lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.
Subcellular Localization:
Nucleus.
Sequence:
MDPLCTASSGPRKKRPRQVGASMASPPHDIKFQNLVLFILEKKMGTTRRNFLMELARRKGFRVENELSDSVTHIVAENNSGSEVLEWLQVQNIRASSQLELLDVSWLIESMGAGKPVEITGKHQLVVRTDYSATPNPGFQKTPPLAVKKISQYACQRKTTLNNYNHIFTDAFEILAENSEFKENEVSYVTFMRAASVLKSLPFTIISMKDTEGIPCLGDKVKCIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRSLSKIMSDKTLKFTKMQKAGFLYYEDLVSCVTRAEAEAVGVLVKEAVWAFLPDAFVTMTGGFRRGKKIGHDVDFLITSPGSAEDEEQLLPKVINLWEKKGLLLYYDLVESTFEKFKLPSRQVDTLDHFQKCFLILKLHHQRVDSSKSNQQEGKTWKAIRVDLVMCPYENRAFALLGWTGSRQFERDIRRYATHERKMMLDNHALYDKTKRVFLKAESEEEIFAHLGLDYIEPWERNA
The following text describes a protein:
Function:
Lipid tetraspanin-associated transmembrane adapter/mediator that acts as a scaffold for Src-family kinases and other signaling proteins in immune cells. It is involved in major histocompatibility complex class II (MHC-II) signaling transduction in B cells, where it is required in generating the calcium response and enhancing ERK activity upon MHC-II stimulation. In dendritic cells, it is involved in sustaining CLEC7A/DECTIN1 signaling after CLEC7A activation by fungal beta-glucans (By similarity). It also acts as an agonist-inducible signaling adapter for TLR1, TLR2, TLR3, TLR4, and TLR7 by selectively enabling the expression of pro-inflammatory cytokines IL6 and IL12B in macrophages and acting as a scaffold for phosphorylation of Toll-like receptors by Src-family kinases (By similarity).
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Cell membrane; Lipid-anchor. Cytoplasmic vesicle, phagosome. Cell projection, ruffle. Cell projection, filopodium. Note=Together with MHC-II, associates with lipid-enriched microdomains called tetraspanin-enriched microdomains (TEMs). Rapidly translocates into immunological synapse (IS) at cell-cell contacts between antigen-presenting cells (APCs) and T-cells. Colocalized with tetraspanins CD37, CD53, and CD81 at the uropod. Present at regions of cell-cell contacts but also at the leading edge of migrating cells. Localizes to phagosomes in dendritic cells after exposure to particulate beta-glucan (By similarity).
Sequence:
MDTFTVQDSTAMSWWRNNFWIILAVAIIVVSVGLGLILYCVCKWQLRRGKKWEIAKPLKHKQVDEEKMYENVLNESPVQLPPLPPRNWPSLEDSSPQEAPSQPPATYSLVNKVKNKKTVSIPSYIEPEDDYDDVEIPANTEKASF
The following text describes a protein:
Function:
Permease that is involved in the active transport across the cytoplasmic membrane of all three aromatic amino acids, phenylalanine, tyrosine and tryptophan.
