lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Has weak lytic activity toward S.aureus cells. Full-length protein has no activity, but fusion of the Peptidase C51 domain to the lysostaphin SH3 cell wall binding domain yields an active chimeric enzyme, suggesting that PH may be functional.
Sequence:
MLITKNQAEKWFDNSLGKQFNPDLFYGFQCYDYANMFFMIATGERLQGLYAYNIPFDNKARIEKYGQIIKNYDSFLPQKLDIVVFPSKYGGGAGHVEIVESANLNTFTSFGQNWNGKGWTNGVAQPGWGPETVTRHVHYYDDPMYFIRLNFPDKVSVGDKAKSVIKQATAKKQAVIKPKKIMLVAGHGYNDPGAVGNGTNERDFIRKYITPNIAKYLRHAGHEVALYGGSSQSQDMYQDTAYGVNVGNNKDYGLYWVKSHGYDIVLEIHLDAAGESASGGHVIISSQFNADTIDKSIQDVIKNNLGQIRGVTPRNDLLNVNVSAEININYRLSELGFITNKNDMDWIKKNYDLYSKLIAGAIHGKPIGGLVAGNVKTSAKNQKNPPVPAGYTLDKNNVPYKKETGYYTVANVKGNNVRDGYSTNSRITGVLPNNATIKYDGAYCINGYRWITYIANSGQRRYIATGEVDKAGNRISSFGKFSTI
The following text describes a protein:
Function:
Induces activation of MAPK14/p38 cascade, when overexpressed. Induces apoptosis, when overexpressed.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MSEPQPDLEPPQHGLYMLFLLVLVFFLMGLVGFMICHVLKKKGYRCRTSRGSEPDDAQLQPPEDDDMNEDTVERIVRCIIQNEANAEALKEMLGDSEGEGTVQLSSVDATSSLQDGAPSHHHTVHLGSAAPCLHCSRSKRPPLVRQGRSKEGKSRPRTGETTVFSVGRFRVTHIEKRYGLHEHRDGSPTDRSWGSGGGQDPGGGQGSGGGQPKAGMPAMERLPPERPQPQVLASPPVQNGGLRDSSLTPRALEGNPRASAEPTLRAGGRGPSPGLPTQEANGQPSKPDTSDHQVSLPQGAGSM
The following text describes a protein:
Function:
Putative sodium-dependent transporter which is required for viability, early imaginal disk development and adult motor coordination. Also has a role in the fate commitment of the R3/R4 photoreceptor cells. May function in ommatidial polarity by regulating the activity of the core polarity genes, acting upstream of (or in parallel to) Vang, dsh, pk, stan, and dgo, but downstream or independently of fz.
Miscellaneous:
MISCELLANEOUS: The name 'bedraggled' derives from escaper mutant adults which upon eclosion, immediately fall into their food and die due to severe defects in motor coordination.