lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Essential protein required for siroheme biosynthesis. Catalyzes the two successive C-2 and C-7 methylation reactions involved in the conversion of uroporphyrinogen III to precorrin-2 via the intermediate formation of precorrin-1. It is a step in the biosynthesis of siroheme. Promotes nitrogen and sulfur assimilation as well as photosynthesis efficiency by triggering chlorophyll, nitrite reductase (NiR) and sulfite reductase (SiR) biosynthesis.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MALVQRIPISSSSIRNWQQARTNLTPICCLHYNTASSSSSPFTEKHSVERYQRDQWLYKAVEPTPPSTPSPSPFEDEVFVRENDIASQLPELKKLLAVLKEKRVKGCKGGDCGPGDVYLVGTGPGDPELLTLKAVRVIQSADLLLYDRLVSNDVLELVAPDARLLYVGKTAGYHSRTQEEIHELLLNFAEAGATVVRLKGGDPLVFGRGGEEMDFLQQQGIRVQVIPGITAASGIAAELGIPLTHRGVATSVRFLTGHSRKGGTDPLFVAENAADPDTTLVVYMGLGTLPSLAQKLMDHGLPSDTPAVAVERGTTPLQRTVFAELKDFATEIQSAGLVSPTLIIIGKVVELSPLWPHCTKESSCLVETR
The following text describes a protein:
Function:
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular Localization:
Mitochondrion.
Sequence:
MTTASGAVVGPHAAAMSSTPVLPSVGSGMPYILSSCNEAVSESRLHELAAEEEERRVTRQKKLFEDLLVFEGGAVADHESLGTELIMRDFIHFALYHKKWGYYPKLYRKYRQLMTTGYFDPIPFGSLRNQQDYERYVGKIHDSTPSCVTPTQLFQPHYGWVIAEYLVTMMRAKFDPRDPLVVYDIGAGSGALAVSVLDYLSEHFPSVYEQCEYHVVEINPQLVQVLRNRLIMHYHHVKIHNISILNWREVERRRCVVFGVELLSGMPHDCVVLSADGVCNEQWFHFQQHDNLSTAHERYFSVKDPVILRYLRYARWMQEESFHSLKVLCLTGGRDNIDPPPFTSIEPNMYDPLRVVITKMMWMHSPFRTLWLPTVSMLFLETCATYFPRHHLFLVDWGSVRQGLPGVNGPVLQSKTRIAKDIYLRRPADSLHGNAGMIDICFPTDFDLLKAVYRNICGAYKEVSSMSHPQFWKTFGGDKTSIFTTRSGFNPLLEDFDPLHVFVTHHPSEM
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MARPRPRPQLLQETLIIDSNGNSRLDAKSELFYCPMCTTTAPIIHKSSFGSCGHAFCNSCVATYIAVRQRENAALPVECPDCEHEDGLLPMPMVRHEIDPTTVTDGNEDSPAVDGNGRRFYCAKCMHVVPCACIRRSFTSCAHDFCSSCVSRRLRGRRGDGKHFYCTKCMHVVPCACIRPSFTSCAHDFCSSCVARPTSQRQGLRRRAGKMPQHQPADLVPVDMLLLTEGNGDSPVYGHGELFDCAICMETVPGTLKFSVNSCGHAFCSSCVTQYVVLKLDDKVALIECPHPGCEGGTIEPESCHGIIPTDLHDKWGLLLCELAVGAKRIYCPYLECSALLLTDGEAGAAAIAEAECPHCHRLFCARCAVPWHDGFGCEEFQKLGQDERGREDLLLRRLVGMEGWQRCPKCQMFVEKSEGCNYIKCRCGYSFCYRCASELSAQNHYCNKCMR
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; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Miscellaneous:
MISCELLANEOUS: In plastids the F-type ATPase is also known as CF(1)CF(0).
