lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
FFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIVA
The following text describes a protein:
Function:
Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MASTSKNAQRAAASVAHSYHVCLARRMSRLPTLLSNISAPAASKALDRYESKRIHSRSFSSSLAAQRVQRPTSAGPILTNPISDHEKDNDELRSLFDAPPTSSSANHLRSSGPSTGLFEIPSLTSPQNFLVLAQQTLARAQLLVDRIDRAGSADASTAQGIKELKEVVRNLDRLSDLLCGVIDMAELVRNAHPDPEWAEAANAAYEYLCGYMNVLNTHTGLYSVLKNILSIKEVAETLSKEATAVAQVFLRDFEKSGIHLPPAERERFVQLSDEILVLGRGFLQDIAGNDASDDFARIASAQADADKSDMVGLPTHWLEDVNPTILKAVRASAITDTDGLLTFSAADQPWVFQTLLKYAPDERARKVAFRAANYGSQAQVQRLERLLKARAELATLTGASSYAEMALGDKMAKEPQNVEEFLRALTKHHRPRASHDLDKLRRLKHNATVSEPAQNTRQSTFNTNSTLPEFAPWDRDMYTEQHFRSASLSNVQPLSPYLSVGSVFAGLSRLFSALYGIRFRASMVAPGEVWSEGAGDVMKVEVLDESEGARGTSGSAEGLIGTIYADLWSREGKPGGAAHYTVRCSRRVDKDDEAGDFTYGRAEDGRVVRPQDLGGEGCGNPLQAPTFEQRERPGRYQLPVVVLMCDFARPGNANQGPCLLGWHEVETLFHEMGHAIHSMIGRTSYHNVSGTRCATDFVELPSILMEHFVSSPQVVHLLARHHSTGASLPFEHLSSHLAASKSLEGLDTYHQILLARLDQLYHSQLAASPSFSSTTTYSDLDRQMHLPGAPNLSYTEGAHPQVRFGHLFGYGSTYYSYLLDRVIASKVWNHLFANNPLDRYAGQVFKNQCLKYGGGKDPWHILADVLNEDSVRQGDSRAMQQVGKWGIEC
The following text describes a protein:
Function:
Subunit OSCP, 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 (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (By similarity). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MAAPAVSGVSQQVRYFGTSVVRPFAKLVRPPVQVYGVEGRYATALYSAASKQKKLEQVEKELLRVAQILKEPKVAASVLNPYVKHSIKVKSLSDIIAKERFSPLTTNLINLLAENGRLSNTQGVVSAFSTMMSVHRGEVPCTVTTASPLEEATLSELKTVLKSFLSQGQILKLEVKTDPSIMGGMIVRIGEKYVDMSAKTKIQKLSKAMREVI
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MTSKIVSVNPLIKPVENCFEEMKVQLSLQLPPMDTQSLCSGTKSMLDRLVFKYKTELGGIIISYYDVIHTDKEAKIFYDSPYLGMNIHVKFLVFKPFKDQILNGVVKRVSTTHISLLVFGTISASIPKSNIPKSFAFDHSSNMFMNKQTKATISVGTKIAFKVIDVSADRHNIGIQGDMTDLTSTGIIGFDENQSLQFGSQYETPNKNVKNNKYNNNNNNNNNGNNNTTLINTENNNNITKFDDDSEKESEEEPKPIIIKEEPKIVSVKVESKKVVVKEEEQKSSKKDKDIKKEKESKKRKKDSSDESDESEEDKKKKSTKKEKESSSKKSSKKVKVESSSESSEDEKEKKKKKKK
The following text describes a protein:
Function:
Involved in the biosynthesis of the antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid (AMB), a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Adenylates L-alanine and loads it onto its peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety. In addition, loads activated L-Ala in trans onto the second carrier domain of AmbE. Can also activate L-Ser, Gly and D-Ala, albeit to a lower extent. The condensation domain of AmbB probably condenses the activated L-Ala and the L-Glu loaded on AmbE to form a L-Glu-L-Ala dipeptide at the first carrier domain of AmbE.
Domain:
Modular protein that contains an adenylation domain which activates the alanine residue into an aminoacyl-AMP ester, a peptidyl carrier protein domain which bears a phosphopantetheinyl arm to attach the activated alanine and a condensation domain involved in the condensation of this amino acid with a second amino acid bound at the carrier protein domain of another module.