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSSKEQQAAGRDFKRNSNAYSSLPPTGTGAGCSGAALGSGTGTGKRARSKQHQLEHEQFGLSNSLSSESIRQACAYYDDELSDEDLIEIQQTPQAFHQQTKQPLQLQPISFRLGDELGDERSAFCGSQEMQQVPLSTPIKQAAETDEALCVLSELDAILDVHDVSQLNGTCSSGSVNSGSDDDKVEDYLMDLDNYLEEMDNALNREDSLIIIDGHTSLKREPRTRTLPLSRKKKSSKKKSEDQEAAQGDFQREHQLRKTFSCSLRPTSQIASSSGSLETSTEPVMDVWRRQSMRRALEQEDTKATVAMEREEDDIPTLLVELPPRRDAEMRRCFSQGDCQASVAPTVGSQMLTEAHIFDNLLQTNARASSEEPRPRQYGRRLEGPPTPVRPLILAQSRPQSAPTRVQMREPQLQDTPTHPIMSTCSELSSARSSRMPSPVSLPSDSSSSGSSSAEHDQEPDPVQTTTMCSASSTTPLEPLHQLQLLLREKCGFNSQWPHAGSRTLALIGCTLGVFNMCRFAVLTINFGGNFLLQFLLLSVIFGIPLLWLQMCLGAKIRAGPVSMWKISPICAGVGIALVMQQCFLALYSTVSLAWILVYLRDVFPTAARSGYRWQEMAFPYRYDASNATGNLTQTVAEYFNVVVLQRLHLANHPDASGIRFHVNDRQLAFYLALIWAAVFLILCKGLKSLGKLAYIIYTLPLVALAVVTAKFVYVVDPSRIQNIFAASDFDDFLVNSNSWTAATQETFLTWGLLGASVIAITSRSHTNANKAALRRDAILLVLFTLIGLGLMALLALCCAQILWQHGYVYVPGSFENPDCYTSIYSLQSNTNPYLLSYPRSLIPHYSSFIGETYRRNRTMIHVESGFQALRFISEIFPAVLSLASDSISWVWAAVAFATFAGFGLAQLCVMWKPISSALGNSTSSVLLSCVTGLLLSIPFATEMGISILYYVDFLLGGSWFIPIIWTAQIFGVFLIRGRPYNGDDLVNDLRLCGSMSAFLALSWNVLLPIGLITLSVVDYKASLSNQFYYWRGKSYFTYWSRKMGSLIQIGVLLVIPVTAIIQIYRYLAHGPPDILERIQLLYRPPEEGEEPRRPSARQTASQSRRNALGQTTEGGQHDAQNDAPPKYTPPPSYTTATGARLAKLLRQSIRRSVRRVLGDSSRTRPVLSLDAESASPAAPPDYLTILTNPAGSSFNADPSPASSSSPESIEIDQRPVGYSQRSQSLGRKLHRSGASTLERRPYTAEDVVTILRSSVRHRQSQGGGNLVTASTLPRPPTAAMSTHLEDASFRSIENLVLNAEPPDRTPGVELELELEAGQAEECARNNTSVI
The following text describes a protein:
Function:
Required for correct initiation of floral organ primordia and for proper development of organ primordia. Phosphorylates in vitro ASF1B/SGA1, the C-terminal part of TKI1 and histone H3.
Subcellular Localization:
Nucleus.
Domain:
The first coiled coil domain is essential for oligomerization.
Sequence:
MSDDMVLHFSSNSSNQSDHSLPDKIAKLEARLTGKTPSSAKPPQQQQQQQQQVSLWSSASAAVKVVTSTPPGLSETSISDSDDENTGDFLIRANTKKRQKVQESNNFSVVDHVEPQEAAYDGRKNDAESKTGLDVSKKKQGRGRASSTGRGRGSKTNNDVTKSQFVVAPVSAASQLDASDQKDFRPDGQLRNGECSLQDEDLKSLRAKIAMLEEELRKSRQDSSEYHHLVRNLENEVKDLKDQEQQGKQKTTKVISDLLISVSKTERQEARTKVRNESLRLGSVGVLRTGTIIAETWEDGQMLKDLNAQLRQLLETKEAIERQRKLLKKRQNGDKNDGTDTESGAQEEDIIPDEVYKSRLTSIKREEEAVLRERERYTLEKGLLMREMKRIRDEDGSRFNHFPVLNSRYALLNLLGKGGFSEVYKAYDLVDHRYVACKLHGLNAQWSEEKKQSYIRHANRECEIHKSLVHHHIVRLWDKFHIDMHTFCTVLEYCSGKDLDAVLKATSNLPEKEARIIIVQIVQGLVYLNKKSQKIIHYDLKPGNVLFDEFGVAKVTDFGLSKIVEDNVGSQGMELTSQGAGTYWYLPPECFELNKTPMISSKVDVWSVGVLFYQMLFGKRPFGHDQSQERILREDTIIKAKKVEFPVTRPAISNEAKDLIRRCLTYNQEDRPDVLTMAQDPYLAYSKK
The following text describes a protein:
Function:
Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle.
