lhallee/plat_data huggingface dataset:
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. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and rpc2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MDPESVGYCNNPDFLHKGSMDELYNISKLTDDIKPVEEKWKLVPAFMKCRGLVKQHIDSFNFFINVEMKKIVKANERLTAENDPSYFVRFTDINVGSPTSTEDNLDSVQLTPQRCRLRDMTYSAPIFVNIEYTRNKQIISKRDVHIGNIPIMLRSSNCVLSKKTPEQMAALGECPMDPGGYFIVRGQEKVILNHEQLSKNRIIIEMDSKGLPSASVTSSTHERKSRTGVTLKNEKLYLKHNTFGEDIPVAIVLKGMGVETDQEMAQLVGSDDVFLNAITPSLEECQKCGVHTAAQALDYLGSRIKVFRRPYGVQNKKTKSEEARDILAGVVLNHVPVRRYNFRLKVIYLSLMIRRIIMASKDKSCLDDKDYYGNKRIELSGQLISLLFEDCFKKFQSELKKSVDQAIAKANRAENLDLPKLIRTDTITNGFTHAISSGQWNLKRFRMERSGVSQVLSRLSYISCMGMMTRIQSQFEKTRKVAGPRSLQPSQWGMLCPSDTPEGEACLHPDTIITMSNGQQKPIRQLKDGDSIITLDPITMEAHSTRIYSHFIKSSSQYGKQLLKITTITGKEIICTNDHRFLTSNGNWKQSKDLLLNDKLFLISSSNQLEFNNNNNENNNENNNDIIEILNENQLINQGVVPIKIIQELKSIELLPLLNNNEKLITISRIIGSIDKIGSNKQNEPIIQYQFNLISDFDQFLKDLQYLGFINPIYKLNEEQQQQQQQKIDHQQQQQQQVEQQQKSIIIDFIGSSFGYFIQSLLNEKNWIEKSNNQFVKKEFLSSFISNVNRIQFNIIEEINQQNNDSNFKILLNYKQQKQQQNEKEERAVVDHDNEIFNIKSLQILLNQFNVISSIDFEESNLIIINSSLKKFIDLINIKFNQKLNNQIIQIREYLNYINYNNNNNNNEEINIKKKDFGYFKKLKIKRNSFEIEIEKIEQLNYQDCPEISDFTTESDYHSMISNGFVSHNCGLVKNFALMSHVTTDDSEGPLLRLAYNLGVQDILLVTGEELNSRNAYLVLLNGQIIGIHNSPDYFVTTLRKMRRAGRIREFVSICKNKAQQTISVACDGGRLCRPVIIVDDQRPRLTQEHIEDLKDGLRTFDDFIREGIIEYLDVNEENDSFLAWREAAIQPWTTHLEIEPFTMLGCVAGLIPYPHHNQSPRNTYQCAMGKQAIGAIAYNQLTRIDTLLYLLVHTQRPLCQTRTIDLLNWYKLPAGHNATVAVMSYSGYDIEDALVMNKASLDRGFGRCIVLKKQVTSIKKHGNDTSDRIFPPTPNDLRQPKYGLLDSDGIAKPGELAQKGQILVNKYSPLNTIDATPNPELIPDSAYKSSYMGYKYDNPAFIDKVLLTSGDDEQLLIKMLMRSTRRPELGDKFSSRHGQKGVCGIIVKQEDMPFSDLGICPDIIMNPHGFPSRMTIGKMIELLAGKAGVLSGKFGFGTCFGGDRVENISKVLISKGFSYGGKDYVTSGVTGEPLACFIFFGPIFYQKLKHMVMDKMHARARGPTVTLTRQPTEGRARGGGLRLGEMERDCLIGYGASALIMERLMISSDRFTVYACKNCGFLGYEGYCQYCKSSVDISTIQIPYACKLLFQELQAMNIVPRLKLVDS
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MQLPPALCARLAAGPGAAEPLPVERDPAAGAAPFRFVARPVRFPREHQFFEDGDVQRHLYLQDVIMQVADVPEKPRVPAFACQVAGCCQVFDALDDYEHHYHTLHGNVCSFCKRAFPSGHLLDAHILEWHDSLFQILSERQDMYQCLVEGCTEKFKTSRDRKDHMVRMHLYPADFRFDKPKKSRSPASAEAPGDSGERSEGEAMEICSEPVAASPAPAGERRIYRHRIPSTICFGQGAARGFKSNKKKTKQC
The following text describes a protein:
Function:
