRNDANIDLAALCDSITDPKDARLREFGPLFKKTVADSNAPVQEKALDALLAFQRAADADASRYAKEVCDAIVAKCLTGRPKTVEKAQAAFLLWVELEAAEVFLESMEKAVKNKVAKAVVPAIDVMFQALSEFGAKVVPPKKILKMLPELFDHPDQNVRASSKGLTLELCRWIGKEPVKAILFEKMRDTMKKELEAELANVSGIAKPTRKIRSEQEKELEEEVVPEAAGTNNSEEAVPEAPMEIDEYDLVDPVDILTPLEKSGFWDGVKATKWSERRDAVAELTKLASTKKIAPGDFHEICRTLKKLITDVNLAVSVEATQAIGNLAKGLRTHFSGNSRVLLPVLLEKLKEKKPTMTEALSQTLQAMHKSGCITLLDVIEDVRVAVKNKVPLVRSLTLNWVAFCIETSNKATVLKLHKEYVPICMECLNDGTPEVRDASFSVLTAIAKMVGMKPLERSLEKLDDVRKKKLSDMIGSASDTTSGTVAASNTGVGTSAREVMDSSSMRRSAASMLSGKKPVQAVPATKKSGPAKSATAKKTDGGPQSKASAAPVIEDVEPSEMSLEEIEEKLSSVVKSETISQLKSTVWKERLEAISMLKQEVESLTELDKSAELLVRLLCAVPGWSEKNVQVQQQVIEVSTYIASTVNRFPKRCVVLCLLGISERVADIKTRGHAMKCLTAFCEAVGPGFVFERLYKIMKEHKNPKVLSEGILWMVSAVEDFGISNLKLKDTIDFCKDIGLQSSAAATRNATIKLIGVLHKFVGPDIKGFLSDVKPALLSTLDAEYEKNPFEGTASAPKRTVRAADAVSSASSGTSDGLPREDISAKITPTLLKNLGSPDWKLRLESIDAVSKIVEEAHKRIQPTGTVELFTALRARLYDSNKNLVMATLSTIGGLASAMGPAVEKSSKGILADVLKCLGDNKKHMRECTLTALDLWVAAAQLDKMVPYITVTLGDQKTGSEGRKDLFDWLSKHASNMSDPSEALPLLKPSASSLMDKSSEVRKAAESFMNEILKICGQDVVAKNLKDLPSPTLAIVAERLKLSTVHEGFSDSVKMVTTSMSLPSKAGSKNNKHGPNDRGSNVSKAVSQRGIPARSSVTMISSQDSIQSQALFNIKDSNKEERERRVLVRKFKFEEPRREQIDELKIELFRHFREDVSLRLWNSDFKRQIDGIELLQKALPSSRKEVIELLDILLRWFVLRFCESNTTCLLKVLDFLPELFDVLKDQSYMLTEAEAAIFLPCLMEKSGHNIEKVREKMGELIKQMVNIYSLPKLLPYILEGLRSKNNRTRIECVDIIGYFMDHHGTEVSGLLKNLPSVAALTAERDGEIRKAALNTLATAYKNLGDDVWRYVGKLSDAQRSMLDDRFKWKAREMDKRREGRPGDARAALRRSVRENGSDIAEQSGEAVSRSMAGSMISRENFGYSDAHMVPRQMATATPGPADWREALDIVALGLPEQSVEGMKVICHELTQAVDPESSVLDDLIKEADRLVSCLAVMVPKTFNFSLSGASSRSCKYVLNTLMQTFQIKRLAHAVKEGTLDNLITELLLWLLDERVPLMDDGSQLLKALNVLMLKILDNAERTSSFVVLINLLRPLDPSRWPSPTPPESLAVKNQKFSDLVVKCLIKLTKVLQSTIYEVDLDRILQSIHIYLQELGMEEIRRRAGADDKPLRMVKTVLHELVKLRGTAIKGHLSMVPIDAEPQPIILAYIDLNLQTLAAARMLTPSGTMGQTHWGDAGSNNPNPSTHSTDAQLKQELAAVFKKIGDKQTCTIGLYELYRITQLYPKVDIFAQLQNASEAFRTYIRDGLAQVEKNAAAGRTPSSLPLSTPPPIAPIPSPKFAPSPVHTKSINNKTDCNEDDAGGDTHPFRGQGEIDNRLQTTNLQTDRYQSSGTLDALRERMKSIQAAAVGANFDGVQARPLPSMNGNTLHGGTRLDADPQTQNIIPPMDERALSGLQARMERLKSGSMEPL
The following text describes a protein:
Function:
Has a role in transcriptional regulation. Acts in parallel with the Ras/MAPK and the PI3K/PKB pathways in the control of cell identity and cellular growth. Essential for regulation of the cytoskeleton and cell growth but not for cell proliferation or growth rate. Required specifically for the microtubule-based basal transport of lipid droplets. Plays a partially redundant function downstream of Raf in cell fate specification in the developing eye. Pair-rule protein that regulates embryonic cellularization, gastrulation and segmentation.