Subcellular Localization:
Cell membrane; Lipid-anchor. Cytoplasmic vesicle, secretory vesicle membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MASFTSTCGSKVDRGSHHRGDSKGTPSESDCSAVIEKTREFFQICDVEGKGFITRRDMQRLNGELPLSADDLENVFDSLDADANGYLTFEEFSSGFSEFMFGPSVVPADPHGGEELVSRKSPEMLYESQWEERLSRGEDDEEKHFCMLMENLGASNIFEDPEEVRSLWVQLRRDEPHLLSNFEEFLARVTYQIKEANQEKKEMETALKRKSATHDDEIQRLYEEMEQQIKNEKDRILLEDSERFLTRSQDMEHQLLSKEKELEILSNKQKRLERQCRDLLSEQRETSVENVKLKRYNEDLSRELDHTSQELSLAQEQLMLLQEQSSRLHEEREMEIYRVTESLQRERTSLLKQLDLLREMNKHLRDEKDISYQKPKTSAMKISWTQRSGSIAMKHAERKQSFKSDEDEDVLPNSKRKNLIGINGHSMDLEDIVDGRHPSKNQLRRIISIEEDPLPQLLQQGYQAQLREWSEDEELEETIDLQMSNIYPTTSTPTSASPPPAVSHTPTSPRGQPVGKETVQSEEGASSGPDRLFKVVLVGNSSVGKTSLLRRFCDDCFHSGTCATVGIDYSVKTLSVDNSQIALQMWDTAGQERFRTITTAYYRGAMGIMLVYDITSEKSFENIKNWIRNIEEHASSDVEKMILGNKCDMNERRQVSKERGEKLAIDYGIKFLETSAKTSINVEEAFFTLARDIMARLNRKMNDGSQADGGGPVKISEKRSKKHSIFKCALL
The following text describes a protein:
Function:
Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.
Sequence:
MKDFEFFAPKTLEEAKGLLHQYKDVPPAIIAGGTDLVIEINDRWEKPDVVIDIKKLKELEYIRVEENTIHIGALSTFTQIENHPFIRSHVRALYKAASQVGSPQIRNLGTIGGNLSTSSVAGDGVSAMTTLDATVVLESVRGTRQMKLTDFFDGEGFKRRNALEADEIMTEVIIDRPDAHSASAFYKLAKRKSLAISVIGGGMAVKVDDAGVCTWASMRGGCIGRYPLHFKQAEEMLVGAPLTMETMEATLPILHDTVYDMARARPSVLYKKESVQGVFKKLFVDILDQLEGGCNE
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Nucleus.
Sequence:
MVPLLFHSSPLPSPLPPLDPISLLPTDTDKDVLLRPHSRWLVRKDRTRIFLMQSARVALPRKGGSSGGAGVGVATAGLLLETSLGPLAIDFFGADCSALTANFLNLCRAQLWNGAVATEVVPEVVVFFSLAADPVYKELLEKLLRSHSAGAAAPPGPGPLNFWSLLPRQERAEGDTSRTASTATVSLHSHAAASVHSTTDPVEQQETAVRQAMQQEARLCKRRRCVGLALPRAGGSNTKGGYQPVYVPASGSSGAAVATDAAHASASHSASSPCTVCRSGSLLVDASAPTLRFGLTLSDRAMDFLDKQYITIGVVREGEEVLRRIRRAPVRDRCGDDAPTTAGADPLAAVDNVAGRPALSWPRPVRMLRVKRATVLPTAGTEKYVAVPPSAWWGVSSTASSAAAMKQQRQLTAAALHQAGCFEWWASEAAVRAAHRQLVDLVRTSLAAHGYVVITRPRTVADASIYLQKAAASTGRHAAQPLIVVAAAPAQTRSDDEAATSPGEPELVCNLHYAGDYLSSEDDDAEGFHNGGQTLPHSATAALSAKQLEERRKSFMQQHQEKANETLSLMLNLLNGVADVRGDIKPPDNVLFVCKLNPVTTGEGLALCFSQFGRVTSADVIYDAKTKQSLCYGFVEFESVEACFRAFQKMDRALVDDCRIHVDFSQSVSRLWAQRQREMRKRDRVALE
The following text describes a protein:
Function:
Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance.
Miscellaneous:
MISCELLANEOUS: Knockdown significantly reduces the adhesion of cancer cells to lung microvascular endothelial cells and the reciprocal effect is observed following overexpression.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein. Cell junction, tight junction. Nucleus, nucleolus. Cytoplasm, perinuclear region. Note=In epithelial cells, recruited to tight junctions (TJ) during the maturation of the TJ complexes. A nucleolar staining may be due to nuclear targeting of an isoform lacking the transmembrane domain (By similarity). TNF-alpha causes translocation from the cytoplasm to the nucleus.
