lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain. Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA. Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly). Required for normal survival after DNA damage. May inhibit apoptosis and promote cell survival and angiogenesis.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSVNLLDNFSSSPTNVLCLINAGLLNGFTREEILDIFERFGDVENLIMLEGKSYCVLSFKKENNSAESYQKLNGSFCLKDESKPLYLCFLKYTLLSFQETSKVWPTGLILKKNFISLGEEEKLLFFTHTQQSESQTSQLKHRTVKHYGFEFLYGSNKVDKNPLSSGIPVEMEPLIEKFMEFGLARPNQLTVNHYVPGQGIPLHTDTHSSFEDGIISVSLGSDIVMDFKNNKGGECVSITLPRRSCLIMTNESRYMWSHGITPRKSDVVDAELGGLTILRREKRTSLTFRKIRTSECDCKFTEWCDSLSSKIVDFSEEAADQIEKNHVFHVYDGIASHFSATRHSPWPNVKSFIMSFPVGSLLVDIGCGNGKYFNCSSSLFNIGTDRSSQLLKICRNRDDHQVVKADCRVSPFRDSIADAAICIAVIHHLTTDERRLKTLIDISRVLVKGGRALIYVWARDQQIGIEKSTYLLQKKSEVSSRAEAYPTAVLPVHENRTNFKHADILVPWKLNFRNSNSEELEYRGSSESNPSTYLRFYHVFKEGELEYLCSKVSNITVCRSFYDQGNWCVEFKKE
The following text describes a protein:
Function:
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MKKKIVPINPLKADEILAVSHLSCVFNSKTNNPIKVIDDFSYTFQKNQIYCIIGDSGSGKSTLVNHFNGLIKPNQGDIWVKDIYIGAKQRKIKNFKKLRKTISIVFQFPEYQLFKDTVEKDIMFGPVALGQSKYDARQKAAYYLEMMGLKYPFLERNPFELSGGQKRRVAIAGILAIEPEILIFDEPTAGLDPEGEREMMQLIKTAKQQQRTVFMITHQMENVLEVADVVLVLAKGKLVKAASPYEVFMDQTFLEKTTIVLPPVIQVIKDLIAINAHFNKLIELQPKNLEQLASAINKTIANHG
The following text describes a protein:
Function:
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes; Regulates also the sphingolipid metabolism.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MRCVHCGSPVIGTFVQYSPGNLRLRKCPKCGCVADEYVECEPIIVFVDIVLHKPEAYRHLFFNSNALSSKVVVMAVLLLVVLEACLYDYFSTERAAAISYRSTKMLAKAAVTFSSYITGIWIMHRLFTKKRSSSTSLMDILTAITSSSYFKLFIFAMMIWDFSPHIALVIEVLVLISNGVALQVVLNTSANISMVLVAASAAPTFFWKLFLYYSLWANPQPQL
The following text describes a protein:
Function:
Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. Together with SUVH2 and SUVH9, regulates the silencing of some transposable elements (TEs). Exhibits ATPase activity. May also be involved in the regulation of chromatin architecture/condensation to maintain gene silencing. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair (By similarity). Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa).
Subcellular Localization:
Nucleus. Note=Present in nuclear bodies near chromocenters.