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
Sequence:
MKNLTDSFVYLGHWPSAGSFGFNTDILATNPINLSVVFGVLIFFGKGVLNDLLDNRKQRILNTIRNSEELREGAIQQLENARARLRNVETEADKFRVNGYSEIEREKLNLINSTYKTLKQLENYKNETILFEQQRTINQVRERVFQQALQGAIGTLNSCLSNELHLRTINANIGMFGTMKEITD
The following text describes a protein:
Function:
FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Bacterial flagellum basal body.
Sequence:
MSENRLAAKLTKVDKAAILLLSLGETDAAQVLRHMGPKEVQRVGVAMASMRNVHREQVEQVMGEFVEVVGDQTSLGVGADGYIRKMLTQALGEDKANNLIDRILLGGSTSGLDSLKWMEPRAVADVIRYEHPQIQAIVVAYLDPDQAAEVLSHFDHKVRLDIVLRVSSLNTVQPSALKELNLILEKQFAGNSNATRTTMGGVKRAADIMNYLDSSIEGQLMDSIREVDEDLSGQIEDLMFVFDNLADVDDRGIQALLREVSSDVLVLALKGSDEAIREKVFKNMSKRAAELLRDDLEAKGPVRVSEVEGAQKEILTIARRMAESGDIVLGGKGGEEMI
The following text describes a protein:
Function:
Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MPKSKRDRKVSLTRTPRKGLEAKQALIAELRRCVDTYKHIFIFSVANMRNNKLKDVRNAWKHSRIFFGKNKVMMVALGREPSSEYRENLHQVSKHLRGEVGLLFTNRTKEEVDEPFYIYDKAHSSALSHSALYQNMPPAQSSVPRAALPAALSAHLPQVVLQLQGGGLCTSGEQGDVHRQPGHGALGAVPPLHGASAAAAGIANSFKERSGDAAFRLRSLQRRGHSDPRASTCPETLWLRDGRV
The following text describes a protein:
Function:
Transcription factor. Binds to a sequence motif, 5'-TTATTGGCTTCGTTAA-3', which may be involved in AIY interneuron function, in the regulatory elements of target genes; binding is more efficient, in vitro, together with LIM/homeobox protein ttx-3. Required for larval development and for cell fate specification and migration of CAN neurons. Required for generation, or placement, and differentiation of the ALA neuron, and may play a role in ALA axon migration. Involved in development and function of the AIY interneurons, acting by regulating expression of LIM/homeobox protein ttx-3. Also acts in an autoregulatory feedback loop to maintain its own expression. Modulates lifespan, perhaps acting in the AIY interneurons. Plays a role in fertility and egg-laying behavior.
Subcellular Localization:
Nucleus.
Sequence:
MAVDEMQLAASMQMSNQMSNSQRMSFAIHEILGIQGNAYLSHGYCPQGTFLSNQPNFMDIGSCGVSGFDRQLCGTDSIGNAPAPLMYRMPISTSEVITSEPQTHVSSSSILSSATTSNSSGGGSSGGGGKASKRKKRRHRTIFTQYQIDELEKAFQDSHYPDIYAREVLAGKTELQEDRIQVWFQNRRAKWRKTEKTWGKSTIMAEYGLYGAMVRHSLPLPETITKSAEAADPQQSAAPWLLGMHKKSMEAAAHLESVEKCDMSDSDDDDRPVTPPVQRQVKNEYKPRIIEHVQQQAPQHQSSLNFDTSLVVSSSLSQLHFQDSQMIPNNNASLKLYHDYNNPM
The following text describes a protein:
Function:
Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage. Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR. It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MEDDRDTLRILVATDCHLGYMEKDEIRRFDSFEAFEEICSLAKQKEVDFVLLGGDLFHENKPSRSTLVKTIEILRRYCLNDLPVKFQVVSDQTVNFPNRFGHVNYEDPHFNVGLPVFTIHGNHDDPAGVDNLSAIDILSACNLVNYFGKMDLGGSGVGQIAVHPVLVKKGTTTVALYGLGNIRDERLNRMFQTPHSVQWMRPESQEGLSVSDWFNILVLHQNRIKTNPKSAINEHFLPRFLDFVVWGHEHECLIDPQEVPGMGFHITQPGSSVATSLIDGEAKPKHVLLLEIKGNQYRPNKIPLMTVRPFEYAEVVLKDEADVDPNDQASVLEHLDKIVRNLIEKSSQPTASRSEAKLPLVRIKVDYSGFSTINPQRFGQKYVGKVANPQDILIFSKAAKKRQTTTGENIDESEKLRPEELNQQTIEALVAENNLKMEILPVDDLDIALHDFVSKDDKTAFYACLQRNLDETRKKLNSEAEKFKIEEEDIIVKVGECMQERVKEISLHSKGDTGLASSTQNLDSTRGKSVAAESSLNTFSDDEDTRELLLGTRSTRSTAGFTRPSKDATGAARGGASKRGRGKGSLKQTTLSFSQSRSSAAIRSEEVDSSSDEDAANEANEVVENSDPEDSFPQSGRKRPAPRGRGRARGTTTAKRGRKADTGSMPSMVMSKDDDSDEDDKPKKPPPRVTRNYGAVKRR
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:
MNTHDLVAFVAVVETGSIVAASARLNLTQPGVTRRIQNLEEMLGAKLLDRLSKPLKPTAAGHEAYEQGRRLLRMLDDLKSGVANDGVVRGEFRLGLTPFLSEAGLTGPLDAVRAEFPALAVRVVSGWSPNQLERVCRNELDAAAICLPDGAVPPSDLAADDLGAQPVVFVVARDMKIPRIVDLERLSQLSWVINQDGCGFRDSLKRKFDAEHLPFSIAVEALDSELRLSLVSRGLGVGLVTPIALKRSAFRDKLKPVVARDFKPAVRAWIVHRAPAGRLERPIKLFRDGLDRELQAMIGS
The following text describes a protein:
Function:
Metal transporter.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MIIKILFLFFLLCIQNVRIDGKLDVKPTVSGVRVESDVGAPGFLGYSDAGEIMVEADSIVDIVIFGHGLEDVDMVAFTDSVCVTSEFNISESTFYIHKDMKIVFKYSFVAWPTPWRICLKSESHGLIQIDDDRTWIQAVEKTHETYMPIWMQSAILCLLFSISALCSGLTLGLMALTPQELSILMKSGTPSEKKYASAIYPLRIHGNRLLCTVIIMNVIVNTGIALLFDDMAEGLVAFVASTVGIVIFGEILPQSICVKYGLAVGANTIFITKFFMIILFPLTWPLGKILDKYAGVDIDVVNRSRMIEMLKMNMENEACDIDLSTLKIAIGAMELIKKSVKDVMTDIDDVFMLSEDQVLNAETMTKISDSGYTRIPVYEGNNRNKVKNLLYVSDLALIGKDNNITVKAVAGFNKRRLRIVDEHMPVTALMDEFKMGDYHLAMVAKAHDVKKHHHGKFVDDKMDNFIMKSMKLVEATMLPEAPEEHAITLVGLITLEDITEELLQAEITDETDCYITDDAQKKRRTNTSKKSVAELFCSEKKSERLSLHMLEMTEKWLLEKTPLFGEMNPKAFENLIQRNIREVRIYQRYQHNYLFKVLIVPPKNSTSPGTLNLFEAGEMSKRFVLILEGKASIKFNEKDLLFECGPWTCFGEAILNKMELCIKDGKEPPTGFFFVPDYTLTVSGPCRFLQISTSSLLHSLRITQFVKEIRTPKISVTSDDDPGLVSRKVSIMGNSPTEARKRSSTSVMTNLALPTARLAAKIASVEELKPLIE
The following text describes a protein:
Function:
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Sequence:
MSYLDTQRFPYELEFPIDDSDMEDPRRYQNGGFHPILLGDRLGPRSNGRFRVVNKLGAGGYGTVWLCQDTHHKPSTVTKWRVVKVIAAGKSTPDCPDLKILGHFRDVDRSFLDAFGICLPIEHFWLTGPNGRHLALVFPWHGCTLQIVPDYYSFHTSLIKDMAFELVECLRFLHSRGLCHGDLRPRNVLLRLLPGADEMPESELWEVLPEPQRVRIIRVCDDKFFDELPSADRPNNIPEYIVAPVELPFVSGLYTRHPVLIDLGVSFPSQQPPKEGTTGIPISFAAPESVFRTLYNTSRPLLGPASDIWSLACTLAHLRVSCNPFQSDDVNLSSVARSWEETLSPLPEPYRSKYREIKNIETPLDEVWGDKPDSQLDPVVDPKAVYEGRAERRLARCGTRNWFKERMMRVRRLEIFPEAAREMLEEEKEADPKMKEVLPFSEDMEVVNIYEQGMQVKMDKEEIELFWDLLEGCWRWKPEERMSIEEVVRHPWFEGRQPREIPKPGPWRVVVRVLWSFWDCVRPFTSGWFDRGRVEEWSLIVTKKLPPNVVTAYKTIGKFFFALFGSLTPSALRKKLIWRPKSFPFISPPGTPSQAPADSTDWETW
The following text describes a protein:
Function:
Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5 and CXCL8.
Subcellular Localization:
Secreted.
Sequence:
MEAKTFAFLEIAMFIALGIQTFVAVTDAAGKDDEHFSVDYCGMNCTQQEDGSWTACSGRNGECRCYHESGKRSGLCLSTTYIDFSEYGNLSDSDIAAASPRLSMKESH
The following text describes a protein:
Function:
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Subcellular Localization:
Cytoplasm.
Sequence:
MKMREINMILYIHIPFCENKCGYCAFNSYENKHGLKEEYTQALCLDLKHALSQTDEPIESVFIGGGTPNTLSVKAFERIFESIYQHASLSLDCEITTEANPELITKAWCQGLKGLGINRLSLGVQSFREDKLLFLERQHSKNIAPAIETILKSGIENISIDLIYNTPLDNENSLKEELKLAKELPINHLSAYALSVEKNTNLEKNAKKPSCAHFDNVVREILEGFSFKQYEVSNYARNYQVKHNLAYWGAKDYLGCGAGAVGCVANERFFAKKLIENYIKDPLQRQVETLNKQDKRLEKLFLGLRCVLGVELSFLDENKVKFLIEENKAFIKNNRLIASDFFMADEMALWLL
The following text describes a protein:
Function:
Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MLNSIHRSFHLTSRHQIVLRLCSPSASRTIMSSSPHSPIPKTHTASLDSLNDYEEQFPPLTGGSKTKKFYLGSTNPSTPCQSSQLQNWTSGKDALSLQRNLGCKNRRRRRASRFLHEESNGTTFEVGAGIGSPTSMVHFDSTNPSSSSKSSQSQNLKIRKVRNHRNSGFKSRDQSPQRIKDPPPFDICSSVLERNDTSIKDWILADETNRETVEVSNKHKVIRPGMVLLKDFLTPDIQVDIVKTCRELGVKPTGFYQPGYSVGSKLHLQMMCLGRNWDPQTKYRKNTDIDSKAPEIPVTFNVLVEKAIREAHALIDRESGTEDAERILPVMSPDICIVNFYSETGRLGLHQDRDESEESIARGLPIVSFSIGDSAEFLYGEKRDVEEAQGVILESGDVLIFGGESRMIFHGVKSIIPNSAPMSLLNESKLRTGRLNLTFRHF
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely 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. Does not bind tRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MTIIINVRERIEEWKIRIAAGFIREGKLVAFPTETVYGLGANALDENAVKRIFEAKGRPADNPLIIHIASFEQLEVLAKEIPEEAEMLAKRFWPGPLTLVLPKSEVVPRVITGGLDTVAVRMPAHEIALKLIELSERPIAAPSANISGKPSPTSAHHVAEDFYGKIECIIDGGETRIGVESTVIDLTEWPPVLLRPGGLPLEEIEKVIGEIRIHPAVYGKSVDTAKAPGMKYRHYAPSAEVIVVEGPRDKVRRKIEELIAKFKEEGKKVGVIGSGSYDADEVFYLGDTVEEIARNLFKALRHMDRTGVDVILAEGVEEKGLGLAVMNRLRKASGYRIIKV
The following text describes a protein:
Function:
Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.