Miscellaneous:
MISCELLANEOUS: The general aromatic transport system is not essential for the supply of external aromatic amino acids to protein synthesis.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MMEGQQHGEQLKRGLKNRHIQLIALGGAIGTGLFLGSASVIQSAGPGIILGYAIAGFIAFLIMRQLGEMVVEEPVAGSFSHFAYKYWGSFAGFASGWNYWVLYVLVAMAELTAVGKYIQFWYPEIPTWVSAAVFFVVINAINLTNVKVFGEMEFWFAIIKVIAVVAMIIFGGWLLFSGNGGPQATVSNLWDQGGFLPHGFTGLVMMMAIIMFSFGGLELVGITAAEADNPEQSIPKATNQVIYRILIFYIGSLAVLLSLMPWTRVTADTSPFVLIFHELGDTFVANALNIVVLTAALSVYNSCVYCNSRMLFGLAQQGNAPKALASVDKRGVPVNTILVSALVTALCVLINYLAPESAFGLLMALVVSALVINWAMISLAHMKFRRAKQEQGVVTRFPALLYPLGNWICLLFMAAVLVIMLMTPGMAISVYLIPVWLIVLGIGYLFKEKTAKAVKAH
The following text describes a protein:
Function:
Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSGQWEVVGKKKEKGAKDLSQKVGKQSRNKPENLNVKVEDVLAKSQVKNLYSNGKNKENKPVEVKKDAGPKKAKVQDKVQEAKPKAPKSLESALNLIDSDAFKNIFEKNKTQFPDAPIVHDSVFASKPDNYPLKIVPSGVLSVIEKVAQVVDKNNLLVFYDIALTSMATDMSKNLPALGYKLFLQHIALKEPKLIRANLGKYCVLRTSYQNRPNIGLSILWAVGQAGIRDFQTGLAIFQELMLPLIELKNYSRFIVQYLIKLISGADQATVSKEQFVSLLDVVFSSKKNFPSDLKQDLVTVVPTLKSFLATSKEPTCVDFYLKKIPTVGNDSFKDCLCDVIVDGFNRDQSSLESWGKNYSKNVTSSAILLKYIAKNWQTLSCKINKKVLAHTLNQILLESNELRTRKKKDEGLIEAIRVSEELLGKMANKKSSRSWFKFLFYTTTLLLAIYIYADTKQAGSWQKSNTRKFLVETGVYDYTHKAVGKVQEGWLVVDNKIKENFPTYRQAVIEFSEPYIEFFNSFGQILCNLFANIKEAVIEKYPVVVKSIDSYAPGVVEQSQNAVSTAWSSSVFYVNRSIDYLRTEVFVGQLSPENMQRVVYEAFNTTQTKATEYYHWLYEKVQNTIK
The following text describes a protein:
Function:
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Subcellular Localization:
Cytoplasm.
Domain:
Lacks the Zn(2+) binding motif and the C-terminal dimerization appendix that are found in MetRSs from several organisms including E.coli MetRS.
Sequence:
MKPYYVTTAIAYPNAAPHVGHAYEYIATDAIARFKRLDRYDVRFLTGTDEHGLKVAQAAAAAGVPTAALARRNSDVFQRMQEALNISFDRFIRTTDADHHEASKELWRRMSAAGDIYLDNYSGWYSVRDERFFVESETQLVDGTRLTVETGTPVTWTEEQTYFFRLSAYTDKLLAHYHANPDFIAPETRRNEVISFVSGGLDDLSISRTSFDWGVQVPEHPDHVMYVWVDALTNYLTGAGFPDTDSELFRRYWPADLHMIGKDIIRFHAVYWPAFLMSAGIELPRRIFAHGFLHNRGEKMSKSVGNIVDPVALAEALGVDQVRYFLLREVPFGQDGSYSDEAIVTRINTDLANELGNLAQRSLSMVAKNLDGRVPNPGEFADADAALLATADGLLERVRGHFDAQAMHLALEAIWLMLGDANKYFSVQQPWVLRKSESEADQARFRTTLYVTCEVVRIAALLIQPVMPESAGKILDLLGQAPNQRSFAAVGVRLTPGTALPPPTGVFPRYQPPQPPEGK
The following text describes a protein:
Function:
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
Sequence:
MDFTAIDFETATRRSDSACQLAAVRVRGGEIVDSACWLIRPRPFVFSPANIQIHGITPGMVREEPEFGELWPEIQSTLGDDCLIAHNASFDLGVLMACLESHDHPVPDMQYSCTRAIARRTWPQQPRFGLKPLSDWLGIRFRHHDALEDSIACAKIALAAAEDSGATSLETLESKLSLSRGSAGAWGKKGPTSRRASTRRKSSPRRSPSRAPEVAIAGSTMTSSTISNSTAGSASFAIEPPRPCGISDSGVDLQRLMIRADFIRPLEGRKVVFTGVLQKLQREEAEMLTSRCGGKCQSSVSRKTDLVVVGDPDSRTVQASRTMSVKEATARQLAAEGAPLRIMTEHEFLEMIIAM
The following text describes a protein:
Function:
Binds selectively to the Gram-positive bacteria S.aureus and S.pneumoniae. Does not adhere to the Gram-negative bacteria E.coli and S.enterica. Probably recognizes peptidoglycans expressed on the bacterial cell surface.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MALRDIFLLSMAMTAVTVQACPSACKCTVSLYGEMVVACGGMGLTEIPEDIPHRAVYLVLKDNNITKITSYSFKGLRNLQGIDLSNNKINHISSAALRHLGHLDDIDLSRNELTSVSEKLFDFPISSAKAQGRRFFVYLANNPWGCDCRMAWLAQELAGGSKTFGDRHMECATPAALAGRGLSEIPQTSFVCTGRDISFDSDGIIATPEESTAFPVAYKVAVVFGCITGLVTILLLVLTAMLYQKRRIRLGSKYELRWNKHPEFV
The following text describes a protein:
Function:
Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events (By similarity). Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.
Miscellaneous:
MISCELLANEOUS: rRNA synthesized in the presence of 5-fluorouracil, a pyrimidine analog used in the treatment of solid tumors, is not efficiently degraded by Rrp6.
Subcellular Localization:
Nucleus. Chromosome. Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Midbody. Note=Relocates to the DNA double-strand breaks in response to irradiation, the relocalization is dependent on the activity of the DNA-damage response (DDR) kinases tefu/ATM and mei-41/ATR. Associates with heterochromatic regions, e.g. telomeres and chromocenter, in polytene chromosomes. Distribution during mitosis is dynamic. In prophase, protein is found either in the nucleus or it redistributes to the cytoplasm and separating centrosomes, accumulating on the pericentriolar material. At prometaphase, it is detected on the condensed chromosomes. In metaphase, it localizes to either the spindle and presumptive perichromosomal layer or to the condensing chromosomes. At anaphase, protein transitions exclusively to the chromosomes. During telophase, it associates with the spindle remnant or both the chromosomes and the spindle remnant. During cytokinesis, it is observed on the midbody, astral microtubules, the pericentriolar material and cell cortex, yet is not enriched in the nascently forming nuclei.
Sequence:
MPRTPKRVHQEAKEESAQADQPPKKSASEDVEAFTNKGFKNAIAATKAANAFPQGTARALYLSYPGYARVMEDLTQRVVALIGNVLHSKDIKGDIKKRQPEEQFEMVQECNDVLFERITTNLDIKGGLRRNTQQVVEAQVDVMSSSTSIEPAVASPQTQGTPKAGSWNRTTGTPQRSMVSARLFTAKNIVRPQTQFREPVDNSAQNPFVPRLKEKPNSLKPLALLPEYDDAGNVQSYLHPYEFELLKFQPPEEQFQKQKPVLPALMAETELMVVDTVEKLKQALEELRQAPQIAIDVEHHSYRTFMGITCLVQMSTRSKDYIFDTLILRDDMHILNLVLTDPKKLKILHGADLDIEWLQRDLSLYIVNMFDTHRAAKALNMARLSLAYLLKHYLDLDVDKSLQLADWRMRPLPQQLVDYARQDTHFLIYVYGRMTNDLLQQHAEPGLLGSVYQQSTDVCKKRYNKPHIGPESHLDLVRKTKRSFDNRQLYALRGIFEWRDATARSEDESYGYVLPNHMMLQIAESLPREMQGILACCNPIPPLVRQQLHTLHQIVLKARDQPLVKPILEAHSSTQAALPPSTKDFSSKLYCPHDFSQLEEIRDDLPTLLKRNSTTGKLEVPNKEEVAKVDPTLAAPAMALFEKQSKPTQEEEQRWAHLRKESQTMRMPYKRYLAILPLMVQLKADQLARERSELQKRQLCPAAPTVEQNIKLEAHAIGKEDDDMYSVPLKEQLKRKHPQANVKTDPEQQPTASKRPRKDENSQTKPPVKIEPVEKVQQALGESDDEVVEVPIERQATEPPKPSPAQNNRKQKKNQFQRGFKAKNRGNHPQSSSQQVPQHKGTGNFDYKNVDFRQFKGGAQRARGTEIKQQIRGKNRPNNRNNKQFNKLFTFSNVRKEGKK
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MYSLNRLPRSAAFKSSANLLRRNASTTSAGGVNVVGFENKGPAATSSLTVAIKAGSRYETTPGVAHVLKSFAYKATASASALRTAREAELYGGVLSAALTREHLLLSAEFLRGDEEHFLNVLASVLSSSQFYRHELSELVLPVVEAETISSQAIPSTIALDLAHSLAFRRGLGNSLYANKNYPVSIDDVKSFGEAAFAKSNIAVIGTGVSTEALAKAVSNAFGAGTSSGSKLSTPKANYYGGETRVPLDIHAPATATPTMVIAFGTSSPASADLKVLKHLLGGETSVKWTPGASPLAQAADKIPGASAKAFLLPYSDAALFGVVLSAPTSAETKTLAQEVASIVKNAGEFKEEEVKRAVAKATFEDAASTETLSGFVAAAGPAALVGSVPEAQSFSGVSASSISKAAGELLKGKPTVVSIGNISVLPYADELGL
The following text describes a protein:
Function:
Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSTAEIHRQITADEIAHTFEEEATPKVDLGIYAFEDWVALAIFWVMALAVFLQFFTRYVLNDSYAWTEEIATYCLIGVVFIGASMCVRLSRHIQVDLIYRYLPHLVARTLSTVIDLIRIAFFGYAIKLVWVYIQIIGDESMTTINLPKDYVYYAVLAGFVLMFARSVQVALQHLRQGYSILERPGAYDGFEG
The following text describes a protein:
Function:
Substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MGDTYSLVLVAGYLSIFLFIGAIGYFYLSKPRIPSSNVNEQQQQQQQQQQQQQQPQINIEDEPQQRGGIGRMNLRNRRQPIINQRDEDTESSGSDSDNSTNSDNYDDDNGQEGEGEDIGVVAPGIVSNRSGKKIGKKKLEKLKLKDEKRKAREYQEYLREEKKKTDLEKEEALKEKRLEEKENEKLRKEEEERIRIEKERKEDEEYNLLKSQISLQESGITKNEDYDKSLLQLFIKYLKEHKICLLEDIAIEFNIKTNEVIDRIKTLDKQGLISGVIDDRGKFIYITKEEMEAVAKFVNKKGRVNIEQIALESNRLIDFSKKVVDNNDQDPVDTN
The following text describes a protein:
Function:
Fatty acid synthase beta subunit; part of the pki gene cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde. The first step in the pathway is the generation of the decanoyl starter unit by the FAS composed of subunits pkiB and pkiC, which is then transferred directly from the FAS to the SAT domain of the non-reducing polyketide synthase pkiA. PkiA condenses the decanoyyl starter unit with 4 malonyl-CoA units and performs one methylation step to yield 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde.