Sequence:
MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET
The following text describes a protein:
Function:
Plays a role in intracellular Ca(2+) homeostasis. Involved in modulating Ca(2+)-induced swarming motility and pyocyanine production. Plays a role in regulating virulence in a Ca(2+)-dependent manner. Involved in cell protection against oxidative stress in the presence of elevated Ca(2+).
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Periplasmic side.
Sequence:
MTIHAQTPEPFSMSRAFTPRRLLLAVLLVALSALVLLGQSFRVFDRAWFAVQEWRHADAWKERSIWLPDYRVRIEAQPIEGLNDDVSALTFDPDRRTLFTVTNQPAQIIELSLQGKVLRTIPLTGFGDAEAIEYISRGVYVITDERQQRLVKVRLEDDTRFIDAADAQQLSLGIGLNGNKGFEGLAYDAEGKRLFVAKERDPVRIYEIHGFPHTQADKPFAVHVVDDPGRDKRLFVRDLSSLQFDEGTGHLLALSDESRLVVELDTDGEPVSTLSLLRGMHGLKRSVPQAEGVAMDDRGVLYLVSEPNLFYVFSKDEPAQP
The following text describes a protein:
Function:
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Sequence:
MNYIQTEIDGVWLIEPNVYSDERGYFMEAFKKEEFEAKIGPVDFVQDNESKSSFGVLRGLHYQKGEYSQAKLVRVLKGKVLDVAVDLRRSSPTFGKHVSALLSEENKRQFFIPRGFAHGFVVLSEEAVFMYKVDNKYAPQAEASIVYNDETLGIDWMLGESQMLLSPKDKEGMAFRDAVYFE
The following text describes a protein:
Function:
Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U).
Subcellular Localization:
Nucleus.
Sequence:
MQEIIASVDHIKFDLEIAVEQQLGAQPLPFPGMDKSGAAVCEFFLKAACGKGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSKFGPLCRHRHTRRVICVNYLVGFCPEGPSCKFMHPRFELPMGTTEQPPLPQQTQPPAKRTPQVIGVMQSQNSSVGNRGPRPLEQVTCYKCGEKGHYANRCTKGHLAFLSGQ
The following text describes a protein:
Function:
N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MRSSVYSENTYNCIRTSKEHLTERRRVAMAPMFQHFLNLCVEKFPESIEHKDTDGNGNFTTAILEREIIYIPEDDTDSIDSVDSLKCINYKLHKSRGDQVLDACVQLIDKHLGAKYRRASRIMYGNRKPWKANKLAEMKSAGLVYVCYWDNGVLGAFTSFMLTEETGLVEGDALHEVSVPVIYLYEVHVASAHRGHGIGRRLLEHALCDGVARHTRRMCDNFFGVALTVFSDNTRARRLYEALGFYRAPGSPAPASPTIRHTRHGGGRVVVPCDPLYYVYCLHMP
The following text describes a protein:
Function:
Involved in the mitochondrial activation of SOD2 by specifically facilitating insertion of the essential manganese cofactor. Has the ability to activate iron regulon in an iron-dependent manner. Responds to calorie restriction (CR) strength.
Miscellaneous:
MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MSDRNTSNSLTLKERMLSAGAGSVLTSLILTPMDVVRIRLQQQQMIPDCSCDGAAEVPNAVSSGSKMKTFTNVGGQNLNNAKIFWESACFQELHCKNSSLKFNGTLEAFTKIASVEGITSLWRGISLTLLMAIPANMVYFSGYEYIRDVSPIASTYPTLNPLFCGAIARVFAATSIAPLELVKTKLQSIPRSSKSTKTWMMVKDLLNETRQEMKMVGPSRALFKGLEITLWRDVPFSAIYWSSYELCKERLWLDSTRFASKDANWVHFINSFASGCISGMIAAICTHPFDVGKTRWQISMMNNSDPKGGNRSRNMFKFLETIWRTEGLAALYTGLAARVIKIRPSCAIMISSYEISKKVFGNKLHQ
The following text describes a protein:
Function:
Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages. Acts as a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5): cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. Also cleaves mouse Nlrp1b: host Nlrp1b cleavage promotes ubiquitination and degradation of the N-terminal part of Nlrp1b by the proteasome, thereby releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis. Able to cleave mouse Nlrp1b alleles 1 and 5, while it is not able to cleave Nlrp1b alleles 2, 3 and 4. In contrast, does not cleave NLRP1 human ortholog. LF is not toxic by itself and only acts as a lethal factor when associated with protective antigen (PA) to form the lethal toxin (LeTx): PA is required for LF translocation into the host cytosol.