Subcellular Localization:
Nucleus.
Sequence:
MDIRANGRLGISQDNSKSSEEKDMDSILAYDPTSHPDDKPPDYVSSRPRRLSPDEAKLDELSNYAKPYLRNGNFHEVIGILGGTTLREFNKCREGKTIPPYIRSSDPRSHNVHHKVDEVNNQGSNDNKSLQEAHSDDSDKRTSKKSSLSSNTGLERNKSIKKERHYDGNQEIESTSDQALSSSYHRGVPSDRKVKTEISNGPDSCLPSALSSSYHRGVPSDRKVKTEISNGPDSFLPSVSNETIAKTTTLSKRNQGQPSANNDFCVADDTKTSQNKEDTKTKDEDELLQASENNNKIKRQKADNDTKATTVRPKELKIDIIQNGIAKGMIQSTSDEKVSMIAKVKQICEEMVGLPPPISAIRTPSSSSSAFPAFQQKDEATSNRKDIKKESEENNFTDDQNCLEQDLELTDDSDSDNQSDAVEDLTRNGNNAISGKLFPIIDPTPLSESSSESDNDSDIGAVKQVKKRKTPSSDNRKHSPRQKKTPQSYHSAAQSNRIANNIIREVLQYQIPVLSPLRNIHYEKCRNDDDFGRRSYDSAMKSTHCDDCSTSHGKCLSDLSVDDKKFLVSSRSNNDINPDKRKEGQLNPSSNLLRLSAARVALGDINDLIRLTSLSPIRQSGHNVTIGQSNRNNLHLRSKRSRHNFRDTSKLEWPYRRKNMHLTTANPELIGKIYASDNTRHFDCRKGLLKKRNVLSPVKKAYSPAKRKRVLQEVYDFLRIIDCSSLRSYERNRNSLNISNGGEQRHLRTISKNIEADIVVGNSDIAHANTNSKSNQCHDIQMMANVALVSRHQILQEMRNFLRIIELSPLRFGKAFKPAKKPAVFVLATDKETPKIRSTSVRRKLFDHSDTQNLANCIDNIVVSSATSSAQERLPTNLFYRDQWNRSLHDSDSQCDSTSSNPKTDLQHQHVTNENKNSSTLREISVSNVTVDYNTDCVDISSSSCSSQTSTLIRQSIALHDDNVTCSCNGTQDVQCLSNTSSVLRLAKIDNTSEKEENKAAADQHNELFEDVDNSDQQQQQRSPIQNDAVVSSTLPPTADKSYPVSFDLSRLKSIKLSTSKAKKHQDEQAQGFKDKKINVDKQLTSTSGSKDGSLSSGISKSKRINNHNNEGHPLKKKIRNKMAESSDEANVTAVSSRKGISPERNEMKRNKKSDDFKVVSHGKVSEKERLKKASRSIIGSEDDSALLRHKKDKKRKKEIRRVKTSDDDSSSHHRTPPPFKNDNDQSEVQDRGKNCDYKASQSKHLDSDNTQRRKKSVAKESNKDYRSDMAATTFNKQTLKKNTEEVSTIEDLRIKSENLRKQATEHKRSGDANPNIEVKAIKYTEAAMLFIEQALIEEKLDKEKHESRKKEPYYEILNTTATFLNDRSRALLVHKIFLRSRNEIRTLLQNVNEYCAKDKQQMGSISKKLFPFRYYYIFTFSSRTSDLSVSPTFTPGSQSSTSSSSTQNDNFISIPNKIMSMQLRLNHLWNQETYAMDLWENGNLIMKEFEDFFTQLHQRNILHYDSTLADLLNYVRRGMKLISKN
The following text describes a protein:
Function:
Probable member of the two-component regulatory system involved in the regulation of the hydrogenase activity. HoxA is probably phosphorylated by a sensory component (which could be HoxX) and then acts in conjunction with sigma-54 as a transcriptional activator.
Subcellular Localization:
Cytoplasm.
Sequence:
MSIQGTILVVDDEVRSQEALRRVLREDFEVLCVGNATDAEKLLEGEIVHAILCDQRMPHESGVSFLKRVRELWPDPVRMIISGYSESEDIIAGLNEAGIYQYITKPWQPDQLVETVKEAVQLYRLQKETETAGVDVKATSGHIKKVVSVKRGVAKQLYDFDRIVHSTESPMHAVIELGRRAADYDISVLITGESGTGKELLARAIHYGSARANRAFVVENCGALPDELLESELFGCKKGAFTGAYQDRIGLFEVADGGTIFLDEIGETSPAFQVKLLRVLQESEIRPLGAQRVRKVDVRVVAATNRDLEAEVEAGRFRRDLYYRLAAFPVHMPALRERPMDIPLIAEGVLSAVKSSFNRPNLRFARSALEEFGKYHWPGNVRELQNEIQRMAVLADRDELAAPPLLGRRNGKRSAPLPAHGRLNGSASLKDKVEDLEKSVIMNCLERNDGNISRVASELGLSRVGLRNKLSRYDLRKNAKGDAFS