Sequence:
MALEEVPSVSRDLDHSALRALSSASPSSLPSSCSRSTTSLLFQSKGIEFRLSIPDTFLSLVEPHRNAFLASYSTQGNTQSPLELALSFLYFLLDQKVSPLVLSSVLRAFNLEFLGNRSEIHSLIADLTPIPKQRQRWLGIYYRFLEASDDKRAEIPLSSIFQHARTNEFQLMAVFGGQGECSRTCLNEFAELYSSYEPMLRRLVGVIGPCLYNLSTSDEYSSYYRNQPLDLKAWITDENHVPDLGFVASAPVSVPVIGALSLARYCVTCHITGCNPGLMRSMLRTATGHSQGLLAAIVVAVSHSWDSFYQATEEVIELLFRLGWECHHAAPCSMVPAANYADVDGANGPSYMLSLRGLKRQETEATIDHVNASLPEDKRLYLALINAYDQFVVAGPVASLLRLESHLVEITSKDIDQSRIPFRDRKPYIQHSFLPVSTPFHTPYLTRAAARVKKQFAARPIPTRRLAIPVYHTHTGLDLRKQGGCALSIAIDAIASEPCNWPCAVASYHASHILTFDRGGLAPLIKRVREGCGVRVVQVADLDTRDSEMATMRDLFATKLLPTSTKLQSWGQQFRPGLASGPKIQLETRLNRVLGAPPIMVAGMTPTTVHPDFVAAIMNAGYHAELAGGGYHNASAMEAAIYDLVSSIPKERGITCNLIYANPRSISWQIELLRRLSNGNVRIDGLTIGAGVPSLTVASEYIETLGLRHISFKPGSVAAIRKVVEIAREHPDFPVILQWTGGRGGGHHSFEDFHAPIIATYGIIRQEPNVYLVAGSGFGDSDSVYPYLTGSWSVAMGHPAMPFDGILLGSRMMVAKEAHTSPAVRRIIAATPGVSDSEWEKTYSGPAGGVITVTSEMGEPIHKIATRGVCLWADLDKTVFSLSRRDRLTYLAQHRRSIIQRLNADFAKPWFGCNSDGEAVDLEDMTYLEVLKRLTALMFVPNKQWIDASYIEFTMTIAQRWLQRLQFDSEAAASLTISLLRKAPDRFLAIFADVCPTAEGDLLNPEDISFFLMQCKTPGRKPVNFIPALDDDFEFYFKKDSLWQAEDVDAVLDQDAERVCILHGPIAARYSKSDSEPAGYILDSILNGVVARLRETSTAEMLLPKLERGHTTPASWSTLSLTERDTSEETSDTSITSLSELIENHSFSSGGVDSVPRPSHPLWMRALLEDDVVLQGTLRQKNPFRDLIQSSPNTVVNYNQDSSELMVTAQEPYHISSFMRAVCHDGVMDKRNERIKSFYSLLWFGHDCDTSQSLNGVFYGPDITLTEDLLDEYNATIGPAYSDHRQMVPSTDVLPISMGIIIAWDVISRPLILRQIGGDLLRLVHRSNTFEYYSDTRLRLGDSVSSRSEVQAVYDDDGGRVVIVEAQILRSRVPVMTVTSTFLFRGSKGTTVPAFRRAREQKWTYDVTSEFEESILLSRNWFRPCDPSLTLVGKSMIFDLNSLVKYHDDGNMELHVQGTAMSQTNGQQQKLAIVDFRNTCTGNPVLDFLQRRGKLAEPRTEFKIPGWAGKSTMDIQMPPSNEPYAQLSKDFNPIHTSPIFSSLAGVPGTLCHGMCTSAIAERVLEHLGLGGDRERLRRFEARFTDMVMPLEKLVVEIKHTGMVDGRMCFSILAKRKETDERVLEGDAEVEQPRTAYLFTGQGSQSKGMGMDLYKTSTGQFLLTNKGGLFWTSCKTTQSPLPIRQKYLDITTEVVLPNGKRVQKPVFPGLTPTSTSYTFRHPRGLLYSTQFAQPAILLFEAAAFAELRAKGYVSHGAVYAGHSLGEFGALSALSRSVPTGALVELAFYRGSVMQASVASDNDGGTTYGMVAMNPKRVGTFFTQTTLDRLVSQIAAQSQELLEIVNFNIEGEQYVCSGTIDRPISGGTWPSLSG
The following text describes a protein:
Function:
Involved in viral genome packaging through its interaction with packaging proteins 1 and 2. After proteolytic cleavage by adenovirus protease, L1 52/55k protein is removed from the capsid during viral maturation.
Miscellaneous:
MISCELLANEOUS: All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.
Subcellular Localization:
Host nucleus. Note=Nuclear protein present in empty capsids and assembly intermediates.
Sequence:
MHPVLRQMRPPPQQRQEQEQRQTCRAPSPPPTASGGATSAVDAAADGDYEPPRRRARHYLDLEEGEGLARLGAPSPERYPRVQLKRDTREAYVPRQNLFRDREGEEPEEMRDRKFHAGRELRHGLNRERLLREEDFEPDARTGISPARAHVAAADLVTAYEQTVNQEINFQKSFNNHVRTLVAREEVAIGLMHLWDFVSALEQNPNSKPLMAQLFLIVQHSRDNEAFRDALLNIVEPEGRWLLDLINILQSIVVQERSLSLADKVAAINYSMLSLGKFYARKIYHTPYVPIDKEVKIEGFYMRMALKVLTLSDDLGVYRNERIHKAVSVSRRRELSDRELMHSLQRALAGTGSGDREAESYFDAGADLRWAPSRRALEAAGAGPGLAVAPARAGNVGGVEEYDEDDEYEPEDGEY
The following text describes a protein:
Function:
Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle.
Subcellular Localization:
Cytoplasm, cytosol. Peroxisome matrix. Note=Cycles between the cytosol and the peroxisome matrix. Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol. Cys-10 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzyme UBP15, resetting PEX5 for a subsequent import cycle (By similarity).
Domain:
The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type); The WxxxF/Y motifs mediate interaction with PEX14, promoting association with the PEX13-PEX14 docking complex; The amphipathic helix 1 and 2 (AH1 and AH2, respectively) are required for PEX5 retrotranslocation and recycling. AH2 mediates interaction with lumenal side of the PEX2-PEX10-PEX12 ligase complex, while AH1 is required for extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex.
Sequence:
MSFVGGGSECSVNGNAVAQFNKHTQQDRSLQQQVANQHGNVAQNQGFKKDNLMNVRDRANLDQFMNNGAPQNSFQFQPMRHELNTIQNQPNAIHQQQSNWSQDFVAQSPSAQITTPIAKTGSPVNAQWASEFSQAPATQQHNQRPGQFGPRLGGYRPMMGMSMAYQSQPQQQQQQQHNQEPQVDWENQFKEIEELTNKAEEVEEIQREQSPEIVVDDKYQATFQEVWDSLNSESFENDFINQQYEDFKRTQKDGFPADMNQWEKDFAKYASTRAHFGDYQFEDKQSNQFLDLPKDQDPYEIGLQLMENGAKLSEAALAFEAAIQRDENHVDAWLKLGEVQTQNEKEIAGISALEKCLELHPENSEALMNLAISYINEGYDNAAFATLERWISTKYPQIVEKARQENPTITDEDRFSLNKRVTELFLNAAQLSPNQASMDADVQMGLGVLFYANEEFDKTIDCFKAALSIRPDDAILWNRLGASLANSNRSEEAVDAYFKALQLKPTFVRARYNLGVSCINIGCYKEAAEHLLSGLSMHQVEGVDTVSTLNHNQSTSLTETLKRAFIAMERRDLLELVKPNMDLNQFRGEFSF
The following text describes a protein:
Function:
Ribosome-binding protein involved in ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation. Acts via its association with eiF5a (EIF5A and EIF5A2) at the polypeptide exit tunnel of the ribosome, preventing mRNA translation. Involved in ribosome hibernation in the mature oocyte by preventing mRNA translation, leading to ribosome inactivation. Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also acts as a negative regulator of autophagy. Involved in mediating interferon-gamma-induced cell death (By similarity).
Sequence:
MSSPPEGKLETKAGHPPAVKVAGIRIVQKHPHTGDGKEKKDKDDQEWESTSPPKPTVYISGVIARGDKDFPPAAAQVAHQKPHASMDKHVSPRTQHIQQPRK
The following text describes a protein:
Function:
Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Subcellular Localization:
Cell membrane.
Sequence:
MLYNLAIVIYDLLVHFAAPFSRKPRKMMKGHWVVYELLRQQVEKGEQYIWFHAASLGEFEQGRPLIEMIREKYPDYKILLTFFSPSGYEVRKHYRGADIVCYLPFDKPRNVKKFLDIANPCMAFFIKYEFWKNYLDELHKRRIPVYSVSSIFRRDQIFFKWYGGTYRNVLKDFDHLFVQNEASKRYLSKIGICRVTVVGDTRFDRVLQIREEAKDLPLVKMFKGDNAFTFVAGSSWGPDEDLFLEYFNTHPEMKLIIAPHVIDENHLVEIISKLKRPYVRYTRADEKNVLKVDCLIIDCFGLLSSIYRYGEVAYIGGGFGVGIHNTLEAAVYGIPVIFGPKYQKFMEAIRLLEAKGAYSIKDYHELKTLLDRFQADDVFMRETGANAGYYVTSNAGATEKIMHMINF
The following text describes a protein:
Function:
Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage.
Domain:
Residues 239-252 form a flexible loop which appears to affect the polymerase fidelity.
Sequence:
MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEIKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVHFITDTLSKGETKFMGVCQLPSEKDGKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYREPKDRSE
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Probably binds BUB3 as part of transport cargo. Required for the efficient progression through mitosis.
Subcellular Localization:
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton. Nucleus.
Sequence:
TGRGLPGGQCAAAELDLRVAPPSGESAPPWRSTIATATRYRPSAACERPLPPPALVRFLGRVVSRRLVARRVGVGFNADEAHNIIKECIDGVLGGEDYNQNNINQWTASIVEQSLAHLVKLGKAYKYIVTCAVVQRSAYGFHTASSCFWDTTSDGTCTVRWENRTMNCIVNVFAIAIVL
The following text describes a protein:
Function:
Plays an important role in several reproductive functions, including Muellerian duct regression during male fetal sexua,l differentiation and in the adult plays a role in Leydig cell differentiation and function. In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles. Binds to its sole type II receptor, AMHR2 that recruits type I receptors ACVR1 and BMPR1A which subsequently activates the Smad pathway (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MQGPHLSPLVLLLATMGAVLQPEAVENLATNTRGLIFLEDELWPPSSPPEPLCLVTVRGEGNTSRASLRVVGGLNSYEYAFLEAVQESRWGPQDLATFGVCSTDSQATLPALQRLGAWLGETGEQQLLVLHLAEVIWEPELLLKFQEPPPGGASRWEQALLVLYPGPGPQVTVTGTGLRGTQNLCPTRDTRYLVLTVDFPAGAWSGSGLILTLQPSREGATLSIDQLQAFLFGSDSRCFTRMTPTLVVLPPAEPSPQPAHGQLDTMPFPQPGLSLEPEALPHSADPFLETLTRLVRALRGPLTQASNTQLALDPGALASFPQGLVNLSDPAALGRLLDWEEPLLLLLSPAAATEREPMPLHGPASAPWAAGLQRRVAVELQAAASELRDLPGLPPTAPPLLARLLALCPNDSRSSGDPLRALLLLKALQGLRAEWHGREGRGRTGRSAGTGTDGPCALRELSVDLRAERSVLIPETYQANNCQGACAWPQSDRNPRYGNHVVLLLKMQARGAALGRLPCCVPTAYAGKLLISLSEERISAHHVPNMVATECGCV