lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis.
Subcellular Localization:
Nucleus.
Sequence:
MFLYEKIPVSKSFNIYTWRSMAGFKRGYDGKIAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEDGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPSRVSKECKDLITRMLQRDPKRRASLEEIENHPWLQGVDPSPATKYNIPLVSYKNLSEEEHNSIIQRMVLGDIADRDTIVEALETNKYNHITATYFLLAERILREKQEKEIQTRSASPSNIKAQFRQSWPTKIDVPQDLDDDLTASPLSHGAVPQSPARTAENVLNGHRSKALNDSSKKEDIPDLAGPALSVVPSVSLKPTTSGRKCLFRVEEDEEEDEEDKKSVSLSTQVVLRRKPSVTNRLTSRKSAPVLNQIFEEGESDDEFDMDENLPPKLSRLKMNIASPSTVHKRYHRRKSQGRGSSCSSSETSDDDSESRRRLDKDSGFTYSWHRRDSSEGPPGNQGDGSGQGKPSNGNGGVDKTSPGDNSKGGGNPSGSSGGSTNNNSGSTRRCAGSGNSMQLSSKSAGDLVESLKLMSLCLGSQIHSSTKYIIDPQSAISFSSVKVQEKSTWKMCISSAANVNPVSSLGSIKFFSDQMSDTANELERIKSKNLKNNVLQLPLCEKTISVNIQRNPKEGLLCTSGQTTCCHVV
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MHAELQFLNIFNYCFVSPTYLHLDSLTNRYEFQCRNVYWMVTLLAVLVTCSFSCATFLMLEILRNHLASVMTTTTILLYMMRYLVMVPHIMWILLYRGRLKHDCAFALSIVQEKDKRLFQMPKLADQRRKRKTLQLYWVQIGCIVVSLLLGSVVQSYTLWSIASASREHLFGYYLFNLLALVVMIFISLMHLMYAQCWALLISFYLEELVWITKSEHLELGSLRTVIALWDDLTYFKQRVASTFGLMNVLHLLDILITCATESYAIIYFYEFGFNLLGALLSIVILVLYTGSCFLFAYAHDLVEVKEAELKDALKSMQYTNLKRQSRDQKDFYDLVNLKLMMESPKITACGLFEINLQIFYNVFAAIITYIVILFQFRGFEKSP
The following text describes a protein:
Function:
Involved in olefin biosynthesis. Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate. Is active with fatty acyl-CoA substrates that ranged from C(8) to C(16) in length, and is the most active with palmitoyl-CoA and myristoyl-CoA.
Subcellular Localization:
Cytoplasm.
Domain:
Contains three extended channels that together form a T-shaped, three-channel nexus. Contains an active site base originating from the second monomer of the dimer.
Sequence:
MLFQNVSIAGLAHIDAPHTLTSKEINERLQPTYDRLGIKTDVLGDVAGIHARRLWDQDVQASDAATQAARKALIDANIGIEKIGLLINTSVSRDYLEPSTASIVSGNLGVSDHCMTFDVANACLAFINGMDIAARMLERGEIDYALVVDGETANLVYEKTLERMTSPDVTEEEFRNELAALTLGCGAAAMVMARSELVPDAPRYKGGVTRSATEWNKLCRGNLDRMVTDTRLLLIEGIKLAQKTFVAAKQVLGWAVEELDQFVIHQVSRPHTAAFVKSFGIDPAKVMTIFGEHGNIGPASVPIVLSKLKELGRLKKGDRIALLGIGSGLNCSMAEVVW
The following text describes a protein:
Function:
May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1.
Sequence:
MEASVILPILKKKLAFLSGGKDRRSGLILTIPLCLEQTNMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQWNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDKKVTHFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDHMDWLNKRLVFEKFTKESTSLLDELALINNGSDKGNQQEKERSVDLNFLPSVDPETVLQTGHELLSELQQRRFNGSEGGVSWSPMDDELLAQPQVMKLLDSLREQYTRYQEVCRQRSKRTQLEEIQQKVLQVVNWLEGPGSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLVELKSLQQQLSDVCYRQASQLEFRQNLLQAALEFHGVAQDLSQQLDGLLGMLCVDVAPADGASIQQTLKLLEEKLKSVDVGLQGLREKGQGLLDQISNQASWAYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMVDVRRLKMLQMVQLFKCEEDAAQAVEWLSELLDALLKTHIRLGDDAQETKVLLEKHRKFVDVAQSTYDYGRQLLQATVVLCQSLRCTSRSSGETLPRLNRVWKQFTVASEERVHRLEMAIAFHSNAEKILQDCPEEPEAINDEEQFDEIEAVGKSLLDRLTVPVVYPDGTLPQPHGLHFAASCHSLPFYSVSLAASSLVFLLGFSSCVPQ
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity).
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MDETVYQIKAIIVLDNNGKRLCSCFYDPPGTPITPLTEKDKFEKLIFEKCKTSNCELEIIDNKVVIGSKQSDVWIFVVGNSLNSNELALLDVLNTLISLFKKACATDESIMITKKTFLENYALIRLYIDEIVSDGIIFEVDEETILNRVPIADNAAQSLNEAIEMAKEKAKGFGFGFL
The following text describes a protein:
Function:
A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MDLLQILLAIAGLLAILLLQKQWRTKTSPGAKAGRKLPPEPAGAWPVIGHLHKLGGPNPIYRNLAEWSDKYGPVMTLKLGMQNAVVVSDREAIKECFTTNDKALADRPPSSIGLHLGFNYAAIGAAPYGPYWRDMRKLVLLEVLSSRRLEMLRNVRISEIGTSIKELYSNIIRSSGGSGPAKVVISHWIEQLTLNYILRTIAGRRFSDDSSKDAQYVKGVINDFMYFAGQFVVSDVIPIPLLRWLDPQGHLKGMKRVAKEVDTMCEAWIQEHVQRRMREKPGPGQEQDFIDVLLNNRDVMRKAQEEIDNHVGKERWVDETDLKHLVYLQAIVKEGLRLYPPGPLGAPHRAIEDCQVGGYFIPKGTQLLVNVWKLHRDPRVWSEPEKFMPERFLTRQAEVDVFGHHFELLPFGSGRRACPGITFAVQVMHLTVARLLQGFDMTTPSNLPVDMTEGPGVTMPKAHPVEVLMMPRLPSALYEP
The following text describes a protein:
Function:
Induces apoptosis.
Subcellular Localization:
Nucleus.
Sequence:
MASPPAPPAKKRKMNFSEREVEIIVEELERGKHLLINHFNAGVPLAAKAAAWHDILRRVNAVATCHRELPEVKKKWSDLKTEVRRKVAQVRAAMEGGGESQNGGGAGTEGEDPTGATAAPVILTPMQQRICNLLGEATIISLPSGDCGAGRRDRDPHHRLRHHRHADPGVSAAPSEVPAETTYHSLEDGVVEYCTTEAPTTVTAEAPLEMMAHQHEVSAKPQELKSRIALNSAKLLQEQRVTNLHVKEIAQHLEQQNDLLQMIRRSQEVQACAQERQAQAMEGTQAALSALIQVLRPMIKDFRRFLQSNTPSPSVTADPNQTGQQDGIIQ
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Sequence:
NQCSTCKKNEAKYTCPSCLRKSCCVSCVKQHKTNHSCSGQRNRVAYVPLGEFADRHLLNDYHFLEDVARVADNSKRDSIIQGPKRSRRKMLNIFRNESRNLGINVKIMPEKFTKRSENTTYWHIRDKCILWRIKWIFPQEQVDFVDDRVKDTLLVSSLLNRFIHPSEGDPMLLHRLKRYCKVSHQDIYVLLKNDCKETHVSSYFILDKDKSLRDNLIGKTIVEFPTLVVVLHNALCDFLDKKNADQSSGLDLALLITAKYTMHFDFGIVL
The following text describes a protein:
Function:
Antimicrobial peptides that have antibacterial activity against the Gram-negative bacteria S.marcescens. Has antifungal activity against D.coniospora. May play a role in response to physical injury and osmotic stress. Through the neuropeptide receptor nlp-29, induces sleep upon activation of the innate immune response to molting and injury to the adult epidermis.
Subcellular Localization:
Secreted.
Sequence:
MISTSSILVLVVLLACFMAASAQWGYGGYGRGYGGYGGYGRGMYGGYGRGMYGGYGRGMYGGYGRGMYGGWGK
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:
MADNPLLSILDQIENLTRETLRKVNVNIRDTSNASKEIDLIANKDEEFRKALVDAQGKIEVYNKIRKCNEAVVQQDRVIVQLMDKLKQAESSLMSAIENAKEVLPCEESRSVNSEDLIKYAYEISSNHAVCAPTNWQQGDSRRPYPIDIEMRAGILGKLTEYNVNGDNAIDVDYGISNSNKNSEAVDDSNKQNENLSDQPSESDNEVENLENDQGINNNIGMMSTDSSSDS
The following text describes a protein:
Function:
Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory-like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC. Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (By similarity). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (By similarity). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (By similarity). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Secreted. Note=Also exists as a soluble receptor.
Sequence:
MWQLLLPTALLLLVSAGMRAEDLPKAVVFLEPQWYRVLEKDRVTLKCQGAYSPEDNSTRWFHNESLISSQTSSYFIAAARVNNSGEYRCQTSLSTLSDPVQLEVHIGWLLLQAPRWVFKEEESIHLRCHSWKNTLLHKVTYLQNGKGRKYFHQNSDFYIPKATLKDSGSYFCRGLIGSKNVSSETVNITITQDLAVSSISSFFPPGYQVSFCLVMVLLFAVDTGLYFSMKKSIPSSTRDWEDHKFKWSKDPQDK
The following text describes a protein:
Function:
Probable transcription factor that forms a heterodimer with the MADS-box protein AGL104 and is involved in the regulation of pollen maturation at the late stages of pollen development and pollen tube growth.
Subcellular Localization:
Nucleus.
Sequence:
MGRVKLKIKRLESTSNRQVTYTKRKNGILKKAKELSILCDIDIVLLMFSPTGRATAFHGEHSCIEEVISKFAQLTPQERTKRKLESLEALKKTFKKLDHDVNIHDFLGARNQTIEGLSNQVAIYQAQLMECHRRLSCWTNIDRIENTEHLDLLEESLRKSIERIQIHKEHYRKNQLLPIECATTQFHSGIQLPMAMGGNSSMQEAHSMSWLPDNDHQQTILPGDSSFLPHREMDGSIPVYSSCFFESTKPEDQICSNPGQQFEQLEQQGNGCLGLQQLGEEYSYPTPFGTTLGMEEDQEKKIKSEMELNNLQQQQQQQQQQQQQDPSMYDPMANNNGGCFQIPHDQSMFVNDHHHHHHHHHQNWVPDSMFGQTSYNQVCVFTPPLELSR
The following text describes a protein:
Function:
Transcriptional regulator with a general role in all morphogenetically distinct forms of filamentous growth, namely haploid invasive growth, biofilm formation, and diploid pseudohyphal growth. May control FLO11 gene expression as part of a promoter-bound complex with FLO8 and MSS1.
Miscellaneous:
MISCELLANEOUS: Present with 1010 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MYQGPPQPPPQAVPMPYIVNNNTPPYPNGNINFPPTAQQNIPPTVYPQQVPFPGQPQGGQFPQPSSEQQVFNQLPQVTQTFHNSAQNTNATGGPGSGSMPMFTPVASFPHPMATAATAAAPLPRSASQASLSMLRVPYHVRKYLSNLAMLKLYEIINEVNTAMGKIGLLSFWTELISDIFTPDAVIRYSKKSMTDYREFEFIIPVFPVICSTLGRFGIVRMEVKVLQLKTQVLSNSTIFFNCPRVTFVYYYPDGSYITHFSQMKGAFDLDLKINWLDVSMHSFVPDIEWNAVERLLSDDTKSTEIEQIFRKLKQEDVKEQGNSFAENNATNVPPNFEAITQLRSYFDVFRNVSVFGTQEGLMRVMQISTVMSTLKNLRKFQIEKNIDSPVTALSAYIDADKKDSGSEPLHAKRRRNSGISPRTTTLGPNGNSNTSNEELPTSDVNDINKDMTKKKMKF
The following text describes a protein:
Function:
F-actin cross-linking protein. Stabilizes actin and acts as a negative regulator of primary cilium formation. Positively regulates the phosphorylation of both myosin II and protein phosphatase 1 regulatory subunit PPP1R12A/MYPT1 and promotes the assembly of myosin II stacks within actin stress fibers. Inhibits the phosphorylation of myosin light chain MYL9 by DAPK3 and suppresses the constriction velocity of the contractile ring during cytokinesis. Binds to microtubules and promotes epithelial cell apical constriction by up-regulating levels of diphosphorylated myosin light chain (MLC) through microtubule-dependent inhibition of MLC dephosphorylation by myosin phosphatase (By similarity). Involved in regulation of cell migration, nuclear size and centriole number, probably through regulation of the actin cytoskeleton (By similarity). Component of the CERF-1 and CERF-5 chromatin remodeling complexes in embryonic stem cells where it acts to stabilize the complexes (By similarity). Plays a role in embryonic brain and cardiovascular development (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body. Midbody. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, stress fiber. Nucleus. Cell projection, dendrite. Perikaryon. Cell junction, tight junction. Note=Localizes to the proximal end of basal bodies. During mitosis, localizes at the inner centromere in metaphase, at the central spindle in anaphase, and at the midbody in telophase. Central spindle localization requires KIF20A while centromere localization requires the kinase activity of the chromosomal passenger complex.
Sequence:
MAEFTSYKETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFLSSKGRHERTKFRGHGSEASVSKHTARELSPQHKRERLRNREFALNNENYSLSNRQVSSPSFTNRRAAKASHMGVSTDSGTQETKKTEDRFVPGSSQSEGKKSREQPSVLSRYPPAAQEHSKAWKGTSKPGTESGLKGKVEKTTRTFSDTTHGSVPSDPLGRADKASDTSSETVFGKRGHVLGNGSQVTQAANSGCSKAIGALASSRRSSSEGLSKGKKAANGLEADNSCPNSKAPVLSKYPYSCRSQENILQGFSTSHKEGVNQPAAVVMEDSSPHEALRCRVIKSSGREKPDSDDDLDIASLVTAKLVNTTITPEPEPKPQPNSREKAKTRGAPRTSLFENDKDAGMENESVKSVRASTNTMELPDTNGAGVKSQRPFSPREALRSRAIIKPVIVDKDVKKIMGGSGTETTLEKQKPVSKPGPNKVTSSITIYPSDSSSPRAAPGEALRERHTSTSNIQVGLAELTSVSNHVSSPFELSIHKHDITLQLAEAERMADGPLKDRPETVVSRSSIIIKPSDPVERNSHAPPAETIRWKSHSAPSEVGFSDARHVTVRNAWKSRRDLKSLEDPPTRIGKNVESTNSNAYTQRSSTDFSELEQPRSCLFEQGTRRVGPSSGDAPEPSSRRTQSSLTVSEVLTRRNRVGDTITVAAWNHSASMEEEGEDCTLSVYRQLHNSLDPSELPGKQGLPESGRVRAEERLRPTRPCAEEN
The following text describes a protein:
Function:
May contribute to the structure of the coat at the interface between the middle, cellulosic layer and the outer, electron-dense, proteinaceous layer.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle. Spore coat. Note=Accumulates specifically in regulated secretory vesicles of prespore cells (prespore vesicles). The protein later accumulates extracellularly in the spore coat.
Sequence:
MLFLKNIGVFFMIFLVSKSYATDCNKITNEEECHKSSECIVINYTPCCGEQKWACSKGTFDTCTYENSCYRNSSNNQVVEVSNKCFNLDGFIKITTPTEYSCSDAKIKECALLGKSCSFQKNSCSNPTSCCPGESICEGLSSGSSTSGGGSSGGTSGGSSSGGTSGGSSSGGTSGSSSSGSSSGGVSSCSTTHCPEGYHCSMVNDVATCLASTTGGTGLPGTSSSTAGVSSCLTTLCPIGHICVEDSNGVNCVPNGGGTSGGSSSTGTSGGHPDPCRDVDCPDGFHCECKDGKTAKCVPSPTTGSSSTSGGHPDPCKDVTCPDGFHCECKDGKTAKCVPSPTTGSSSTSGGNTNPCSNVNCPDGFYCECKDGKTAKCVPSGPTQPPKPPVCSLRCPPNHECRFNDQGHQCCVKVHHDRCSLRCPHGHECKVDHNGKECCVRSHRPPPPEVCSLRCPPKHECKFDDHGKKCCVKIHCDEVCDLDCGRGFECKIRHDGSKCCVRSERPHPPQHEKCNKRCPPGHECKVDQHGKECCVVAHRPPPKCSLRCPPRHECRVNHFGEECCVKVHHDKCSLRCPPGHECKVDQHGKECCVVAHRPPPKCSLRCPPKHECRINHFGEECCVKSRNDCLTCEDLNCERKGLHCAMKTVPIDKENCCEKVPVCYSTNPLLDGGHGFI
The following text describes a protein:
Function:
May play an important role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MFLNSILVVITDLAAGLLGNTSFRRHFHLLLSALLLFGPLLSLWVSHYSVFAKRTHFLYRVFLRSGWGWTCIFVGSFVFVLSFSVRRSLTLSLRHLSRLAVAGGLWLGFRKLLCLLENATGSCYEPLSAALEMTSGTNGEGQPLLLLREAETKETCVRSGMLWRGYEVSEDALLLCLCCLLLAEETAVFGPYLNLGGPSEAPLRILFLFCVLLLSLWVFLLLCLLAYFPEFPTQLLGGALGCLSWRALYQGWYRLRPSWYCPGRPGVGLLSTQSKQDELLETQTNAKEID
The following text describes a protein:
Function:
Required for establishment of the axial budding pattern in yeast cells. May be involved in the selection of future sites of septation in hyphal cells. Contributes to morphogenesis and is important for induction of hyphal growth. Also plays a role in epithelial adherence, and is involved in intestinal colonization and systemic infection. The role in adhesion is probably minor compared with its role in morphogenesis.
Subcellular Localization:
Cell surface. Bud neck. Spore, perispore. Note=Localizes to a ring at the mother-bud neck of yeast and pseudohyphal cells. Localizes to single or double rings distal to the junction of the mother cell and germ tube in hyphal cells. Requires septins for proper localization. Also found at the cell-surface of blastospores.
Sequence:
MQTSISTTTIEDHLHHYSPEESQKLLSRESSINTDLFKHENESVDLLLKEMNSTPSKLLPIDKHSHLQLQPQSSSASIFNSPTKPLNFPRTNSKPSLDPNSSSDTYTSEQDQEKGKEEKKDTAFQTSFDRNFDLDNSIDIQQTIQHQQQQPQQQQQLPQTDNNLIDEFSFQTPMTSTLDLTKQNPTVDKINENHAPTYINTSPNKSIMKKATPKASPKKVAFTATNPEIHHYPDNRVEEEDQSQQKEDSVEPPSIQHQWKDPSQFNYSDEDTNASVPPTPPLHTTKPTFAQLLNKNNEVNSEPEALTDMKLKHENFSNLSLDEKVNLYLSPTNNNNSKNVSDMDSHLQNLQDASKNKTNENIHNLSFALKAPKNDIENPLNSLTNADISLRSSGSSQSSLQSLRDDNRVLESTPGSPKKVNPGLSLNDGIKGFSDEVVESLLPRDLSRDKLETTKENDAPEHNNENFIDAKSTNTNKGQLLVSSDDHLDSFDRSYNHTEQSILNLLNSASQSQISLNALEKQKQIQEQEQTQAAEPEEETSFSDNIKVKQEPKSNLEFVKVTIKKEPVSATEIKAPKREFSSRILRIKNEDEIAEPADIHPKKENEANSHVEDTDALLKKALNDDEESDTTQNSTKMSIRFHIDSDWKLEDSNDGDREDNDDISRFEKSDILNDVSQTSDIIGDKYGNSSSEITTKTLAPPRSDNNDKENSKSFEDPANNESSQQQLEVPHTKEDDSILANSSNIAPPEELTLPVVEANDYSSFNDVTKTFDAYSSFEESLSREHETDSKPINFISIWHKQEKQKKHQIHKVPTKQIIASYQQYKNEQESRVTSDKVKIPNAIQSKKFKEVNVMSRRVVSPDMDDLNVSQFLPELSEDSGFKDLNFANYSNNTNRPRSFTPLSTKNVLSNIDNDPNVVEPPEPKSYAEIRNARRLSANKAAPNQAPPLPPQRQPSSTRSNSNKRVSRFRVPTFEIRRTSSALAPCDMYNDIFDDFGAGSKPTIKAEGMKTLPSMDKDDVKRILNAKKGVTQDEYINAKLVDQKPKKNSIVTDPEDRYEELQQTASIHNATIDSSIYGRPDSISTDMLPYLSDELKKPPTALLSADRLFMEQEVHPLRSNSVLVHPGAGAATNSSMLPEPDFELINSPTRNVSNNSDNVAISGNASTISFNQLDMNFDDQATIGQKIQEQPASKSANTVRGDDDGLASAPETPRTPTKKESISSKPAKLSSASPRKSPIKIGSPVRVIKKNGSIAGIEPIPKATHKPKKSFQGNEISNHKVRDGGISPSSGSEHQQHNPSMVSVPSQYTDATSTVPDENKDVQHKPREKQKQKHHHRHHHHKQKTDIPGVVDDEIPDVGLQERGKLFFRVLGIKNINLPDINTHKGRFTLTLDNGVHCVTTPEYNMDDHNVAIGKEFELTVADSLEFILTLKASYEKPRGTLVEVTEKKVVKSRNRLSRLFGSKDIITTTKFVPTEVKDTWANKFAPDGSFARCYIDLQQFEDQITGKALQFDLNCFNEWETMSNGNQPMKRGKPYKIAQLEVKMLYVPRSDPREILPTSIRSAYESINELNNEQNNYFEGYLHQEGGDCPIFKKRFFKLMGTSLLAHSEISHKTRAKINLSKVVDLIYVDKENIDRSNHRNFSDVLLLDHAFKIKFANGELIDFCAPNKHEMKIWIQNLQEIIYRNRFRRQPWVNLMLQQQQQQQSSQQ
The following text describes a protein:
Function:
Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity.
Sequence:
MTKYRLVLLRHGEGAWNKENRFCSWVDQKLSSDGVTEAQNCGRHLKALGFEFDLVFTSILSRSIQTAWHVLEQMGQEWVPTEASWRLNERHYGALIGLNRAEMALNHGEEQVKRWRRSYDVTPPPITESHPYYHEIYNDRRYKHCDVLLEKLPKAESLKEVLDRLLPYWNGRIAPEVKRGKMVLISAHGNSTRALLKHLENISDEAIVNVTLPTGIPVLLELDENLHALGKHQFLGDQEAIQAAIKKVEDQGKAKPVV
The following text describes a protein:
Function:
Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1 to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1.
Subcellular Localization:
Nucleus.
Sequence:
MLPAVKTVEAEEEYAEDCPELVPIETKNQEEENLDFITKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEGSAVEKSLAVSQGGELYEEWLELRNGCLCCSVKDSGLRAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEEKPDGLVNEATRQVALADMILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLHAYDILSGISLQKKLQHVSTAPHLDQSIVTVTFEVPGSAKEECLNVFIQNLLWEKNVKNKDGHCMEVIRLKGLVSIKDKPQQMIVQGIHELYDLEESLVNWKDDAERACQLVFIGRNLDKDVLQQLFLTAVAEAEEQRTAPGRDGVCPSH
The following text describes a protein:
Function:
Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MPWLPVKKIRRQFKLLLLLVLLTSAVWVTYLHISLARQGKTLRLPFIYSRDGEKVESTDHARKTGRAQAFLAHSQAGDSSEEASTPDALAWKRERRWNPSESRLNLTDIAVPWNEKYKGKVNLHVFEDWCGGSVLNLKTNLHFPLYPHTRTTVTKLAVSPKWKNYGLRLFGYIHPYKDGDFQFAVASEDNSEFWFSSEESPSSAQLIAYVGRSGSEWTAPGEFTKFSSQVSKPIRLMSSRRYYFEVLHKQDDRGSDHVEVAWRLSLPGMKFEIVDSAYISLYTDETAYRMNEVAHIPRTLSSRPGHRWGVDKEQPAADMLMDDPRNDFFMTPLIEQSRVESVLVPCAYKPTYVVKDFPIARYQGLQFVYLTFVYPNDFTRLTHMETENKCFYRESPLYLEKFGFYKYMKMDDEESPQVPFLFFNRQHFMEEDDDDEEALFAGSKLNHKIKDEFPGYPMPPNTDHREDTRIPLSVPPELTYGINVSTVAQIHGRSLKWTSREHPPPGHRGQRRPLIPTLEGPIKRARRSPTDGTLDLRLITESEVLTREHRVTGKSKNGQMSHVRKRDKKSELRNRARKLDSLMVGLKTEFTEKPELSEVRPTEEGRLESVTSEAMLKQNLKDTLRVKNKHKPEKVYVTRLLSKVRKSQNRLLPGMLLHQPKPRRSPSPHAHLHAPHTPKTSRGGRRSKGWGLPDTSELGLFSWDGQTEKPGAPVPTSPGQPNGPPSLSMSSDSPAEVQEQDYSYEEEEPRQRWPEDAINWQRTFSVGTVDFEMLRSDWNDLRCNVSGNLQLSEAETVDLVAQYMEKLNEKNGGIYTLLRIINVEKRRDSARGNRYFIELELQERGSRKVRLAEYVYLLLHRGTGGDSDESPPAETPEIFPSPQLPLYSKPILCRPVSLNWNPRATVHFVVPVKNQARWVQQLISDLEFLYTNTQDDQFNLILVDYDSEDMDVERALRTAKLPSYKYLKRSGNFERSAGLQAGVDTIQDNHSIVFLCDLHIHFPLSVLDSVRKHCVEGRLAFAPIVMRLSCGSSPYNPRGYWEVNGFGLFGIYKSDFDRIGGMNTEEFKDRWGGEDWELLDRVLQNGLEVERLRLRNFFHYYHSKRGMWNTQSQESVVKD
The following text describes a protein:
Function:
Component of the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex. Component of the retriever complex, which 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 retriever 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.
Subcellular Localization:
Endosome.
Sequence:
MSSLLFDIKLKRENKVYHENDMLLGCVQFQCAQETKHEGIILYLEGIVNLQLSAKTVGLFDAFYNSVKPINLLQNSLELSAPGKLSAGRSEFHFELPLVCKKEPRILYETYHGVFINVNYQLTCTVKRNFLGKATTKIQQFCVQYKPVPLSEDSKKVVPFSLSPDSLQKNASAKERLSMPRFLITGRLDRSEFCVTTPITGSITVQHTEAAIKSIEMQLVRVETCGCDEGYSKDATEIQTIQIADGNVLPKLELPIHMVLPRLFTCPTLLTKNFKIEFELNLIVVFKEDYTVSENFKIVLKRSTGPLPSKVTTAGR