Sequence:
MQERHGLPLRSFSSGKALTAGRAVRPEVAQERRYLQGAPLGLELPGRIALRDPHCAWQWFEPEAAAEAFPAAHWLAAFLVLLGRYGNEEITLGFPEPITVRGRQAPALLRSSYRAMESSAERSARLAEELDDARRQLSADGQERAALAGRCAVQVLAARPTASSPGWLALVLAADGSVGLALRDPQYDELRRIAGHLARLARGLVDAQACVGRLPWLDADEERRLQALRSEPQAAPSRGVLHHLFEAQARRTPQRIAVHAADRSLSYAELERESAALAVRLRAAGVAPEQRVGVCLRRDSGLLVGLLGVLRAGGCYVPLDPAYPEERVAYMLDDADCLLVLVDASTRERVAALGRPCLTLEEGGDQANDLALPASEVGADHLAYIIYTSGSTGRPKGVAIEHGSAHAFLRWAGQHYAAEEWSGVLAATSVCFDLSVYELFGTLAEGGTLHLVENLFSLPDYPRRDEISLLNTVPSVCAALLALGDLPGGVRTLNLAGEPLRGHLVRQIRGQPQVRRLVNLYGPTEDTTYSTVHELDLHAEALDEPPIGRPLPGTTVEVLDGFEAPLPLGVAGELYLGGIGLARGYFGKPEQTAERFRVDPGSGERRYRTGDRVRMREDGVLEHLGRLDDQVKFNGFRIELGEIASCLASFPGVSEACAMLTEDSAGLRRLVGYLAAPFAPPLQALNEHLGQSLPHYMLPSAFVVLAELPKTLNGKIDRKALPRPQATGAEPQALPSDPLEQALHQAWQAQLGAPPRAGQGFYAAGGDSLRAVHLLATLRQRLSRRVPLQAFAGGPATPEALLELLRQAAPEGDEPEPSAGAAGLSLAERRLWVAQQLAPEDTSYNLLAHLRIVGATADAIEQALRQLLERHVALRRRVETGVDGPQPHALAAHAVPLQRLLASDAVHAERLLEDGVRREGARVFDLAHEAPARLLLVVTRDSARADLLLSVHHYAFDDVSLAVFAAELKTLLDGGRLGVLASTPEQVAARERAALASGRLDRVAERWAERLLPLAKAPGAAPARPEESGGRAGQRLALPVSAAVHAACRALAERTSVSPFSAALQAFAEVLGAELGVDDLLVGVALAGRSRLEMQGLVGCFVNLLPLAVGLRPEQSVEWRLRQVGHDLLELLEHQDVPLECVTQALRQRGASGLPIRIACGAHNGRAAPAVDAGVRVEADFIPVPGARLDLTLWLEDQPQGWLAVWTGVSAIFDLHRIERLHQAWERRLLANAGEPISKRMSPEGCNAS
The following text describes a protein:
Function:
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
Subcellular Localization:
Cell outer membrane.