Subcellular Localization:
Secreted. Host cytoplasm, host cytosol. Note=Translocation into host cytosol is mediated via interaction with the cleaved form of protective antigen (PA-63): following secretion, LF binds via its N-terminal region to the upper rim of the ring-shaped homooligomer formed by PA-63 on the host cell membrane. In this PA-63 pre-pore state, the N-terminal segment of LF refolds into an alpha helix engaged in the alpha-clamp of the PA-63 pre-pore. Loaded complexes are then endocytosed, followed by a conformational change of oligomerized PA-63 from the pre-pore to pore state, which is triggered by the low pH in the endosome. LF is then unfolded to pass through the PA-63 pore and translocate into the host cytosol.
Domain:
Lethal factor (LF) is composed of four domains: domain I contains the first ATLF domain that binds the membrane-translocating component protective antigen (PA); domains II, III and IV together create a long deep groove that holds the 16-residue N-terminal tail of MAPKK before cleavage. Domain IV contains the catalytic center.
Sequence:
MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. 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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein.
Sequence:
MNSINVKTLRWSALVLGLGAGMYEHRSHIQCQKQKEIDENYHRQESLIESAKIAYLNTKNTPPKEDSMLPNLKKDSEDFDMDEFVKELEKNV
The following text describes a protein:
Function:
IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells (By similarity).
Subcellular Localization:
Golgi apparatus, trans-Golgi network. Cell membrane; Single-pass type II membrane protein. Cell membrane; Lipid-anchor, GPI-anchor. Late endosome. Membrane raft. Cytoplasm. Apical cell membrane. Note=Shuttles between the cell membrane, where it is present predominantly in membrane/lipid rafts, and the trans-Golgi network. Forms a complex with MMP14 and localizes to the cytoplasm (By similarity).
Domain:
The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading.
Sequence:
MAPTFYHYHPLPMDQKEPGCGIRWRCLAAASVLILVALVIPLIIFAVKANSEACRDGLRAQEECSNTTRLLQRQLTRSQDNLAQAEAQASTCNRTVVTLQDSLEKKVSQIQEKQALIQEQEAQIKEQEAQIKEQEAQIKEQKAHIQEQQVRIQKLEGEVEEFEQKLKKLRTAEEASITSKQNSAGSMAVSSLLVLAVPLFLLF
The following text describes a protein:
Function:
This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGWHDGCIRCMVGVPFASVIATVLCFAGVALFCGCGHEALSGTEKLIETYFSKNYQEYEYLIHVINAFQYVIYGIAIFFFLFGILLLAEGFYTTTAIKHILGEFKPPAIKGGLISTVTGGTPKGRSTRGRQPVHTIELICRCLGKWLGHPDKFVGVTYIITILWILIFACSAVPVYIYFNTWVTCQSIAFPGKTTTSVSTLCSDARMYGVLPWNAFPGKVCGTSLLAICKTSEFQMTFHLFIAAFVGAAATLVALIHALMCLSANRVYQQRVLETGKSQETPQAESSELTEILPEPPQRSAENLV
The following text describes a protein:
Function:
Involved in the sodium-dependent cotransport of myo-inositol (MI) with a Na(+):MI stoichiometry of 2:1. Exclusively responsible for apical MI transport and absorption in intestine. Can also transport D-chiro-inositol (DCI) but not L-fucose. Exhibits stereospecific cotransport of both D-glucose and D-xylose. May induce apoptosis through the TNF-alpha, PDCD1 pathway. May play a role in the regulation of MI concentration in serum, involving reabsorption in at least the proximal tubule of the kidney.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein.
Sequence:
MYKTNRGNASGYFLAGRSMWWLPIGASLFASNIGTGHFIGLAGTGATSGLAVAAYEVMSGYAILLLGWIFLPVYVSSGVYTMPEYLRVRYGGQRLRIAMSILALFLYVFTKISVDIFAGAVFIQQAFKWNIYASIFVLLAVTAVYTITGGLAAVIYTDTLQVVIMLVGGSFLMVTSFMKIGSLERLRLEYMQSFPSSVLNDTDTTCGYPRQDAFSMIRDATTSDQPWPGTALGIMVIGTWYWCTDQVIVQRSLAAKNVTHAKGASIVASYLKFLPQFLIVMPGMIARVLYTDEVACVDSESCMKYCQNPTSCSNIAYPLLILRLMPIGARGLMMAVMIAALMSSLTSIFNSGSTIFTMDIWRRIRPNAKNRELMIVGRLFVLVLVGISILWVPIVQVAQGGQLFQYIQSLQSYFAPPIFVCFVTGVVWVRNNEKGAFWGFIIGVVLGVIRMILDIVYPAPACGLQDDRPSIVKNVHFLYYNCIVTLVCLVVTVTVSLMTPKPTINQILGKTFWTRGMNPKPEQLTFSDETNNHAESKEVRKRVQLHDNKLEDPTAEGVRQPDLSCQEHTEKSGKYQKGYICCINEKSLNILDKKGRQSTFCS
The following text describes a protein:
Function:
Binds double-stranded DNA (dsDNA) with high affinity. Binds double-stranded RNA. Binds single-stranded DNA with lower affinity and with a preference for purine-rich sequences. Shows residual nuclease activity for dsDNA. May facilitate blood meal intake by lowering the local viscosity created by the release of host DNA.
Subcellular Localization:
Secreted.
Sequence:
MALKLVYGVFTLALLGISSVNADCSLKIPESVENEKTPVIMVRKSLKTFEYDLFQPTGEVTNFPERTELLLACTGAQNYFKNGEESVTLMCHNNEFDDGQGNGLDLFTCVKTPTAELRKTKERCSLGDLYVYDVVFRISEEELVGPVYDICYNEYSQKPAYSRNIINGAAVNYRVPESETDLTVSLAKDFTTRDVNNYFKLENQKQRFQGYTIDGKPLVDDKNFFAPGQLAPDTSMITPADKLSTYDYANIVPQYKTVYDGNVWRVENITRDLAVNRQAKFEVYTGGYERLTALHNGKEEEIFLSAKKYVHEIPKYIYKFVVDKENDAGIVFFTLNNPHVKNVKGTEFCKNQCEEANVLDSNFKDWTQGYTFCCTWNNVKDYVRALPQDIEINNLLKFN
The following text describes a protein:
Function:
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Sequence:
MATIELHAWYRQYRKLKEEAADAILLFRFGDFYETFDDDAKLIAELLDITLTRKEYAVDKRLPKDQQKLYAPMAGMPYHAVDRYVSELIARGYRVAIAEQLSETEAMRNDTRPRSVYAAGLTPVESSGKMVQRAIVRVITPGTVIDPAMLPDRTNNYLAAVIVEQGKVGLAYADLSTGEFAAAEFTDARALMQLQAELARLSPAEVLVPDDEALRLPNLEPVQARLSQDLAPLTKEEREALLPHERVARRLEGASAASWTQGYVTEWPLWRWELATTTEVLCEHLALPSLAVCGLDGRPLATRAAGALLQYAQVTQRQRVSQLRALRVYHTGAYMLLDPQTRRNLELLESGGRQGAKASLIAVLDRTCTAMGARLLRRWITQPLIVIEPLQVRQHAVARLVAETMARLEVRSALADLPDMERALNRIAQGITVATPRDMTQLRAALRKLPAVAQAVQALLPDLLAAEMPGEPPLVFDVCADVLDLLERALDDDPPALLGSSNYLRAAEEGGERPRRVIRPGFDQRLDALIRASRHAQEFIDRLESKERERTGIRSLKVGYNQVFGYYIEISRAVDAKLIPAHYERKQTLVNAERYVTEELKYYEGLLSDARLKLVDLERDIFQRLCDELQPHLDRLRATIAAVARIDALAALAEVAVRGRYVQPRLRTDRVLRIKQGRHPVVERTLSEPFIGNDIDLDGEQAQILIITGPNMAGKSTFLRQVALITLMAQIGSFVPADEAEIGLVDRIFTRIGAQDDIATGQSTFMVEMTETAALLMQSTPRSLIILDEVGRGTSTYDGMAIARAVVEYIHDHPRLGCRTLFATHYHELIALERELPRVRNYHMAAVERDGRVVFLHELRPGGADRSYGIHVAELAGIPPEVIRRASALLADLEGQRPPSSPAQPPAPPAPVVVPAQETGQGMQLSFFDLAPHPVVEYLRRLRIEELTPLEALNRLAELQRLAGQG
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MTTVGQLPFTPSTSKPLPKKPIFEAGSAEDEEDSDHLVERKKKTKRTELKSKPPLPAVPDRTGPPMIPLGVLLDFAVQQLYHEVTVLTELLPKKQDSERKVTLVQFAYNTRILFVKLLAIVKWLKVSKRFDNCTSICYFLEQQSQMFVDTADRLVQLAREELIYARLPVFQVTPAIDVLASGTFPRLPTCIKNRFIRESKITPREQACTLARINQVLNFRISRIASKLSPRIEKIEVKNGMATFTVPGEFEVKVTILGEMEKLKWTLLRVKILVEDYEIGFGKPLVHPLQMDMVHTGLQQRMDESAEPISEMYAVLHSLAQMLQLDVLVCQATQLQAGRLKDKIVIEKYDEKERVLTIGYWLQHERGKRAAGRLNKFSPTYRVQIYGDPTDHDATLRVRHLPAGPEFTNVDTRSGRLSLTTILSCSFDARCKNRLLRIKKRLEAAEPNAKLFQSGVAAPSLRFVLLADADVPAPNPTDDETLNITVNMFSGKVLCQLSAIQSHPTVRELETALYSGSTTTATLQQKLLDLKIQLLIERYRKAVTVLQVRVIGEQQMKPLLDKHSNLPKRRLCLQFVREDNFILIVGFVEDKDIVIATKLFLLEKPSLSLTSINDDIDFLPPSIMPYLRRDHKKFLAPSKTGPSSHLASWERPLTCAIASIDDQIGFQRVAAELAKKKYGFTRVMNEPIVGGLCLNITDVSEAIPERCIDFFSSLVRCCLRLDSRARLLWPFECCLVNSPLVNDFLPNKKGNSNSCLVLEMAASASGTPVSETITALVADRLITYCHIYDLVVRFASVYENYKNMCSVRHFTYHKLVLAYGPRRDRLLVLNYKPRSANSAAKFIINFGQCTPIDYLDKDGADVSLPSNSTEEVQWNPHVMMSQILSERINQEWDLVELVHYLITTLAPLDALHNFYKFRFQSQKVFAWMVSNDNYFPLAFKCHLIMISEHVVRLIYGHIHLEFTMTENSSVFVRDVSRRGSAAVGLFRFFHLLSGGTCELTEPASVGGVFGAATPASVKHDTSSGPSPTPAVESSSSTATVVHAPSGPLSCAARLDVSAAPSPLNAATTRMPRSVPQNYMTMGSPAQPGSNVAPQSAAEGGGGQEDHPHCARRSAELTLSGSFIQIDHATLSKACVFTDTVAGSARVSPLDDYLNAVVYIKRLGIALDTYRRDANSKKYIDFVHVSYNPEQVRVSVNGQMEPNGRPAIHFNFHLDPATMKLKLKLEYVGGTYPSSSIVTILEQYFEKCVAPLHNEFAVISFINLCRCTAYKAVADFAMIMRRQMEPSSCESHYISFVHTSQKSPKDPQSKEVSLTTIVEPTDRAVLITLCIRPKEKKATDTNKYHLTLIYNFQGNALSVRSATFSLEGDVDLIPFVKSIQSQRTSSTECSIWPTVCKLMAKMSSTRLSNVSVSATPGSVGQHPPSVGPASVNAPGSNASQRQ