The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MLRGTLLCAVLGLLRAQPFPCPPACKCVFRDAAQCSGGDVARISALGLPTNLTHILLFGMGRGVLQSHSFSGMTVLQRLMISDSHISAVAPGTFNDLIKLKTLRLSRNKITHLPGALLDKMVLLEQLFLDHNALRGIDQNMFQKLVNLQELALNQNQLDFLPASLFTNLENLKLLDLSGNNLTHLPKGLLGAQAKLERLLLHSNRLVSLDSGPLNSLGALTELQFHRNHIRSIAPGAFDRLPNLSSLTLSRNHLAFLPSALFLHSHNLTLLTLFENPLAELPGVLFGEMGGLQELWLNRTQLRTLPAAAFRNLSRLRSLGVTLSPRLSALPQGAFQGLGELQVLALHSNGLTALPDGLLRGLGKLRQVSLRRNRLRALPRALFRNLSSLESVQLDHNQLETLPGDVFGALPRLTEVLLGHNSWRCDCGLGPFLGWLRQHLGLVGGEEPPRCAGPGAHAGLPLWALPGGDAECPGPRGPPPRPAADSSSEAPVHPALAPNSSEPWVWAQPVTTGKGEDHSPFWGFYFLLLAVQAMITVIIVFAMIKIGQLFRKLIRERALG
The following text describes a protein:
Function:
Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular Localization:
Nucleus.
Domain:
The N-terminal half of the protein contains two conserved domains I and II. Domain I includes a slightly degenerated ERF-associated amphiphilic repression (EAR) motif which seems to be involved in the activity of transcriptional repression. Domain II is required for the correct degradation of the protein through the SCF-mediated ubiquitin-proteasome pathway. Interactions between Aux/IAA proteins and auxin response factors (ARFs) occur through their C-terminal dimerization domains III and IV.
Sequence:
MNGLQEVCSSSGSVMIGLPAEEDENAAHSSEDSSCPDESVSETELDLALGLSIGRRKVRSSLSSSSSSLTRESGTKRSADSSPAAASNATRQVAVGWPPLRTYRINSLVNQAKSLATEGGLSSGIQKETTKSVVVAAKNDDACFIKSSRTSMLVKVTMDGVIIGRKVDLNALDSYAALEKTLDLMFFQIPSPVTRSNTQGYKTIKETCTSKLLDGSSEYIITYQDKDGDWMLVGDVPWQMFLGSVTRLRIMKTSIGAGVGK
The following text describes a protein:
Function:
ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose. Specifically acts as a glutamate mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to glutamate residues on proteins. Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG to become a substrate for OARD1. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.
Subcellular Localization:
Nucleus, nucleoplasm. Nucleus, nucleolus. Chromosome. Note=Localizes both in the nucleoplasm and in the nucleolus. Relocalizes to the nucleoplasm in response to DNA damage. Recruited to DNA lesion regions following DNA damage.
Sequence:
MAGSPNEDSEGSRITYVKGDLFACPQTDSLVHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLRKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAIIEEVFEATDIRITVYTL
The following text describes a protein:
Function:
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Sequence:
MSETDSTDFHEMREPRIEKVVVHMGVGQGGVELQNAETILEAITGQQTVRTKAKSPEPEFGLRQGDPIGAKVTLRDDTAVDFLERALPAADLDRRQFDNTGNVSFGIEEHTDFPSQEYDPNIGIYGMDVTVNLTRPGYRVAKRDQGTRQIPSNHRLNSEDAVSFLVSNFDVEVNE
The following text describes a protein:
Function:
Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.
Subcellular Localization:
Cytoplasm.