Sequence:
MDQADIPALLSRLASDEDAARKMAVFKLQSSINDPAFADVFIASGGLVVLRRLIMTTGGNTLAYSLQSLSRLLEVDMGWDIFEGPNAGELVERVVELIVTNPLVNILRGAMSILVGLVSHSQSTARGGTPRTPGTFGFRALKPAVAVYPQFFELVIMQLQSADHALCANALMLINALIRDAVSNDSGPTLLVSSAKGTVPPGEEWSKFIKKLQDLGLIKAVYNLMQSSSLQDLAHSLLEFQTLTKILLQKWRAVRVDLERPEHRRALKGLHLASAPDRRQTNGGLTTLSPTGRPSTAATVVASEEGGKETGGEPAAGRKSSRRHNPEKWRRLGFETESPASEFEVAGFLGMMDLTDYVRKNEDGFQKLLLEQSSRPLNERCPVARASLAVTMILYEHFEIEKCDLDDIRNGGYYQLIDGGGKAHDKLFRPLLLQWSRLHTAGLHAFFRMWKATGATRYDFDKVAELVRILIDQVVGQASRNKDVLEVEDELHEYDSGRLRELQMDLLELSFEDQWGSHLFQVREELKHEALQFVKEQRIRCLLQGSWFSKPQPHRSDHSRSESLKPGQEKGSRLYQPWRFAKLSHNRRYLHYADFAEQTAHDPGLEALTEKIDLLSTSSVVSNVSNADDAAAAGENGNQASSSLTSLTKDANSASATAKSTTKITIYSLSENVSPELASLATAGKTKEQPILTLHPLNHSLASEWLDGLLMLLNQAPITAETNKLVTLVSEYGLKIRLLNVRAEAVDNGPVPGAGQVPSREGLDEDYYYEI
The following text describes a protein:
Function:
Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding; The box 1 motif is required for JAK interaction and/or activation; Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Sequence:
MGAPSSLLFSTAHWRTVPFLLAFWVLLSTGTAEDPTMTPEFLRHISEKIPEEYQNPHCFTRDLNDFICFWEGERRKNASFSYSEDDQIKWCQLRTEVASNNTWWYICEFPVTDVVLFAGITISAYPCHKCQTAREIYINELVLLNPPLNVTVKEKQDPRGLLISWKPPHFQKNHDINNEIKYQVNYSTPGADMQTVEVEAGNTEIFLTDIVPAAYTVTVRCKADGVSYNGYWSDWTAPITIATIIDLRLLLLLSIAIFVALIAGVGVYIFMRHGMYLKHKVWPQVPTPENNFQGLFTTHKGNFKLWLGQADAYLLWISRHVFQEDPSSTLEVLSELPPAALPQSFNPNPLKDSYVVLDENRMPCSLEWLEAQRHKTVIVGAESMDSRLQTVNKDVVLEDTSKGQIAVKANNRVHSLEGDGSQGEAFREDEYVEAPRMEHERHRVSRENSVSSDGKQSIPSSFEYTELQTCEGLLSPKPRPVPPRMPLKYAYLDMSSSGEHSPPPSPNFYQNSPITNFLAPIYSQS
The following text describes a protein:
Function:
Anchors the radial spoke 1 (RS1) complex to the A microtubule of outer doublet microtubules in axonemes. The triple radial spokes (RS1, RS2 and RS3) are required to modulate beating of the sperm flagellum. May play a role in inhibiting signaling via MAPK1/ERK2 and MAPK3/ERK1. Additionally, may play a role in the functioning of cilia. Not required for the functioning of tracheal or ependymal cilia.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. Cell projection, cilium. Note=Localizes to the axoneme of sperm cells and the cilia of tracheal epithelial cells.
