lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes.
Subcellular Localization:
Cytoplasm.
Sequence:
MSRSETVWIVDDDRSIRWVLEKALQQEGMTTVSFDSADSVIGRLGRQQPDVIISDIRMPGASGLDLLAQIRELHPRLPVIIMTAHSDLDSAVASYQGGAFEYLPKPFDVDEAVSLVKRANQHAQEQQGLELPANQARTPEIIGEAPAMQEVFRAIGRLSHSNITVLINGESGTGKELVAHALHRHSPRAASPFIALNMAAIPKDLMESELFGHEKGAFTGAAAQRRGRFEQADGGTLFLDEIGDMPADTQTRLLRVLADGEFYRVGGHTPVKVDVRIIAATHQNLESLVRDGKFREDLFHRLNVIRIHIPRLADRREDIPALARHFLSRAAQELAVEPKLLKAETEEYLKNLGWPGNVRQLENTCRWITVMASGREVHIDDLPPELLTQPQDSAPAANWEQALRQWADQALGRGQSNLLDSAVPAFERIMIETALKHTAGRRRDAAVLLGWGRNTLTRKIKELGMNVDGADDEGDD
The following text describes a protein:
Function:
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site; In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.
Sequence:
MSNIIKQLEQEQMKQDVPSFRPGDTVEVKVWVVEGSKKRLQAFEGVVIAIRNRGLHSAFTVRKISNGEGVERVFQTHSPVVDSISVKRRGAVRKAKLYYLRERTGKAARIKERLN
The following text describes a protein:
Function:
Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
Sequence:
MVEFVCSIPSLKTFTEVPKITAWNSYQLMNLMRGKDGEEMQIIINYMGELSAIAQGLRGPITSVDRLLQSFQKIYLLTSSVPGNSGHILAQGILKVGQKHLFIRRTPNAPLVEISPLCVLDFYVHESYQRQGLGHMLFRSMLEQEKKRPCQLGYDKPSNKLLSFMSKYYNLRSYNDQANQFVVYNDYFVDAKNEAQKEKENRDKELNGTPDIGTNPRKDEVLHDSQANLQVIDVDDQCSSNRSDISRLTTAEARPPNLHVKEPPKQPLFRGGRKKIWQSKQGYSEKPPNSADTLHTTDARSSLQSPTKATLSLKDAYRQGLNDQGISLHARKSSNSLSSEPKRCQENHGANNLHEPGVTLLYSVIGEEERLKIQSMCTPSLAQKMNVKHPTRANHKDPKPIKPRPNMGSPVTRPTRQLTQKDPPPSCPLWADAKELSESQHWQERNPVDYKRTGKVCC
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:
MPGPSTPPPPTPSDHRHEHQKEKMRWKQFSLATIGLSASSWLASVSSDQVVLDLPQFAVPSSLPARVTNYLRTIDISGTITREQLILHLRRTQHDSMNWYLPVEPHRAANLSSMEIYEGKANKTGGPGNRGLKIEPMGYDSGKEIHVIEVEWPHPDNDEAVITINSHFLGLTSPRPKYLAQDEGAKQGLYWEGDLLAGFGALKGTLTDDAQVKIKVKTPTPRVFQKHAPSGFDVQQTSGSNQVTFTSKINGAKLSDEPQVAHVHYFQPFPLMVIGNLTRLVEVSHWGNNVAIEDQIHLENRGPTLKGSFSRVVHHNAIYSRAPGATAHILTGLTLELPQGAMNPYYIDTIGNVSTSRFRPSMPSTATIGKNQPKFKKIKEAKSSKLELTPRYPIAGGWNYTFTVGYNLEAGRLLKIHEPGQYILKVPFFTNALDVPIDLANLRVRLPEGAFNIEVYTPFPVTELQDDLIDKTYLDTTGRPTISIKKLRCTEKHAEDIYITYFRPPIISLQKPLAIAGWMMALFVIAAGFRRFEWKIGHH
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MKWPFSSMANNLATQAESRFFQNYNSSPIVSSNSKSSPLKNYKFTTKDSRKNSEHLRKPESTLTILYMGEVHIFQDITPEKAEVIMDLASKSTTLHMTEISEMANKEKYEENKSEPSTPNASTNYAKGALAMARRATLARFLEKRKHRLITARPYQYGEKTPKFPFEMHQEEETASSSFHWES
The following text describes a protein:
Function:
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Miscellaneous:
MISCELLANEOUS: In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
Subcellular Localization:
Nucleus.