Sequence:
MNIITVKINGVEYNLKGEEQEDYLHKVARYVDKKIADILENNPKLSTSSASILTAINAIDEGLKKEEQIENLQLEIDKLKKVQHHQNLKVEEIRNLLAEEKEKNKDLEAQDVDDSAKEYKEKLEKLQVQMELMEKTAKKYMEENNKIKIQNKELKFQLQSSKYKVLDLEKKLMDSQLTLAKEKKKLNPLQVKDMKK
The following text describes a protein:
Function:
This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG) (By similarity).
Subcellular Localization:
Nucleus, nucleoplasm.
Sequence:
MMLSTEGREGFVVKVRGLPWSCSAEEVMRFFSDCKIQNGTSGVRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNSVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGMTLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMTMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYGGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSSFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPMRVHIEIGPDGRVTGEADVEFATHEDAVAAMAKDKANMQHRYVELFLNSTAGTSGGAYDHSYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSAGYGGGYGGQSSMSGYDQVLQENSSDYQSNLA
The following text describes a protein:
Function:
Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Inhibits in vitro tube formation and mobilization of endothelial cells. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization.
Subcellular Localization:
Endomembrane system; Single-pass membrane protein. Secreted, extracellular space, extracellular matrix.
Sequence:
MTENSDKVPIALVGPDDVEFCSPPAYATVTVKPSSPARLLKVGAVVLISGAVLLLFGAIGAFYFWKGSDSHIYNVHYTMSINGKLQDGSMEIDAGNNLETFKMGSGAEEAIEVNDFQNGITGIRFAGGEKCYIKAQVKARIPEVGAVTKQSISSELEGKIMPVKYEDNSLIWVAVDQPVKDNSFLSSKVLELCGDLPIFWLKPTYPKEIQRERREVVRKIVPTTTKRPRNGPQGNPGAGRLNNETRPSIQEDSQAFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPLGGYYPWPYNYQGCRSACRVIMPCSWWVARILGMV
The following text describes a protein:
Function:
Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane. Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1-arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA). Also displays an ester hydrolase activity against acetyl ester, butanoate ester and hexadecanoate ester. Plays a key role in sperm capacitation in response to progesterone by mediating degradation of 2AG, an inhibitor of the sperm calcium channel CatSper, leading to calcium influx via CatSper and sperm activation (By similarity). May also play a role in smooth muscle cells migration (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MNAMLETPELPAVFDGVKLAAVAAVLYVIVRCLNLKSPTAPPDLYFQDSGLSRFLLKSCPLLTKEYIPPLIWGKSGHIQTALYGKMGRVRSPHPYGHRKFITMSDGATSTFDLFEPLAEHCVGDDITMVICPGIANHSEKQYIRTFVDYAQKNGYRCAVLNHLGALPNIELTSPRMFTYGCTWEFGAMVNYIKKTYPLTQLVVVGFSLGGNIVCKYLGETQANQEKVLCCVSVCQGYSALRAQETFMQWDQCRRFYNFLMADNMKKIILSHRQALFGDHVKKPQSLEDTDLSRLYTATSLMQIDDNVMRKFHGYNSLKEYYEEESCMRYLHRIYVPLMLVNAADDPLVHESLLTIPKSLSEKRENVMFVLPLHGGHLGFFEGSVLFPEPLTWMDKLVVEYANAICQWERNKSQCSDTEQVEADLE
The following text describes a protein:
Function:
Neurotoxin that produces dose-dependent hypolocomotion and hyperalgesia in mice. May directly act on the central nervous system, as it is 6500-fold more potent when administered intracerebroventricularly than intraperitoneal.