Sequence:
MSDPEEERVADSTAHYEEAGKVISIPRPSDEAEGSDVMPEQDDEVQELTTESEENVERHSEFSLSTPKSDDSKPREEVTSLGSASGSQDQDYRLLDYQKGEDDELLFLHKIKAIKETLQTSVRESIATVKIVLIPAGQEIIMPFRVDAPFRFLKEHFAHLLHIPHYVLQITHEGIIVGNNESLIQYGIKPQEIVQVEVFSTLPDQYPVRRIEGLSEGSQIITVTIQTSIDRYEEVAVEIIKSDFHKPFLGGFRHKITGLEYHNAGTQTVPRKIPEKDNLFCRDTQTVFQKKKLQQTTNTTSTQMTKIGVYVSNMTDKLLKPGNYFSAAEYHARRLHAVIVIQTSYRRWHAKRYVESLRKQKKLRLEWEEEQELLKIQEKEEWIRMDYYRRHNPKTTEDFELLYNALELWRQEEVEQICHYSSEAERKAALCELLEKETQMIASIGRHRSAARMERQDAAIQAFLDKCSAPNVWRRGDGKTIEMDTQFTIRARELQSIYKCILLKDLSQDERLDILLTLKHTVKEHECKLTQEILELIDREVDLMMRGVKPHNLEGLRKRITTLFIHYIKTPLFNPEVAKYLKVPQDPLKFYDTIYFCHSCQNYLPSVEFSVSPTSHRVYRCRHCINLENETQRRESFLKYKCLLQRLYYSEADYGDNSQIAFLMQLQDIKYLTENIWASQSALSAWDDLNDLVMVRWDKHVEWSPWNCILLTKDESTAHLRLPSIEKGYGHHFVHKIKHKHILAKNYFSQIPTLASLILNDDEVEDIRSKHSTKSPPKIIITRRIQPH
The following text describes a protein:
Function:
Microprotein involved in mitochondrial respiratory chain complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV (mitochondrial cytochrome c oxidase complex) assembly (By similarity). Required for the formation of mitochondrial supercomplexes (SCs) (By similarity). Also required for the activation of the NLRP3 inflammasome (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion outer membrane; Single-pass membrane protein. Mitochondrion intermembrane space.
Sequence:
MMQFILGFTLGNVVGMYLAQNYEVPNISKKIEAFKKDVEAKKKPPE
The following text describes a protein:
Function:
Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is possibly due to local fusion between the inner and outer membrane performed by the spanin complex (By similarity).
Subcellular Localization:
Host cell outer membrane; Lipid-anchor; Periplasmic side.
Sequence:
MIKLSAVILSIGLLVGCSTKPLEVKKETVHPNWPVQIKSYDEAKLSWQVKVIDGKAWVGMPFEDSQEFRIWLNDVKRYVHDQKTMXCYYRQELKEDKCK
The following text describes a protein:
Function:
Acts as a component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. In the endosomes, drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association with the CCC complex and cooperation with the WASH complex on early endosomes. Seems not to be required for CCC complex stability.
Subcellular Localization:
Membrane; Single-pass membrane protein. Endosome. Note=Endosome location is dependent of the association with the CCC and WASH complexes.