Sequence:
MAHSHRLTYRRKHRNQAQEIIDTISFVCEDFVELRPAMNNNIAQFYKPESYESMSTMCEKYNRAIDGIRQLVYGETSFSLMTQILKILNPTPDDVFIDLGSGVGQAVLQAAASTNCKECWGIEKADIPAKFAKEIDKSFRKWMKWFGKSFCKYQLVKGDFLAPEYEGLIPKCTLIFVNNFAFGPAVDHQLKQIFANLVEGAKIVSSREFMPLNFRISSRNLSDIGSMMRIEELASLRGGVSWTGKPVKYYLHTVDSTAENNQTENLSSNGAKSTLSNFIDDEGVDDVTVFESGNANISFNSIKTSRTCENRQEKSQKSLLDIQKIPVLNERNSEISKIKKRKKQHSQFSIMDAKLKAGVASTDNDSEYNNLNEKVIKKLKKHQGIKLKKKEKKIKSNSIKEALTSTADAEELINNQKNRKTIKAKISSKLGKSKKRQKNATEGSVTKNEQLLYNSSGIQNVHSDNVATLSKDVQYSGNHGAMPRSLLNKITHVNKHHHQALAGYDQILTSIAQNVTLPEFQQQLKHEHDSLLQQESELTKHLKWLKSENRSLLDTNARLADKALKEFNEIKAIVGPNVGEISTFEPFKINQLLSITKDSTNLPFNINREGRQNKISTSSDLSCTQKTNHSVIVNGTSSPRSEVQVDYEVNNLHPEESQTIQKMKMSDYPDPNTFKANVNTNLLDNCEQLGAKSEPFDSKQQEKASVNDSELKLQSGYRNHCYDVKIANGINVSNGTTELDSNHYNECTELKTQHKSVLMNHKTPVGNNGITENGFTTVKSCID
The following text describes a protein:
Function:
With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MHSILQTIHAYLALFISWISNTFQKITLSILVLGPVPKHVAFVMDGNRRFAKRLHLQPSEGHQLGFKKLEETLDWCMKLGIKVVTVYAFSIENFKRPKEEVDVLMELAERKFGEFVTKSDLVQKHGISIRVIGDTKLLREPVYKAACKVTSETCNNTGAILNICCPYTSQNEILVAMQEVVQGVQSGKVLESDVCEKMIEQCLYTEECPPLDVLVRTSGEARLSDFMLWQAGRDCLLHFPKKLWPEFSFWDMLPILLHYQANYAKIKVSRFIPITQLLAVFDMIHAVVTFIPII
The following text describes a protein:
Function:
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins; Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLGFLKRPVVVTADINLNVVALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDGSGPPFGHMLLALGGYLGGFDGNFLWNRIGAEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFSNSQKHRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPTLMYLLFFYVHLILVYRSGPHDQIMSSAFQASLEGGLARITQGQPLEVAYGSQVTLKNVFGKPVPCWLHSHQSTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPGRHQLVVNNPPRPVRHGDVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYVDYNISMPSQNLWRLDIVNRESDTEVWKTILSEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSRGYHESMVWNVEEHRYGKSQEQKERELELHSPAQMDVSRNLSFMARFLELQWRMLTAKSDDSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQIHLLGNIVIWASASLAMVVYVLLFFWYLLRRRRSICDIPEETKCCRCIPTLLEASSGKCKDQAGIAVTPGYSWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALTFQILLLPVVLQHVSDHLCRSQLLRSLFSALVVAWYSCACHVFNTLRPLTYGDKSLSPSELKALRWKDSWDILIRKH
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a 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.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MNPLIVVASVIAAGLAVGLASIGPGVGQGTIAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFVNPFV
The following text describes a protein:
Function:
Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA (pre-rRNA). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSGLFIKKKSGVTPRRRRAEGNDAEATSQKKKKPKDTHLREEIESDSDTEIAPARTKPRQDEEDLDETAQEKKLRLAKEYLKQLQQQEEEQKEDEDQDTIANRLQEDVLEQRGRLQRPLAKELLPPEPSEIRLLRGHQGPITCLVISPDDSYLFSGSKDCSIIKWSVSDGKKIHKIPGGRKGTESTHVGHTGHVLCMALSSDGKYLASGDRNKLIFIWDPVTCQNLHKFQGHRDAVSGLSFQKGTHQLFSVSHDRSVKVWNVEENAYIETLFGHQDAITGLDSLSRERCVTVGGRDGTMRIWKIAEETQLVFSGHEGSIDCVRLINEEHIVTGADDGSLALWTVGKKKPLTQMKCAHGSHGDAGLEQPYWISSIAAALNSDVVASGSHDGFVHVWRCGEGFRSLSPLFTVPVVGFVNSLQFSSSANFLVAGVGQEHRLGRWWRKKEAKNALCIIPFKRTLVLGS
The following text describes a protein:
Function:
Malate transporter critical for aluminum tolerance. The STOP1 transcription factor is required for ALMT1 expression.