Sequence:
MSHDRSVNVSHDAVIAKPERGTMLQSFSPRSHGSKGYSLPQDSEENRGSVGQSAGQSSTSVVDQVRSPADDAGVTSSSTICPAPVCRQFWKAGSYNDELSSKSQQPNGKNYLHVHPMFLHSNATSHKWAFGAVAELLDNAVDEIQNGATFVIVDKTTNPRDGATALLIQDDGGGMDPQAMRHCMGFGFSDKKSDSAIGRYGNGFKTSTMRLGADVIVFSRHSKNQTLTQSIGLLSYTYLTRTGHDRIVVPILDYEFNASAGEFKTLQDREHFISSLSILLEWSPFSTEAELLQQFDDVGPHGTKVIIYNMWLNSDAKLELDFDSVAEDILIEGSIKKTGSKIVNDHIASRFSYSLRVYLSILYLRIPETFKIILRGKVVEHHNVADDLMHPQYILYKPQAAGSEEALVVTTIGFLKEAPKVNLHGFCVYHKNRLIMPFWQVINYSSSRGRGVVGVLEANFVEPTHNKQDFEKTVLLQKLENRLKEMTVEYWSCHCVLIGYQVNKKPRLQIPQKVQPAGRQALSPPPGFQAVFPQGNTTSLPRVSTQPVLLEKRKEHPDSVASAALKRKVGNDDFTVPGHIRVEQFIHGSASQSQDIETVKLMEENKKLRAKCLDRKVRSQNLEVKAMNLRSELENYKSEYERLMVELQALDLVKDEHRRNVNT
The following text describes a protein:
Function:
Transcriptional activator of the xylanolytic system. Involved in the regulation of extracellular cellulolytic and xylanolytic genes and in the regulation of the intracellular activities of D-xylose catabolic genes in the pentose catabolic pathway (PCP) in response to the presence of D-xylose. Binds to the DNA sequence 5'-GGCTAAA-3' (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSTPSIPQFTSPFSPFSSGSHSTGMAPSQTVGLDTLAEGSQYVLEQLQLSRDAAGSGAGDGAPSTSLRNSMSHTKDQPPFDNEKNQSTGSGFRDALQRDPLVEARSAIRKTSSSAPVRRRISRACDQCNQLRTKCDGQHPCAHCIEFGLTCEYARERKKRGKASKKDLAAAAAAATQGSNGHSGQANASLMGERTSEDSRPGQDVNGTYDSAFESHHLSSQPSHMQHASTAGISGLHESQTAPSHSQPSLGTTIDAMHLNHFNTMNDSGRPAMSISDLRSLPPSVLPPQGLSSGYNASAFALVNPQEPGSPANQFRLGSSAENPTAPFLGLSPPGQSPGWLPLPSPSPANFPSFSLHPFSSTLRYPVLQPVLPHIASIIPQSLACDLLDVYFTSSSSSHLSPLSPYVVGYIFRKQSFLHPTKPRICSPGLLASMLWVAAQTSEAAFLTSPPSARGRVCQKLLELTIGLLRPLVHGPATGEASPNYAANMVINGVALGGFGVSMDQLGAQSSATGAVDDVATYVHLATVVSASEYKAASMRWWTAAWSLARELKLGRELPPNVSHARQDGERDGDGEADKRHPPTLITSLGHGSGSSGINVTEEEREERRRLWWLLYATDRHLALCYNRPLTLLDKECGGLLQPMNDDLWQVGDFAAAAYRQVGPPVECTGHSMYGYFLPLMTILGGIVDLHHAENHPRFGLAFRNSPEWERQVLDVTRQLDTYGRSLKEFEARYTSNLTLGATDNEPVVEGAHLDHTSPSGRSSSTVGSRVSESIVHTRMVVAYGTHIMHVLHILLAGKWDPVNLLEDHDLWISSESFVSAMSHAVGAAEAAAEILEYDPDLSFMPFFFGIYLLQGSFLLLLAADKLQGDASPSVVRACETIVRAHEACVVTLNTEYQRTFRKVMRSALAQVRGRIPEDFGEQQQRRREVLALYRWSGDGSGLAL
The following text describes a protein:
Function:
Involved in floral organ shedding.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDKTDQTAIDESALVLNRTEKSAEAVLRVASMALSITGLVIMIKNSISNEFGSVSYSNIGAFMYLVSANGVCAAYSLLSALAILALPCPISKVQVRTLFLLDQVVTYVVLAAGAVSAETVYLAYYGNIPITWSSACDSYGSFCHNALISVVFTFVVSLLYMLLSLISSYRLFTRFEAP
The following text describes a protein:
Function:
Hydrolyzes allophanate to NH(3) and CO(2). Can also use malonamate, but with much lower efficiency.