Sequence:
MAVFPWHSRNRNYKAELASCRLETVPLECGDYHPLKPITVTESKTKKVSRKGSTSSTSSSSSSSVIDPLSSVLDGTDPLSMFAATSDPAATGTVTDSSRKKRDKDENSFVGPDFEPWANKRVEILARYTTTEKLSINLFMGSEKGRGGAAASAMSEKVRTRLEELDDFEEGSQKELLNLTQQDYVNRIEELNQSLKDAWASDQKVKALKIVIQCSKLLSDTSVIQFYPSKFVLITDILDTFGKLVYERISSMCVDSRSALPDHFSPENVNDTAKETCLNWFFKIASIRELIPRFYVEASILKCNKFLSKTGISECLPRLTCMIRGIGDPLVSVYARAYLCRVGIEVAPHLKESLNKNFFDFLLTFKQIHGDTVQNQLVAQGVELLSYLPLYSPAMGWIFQCVSYHAPEALLTEMMERCKKLGNNALLLNSVMSAFRAEFVATRSMDFIGMIKECDESGFPKHLLFRSLGLNLALADPPENDRLQILNEAWKVITKLKSPQDYINCAEVWVEYTCRHFTKREVNTVLADVIKHMTPDRAFEDSYPQLQSIIQKVIAHFHDFSVLFSVEKFLPFLDMFQKESVRVEVCKCIMEAFIKHQQEPTKDPVILNALLHICKTMHDSVNALTLEDEKRTLAHLINGFIKMVSFGRDFEQQLSFYVESRSMFCNLEPVLVQLIHSVNRLAMETRKVMKGNHSRKTAAFVRACVAYCFITIPSLVGIFTRLNLYLHSGQVALANQCLSQADAFFKAAIGLVPEVPKTISIDGKLRPSEPFLLEFLCNFFSTLLIVPDHPEHGVLFLVRELLNVIQDYTWEDSSDDKIRIYTSVLHLLSAMSQDTYLYHIDKVDSNDSLYGGDSKFLAENSKLCEAVMAQILEHLKTLAKDEALKRQSLLGLSFFNSILAHGDLRNNKLNQLSVNLWHLAQRHGCADTRTMVKTLDYIKKRSKQPDMNHLSELALRLPLQTRT
The following text describes a protein:
Function:
May be involved in protection from oxidative damage.
Subcellular Localization:
Mitochondrion.
Sequence:
MEPLQHTPRLKKKSQSVDIGSQGFPARLIPSLSLNRSSPPAAKTNTSEVQENNTTNAQRRVPRCSDLKRGYTIDTGQKKTPEKKDGRRMSFQRPKGTIEYSVESRDTLNNIALKFDTTPNELVQLNKLFSRNVVPGQVLYVPDPEYVSSAGSSPSFSPSSPLSPTSSEADLEKVTTDSNGPPRSDAPAPPVLSALRSSRVVSSTSEEEEALTEKFLKINCKYITDGKGVVSGVLLVTPNNIMFDPHRTDPLVLEKGCEEYGIMCPLEEVQSAAVYKEIIDSKIRDSVTDLEAVFSSFSHQTDQRYDSASTAPRSTEGSFSEDVFTESELSPIREEHQSTEELQQEDKSSGASSQSVKTLLQEPQSHTEEKDNDGEPAGDTAKPIQDEPTSRDHQQTPHCQTEGEPAAQESSAEGVKLTRDGTRDSETDVEELRKMCKTHTMQQAKEQRESVQQAQRESEQQTTEQSQRLSSAEGPVVSKERQKSHKFLCLRVGKAMKKTFVSNASASMQQYAQRDRKHEYWFAVPQERSDHLYVFFIQWSPDVFGDGLGSISRDPGFIVVKKIEESEANEEQQPEENSEKEWEITTKEDVNSKHGTSITASLEPETFKPNLNEPSDLLEAEQIEKLAKHLPPRTIGYPWNLAFSTSKHGMSIKTLYRAMQDQDSPMLLVIKDSDGQIFGALASEPFKVSEGFYGTGETFLFTFYPEFEAYKWTGDNLFFIKGDMDSLAFGGGSGEFGLWLDGDLYHGRNHSCKTFGNPMLSMKEDFFVQDIEIWSFE
The following text describes a protein:
Function:
Functions probably as a transcriptional factor that activates genes involved in secondary cell wall biosynthesis. May play a role in both transcriptional and post-transcriptional regulation. Binds to ssDNA, dsDNA, and ribohomopolymers in vitro. Maybe involved in post-transcriptional regulation of its target genes. Targets RNA of a polygalacturonase, a well-known cell wall modifying gene. Functions redudantly with C3H15 to regulate secondary cell wall formation. C3H14 and C3H15 have overlapping roles in the regulation of secondary cell wall formation and anther development. C3H14 may contribute more to secondary cell wall thickening while C3H15 could be more important in anther development. May regulate at both the transcriptional and post-transcriptional levels the expression of many genes involved in various biological processes, particularly those associated with cell wall metabolism and pollen development.