Sequence:
MDAEGPANRLCEEATCPLCLDFFKDPVIIDCGHNFCSSCLAKCWGEPVPEASCPQCREKIPQRTFRPNRQLANMAELVQKLQEGRKKEEGRRDACKMHQEPLKLFCREDEAPICTVCDRAKEHRGHNVIPLEEAFQEYKEKTKLQLESLKKKREEFKGQRYVQELRRKDYQTQLDLEKMMIKSLFEGMQRFLEEKQHFCLAQLEDLEKEMEKRQDKTLAKLTEEISQLTLLIREMEEKCLQPASDFLQGIKNSLVRCEKNLGGYVLDVSPNLNERLKMTSQKISALQKATESYKESLEEALIKAVWEQNVNTGDVGCIFNTPSFSFIVYVTLDPETACSRLILSEDLKNARILGCTPRQYNDFPNKCNIFPQEAFVLGRERFTSGRHCWEVYVFSDQWAVGISRDSVRKKGNINPNTDDSIWAVGVKPGRLCGSEVCIFPAVGSSSLKKNINKLYVVLNYEVGRVEFYSYKEFIYAFSSISFSGEEIRPFFWVPNDGYLICC
The following text describes a protein:
Function:
RNA-binding protein that plays a central role in oogenesis, but not for spermatogenesis. Required for meiotic entry and germline differentiation, at the pachytene stage of meiosis I of female germline regardless of the sex of the soma. May act by regulating translation of specific mRNAs, possibly by binding to their 3'-UTR.
Sequence:
MMSPPLRYQKDQQNQQHQQNQSQQAAHQMVSFMPQTPTSLPSTPIQLYPTGAAALIPAPPTYELIPNRIFVGGFPTSTTETELREHFEKFFAVKDVKMVKSLDGQSKGYGFITFETEDQAEEIRKLTPKQLEFRSRKLNLGPAIRKINSNSFQPSYAIATPSQLVAASPGPFSYAIPASPSPYSGYSYPASPQMFVYPPLRSQDQSRQQSEQQTTPQNSPTNLQHQQSPQVFFGGDQDPIRSYASAVAGVEKSEVSPEKHESVSPQPLLPNQNVLNTQYSQGQQQWNSNVQQQQQQQMDSNNGGPYYNENYSQGYTRPHPYQQFAQSGVYMNSQGMYHSSYSYMTPPLAPGQYPQMMSAPYWQQQQQHHQSHAYAGYNPAYNNWVGPSGDMNQFKQNPSNYFYQNYPGNFSQQHTMGNNENTFSLPLQAPRQGKKSRKPSECQDKKTKSPIKGARTERPSSSASTPDAKYQKNHRYPVHLSPLSASLQSLAISSPTKNN
The following text describes a protein:
Function:
Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MGFHHIIIIRFVFSILLGWLSSSVEATNSTKCNQYCGAAGSYSPRVSYPFGFSEGCGIRLDCTESTGEIRIGEYIIQNVTSETLMVNFSMNCSRPIEDLQQFDRTNFGMTWRNGLLLHNCKVPKSECTILSEILSTRLNIQSCDSKKENVSCYSEARADYLDYKKLKNTGCGTVISSILIGMDNDTMKSSAMFIEFQTMELAWGLEGDCACHNDANCTNVSLPGNRKGFRCRCKDGFVGDGFSDGDGCRKVSRCNPSRYLSGRCGGTTRIGVLVGGIIAGAGLMAALAVLCYCIRRRSASLKKRMSARRLLSEAAGSNSVHVFQYKEIERATNSFSEKQRLGIGAYGTVYAGKLHSDEWVAIKKLRHRDPDGVEQVMNEVKLLSSVSHPNLVRLLGCCIENGEQILVYEFMPNGTLAQHLQRERSSGLPWTIRLTIATETAHAIAHLHSAMNPPIYHRDIKSSNILLDYNFNSKVADFGLSRFGMTDDSHISTAPQGTPGYVDPQYHQNYHLSDKSDVYSFGVVLVEIITAMKVVDFSRSHSEINLAALAIDRIGKGRVDEIIDPFLEPHRDAWTLSSVHRVAELAFRCLAFHRDMRPSMTEVADELEQIRLSSWASLEDNVCMTSSVNSSCSSPRSMSETSFRSTTTKKGVGSRRLIVPQKIANSLAIMEEIKDSSPVSVQDPWLSEESPPSTNRLLGNSGR
The following text describes a protein:
Function:
Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation. However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha. The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins. Involved in telomere maintenance. Involved in genome stability (By similarity). May be in involved in telomeric C-strand fill-in during late S/G2 phase.
Subcellular Localization:
Nucleus. Chromosome, telomere. Note=A transmembrane region is predicted by sequence analysis tools (ESKW, MEMSAT and Phobius); however, given the telomeric localization of the protein, the relevance of the transmembrane region is unsure in vivo.