Sequence:
MNDRAPHPERSGRVTPDHLTDLASYQAAYAAGTDAADVISDLYARIKEDGENPIWISLLPLESALAMLADAQQRKDKGEALPLFGIPFGVKDNIDVAGLPTTAGCTGFARTPRQHAFVVQRLVDAGAIPIGKTNLDQFATGLNGTRTPFGIPRCVFNENYVSGGSSSGSAVAVANGTVPFSLGTDTAGSGRIPAAFNNLVGLKPTKGLFSGSGLVPAARSLDCISVLAHTVDDALAVARVAAGYDADDAFSRKAGAAALTEKSWPRRFNFGVPAAEHRQFFGDAEAEALFNKAVRKLEEMGGTCISFDYTPFRQAAELLYAGPWVAERLAAIESLADEHPEVLHPVVRDIILSAKRMSAVDTFNGIYRLADLVRAAESTWEKIDVMLLPTAPTIYTVEDMLADPVRLNSNLGFYTNFVNLMDLSAIAVPAGFRTNGLPFGVTFIGRAFEDGAIASLGKAFVEHDLAKGNAATAAPPKDTVAIAVVGAHLSDQPLNHQLTESGGKLRATTRTAPGYALYALRDATPAKPGMLRDQNAVGSIEVEIWDLPVAGFGAFVSEIPAPLGIGTITLEDGSHVKGFLCEPHAIETALDITHYGGWRAYLAAQ
The following text describes a protein:
Function:
Adapter involved in the TLR2 and TLR4 signaling pathways in the innate immune response.
Subcellular Localization:
Cytoplasm. Cell membrane. Membrane.
Sequence:
MASSTSLPAPGSRPKKPLGKMADWFRQTLLKKPKKRPDSPESTSSNTSQPASQDRLSPSLSLVTSPSLPPTHASDSGSSRWSKDYDVCVCHSEEDLVAAQNLVSYLEGSSTSLRCFLQLRDATPGGAIVSELCQALNNSHCRVLLITPGFLQDPWCKYQMLQALTEAPGAEGRTIPLLSGLSRDAYPPELRFMYYVDGRGPDGGFRQVKEAVMRYLQTLS
The following text describes a protein:
Function:
Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile.
Sequence:
MCEAERMEKNYYVCTGCGMLCDDIEVEAEKNIVNKVYTACRVGVAHMKEGTDNAVFRVGDKPVDEATAVSEAVAILKNAKNPLIFGLGTSSNEAQKLAIELAKKTSATLDDPSSFRLGSLVEALLQNRFKTCTLDDVRNKADVTIYWGTNPSDSHPRHLSKHSYFPRGKEKQRGWEEERTAIAIDVRKSHTAKICGNYFFEIPPGGDAEFIDALIAALSGKLPKTSYNFPPKRILELANILKGAKFGVVFVGLGLVYSLENLEPLFRLMDALNEKANFHLIPMVGYSNTRGFNENLFEETGYVNSVKFEDGAVKHGPEYSIVESLKAKTVDAALIIGYDPFSSLPRSIAKNLLEIPVISLNPFETLTSRNAKVYINTAVGGVESGGTATRMDGVKVDFKPVVETKRLSDEAVLKKIMEAL
The following text describes a protein:
Function:
Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MADPDPRYPRSSIEDDFNYGSSVASATVHIRMAFLRKVYSILSLQVLLTTVTSTVFLYFESVRTFVHESPALILLFALGSLGLIFALILNRHKYPLNLYLLFGFTLLEALTVAVVVTFYDVYIILQAFILTTTVFFGLTVYTLQSKKDFSKFGAGLFALLWILCLSGFLKFFFYSEIMELVLAAAGALLFCGFIIYDTHSLMHKLSPEEYVLAAISLYLDIINLFLHLLRFLEAVNKK
The following text describes a protein:
Function:
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Required for elimination of toxic metabolites.
Domain:
The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence:
MEPEHWSFWDTQRLEDEYSPSKWSRRGPADWVFDNHVKLVTQVSNQVKEEIQCDLDIPYGKREGEKFDIFGAQLLPNDAPVFVYIHGGYWQALDRSISSYSVIPQFKAGHIVVVVGYELAPKVGLKDIILEIQSAISAVLKWAAERGSRSVVIAGHSAGSHLASMLLHDPQWQKSEPHLDLLHGMVHISGVFDVIPLVATSMNLPLNLDNETAKLMSPLHCFNQSMEKVLNIKQLLVVGENDPTEFKRQTSTYAQALLRAGFTDVHCKMMDSLDHFNIVEELRNEDYELTRLIVKLIS
The following text describes a protein:
Function:
Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, a regulatory subunit POLA2 and two primase subunits PRIM1 and PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses.
Miscellaneous:
MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Subcellular Localization:
Nucleus. Cytoplasm, cytosol. Note=In the cytosol, colocalizes with RNA:DNA hybrids with a speckled pattern.
Domain:
The CysA-type zinc finger is required for PCNA-binding.
Sequence:
MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDKRNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMILKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEEEQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSFLPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVFLFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEKIATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVMAFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKEVIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWSKIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTERVVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPELPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALTKDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQKQDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDALLGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPLTFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQPEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQFLSRSGYSEVNLSKLFAGCAVKS
The following text describes a protein:
Function:
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of cognate toxin HipA. Also neutralizes the toxic effect of non-cognate toxin YjjJ. Binds to operator sites with the consensus sequence 5-'TATCCN(8)GGATA-3' to repress the hipBA operon promoter; binding of HipB(2) to DNA induces a 70 degree bend. This forces HipA dimerization, which blocks HipA's active site and thus its toxic action. May play a role in biofilm formation.
Sequence:
MMSFQKIYSPTQLANAMKLVRQQNGWTQSELAKKIGIKQATISNFENNPDNTTLTTFFKILQSLELSMTLCDAKNASPESTEQQNLEW
The following text describes a protein:
Function:
Delta(15) fatty acid desaturase capable of converting hexadecadienoic acid into hexadecatrienoic acid (16:3(9Z,12Z,15Z)). The double bond introduced occurred between carbons 15 and 16 resulting in a terminal double bond aliphatic chain. Can also convert linoleic acid (18:2(9Z,12Z)) into alpha-linolenic acid (18:3(9Z,12Z,15Z)). Involved in the biosynthesis of the aliphatic side chain of sorgoleone, a phytotoxic secondary metabolite playing a direct role in allelopathic interactions.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence:
MAATDHEVEEAVAKAREDDKSRRQVDGFDAGKAPPFRIGDVRAAVPEHCWRKSPWRSLWYVVRDVAVVVALGAAAAAMDSWAVWPLYWAVQGTMFWAFFVLGHDCGHGSFSDNATLNSVVGHLLHSFILIPYHGWRISHRTHHQNHGHVDRDESWHPLTERRYRRLPPRAKKLRFTPPFPLLLFPLYLFYRSPGKRGSHFLPSSPLFSPKDKGDVILSTTCWCIMLAFLLAMSCAFGPLQVLKMYGVPYLVSVMWLDLVTYLHHHGHQERLPWYRGEEWSYLRGGLTTVDRDYGWINSIHHDIGTHVIHHLFPQIPHYHLVEATKAAKPVLGRYYREPHKSGPLPLHLLGVLLRSLRVDHFVSDHGDVVYYQTDHHLNDTTTDDAHKQK
The following text describes a protein:
Function:
Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSKRKVTFQDGDSEITLEEEIPKKKMVDGLTGPGSRFKEKHSLDSDEEDEVEDVDNSSKYDILASDDVEGQEGATIDYDEGVRITPFNLDEEMQEGHFDSEGNYFVNKEKDIRDNWLDNIDWVKVKEQPVKKKKGLAAKRKRRVGDEDEAEEEIKREEQRNDSEDEEEEKEKEPAEDPLAAYSHYQLTEAIIELLLPGETVSAALRRLGGLGGQKKKGRQRNGEEEKKEASNRDADKLDKLTALADRLVGIGEFEIYQQTYEKLAYQLKGMTRGKAAKTLGDEEEDKDELDMFGDDFDEKHDADKNEDNDNRKVSDEVMWEYKWENKESSELYGPFSSQQVQDWVDEGYFNDGVYCRRIGQEGASFYNSKRIDFDLYT
The following text describes a protein:
Function:
May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen-III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Sequence:
MSHRHRIVAVLALALPAVSFVSHVPSSRTTRTTISKQPSPIDHRRNSSPHENDVQAKDNSNRDISYGLYVHIPYCRRRCKYCDFAIVPIGKDQTHNIGFQQMDLTYRQSVVDEISLIGSTTPNKIPLRSIYFGGGTPSLAPLTTLREIMRALLEPDDAPFYLENEGDAEITIEMDPGTFNLTYLEAIKAMGFNRISLGVQSFDDDILATMGRVHRSADVYRSIEMIQEVFGEEDSNYSIDLISGVPGLTLAGWTETLYNAVRLHPRPLHISLYDLQVEQGTYFGKIYGDGRKEDSSTAAPVVVASSKSGNATTHPFLPSSEDCAFMYRYASGYLRSKRYQHYEISSYAYVDDDGLAHRSKHNQIYWEVGGQWYAIGLGSTSNVDGVRFARPRALSDYISWTRELKEAYGKDVNAEPPWLQSSNGNGEENVGGEDDISDIIMTRLRTSEGLDLDWIAEHYDTSHVEAILGGFELALDLDLGERVGNSTERVGLIRLKDPNGFLFSNNIISNIFVELDSVEE
The following text describes a protein:
Function:
C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW or WxxC consensus sequence. C-mannosylates RSPO1, a Wnt signaling regulator, preferentially at the first Trp residue in the sequence WxxW (By similarity). C-mannosylates the netrin receptor UNC5A, preferentially at the third tryptophan of WxxWxxWxxC sequence (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The C-terminal luminal region is essential for C-mannosyltransferase activity.
Sequence:
MMSIRQRREIRATEVSEDFPAQEENVKLENKLPSGCTSRRLWKILSLTIGGTIALCIGLLTSVYLATLHENDLWFSNIKEVEREISFRTECGLYYSYYKQMLQAPTLVQGFYGLIYDNKTESMKTINLLQRMNIYQEVFLSILYRVLPVQKYLEPVYFYIYTLFGLQAIYVTALYITSWLLSGTWLSGLLAAFWYVTNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLDSLDMLPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTGSFLNRLGKLLLHLFMVLCLTLFLNNIIKKILNLKSDEHIFKFLKAKFGLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVAFHNLSDSTNQQSVGKMEKGTVDLKPETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSPEIWELLLKSVHLYNPKRICIMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNHPHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHMMDGPGENDPDLKPADHPRFCEEIKRNLPPYVAYFTRVFQNKTFHVYKLSRNK
The following text describes a protein:
Function:
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB24 is an atypical RAB protein that presents low GTPase activity and thereby exists predominantly in the GTP-bound active state. RAB24 is required for the clearance of late autophagic vacuoles under basal conditions. It is not needed for starvation-induced autophagy. Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation, possibly through regulation of kinetochore-microtubule interaction.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytosol. Cytoplasm, perinuclear region. Cytoplasmic vesicle, autophagosome membrane. Membrane; Lipid-anchor.
Sequence:
DGPLRVPRWSPGRVSQGLPAVRSRPPSSPPCPRAVPPGLGPRGVPTAPLSPRSSLYPHIPHVALPSPERLPHIRRPNVPHASVPASSCPITSPARGLPRVPISDPSVPPLGPTVPPPLPLQTIGAAFVAKVLSVGEQTVTLGIWDTAGSERYEAMSRIYYRGARAAIVCYDLTNSSSFQRAKFWVNELQNCEEGCRIYLCGTKSDLLEEDRRKRDVDFHDVQDYADEVKAELFETSSKTGQNVDELFQKVAEDYVHFTAFQEMTEEKGVDLGQKSSSYLYSCCHH
The following text describes a protein:
Function:
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding.
Sequence:
MFCKEASSSLQTLNIAKSLSSEFTKPSALVNPLSAGHRYKLFPRPNLRGRCTVTTSKFDIDWIAKDNVKKIKVKGIITAKQGLLPSVGVTDLLGVSLLVELISAETDPRTLMKKDPVKDNARRVLLDAHGEDQYECVFDMPEDFGPVGAIRVLNQDLKEIFLKEMKLELPDGSVTFTFNSWVAPKSEDPTKRTFFSNKSYLPLKTPEPLKQLRKQELETLQGKNRERAGEFEKFERVYDYDVYNDLGSPDKDPELARPILGGLSHPYPRRCKTGRKPCDKDPSAETRKALEFYVPRDEEFTTVKGAQFTGTAVLAALPAVFPQIEAALVDPNMPFPHFKSIEDLFEEGIELPKDAGLFPVIPRLVKAAAEADDILQFESPSLLDKDRFSWIRDDEFARQTLAGLNPYCIQLVQEWPLKSKLDPAVYGDPNSLITSEIVEREIKGFMSFDEALENKRLFMLDYHDLLLPYVNKVRELDDSTLYASRALFFLSDDSTLRPVAIELTRPQDKTRPQWRHVFTPGYDATSCWLWTLAKTHAISHDAGYHQLISHWLRTHCCIEPYIIAANRQLSAMHPLYRLLHPHFRYTMEINARARQVLINEGGIIESCFWPGKYSLELSSDVYDKLWRFDREGLPADLISRGLAVEDETAEHGVRLTIPDFPFANDGLMLWDALKEWVTDYVNHYYPDSEQVTLDEELQGWWSEVRNIGHGDKKNEPWWPDLKTQDDLIGVVTTIAWVASGHHAAWPTDEELKEFYEDPEKTMLKTFPSKKQATKVMLTLDLLSAHSPDEEYLGENPEASWAHEPVIYAAYERFKGKLQYLEGVIDERNVNVSLKNRTGAGVVKYELLKPISEPGVTGMGVPYSVSI
The following text describes a protein:
Function:
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. YHC1/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
Miscellaneous:
MISCELLANEOUS: Present with 2140 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MTRYYCEYCHSYLTHDTLSVRKSHLVGKNHLRITADYYRNKARDIINKHNHKRRHIGKRGRKERENSSQNETLKVTCLSNKEKRHIMHVKKMNQKELAQTSIDTLKLLYDGSPGYSKVFVDANRFDIGDLVKASKLPQRANEKSAHHSFKQTSRSRDETCESNPFPRLNNPKKLEPPKILSQWSNTIPKTSIFYSVDILQTTIKESKKRMHSDGIRKPSSANGYKRRRYGN
The following text describes a protein:
Function:
Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells.
Subcellular Localization:
Secreted.
Sequence:
MRALLSACFCFWATTVLLLGVDSFPVGDSSGEDELGDEPQTSSQEYSPQRACTGLFWGLHSTASGWKKELCKEQNACKGSMEMLVQNNLHLPKITPEDGCSYTGFQKETCLRRLSSGLYAYQAYLEYIDDAFSKTVQMSGSLWPRTRQLADILKSMMNNPDIVTMLPPVTQDMVSIKLREQKAWNITVIKFLILQDFISFLEKTARAFCRS
The following text describes a protein:
Function:
This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells.
Subcellular Localization:
Cell membrane; Single-pass type III membrane protein. Note=Linked to the membrane via band 4.1.
Sequence:
MWSTRSPNSTAWPLSLEPDPGMASASTTMHTTTIAEPDPGMSGWPDGRMETSTPTIMDIVVIAGVIAAVAIVLVSLLFVMLRYMYRHKGTYHTNEAKGTEFAESADAALQGDPALQDAGDSSRKEYFI
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKGLAAADASMSGPAIAFMCMGYMATFFLFYFHFCKVKKMNEDGQVGETKILPFYFVLLNCLVWTLFAFVDIKADWAVFILNGLGVLMMAYCFWSVARLDQNIRLYASIFVSAELLGVLILSILIFTKLKTVEDRKYWLGLIGGIAGAVMYIVSVVTDTLALLGRQGDVEQDVGEDFGMLCASMVNTICWCAYGALYGGKYMVVANGIGLILCLVQSGIYIWKKHGIIARIADINWADAYTSLGDSLRGLTPAAS
The following text describes a protein:
Function:
Component of the phenyllactate dehydratase complex FldABC that is involved in the fermentation of L-phenylalanine via a Stickland reaction. This complex catalyzes the reversible syn-dehydration of (R)-phenyllactate to (E)-cinnamate in two steps, a CoA-transfer from cinnamoyl-CoA to phenyllactate, catalyzed by FldA, followed by the dehydration of phenyllactyl-CoA to cinnamoyl-CoA, catalyzed by FldB and FldC. Requires the activator FldI to initiate catalysis.
Sequence:
MSNSDKFFNDFKDIVENPKKYIMKHMEQTGQKAIGCMPLYTPEELVLAAGMFPVGVWGSNTELSKAKTYFPAFICSILQTTLENALNGEYDMLSGMMITNYCDSLKCMGQNFKLTVENIEFIPVTVPQNRKMEAGKEFLKSQYKMNIEQLEKISGNKITDESLEKAIEIYDEHRKVMNDFSMLASKYPGIITPTKRNYVMKSAYYMDKKEHTEKVRQLMDEIKAIEPKPFEGKRVITTGIIADSEDLLKILEENNIAIVGDDIAHESRQYRTLTPEANTPMDRLAEQFANRECSTLYDPEKKRGQYIVEMAKERKADGIIFFMTKFCDPEEYDYPQMKKDFEEAGIPHVLIETDMQMKNYEQARTAIQAFSETL