Miscellaneous:
MISCELLANEOUS: Plants overexpressing C3H14 exhibit small and slightly curled leaves, and retarded stem elongations due to cell elongation defect and ectopic secondary cell wall formation. Plants overexpressing C3H14 are sterile due to stamen elongation defect, despite normal overall flower morphology. Overexpression of C3H14 results in secondary cell wall thickening in fibers and vessels.
Sequence:
MEKLAASTVTDLACVTAINSSPPPLSPISEQSFNNKHQEEFAASFASLYNSIFSPESLSPSPPSSSSPPSRVDTTTEHRLLQAKLILEYDELNEHYELCLNRLQSLMTELDSLRHENDSLRFENSDLLKLIRISTSSSSSVSPPAPIHNRQFRHQISDSRSAKRNNQERNSLPKSISVRSQGYLKINHGFEASDLQTSQLSSNSVSSSQKVCVVQTKGEREALELEVYRQGMMKTELCNKWQETGACCYGDNCQFAHGIDELRPVIRHPRYKTEVCRMMVTGAMCPYGHRCHFRHSLTDQERMMMMMLTR
The following text describes a protein:
Function:
Cell surface proteoglycan.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MARGAGAGAGARGPPGPPKPPPTPRPPPLLLLLMLLLLLGAGRAAGAQRWRYESLERPVDLEGSGDDDSFPDDDLDDLYSGSGSGFFEQESGIETGTRMTTDTAASAPSTTPSGLPAASPVAPGATPSTEPPARSATPEPPEPSAGTRTQLRDTEAPGLPGQEGPTTATTPTVAPMASTTLTGAPPVATTPTTTPTAATTPTVTPTTATTSTATPPAAASPSTGAPTAQPTSAQWLPPLLATTASSAHPTPPATPAPTPETEPTAPAPVSTAVVHPRAEPSPEAGSRATDLPESQPGTSLASTRRPPERAQTSPPQTPPPTAPPSTTAAPAGEAPVSGDFEVPEETAAPELSNEVEPAGAGPTPAGGQGRGGERGPPDLLDNSIDPGSSAAQLPQRSILERKEVLIAVIVGGVVGALFAAFLVMLLVYRMKKKDEGSYTLEEPKPASVTYQKPDKQEEFYA
The following text describes a protein:
Function:
Involved in regulation of gene expression for sexual development. Binds and activates CRE sites (cAMP-response elements, also known as M26 meiotic recombination hotspots).
Subcellular Localization:
Nucleus.
Sequence:
MTAKKKEVDDEKRRRILERNRIAASKFRQKKKEWIKELEQTANAAFEQSKRLQLLLSQLQQEAFRLKSQLLAHQGCQCSVKIRSVLTDFQTAHNALHSQHMAYRPVQPPPGDNMLESVVSVSPTQMHPSLQGLPPNQHPQMPPSSQQPNSDDVQQHMFSAAGLPRSLGGPI