Miscellaneous:
MISCELLANEOUS: Essential factor for aluminum (Al) tolerance but does not represent the major Al tolerance QTL also found on chromosome 1. Acts in parallel but independently of MATE, an aluminum-activated root citrate transporter; MISCELLANEOUS: A reversible phosphorylation acting both at the transcriptional and post-transcriptional levels is required to activate malate release in response to aluminum.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MEKVREIVREGIRVGNEDPRRIIHAFKVGLALVLVSSFYYYQPFGPFTDYFGINAMWAVMTVVVVFEFSVGATLGKGLNRGVATLVAGGLGIGAHQLARLSGATVEPILLVMLVFVQAALSTFVRFFPWVKTKFDYGILIFILTFALISLSGFRDEEIMDLAESRLSTVVIGGVSCILISIFVCPVWAGQDLHSLLASNFDTLSHFLQDFGDEYFEAREKGDYKVVEKRKKNLERYKSVLDSKSDEEALANYAEWEPPHGQFRFRHPWKQYVAVGALLRQCAYRIDALNSYINSDFQIPVDIKKKLETPLRRMSSESGNSMKEMSISLKQMIKSSSSDIHVSNSQAACKSLSTLLKSGILNDVEPLQMISLMTTVSMLIDIVNLTEKISESVHELASAARFKNKMRPTVLYEKSDSGSIGRAMPIDSHEDHHVVTVLHDVDNDRSNNVDDSRGGSSQDSCHHVAIKIVDDNSNHEKHEDGEIHVHTLSNGHLQ
The following text describes a protein:
Function:
May regulate plasma membrane ATPase activity.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MSASILLCDGFDVRRILTGKLNGDESSTVTTEEDDEAVFSGEEWCGESSYCFYFVKQFAYDDPEIKAKIDEADHEVYHCNTDRIHIANRLKSKRAARLSLVASMETLMSMKINEVEKEQEVVRGRIYRLGERLSEIKMEIELLDVQMACVLNQRDKAVERIKFLRMQRDKGNAAFYQSRVVMKKAIELAASGNVRDLEELADSEVEKFMSRWNNDKAFRDNYKKRILPSVNERKLRCDVQIRDLEGNLDTENGNETVVKKAIEYKRFSTEEESDDFDIPVYEKLGKEEKEIDEETLKEKKREEQLEKARLAMERKRKLHEKAAAKAVIRVKKEAEKKRKELDKRAKKKKAVCKSSSVDVDRTTETVSEASKPEKEKLLNGRSVFPKQRSYNYRYHGKGNDAVLKAIIKRRKAYRLWVWTVSSAAVALPLALLVVFYYVR
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Subcellular Localization:
Cytoplasm.
Sequence:
MVIGVTGKIGTGKSTVCEILKNKYGAHVVNVDRIGHEVLEEVKEKLVELFGGSVLEDGKVNRKKLAGIVFESRENLKKLELLVHPLMKKRVQEIINKTSGLIVIEAALLKRMGLDQLCDHVITVVASRETILKRNREADRRLKFQEDIVPQGIVVANNSTLEDLEKKVEEVMKLVWEKRE
The following text describes a protein:
Function:
Selectively cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Converts 5-diphosphoinositol tetrakisphosphate (5-PP-InsP(4)) into inositol pentakisphosphate (InsP(5)), 5-diphosphoinositol pentakisphosphate (5-PP-IP(5) or 5-InsP(7)) into inositol hexakisphosphate (IP(6) or InsP(6)), and 1,5-bisdiphosphoinositol tetrakisphosphate (1,5-PP-IP(5) or InsP(8)) into 1-diphosphoinositol pentakisphosphate (1-PP-IP(5) or 1-InsP(7)). Also has activity on 1,5-bis-diphosphoinositol 2,3,4,6-tetrakisphosphate (1,5-InsP(8)) and 3,5-InsP(8). Modulates inositol pyrophosphate metabolism that may have an influence in stress response. Plays a role in actin filament organization and endocytosis. Functions as a prion suppressing factor possibly due to its phosphatase activity against inositol pyrophosphates, which are signal transduction molecules involved in prion propagation.
Miscellaneous:
MISCELLANEOUS: Present with 4070 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MGLYQAKNDEGSDPKSSSKIDDLIENEAEIIRLIKEDGKLLIDNGDGRDIHNIIQEDKLLSVEFNEVLKRFHGEEKSDIPRKEFDEDEDDGYDSNEHHQKTIEVMNTLNHVINKEVIPPENFSHVVGEIYRSSFPRQENFSFLHERLKLKSILVLIPEEYPQENLNFLKLTGIKLYQVGMSGNKEPFVNIPSHLLTKALEIVLNPANQPILIHCNRGKHRTGCLIGCIRKLQNWSLTMIFDEYRRFAFPKARALDQQFIEMYDDDEIKRIASKNNWLPLQW
The following text describes a protein:
Function:
Component of the matrix of the eggshell.
Subcellular Localization:
Secreted.
Sequence:
MPGLRAALPAALLLLSSFPPAAAERLPWPQVPGVMRPLNPSHREAVWAAWTALHYINSHEASPSRPLALHKVVKAASKMIPRLGWKYYVHCTTEGYIHGENAGSCFATVLYLKKSPPVVHGKCVHAQNKKQIQEEDHRFYEYLQHQKKPITANYIPDSNGNIAHDHLQLWGLAIVGSSYIMWKQSTEHTGYLLAQVSSVKQQIRKDNAVAFKFIVLLHEIPTQQLNVCHMYLVWTLGHPIRVKYSCAPDNHGLEDGSGQDSGSAAGTSHETKGNF
The following text describes a protein:
Function:
GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA. SUP35/eRF3 mediates SUP45/eRF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site. GTP hydrolysis by SUP35/eRF3 induces a conformational change that leads to its dissociation, permitting SUP45/eRF1 to accommodate fully in the A-site. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.
Miscellaneous:
MISCELLANEOUS: [PSI+] is the prion form of SUP35. [PSI+] is the result of a conformational change of the cellular SUP35 protein that becomes self-propagating and infectious. This conformational change generates a form of SUP35 that assembles into amyloid fibrils. [PSI+]-aggregates sequester soluble SUP35, resulting in defects in faithful translation termination by read-through of translation termination codons. [PSI+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PSI+] propagation. It is speculated that the prion form would be at least mildly deleterious in most environments, but it might sometimes increase evolvability in certain harsh environments; MISCELLANEOUS: Present with 78900 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Domain:
The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.
Sequence:
MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDVVFMPVSGYSGANLKDHVDPKECPWYTGPTLLEYLDTMNHVDRHINAPFMLPIAAKMKDLGTIVEGKIESGHIKKGQSTLLMPNKTAVEIQNIYNETENEVDMAMCGEQVKLRIKGVEEEDISPGFVLTSPKNPIKSVTKFVAQIAIVELKSIIAAGFSCVMHVHTAIEEVHIVKLLHKLEKGTNRKSKKPPAFAKKGMKVIAVLETEAPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIAE
The following text describes a protein:
Function:
Chitinase that possesses antifungal activity. Inhibits the growth of the fungal pathogen Rhizoctonia solani by degrading the fungal cell wall. Does not possess inhibiting activity against fungal endo-1,4-beta-D-xylanases belonging to glycoside hydrolase family 10 (GH10) and family 11 (GH11). Involved in the regulation of plant growth by regulating the intracellular calcium ion concentration in roots.
Subcellular Localization:
Secreted, extracellular space, apoplast.
Sequence:
MSLHLLLAVSLCVALASSLPWAAASANGNGNGKPLVAAITKDAATSLYTVPIKDGRPLVLDLAGALVWMSCAAAHPTLECHHHFCMHAHSYHPPGCPHNGYGRADVEDPFRCKCTAHPYNPFSGESATADLTRTRLSANATDGKNPLYPVSFAAVTSCAPDSLLAKLPAGAVGVAGLARTRLALQAQVARSQKVANKFALCLPSGGGGDGVAIFGGGPLFLLPPGRPDVAATLAGETPLHRNKDLPGYFISATKIAVNQEQVQLYTQEPLVVELCTRIPYTALRPDVYRAVVDAFARATAGRKRVTPPPPPAAPFELCYDSRDLGSTRLGYAVPQIDLVLEGGKNWTVFGGNSMAQVSDNTACLAVVKVKGEKGSPPPPAAIIGGFQMENNLVVFDEEKQRLGFSGLLWGRQTTCSNFNFTLAA
The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MRLVLIVIYLILIMPITGLWRAEGSNVLLDPDRVCESKHRKSRRLSGKLADICKNDTSLMREIHRGISLGFRECENQFRHNMWNCSWTIKRSMRRILAKDTRETAFVHAITAAGITYAVTKACTMGDLLECSCQKHLKSKPSDEGGRRGGRGGAGYRPAGGNRRRVGGGNRASNPNSILIAPYQQNVNANPAYSTLTAAEIARNGRAQAVGRRPNSGRSQRHTPKGANGGATGGGGSSAVGQLGPNAAGLPKELPTLTILTGQEDKWKWGGCDDNVNFGVRKSKDFLDARLRKKSDIKTLVRLHNNDAGRLAVKQFMRMECKCHGLSGSCTTKTCWMKLPPFSEVGARLKEHFDGATKVIARNDGHSFMPDDATIKLPTKRDLVYTEDSDDFCEPNAKTGSLGTHGRECNITSSGVDGCSLMCCKRGQTHSQMEVKRNCNCSFKWCCEVTCSTCIDIQDVYTCK
The following text describes a protein:
Function:
Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
Subcellular Localization:
Cytoplasm. Dynein axonemal particle. Note=Localizes in the apical cytoplasm around the gamma-tubulin-positive pericentriolar region, not in the cilia.
Sequence:
MESGSKLEELNLTSDEIDRFSKAFKDEKFREMLKEYAEEISNPENRKKYEEEITMMEQERGMDIQFIHPKPCRVLKTSVRGEQKCFINICSNELIAKPECKPGKGSDDKLGQHWSLPYSLAPGRQDLDSKGNRHMIYDVVFHPDTLYIAGKNERFMKLVDRTAMEGIQKQFNVKLDERNVKVLKMKYKGVPHPAVIRKPLHGHPVKETEPVNPNDPLQFPYPYDKKGNTAQEDNTVIREEKLDYIKPAPNQSNEPTEPRYTIKYRSYIDLQDYTCSRDTAPGPRPKEIVITVDLPLLKSAADAELNVTEKQFLLESKKPAYRLVVTLPYPIDENQGEAKFVKLKKQLVVTLTVLPLKRPTTAQMNTHLVGETLCGKDRFEDLEPGSAEKAENETLADDLVKQQETNVMQSPATPVSPKSQPKELDPSEGVDIIPEPIATDTQKRDADMSHQSRDEDNNIPEETANAACVILSSVDSSVRDEPSSPEAVIQEMEKETNTHAAVKRKQITTCHTACEPVCRFALNKGNSTEQTRPASVKQATMKHSETVGSDLNPSAPCSDSKEVPFTALKTAGTPVATGIGQRASRTAHFKEESGERDGNELDEDDLLTEQKNEFMDSEPAPAIIREINPTDGTVEVLNNHTTSARFSFLNSLLYELD
The following text describes a protein:
Function:
Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MGGDHGHSHGDEGGSFYVHLIAGAAAGFAEHCGMYPIDTIKTHIQAIKPGAMQTSSLQITKHIIQQHGITGLFRGLTAVAAGAAPSHAVHFSIYELLKFKFIGSDEDHHPIKVGIAGAIATMTSEAVASPMDVVKQRLQLQITDYKGLTDCTKRIWVKEGIRGFYSGYTTTLVMNVPYNIVYFASYESLKKIIQPWFNNKNPEERSYQLIDHLVAGGGAGMLAAAFTNPFDVVKTRLQTQSDFIASSTINSAKSIKRYGGMMDAMKTIWIEEGMDGYLRGMKPRMVFHSMSSAIVWSVYEYFKFILGE
The following text describes a protein:
Function:
Component of a CST-like subcomplex of the holoenzyme telomerase ribonucleoprotein complex, which stimulates telomerase complementary-strand synthesis. Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. The CST-like subcomplex (also named 7-4-1) binds telomeric single-stranded DNA and coordinates telomere G-strand and C-strand synthesis.