Sequence:
MAACRAQPPTSEQAWLEAAQTFIQETLCPAGKEVDKELTRSVIACVKETWLSQGENQDLTLPFSYSFVSVQSLKTHQRLPCCSHLSWSQSAYQAWTRGGRPGDGVLPREQLILLGTLVDLLGDSEQECRSGSLYVRDNTGTLDCELIDLDLSWLGHLFLFPSWSYLPSAKRNSLGEGHLELWGTPVPVFPLTVSPGPLIPIPVLYPEKASHLLRYRKKSSIKEINLAGKLVHLSALIITQNKRYFIMTLGELAQAGSQVSIIVQIPAQMVWHRVLRPGRAYVLTKLQVTKTRIHLSCIWTTIPSSTLKPLRPGYVQELELDLEFSKADLKPPPQPTSSKDSRGQEGLVRASKVLHYLGTVTAVLHESAGLYILDGQLILCLAYQKIHGLRRVIRPGVCLELRDVHLLQAVGGATTKPVLALCLHGTVRLQGFSCLKPLTLPSSKVYGASLYEQLVWKCQLGLPLYLWAAKTLEDLIYKLCPHVLRCHQFLKQPSPGKPSLGLQLLAPSWDVLIPPGSPMRHAYSEILEEPHNCPLQKYTPLQTPYSFPTMLALAEEGQHRAWATFDPKAMLPLPEASHLTSCQLNRHLAWSWVCLPSCVFQPAQVLLGVLVASSRKGCLELRDLRGSLPCIPLTESSQPLIDPNLVGCLVRVEKFQLVVEREVRSSFPSWEEMGMARFIQKKQARVYVQFYLADALILPVPRPTFGSEPSQTASSCPEGPHLGQSRLFLLSHKEALMKRNFCLLPGDSSQPAKPTLSFHVSGTWLCGTQRKEGSGWSPPESLAVESKDQKVFLIFLGSSVRWFPFLYPNQVYRLVASGPSQTPVFETEGSAGTSRRPLELADCGSCLTVQEEWTLELGSSQDIPNVLEVPRTLPESSLAQLLGDNSPDSLVSFSAEILSRILCEPPLALRRMKPGNAGAIKTGVKLTVALEMDDCEYPPHLDIYIEDPQLPPQIGLLPGARVHFSQLEKRISRSNIVYCCFRSSTSVQVLSFPPETKASAPLPHIYLAELLQGDRPPFQATTSCHIVYVLSLQILWVCAHCTSICPQGKCSRRDPSCPSQRAVSQANIRLLVEDGTAEATVICRNHLVARALGLSPSEWSSILEHARGPGRVALQFTGLGGQTESASKTHEPLTLLLRTLCTSPFVLRPVKLSFALERRPTDISPREPSRLQQFQCGELPLLTRVNPRLRLVCLSLQEPELPNPPQASAASS
The following text describes a protein:
Function:
Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression.
Sequence:
MLLGQKSQRYKAEEGLQAQGEAPGLMDVQIPTAEEQKAASSSSTLIMGTLEEVTDSGSPSPPQSPEGASSSLTVTDSTLWSQSDEGSSSNEEEGPSTSPDPAHLESLFREALDEKVAELVRFLLRKYQIKEPVTKAEMLESVIKNYKNHFPDIFSKASECMQVIFGIDVKEVDPAGHSYILVTCLGLSYDGLLGDDQSTPKTGLLIIVLGMILMEGSRAPEEAIWEALSVMGLYDGREHSVYWKLRKLLTQEWVQENYLEYRQAPGSDPVRYEFLWGPRALAETSYVKVLEHVVRVNARVRISYPSLHEEALGEEKGV
The following text describes a protein:
Function:
Exhibits chaperone activity toward chloroplast outer envelope membrane, mitochondrion outer membrane, endoplasmic reticulum membrane and peroxisomal proteins, by recruiting specific proteins containing a single transmembrane associated with an AKR2A-binding sequence (ABS) and subsequently binding glycolipids (e.g. monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG)) present in the membrane of the target organelle. Seems to be involved in the regulation of hydrogen peroxide levels during biotic and abiotic stresses by optimizing the ascorbate peroxidase 3 (APX3) hydrogen peroxide-degrading activity. This regulation might be monitored by GRF6. Cytosolic targeting factor for chloroplast outer membrane (COM) proteins that mediates sorting and targeting of nascent chloroplast outer envelope membrane (OEM) proteins to the chloroplast. Facilitates the targeting of OEP7 to chloroplasts. Facilitates the targeting of APX3 to peroxisomes. Involved in cellular metabolism (e.g. peroxisome activity) and required for plant growth and development.