Sequence:
MQIRYLLALSLLPKLVLADESPATSASQCLIEPPVPRIVSQPGLSAADQAKIRIASDRSKAEMGKQAIFTGDVVFSQGDRHIAADEAILDQATEQFDANGNLVFQDSNFTVTADSLQAQMRSNRATLTGAQYWLHGQQVHGDAEKLQITINNNLILTNTNFTTCPPDNVSWLLEAEKIKINSEEEWGEIWNAKLRVADIPVFYIPYMTVPVSDKRKTGFLYPSFSTSTTNGFEVSAPYYWNIAPEYDLTFTPNYMTNRGLFTKTEFRYLAGEAQNGRLNLEYLGSDQMLNGSPNRYLYNWQHQGAIDKNWRVLANFTEVSDNNYFNDLKSDVNRATDNQLSRIGEVSYFERDWDISTRVQDIKVLGEDEKPYQVMPQVNFNYRAADFWNNLDFGFNSELTNFAHQDDDVNTATRLHMAPSLTLPIHGPSGSFTSQLKLMQTNYWQEKNNSKFDSLDDTVSRTIPQVRINGQINFERFTELFEHNYRQTLEPQFQYLYVGYEDQRGIGIYDTAQLQDDYFGLFRDRRFSGLDRIADANQVTLGITTRLFDDHNQEATKFSLGQIFYLQDSKLGYEDNIFEQNQSTSVLAAELDTRLSSNWYLGAAIQYDTNTSDNKKTEVTLDFRPEANKLLQFSYRYVPDLLNSNTNDLVNISQAGVRGAWPINDSLYFVGNWYYDLNETRSIETYTGVQYESCCYAIRLSYHYRIKTNYDDNIGSTIIDEREQFESGVYLNLIIKGLGGSGPLGVSDMLNDGLFNYRKPLYLRN
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGSAHLAAILLCVCIIAGGAIADSQNGTNGVPRPAEVRIGALFTFDSVIGRAVKPAIELAVADVNADPTVLPGTKLSLLMQDTNCSGFVGTIEALQLLAKDVIAVLGPQSSAIAHIISHAVNKLQVPLISFAASDPTLSSLEYPYFVRATQSDYYQMSAVASIISQYQWREVIAIYVDDDYGRGGITALGDALAKKMSKIAYKAKLPPGAGRTAIQDMLMQVNEMESRVYVVHVNPDSGMTVFSAAKSLGMMSSGYVWIATDWLSSVIDSSGHVDSDATENTQGVITLRQHVADSGIQQSLLPKLNNLTRKENRSSFSSYTAHAYDSVWLVAHAVEQFLSAGNAISFSVNQNLQAIKGSSLQLDSLRVLNNGDKLLEKVLQANFTGVSGQVQFTLDRNLIHPAYDILNIGGTGFRTIGYWSNFSGLSVAAPENLHSVPLNSTTNDIQLHDVIWPGQTAEKPRGWVFPYHGKLLRIGVPLRTSYNEFVMQDDGPDGVKGFSVDVFKSAISLLPYPVGCTFVLFGDGLKNPSYSDLVQKVSENYFDAAIGDISIVTNRTRLVDFTQPYTESGLLFLFVGTVVWILEHRTNTEFRGTPRQQIMTVCWFSFSTMFFAHRENTSSALGRFVLLVWLFVVLIINSSYTASLTSLLTVQELSSGVKGLDSLISSSSAIGYQVGSFARNYLVEELNIADSRLVPLNSPSDYARALELGSGNGGVAAIIDELPYVEIFLSKYCKFKTVGQVFTKSGWGFAFPRDSPLADDLSTAILTLSENGDLQRIHDEWLSGMKGCESDDSGMSSNSLSLSSFWGLFVVCGLACVIALLIFFWRILFQYSKYNNQVELEAAIVNRPARLTSIKSLISFVDKREEEVKNALKKKPNGSQQARIGITEEPSTLPL
The following text describes a protein:
Function:
Low water transport activity in yeast cells.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Sequence:
MDDISVSKSNHGNVVVLNIKASSLADTSLPSNKHESSSPPLLSVHFLQKLLAELVGTYYLIFAGCAAIAVNAQHNHVVTLVGIAVVWGIVIMVLVYCLGHLSAHFNPAVTLALASSQRFPLNQVPAYITVQVIGSTLASATLRLLFDLNNDVCSKKHDVFLGSSPSGSDLQAFVMEFIITGFLMLVVCAVTTTKRTTEELEGLIIGATVTLNVIFAGEVSGASMNPARSIGPALVWGCYKGIWIYLLAPTLGAVSGALIHKMLPSIQNAEPEFSKTGSSHKRVTDLPL
The following text describes a protein:
Function:
Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Probably responsible for energy coupling to the transport system.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MSIQLNGINCYYGAHQALFDITLDCPAGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLQIAGNHFDFSRVPGEKAIRELRTNVGMVFQQYNLWPHLSVVHNLIEAPCRVLGLPKEEAMARAQKLLSRLRLTDFADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAGTGITQVIVTHEVEVARKTASRVVYMENGHVVEQGDASHFTQPTTEAFASYLSH
The following text describes a protein:
Function:
ATP-dependent 3'- to 5'-DNA helicase that could disrupt recombinogenic DNA intermediates and facilitate single strand annealing. Unwinds nicked and partial Holliday junctions in vitro. Anneals two single strands into a dsDNA molecule in vitro.
Subcellular Localization:
Nucleus.
Sequence:
MENLPPNRGMWNQEYSHGRISQSFRSAKPLLDRKRPIENAPNSSNPLPQRMKESMDTESVSHNINFNSTPLMELSANTPYKRLKPEIESYADGHPCGLRTPPPRFDLDKEIINGFQTDIYADVGSLSEAFVTPLKEPERVTLSNGCSTSSILDDDFDDSILEEIDLICEQSARKAACQTPTTSIYQTPSKDNKSSDPKASLDFRDVEKFEPDSNVKLKLDEETPTIAADPALLNSMPDECSKYMLSLNDRQRDAACSNISTPLMVIAGPGSGKTSTMVGRVLVLLNEGLLPSNILAMTFTKAATSEMRERIGKSAGKKAAKDITISTFHSFSLQLCRMHADKLQRTSEFSVYGHGQQRRAIIEAVRLYEEEKKNGSKTSVPCESGEGLNGAGAGAVCPEYAKDLSKKWQKFVTQGKASGKSPEQCRKMGNEIGAKILGNYNDILKACDALDYHDLISCSVTLLSDFPEVFKECQDTWKAIIVDEFQDTSTMQYKLLRMLGSHNHITIVGDDDQSIFGFNGADSSGFDSFRRDFPNYKEVRLIKNYRSSRHIVEAASSIIKNNTKRCQSKSISSENSQGSKITVKECHNEEAQCAYVIDKIIEITNDGSTPCCSHGDIAILYRRQVSGKVFQNAFRQRKIPFNVHGVAFYRKKVVQVILAMLKTTFSECDDASYRRVFKALLPFEKEEKKRIIEHIEKISTSRKCSFISAASDIFNAKISGTFKRSQLTQGRKVLQTLDMVAKLVDREQSLSAVVTCVANMIPQKYLLEQRAVVDNDGGKLLNEDNDLRSVLQYLMDDVAEFISTHCTTTEEEDAIKEKKGCNQLHSFINYISERETENFRSRRRDNENSVTLTTIHQSKGLEWDIVFIVKANENEIPLLHESNGNASESGTSLEEERRLLYVAMTRARKKLFFLYVTVDSNWQVLQPSRFLKEIPGHLLQGDMSVNDCRKVHENLPNKTEQSVSSFGTDIKHEESKLTDNDVMNIPEDYASEESIAAYALNGNNFLKRFDVEVRSVVSHLFHNWAKKQAFQEPKRLIDKVRFVIGERLAIKKNKHKDVLRALKSSLTSEEAFQYAEHVLRWEQLPADTRAHIVREKQEHFQKLRIENSMGTSEATSKQIAFLHSLGCTVVPTSRLHASRLIEQYKSL
The following text describes a protein:
Function:
Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Plays a role during spermiogenesis in the development of the sperm tail midpiece and in the normal function of spermatozoa. May play a role in the formation of the mitochondrial sheath formation in the developing spermatid midpiece; Kinesin is a microtubule-associated force-producing protein that play a role in organelle transport.
Subcellular Localization:
Cytoplasm, cytoskeleton. Mitochondrion.
Sequence:
MGRMRGGVRGSGVCDGVRSSGTAMSVQVAAPGSVGLGPERLSPEELVRQTRQVVQGLEALRAEHHGLARHLAEALAGQGLVAGLELLEEKQQVVSHALEAIELGLGEAQVLLALSAHVGSLEAEKQRLRAQARRLAQENSWLREELEETQRRLRASEEAVAQLEEEKSHLEFLGQLRQYDPPAESQRPESPPRRDSLTPLFSSEEEERKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATDLLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGTDHPDVAKQLNNLALLCQNQGKFEEVEQHYARALSIYEALGGPHDPNVAKTKNNLASAYLKQNKYQQAEELYKEILSREDLPAPLGAPNVGTTGDAEQTLRRSSSFSKIRESLRRGSEKLVSRLRGEGVAGAAGMKRAMSLNMLNTDGPKAAGTQFPHQHLSEAARTLSASTQDLGPR
The following text describes a protein:
Function:
Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate using ADP as the phosphate donor.
Subcellular Localization:
Cytoplasm.
Sequence:
MVRELLEKARGLSMFTAYNTNVDAIVYLNGETVQRLIDEFGAEAVKRRMEEYPREINEPLDFVARLVHALKTGKPMAVPLVNEELQAWFDSHFKYDVERMGGQAGIIANLLANLDFREVLVYTPHLAKRQAEMFVKKPNLFYPVVEGGKLVLKHPWEAYRENDPVKVNRIFEFRAGTTFRLGNETITVPFSGRFIVSARFESIRIYTEPELKPFLPEIGQRVDGAILSGYQGIKLRYSDGKDANYYLREAKKDILLLKREKDVKVHLEFASIQNRELRKKVIYNLFPLVDSVGMDEAEIAYVLSALGYDKLAERIFTYNRIEDTVLGGKILIDEMNLELLQIHTIYYIMYIAHANNPLSEAELRQSLELATTLAASRASLGDIASPDQISVGMNVPYNERGEYVKLRFEEAKRRLRTKEYKLVIIPTRLVQNPVSTVGLGDTISTGAFTSYLAMLKEKGEL
The following text describes a protein:
Function:
Protein involved in mitophagy. Accumulates on the mitochondria surface in response to mitochondrial depolarization and acts as a 'eat me' signal by recruiting proteins involved in selective autophagy.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MATRILQRVGKGLHKTNTVLHINGAVTITRSLSGFKSLFIRKVDPRKDAHSNVLSKKEEQNLYKIQFHNVKPECLDAYNELCEAVLPSIHANPEYPSELVGTWNTWYGEQDQAVHLWRYRGGYPALTEVMNKLKQNKEFMEYRKERGKMLLSRRNQLLLEFSFWNEPVPRPGPNIYELRSYQLRPGTMIEWGNYWARAIEIRQKNQEAVGGFFSQIGSLYTVHHLWAYKDLQSRDETRNAAWQQEGWDEVVYYTVPLIQHMESRIMIPMKSSPLK
The following text describes a protein:
Function:
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein. Membrane.
Sequence:
MTEHTPEKKNVKVDQLVVQDKESASNSGKEGFFAYFSNSWSEFKKVVWPKREDAVRMTVFVIVFVAVLSIFIYAADTAISWLFFDVLLRREG
The following text describes a protein:
Function:
Regulation of the glyoxylate bypass operon, which encodes isocitrate lyase, malate synthase as well as isocitrate dehydrogenase kinase/phosphorylase.
Sequence:
MVAPVPAKRGRKPAATTAPVTGQVQSLTRGLKLLEWIAESNGSVALTELAQQAGLPNSTTHRLLTTMQQQGFVRQVGELGHWAVGAHAFIVGSSFLQSRNLLAIVHPILRKLMEDSGETVNLAVLDQSDHQAIIIDQVQCTQLMRMSAPIGGKLPMHASGAGKAFLSQLSEEQVTSLLHRKGLHAYTHATLVSPLHLKDDLAQTRKRGYSFDDEEHALGLRCVASCIYDEHREPFAALSISGPCSRITDDRVTELGAMVIKAAKEVTLAYGGTR
The following text describes a protein:
Function:
Functions as a downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Is involved in pollen tube growth regulation.
Miscellaneous:
MISCELLANEOUS: Over-expression of RIC10 in tobacco germinating pollen increases pollen tube elongation.
Subcellular Localization:
Cytoplasm.
Sequence:
MSMKMKGIYKGFKCISQIFAVEKERDEIEIGFPTDVKHVAHIGWEGSSGSAPGWMSEFKVGAELLSPRPSSFSNARPSTSFFTSSSSTDFDQGSSQRGISDTLRDIPPVTPINLPKNNKKKSSRRKKSSSSSSSPKSSRSSVLSKSSYKSTVSRLI
The following text describes a protein:
Function:
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Subcellular Localization:
Cytoplasm.
Sequence:
MTQITVKALSEEIGTPVDRLLEQLADAGMNKAVADHVSEDEKQKLLAHLRKEHGDATGSEPTRLTLQRKTRSTLSVNAGGGKSKNVQVEVRKKRTYVKRSSVEDEATREAEEAAMRAAEEQAKREAEEAAQRAAEEKAKREAEEAAKREAEAKRMAEEKAKRETQAATQPRSDEEKLKQEAARKEAEALKRRQEEEARRKAEEESRRQLEKVRELAEKNGERWSADKETVGDMQENTDYHVTTSRYAREAEDEADLHEEGARRRSTKANKRKMSSRDDNQERDSRPRGGKAGRKGRINKPMSMQHGFDKTAVVAKADVVVGETIVVSELAQKMSVKATEVIKVMMKMGAMATINQVIDQETAQLVAEEMGHKVVLRKENELEEAILSDRDDKFEEVSRAPVVTIMGHVDHGKTSTLDYIRRTHVASGEAGGITQHIGAYHVETPNGMITFLDTPGHAAFTAMRARGAQATDIVVLVVAADDGVMPQTVEAIQHAKAAGVPLIVAVNKIDKDTANPDNVKTELSQYNVMPEEWGGDNMFVHISAKQGTNIDGLLEAILLQAEVLELKAVKQGMASGVVIESRLDKGRGPVATVLVQSGTLRKGDIVLCGQEYGRVRAMRDEVGNEVEEAGPSIPVEILGLSGVPAAGDEATVVRDERKAREVANYRAGKFREVKLARQQKSKLENMFSNMTAGDVAELNIVLKADVQGSVEAIADSLTKLSTDEVKVNIVGSGVGGITETDAVLAAASNAIVVGFNVRADASARRMIEAENIDLRYYSIIYQLIDEVKQAMSGMLSPEFKQEIIGLAEVRDVFKSPKLGAIAGCMVTEGVIKRNAPIRVLRDNVVIYEGELESLRRFKDDVAEVKNGYECGIGVKNYNDVRVGDQIEVFETIEIQRTID
The following text describes a protein:
Function:
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MDEAIIVDAEFVAPVGTTAGEFVPIDRAPAAGLLLLVAFVVLYAKVISKLGKPAIQEFLWEIITRIVPSKQLRRRKEAQLRAIEVHTQRSNTSSQDQFAKWAKLDREYGKLKVEIEDINNLLTASKARFFTIISSAIFLSTTGMKMFLRIKHRKAAIFWLPKNAFPYPIEYILSFSSAPLGSVSVSAWLMICDAAMDLIVTIFVALVVGVIGMLRSNKVKPKTA
The following text describes a protein:
Function:
NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers.
Sequence:
MTRHDLPHANLLDPRLLRLFDALFTTGSVTKAAERLGQSQPTVSIWLARLRQELDDPLFVRSPEGMLPTPRAEALISTARQALEMLRRLAELRTDFDPATAKRRFSICMTDASHITLLPAILAHVRRVAPGIRIEAAQIGMDTPRMLQSGESDLALGYISDLDAGHFQQALFPQDWVCLANAHHPRIKNRITLRDFRREAHVLIRSGTGHQLLADASREQGIAPDIALELPGFLGLPAIIGTTDLIATLPRHIGETLAHYYGLRVLACPLPIPSFTVKQYWHARFHHDPASQWLRGVCAELFQQQDVRGLHRSARPRRRKAT
The following text describes a protein:
Function:
Probable regulatory protein. Its target is not known.
Sequence:
MMELINNRGMRDWMIFIKVAEVGNLSRAARELDISISAVSKSLSRLENSIEVTLLRRDSHHLELTGAGQTAYASMKRITSSFQSLLDELRNPDKIIRGSIKFSAPAIVCEFLANKWIWEFTASYPDTKIYLDSRERSDFFSKSLEFDELVFKSGIIESEDLVYRKISPLKLVLCASPKYIRKYGRISHPGDLENHIIVGLHNHGLSGPLTLFRQDESYTISGAVNVHLSSNNLLSVLNLVLEGKGINLMTPAWLATKYLKNNELEIILPEWRVPDLPIYLVWRHRQYYSPLFQRFLSFIEDKWNNRPQIDFLNDD
The following text describes a protein:
Function:
Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4. Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF. In response to proNGF binding, the heterodimeric receptor with SORCS2 activates a signaling cascade that leads to decreased Rac activity, reorganization of the actin cytoskeleton and neuronal growth cone collapse. Plays an important role in differentiation and survival of specific neuronal populations during development (By similarity). Can mediate cell survival as well as cell death of neural cells. Plays a role in the inactivation of RHOA (By similarity). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Necessary for the circadian oscillation of the clock genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cytoplasm. Perikaryon. Cell projection, growth cone. Cell projection, dendritic spine.
Domain:
Death domain is responsible for interaction with RANBP9. It also mediates interaction with ARHGDIA and RIPK2 (By similarity); The extracellular domain is responsible for interaction with NTRK1.
Sequence:
MRRAGAACSAMDRLRLLLLLILGVSSGGAKETCSTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDNVTFSDVVSATEPCKPCTECLGLQSMSAPCVEADDAVCRCAYGYYQDEETGHCEACSVCEVGSGLVFSCQDKQNTVCEECPEGTYSDEANHVDPCLPCTVCEDTERQLRECTPWADAECEEIPGRWIPRSTPPEGSDSTAPSTQEPEVPPEQDLVPSTVADMVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQTHTQTASGQALKGDGNLYSSLPLTKREEVEKLLNGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWGAQDSATLDALLAALRRIQRADIVESLCSESTATSPV
The following text describes a protein:
Function:
Probably involved in membrane protein trafficking.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAEKVNNFPPLPKFIPLKPCFYQNFEDEIPIDHRNLVKKIYHLWIFYCITLVMNLIACLAWWIGGGYGVNFGLAILWLLIFSPCSYVCWFQPVYKAFRSDSSFNFMAFFFIFGAQFVLTVIQAIGISGWGVCGWLSTITFFPTNVGAAVVMLLPAIMFSISAVLMAIVLLRVHKIYRGAGGSFQKAQNEWSTGTWKNPPTREAQYNNFSGNSLPEYPTVPNYPTGNQWP
The following text describes a protein:
Function:
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Sequence:
MHPLIDSIARKPSEKFTRPNFSVRRYDIIDEAKKIFKATCLSTVPYANMVMLATQDSVLLVGLLAGVPSYNVPMRRRDGLVSYPNEVNLPRATFSISEATQAFMTKGFFTFTVTGTLLDAHSVGAAHCSFLVTKLKGICRNSTSNDPTAFLDQSTSFMADNSFACAMVRLGNIQVPTGNAKEIRRNCRIFNKPK
The following text describes a protein:
Function:
Catalyzes the de novo synthesis of acetyl-CoA in vitro (By similarity). Promotes acetylation of CTTN, possibly by providing the acetyl donor, ensuring correct dendritic spine morphology and synaptic transmission (By similarity). Binds to follistatin-related protein FSTL1 and may act as a cell surface receptor for FSTL1, contributing to AKT activation and subsequent FSTL1-induced survival and function of endothelial cells and cardiac myocytes.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Mitochondrion. Cell projection, dendritic spine.
Sequence:
MADRGCPLEAAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIPLIQGIDPSLQAENRIPGPSQTTAAAPKQQKSRPTASRDERFRSDVHTEAVQAALAKYKERKMPMPSKRRSVLVHSSVETYTPPDTSSASEDEGSLRRPGRLTSTPLQSHSSVEPWLDRVIQGSSTSSSASSTSSHPGGRPTTAPSAAATPGAAATTALAGLEAHTHIDLHSAPPDVTTGLVEHSYFERPQVASVRSVPRGCSGSMLETADGVPVNSRVSSKIQQLLNTLKRPKRPPLKEFFVDDFEELLEVQQPDPNQPKPEGSETSVLRGEPLTAGVPRPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTSKNEPLLKPGDRVALVFPNSDPVMFMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKARAALVKSRDMHWSLLAQRGQRDVSLSSLRMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDLGGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNVLMCPHTCVTNLPKPRQKQPEVGPASMIVGNLVAGKRIAQASGRELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTGVLRMKGVNLSCVRTCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGCRVNVAICLQGTAGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTVYGEEALHADHFSARLSFGDTQTIWARTGYLGFLRRTELTDASGGRHDALYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIAECAVFTWTNLLVVVVELDGLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINSRGEKQRMHLRDGFLADQLDPIYVAYNM