Subcellular Localization:
Chromosome, telomere.
Sequence:
MQQPKRNFDLYKLITDKQIDFQVADLIQDEQSSFVSVRIYGQFKCFVPKSTIQEQLDKIKNLSSKELAKNKIFKFLSEYNKNNQKQDELSHDYYGYFKVQQHQFILNLENAQREASLAVDDFYFINGRIYKTNHDILILQAHHVYQMQKPTLQLLQAASEINQN
The following text describes a protein:
Function:
Cytoplasmic and mitochondrial threonylcarbamoyl-AMP synthase required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Participates in t(6)A37 formation in cytoplasmic and mitochondrial tRNAs. May regulate the activity of some transporters.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm. Mitochondrion.
Sequence:
MSPARRCGALRAAVAAGAGLSEGPAGSARRGRLLRAPSRLLRLPGGGAVRAASPERAGWTEALRAAVAELRAGAVVAVPTDTLYGLACAASCSAALDAVYRLKGRSHAKPLAVCLGRVADVYRYCRVSVPEGLLRDLLPGPVTLVLERSQELNRDLNPCTPLVGVRIPDHAFIQDLAQVFGEPLALTSANLSSQASSLTVEEFQDLWPQLSLVIDGGPIGDGQSPEYRLGSTVVDLSVPGKFGIIRPGCALESTTAILRQKYGLLPSHGSGSCS
The following text describes a protein:
Function:
May be a ribosome silencing factor (Potential). Involved in plastid biogenesis.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MASSTGLTVAGALLAGDFRLPAVSSLIPRKTSSSLSCLSNRDLSSPYNCCWRLSRGKILTSLSNSRKFAVGKEAEDGFLSNVSEDTDEMFDDLFNKYGKVVFRSTDVKSPTAEVDDDAESLAFAVELAKVASDVKAGDIKVLFVKPLVYWTRFFIIATAFSRPQIDAIGSRMRDLAEKKYGKVANGDVKPNSWTLLDFGDVVIHLFLPPQRTFYNLEDFYGNAMQIELPFEDQSQPRN
The following text describes a protein:
Function:
Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Early endosome. Golgi apparatus.
Sequence:
MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL
The following text describes a protein:
Function:
Molecular chaperone. Has ATPase activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MQKGNIGVTTENIFPIIKKFLYSDHEIFLRELVSNAVDATQKLNTLASIGEFKGELGDLTIHVELGKDTITISDRGIGLTAEEIEKYINQIAFSGANDFLEKYKDDANAIIGHFGLGFYSAFMVAKKVEIITKSYRDEAQAIKWTCDGSPEFTIEEVDKADRGSDIILYIDDDCKEFLEEARVSELLKKYCSFLPVPIAFGKKKEWKDGKQIETTEDNIINDTTPLWTRKPSELSDEDYKSFYTKLYPMSDEPLFWIHLNVDYPFHLTGILYFPKVKSNIELNKNKIQLYCNQVYVTDSVEGIVPDFLTLLHGVIDSPDIPLNVSRSYLQSDSNVKKISTYITKKVSDRLQSIFKNDRKQFEEKWNDLKIFINYGMLTQEDFYEKAQKFALFTDTDNKHYTFEEYQTLIKDNQTDKDGNLIYLYANNKDEQFSYIEAATNKGYNVLLMDGQLDVAMVSMLEQKFEKSRFTRVDSDVIDNLIIKEDKKNETLEGEKQEAITTAFKSQLPKMDKVEFNVMTQALGDNSAPVMITQSEYMRRMKEMANIQAGMSFYGEMPDMFNLVLNSDHKLIKQVLDEEEAACHPEVAPIQTEMNSVSKRRNELKDSQKDKKEEDIPTAEKDELNELDKKWDELKNKKEGIFAGYASNNKVIRQLIDLALLQNNMLKGEALNNFVKRSIELI