Subcellular Localization:
Cytoplasm. Nucleus. Plastid, chloroplast outer membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The ankyrin repeats (ANK) mediate interactions with hexoses-containing lipids present in organellar membranes (e.g. chloroplast), such as monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG).
Sequence:
MASNSEKNPLLSDEKPKSTEENKSSKPESASGSSTSSAMPGLNFNAFDFSNMASILNDPSIREMAEQIAKDPAFNQLAEQLQRSIPNAGQEGGFPNFDPQQYVNTMQQVMHNPEFKTMAEKLGTALVQDPQMSPFLDAFSNPETAEHFTERMARMKEDPELKPILDEIDAGGPSAMMKYWNDPEVLKKLGEAMGMPVAGLPDQTVSAEPEVAEEGEEEESIVHQTASLGDVEGLKAALASGGNKDEEDSEGRTALHFACGYGELKCAQVLIDAGASVNAVDKNKNTPLHYAAGYGRKECVSLLLENGAAVTLQNLDEKTPIDVAKLNSQLEVVKLLEKDAFL
The following text describes a protein:
Function:
Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular Localization:
Nucleus.
Sequence:
MYLSNLGGQSRKTGIRPKTNLKTDKYGMEDVDDFFEDDDDDGINKSKGQKSTIALSRGEEVSNYKSTISQPFNNIARKINFNQEDDETFNLPSTSSSSATVTASSVSNKKSPVTTQQSPLRSPLPEQDYDYNQFDVEEDYGNITEEDKQPSPPPPVPKTKSKAKTKAKASTTNNTNTKSTKAASSFTKKMALGKTKRLPSSFDSVNTSSVTEYYDEDDEDNDRDYGESQQDSIEDSMVDSTFNDYSQPSSNNNKTRRKIIKESPLPSPPPDNPNGLRRSKRTRIKPLAFWRNERIIYSKDLDYDDEQDTTLARDIHNIPLQSIKEVVHIPDNESVDNSGSPNTRTGAAGSTKTRSNRKRTYKQTTTTAPTDYDYESDPEISGSEWFKEDNLSLEVNDNGESKLRKIAYNHKGGNYVKPTDDNYLVASLFDEDKSFFAGGMLQLPSDGFKPPVTVTGSTYMFNVMKGLIQVTLNENMFVVTKGCKVQIPEGNEYSLRNIGQGDAYLFFVQIRKPEEIDTNW
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system. A probable antitoxin for the putative mRNA interferase YeoB (By similarity).
Sequence:
MKAITTTQAKDHLDELINAVISDLEPTIVSNNQGQQAVLISLDEFNSWQETLYLLSNPTNAEHLMASIKQAETGQIIKQKLPDLLEL
The following text describes a protein:
Function:
Sperm-specific solute carrier involved in intracellular pH regulation of spermatozoa. Required for sperm motility and fertility. Involved in sperm cell hyperactivation, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for the expression and bicarbonate regulation of the soluble adenylyl cyclase (sAC).
Subcellular Localization:
Cell projection, cilium, flagellum membrane; Multi-pass membrane protein.
Sequence:
MEFPLLEALGAGNASNSTNGTDSHGGGGGHGDGDIHAHSGHHEQPYIILFLFASFALGALVRTLLKIVPGDLPYTVVLLVLGILLGLASARSPDFAHYTAIVHMNPHLLFHVFLPVLIFESAFAMDTHMFWKSIYQILIMALPGLLLASLLTGILSMYTFNYGWNWYVGMMFGSICSATDPVAVVALLKELGASKQLGTVIEGESLLNDGCGIVIFTMFLNLATGVEWAAADFVIFIVKVMLGGPAFGFVMSKLTSFWLANIFNDALTEITITLASTYITFYVAEVLGVSGVLAVVILGLTMERTSISPEVESFLHRFWEMMAYLANTVIFILVGVMIMEKSIHMIEGGDWFYIITLYFGINVIRLIVIIILSPATSRVGYGLSWRYGVVTAWSGLRGAVGLAMALLVMQQEMTKGSSEDWKMQVANKILIHIAGIVFLTLFINATTIKALLRLLGMSDISAPKRMTMYSAVRRVKDAQNRSFQVLKGDRFLADAEWTLVEKACEIQDPYKTKDEEDILEQPLPTKCAAAIDTCLWQLQYQVSLCFARIRHCQVNAEEFVPFQRMSQCQDCKSMVPNEPSPREYQDMAEEARLRTLKAQKVSYWKQFEHGMLNREAVRVLVQATESAADSVGEFVDIEEIKKHWKIKGLLPRLRNKLEDLVTDKQKDQLPMPEHKFLRTVFIIVGHPAFEWSINVLIILNLIPIIIEFTIEESDPQFPEYQFYLRITNYVFFVIYILEAVLKIIALRKHYFFSHWNQFDLFIIAVSIIDIVLDNIFGNVDFNPAIFRIAKIFRLLRAMRMLRLSKAAIPRMINVIDNLINKQLSFGYDVGKGFVVGEEEVMKLIPTIIDNRSIARDLRQKSDISRRAVIRELGLLQRDHPGIAVSVKTRQSIRAVLNHSRDTIREMQGGGLLDETEAKKLEMVVEIKMKQLARAPPSIPPPNPEQLLRHISWLEGNTELTEFMKARAKLLFHDFGSTLCKQSELPQGLFLIVSGMVKLRGAGVKYTDYETQHSMDDDLEVYEDYLTSGNIIGEMGILNKQPRSTSVSCETSIQTYYISAEDMDMAFDLFSVNFLKERIWRVVAIRISTPLLLKTLAYQGWTHDKVRLRLETGYMPTNLVDRRSFEIDQTMDDVILVQGHALSPHTAEEFVAPCIIPRTIHKLTFSTDSMEEGVLPPQLLVVPNKEVIIEEDTKRRNSLYGGIGPSTTSLCLQHAAQRRSSHNLLAKKSSSSIFRRPKSGKAKSVSIALPSLETASDGTTRRRTDLQPITDPVSNTSTTSASGSLKPVVLPNQVVSREGAWSVQSADFGSEKAWEGNKFQF
The following text describes a protein:
Function:
An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. The most abundant cellular protein in terms of copy number, there can be up to one million Lpp molecules per cell. About one-third of Lpp is bound to the PGN (called bound or periplasmic) the rest is called free or transmembrane. The 'free' form can be surface labeled by membrane impermeable agents and so must cross the outer membrane; it is thought that this transmembrane form is still anchored in the inner leaflet of the outer membrane. Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan maintains the position of the cell wall in the periplasm, holding it approximately equidistant from both the inner and outer membranes. Trimeric Lpp controls the width of the periplasm, adjusts its tilt angle to accommodate to the available space, and can compensate in part for an absence of OmpA (Probable). The role of the cell surface-exposed, free form (transmembrane) of Lpp is unknown.
Miscellaneous:
MISCELLANEOUS: About one-third of Lpp is covalently bound to peptidoglycan.
Subcellular Localization:
Cell outer membrane; Lipid-anchor; Periplasmic side. Secreted, cell wall; Peptidoglycan-anchor. Cell outer membrane; Lipid-anchor; Extracellular side. Note=Attached via its lipidated N-terminus to the inner leaflet of the outer membrane. Attached to the peptidoglycan network (PGN) via its C-terminus (Probable). About one-third of the protein links the outer membrane and the PGN, the rest is not-linked to PGN. PGN-bound and non-bound forms can interconvert. The C-terminus of the non-PGN-bound form is exposed on the cell surface; its N-terminus is probably anchored in the inner leaflet. Targeted by the SRP/Sec/YidC pathway.
Sequence:
MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK