lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable multifunctional globin with a hexacoordinated heme iron required for the catalysis of various reactions depending on redox condition of the cell as well as oxygen availability. Has a nitric oxide dioxygenase (NOD) activity and is most probably involved in cell-mediated and oxygen-dependent nitric oxide consumption. By scavenging this second messenger may regulate several biological processes including endothelium-mediated vasodilation and vascular tone. Under normoxic conditions functions as a nitric oxide dioxygenase (NOD) but under hypoxic conditions the globin may switch its function to that of a nitrite (NO2) reductase (NiR), generating nitric oxide. Could also have peroxidase and superoxide dismutase activities, detoxifying reactive oxygen species and protecting cells against oxidative stress. Also binds dioxygen with low affinity and could function as an oxygen sensor but has probably no function as a respiratory oxygen carrier.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
TLQSLGSRTLGAAPRLPAAGWGRPGAGGSFVLTAAPLEGLASAPSGGRPRRSCLGVFDFESVPRRVKGAHTHPPRHRPQREPGHGAPRPARAGAHSCAARATPPRVTAPSSRDPQHTRHTYTPAPPGGQTPRWPCGWAGASRVPPPPPSLHLARIGSRTRGWGFGADLFFFTFFQQTTFPPPARGPPPPPRTYTLHTHTHTHTHTHTRRAQTDTLPPSGALYPSLARPPSTQPAPAPRAPPPPSEAGLGLELLMEKVPGEMEIERRERSEELSEAERKAVQATWARLYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEEPLEMERSPQLRKHACRVMGALNTVVENLHDPEKVSSVLALVGKAHALKHKVEPVYFKILSGVILEVIAEEFADDFPAETQRAWAKLRSLIYSHVTAAYKEVGWVQQVPNATTPPPTLPSSGP
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.
Sequence:
MRVWVLAPHSLPPASFRPIFEARPPSSPTHSFHLLPTPIYLYITCTDAVDLYVCAVTSLLAEWTTTMFARSTIRWAAGAGHAFMDIAIGSQPPHRVTFELFTKRCPIASENFLKLCTGENVLPQVSSIDGIGEPSFRDQFLPQLTYRNTTVHRVCKGYLVQGGDIVSGQGTGQLSIYGESFDAPEEVKASKFDRMGLLGTAVSAPHLNGSQFFILTADKAPHLNGTCICFGRVVDGWTVVKAIEAIPLTAAGEPAERVVVVECGKL
The following text describes a protein:
Function:
Probable transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MELDDLDLSGSWPLDQITFASNFKSPVIFSSSEQPFSPLWSFSETSGDVGGELYSAAVAPTRFTDYSVLLASSESETTTKENNQVPSPSWGIMPLENPDSYCAIKAKMTQALRYFKESTGQQHVLAQVWAPVKNRGRYVLTTSGQPFVLGPNSNGLNQYRMVSLTYMFSLDGERDGELGLPGRVFRKKLPEWTPNVQYYSSKEFSRLGHALHYNVQGTLALPVFEPSRQLCVGVVELIMTSPKINYAPEVEKVCKALEAVNLKTSEILNHETTQICNEGRQNALAEILEILTVVCETYKLPLAQTWVPCRHRSVLAFGGGFKKSCSSFDGSCMGKVCMSTSDLAVYVVDAHVWGFRDACAEHHLQKGQGVAGRAFQSGNLCFCRDVTRFCKTDYPLVHYARMFKLTSCFAVCLKSTYTGDDEYVLEFFLPPAITDKSEQDCLLGSLLQTMKQHYSSLKVVSETELCENNMSLEVVEASEDGMVYSKLEPIRIHHPAQISKDYLELNAPEQKVSLNSDFMENNEVDDGVERFQTLDPIPEAKTVKKSERKRGKTEKTISLEVLQQYFAGSLKDAAKSLGVCPTTMKRICRQHGISRWPSRKINKVNRSLTRLKHVIDSVQGADGSLNLTSLSPRPWPHQIPPIDIQLAKNCPPTSTSPLSNLQDVKIENRDAEDSAGSSTSRASCKVNPICETRFRLPTHNQEPSRQVALDDSDSSSKNMTNFWAHLTCQDTASPTILQHKLVSIKATYREDIIRFKISPESVSITELKQQVAKRLKLETAAFELKYLDDDREWVSVSCDADLSECLDTSAAKANTLRLSVHDVTFNFGSSCESSEETMMCL
The following text describes a protein:
Function:
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence:
MKFNKILATALGRKPKIAANKGTNVTDKKIDQLLIRDMEEILESWELPSLLGSEEEEEEEEEEEEEEEEEEDNVGGGSENLRCIHVKDEDSWQILVSKSSASEQSHMFHEVLSFWRKKEKEESELKSKEESELKSKENGRFSSSMASSELPTQKVGSENSTNEAVVVFVLGGPGSGKGTQCPKIVEHFGFTNICAGELLQAEVESGSENGEMILKFREEGKIVPSEITMKLLQQAMQQSEKKKFLIDGFPRNEENRTAFENTMKIEPDLVLFFDCPSEVLTKRLLSRNQGRVDDNIYTIQKRLEVYFESTLPVINYYSSKGKVEKIDAQRSIDEVFEDVKGVFSKLKPKSVVGLKNECNILQIGAQVSSII
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MRSATTTAFSLLVYFLLVAFSLGNNKNGSIDDDCNMIMWRIGAIFDPTTRVGKEQKVAMEIAVDEFNSRNSKCSELVINFAYSHAPAASLANYLVNKKQVHAILGPLTHQEAALFSDFGDEAYKGIPIISLSPAVSYSTILPTEPPSLIQMSSDVNSQMQCFAALIGYFKWRKVIAFYEISNSFSNMDVGLITHLSDSLKVVDSSIEHHLAFPPLSSLSSSKSFIQEELVKLRTKNVKVFVLIQCSLDFGLVLFEMANEMGMMGKDYVWIISDNMASLLDSVEPSALLNMQGVIGFKANVNEKNDSFGEFNVKFRRKYRSEYPEEDGYPSPSSYALKAYDATWATGKAMQKLSKSNSSELMKSILLSDFEGLSGKVNFKNGKLYRNQTYRIINVFGKSYREVSFWTPEFGFSDLVESNEMKMRIENGLGWALGSILWPGGKQTVPKGWTIGGVDKPLKIGVPAGGVFNQFVTIKFNQERNETLISGFSVHVFEAVVRQLPYYLPYVLVPFYGTYDDMVVGVSNKSLDAAVGDTEIMPYRYELAEFSQPYIDSGLVMVVTERPRLKKAHFIVIKAFKLKLWILLAVMSMSTGAVIWLNEYVSDNPDFSGSFPQLIGSMLWFSVTVLSFSQPCFTALLSSIMTVPRLEPSVLGVDYLIKTNAAVGCNNKSFIIRYLVNLQFKPENIKEISSFSDYPKAFEKGEISAAFFEAPHAKVFLAKNCKGYTKSGPVYKLGGFGFVFPKGSPLVVDISEAVLKVTQSGEINQLEEQMLISSNCSSPSAEEQGPGLGPELFSGPLLISGVICGIVLLISIARFVRKYWLYISSIIANNAKPALRWASLVLTRCYTRIVRPRSVKDSNTVIEQRPNAQQNVEITEVF
The following text describes a protein:
Function:
Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism).
Sequence:
MFDFASYHRAATLADAINLLADNPQAKLLAGGTDVLIQLHHHNDRYRHIVDIHNLAELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPRGVRFVPINGFHTGPGKVSLEHDEILVAFHFPPQPKEHAGSAHFKYAMRDAMDISTIGCAAHCRLDNGNFSELRLAFGVAAPTPIRCQHAEQTAQNAPLNLQTLEAISESVLQDVAPRSSWRASKEFRLHLIQTMTKKVISEAVAAAGGKLQ
The following text describes a protein:
Function:
Has acyl-CoA dehydrogenase activity on a number of substrates. N-octanoyl-CoA is the best tested, but n-lauroyl-CoA, n-palmitoyl-CoA and isovaleryl-CoA were also used.
Sequence:
MTDTSFIESEERQALRKAVASWVANYGHEYYLDKARKHEHTSELWAEAGKLGFLGVNLPEEYGGGGAGMYELSLVMEEMAAAGSALLLMVVSPAINGTIIAKFGTDDQKKRWLPGIADGSLTMAFAITEPDAGSNSHKITTTARRDGSDWIIKGQKVFISGIDQAQAVLVVGRSEEAKTGKLRPALFVVPTDAPGFSYTPIEMELVSPERQFQVFLDDVRLPADALVGAEDAAIAQLFAGLNPERIMGAASAVGMGRFALGRAVDYVKTRKVWSTPIGAHQGLAHPLAQCHIEVELAKLMTQKAATLYDHGDDFGAAEAANMAKYAAAEASSRAVDQAVQSMGGNGLTKEYGVAAMMTSARLARIAPISREMVLNFVAQTSLGLPRSY
The following text describes a protein:
Function:
Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (By similarity). Negatively regulates ER-Golgi protein transport. Probably in association with MTMR9, plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3-phosphate in membrane ruffles. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+) T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3-phosphate. Negatively regulates proliferation of reactivated CD4(+) T-cells. In complex with MTMR9, negatively regulates DNA damage-induced apoptosis. The formation of the MTMR6-MTMR9 complex stabilizes both MTMR6 and MTMR9 protein levels (By similarity).
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum-Golgi intermediate compartment. Cytoplasm, perinuclear region. Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR9 to the perinuclear region (By similarity). Partially localizes to the endoplasmic reticulum (By similarity). Co-localizes with RAB1B to the endoplasmic reticulum-Golgi intermediate compartment and to the peri-Golgi region.
Domain:
The GRAM domain is required for cell membrane localization; The C-terminus domain (aa 540-655) mediates interaction with MTMR9.
Sequence:
MEHIRTTKVEQVKLLDRFSTNNKSLTGTLYLTATHLLFIDAHQKETWILHHHIASVEKLALTTSGCPLVIQCKNFRIVHFIVPRERDCHDIYNSLLQLSKQAKYEDLYAFSYNPKQNDTERLNGWQLIDLAAEYERMGVPNANWQLSDANREYKVCETYPRELYVPRTASRPVIVGSSNFRSKGRLPVLSYCQQGTEAAICRCSQPLSGFSARCLEDEHLLQAISKANPGNRYMYVVDTRPKLRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDEKKRLNAMANRAAGKGYENEDNYSNIRFQFVGIENIHVMRSSLQKLLEVNGSKGLSVNDFYSGLESSGWLRHIKAVLDAAIFLAKAIVVENASVLVHCSDGWDRTSQVCSLGSLLLDSYYRTMKGFMVLIEKDWISFGHKFSERCGHLDGDPKEVSPVFTQFLECVWHLTEQFPQAFEFNEAFLLQIHEHIHSCQFGNFLGNCQKEREELRLKEKTYSLWPFLLADKKKYLNPLYSSKSQRLTVLEPNTASFNFKFWRNMYHQFDRTLHPRQSVLNIIMNMNEQNKQLEEDVKDLEAKIKQCKSGILTKDLLHAVHPESPSLKTSLCLKEQSLLPVKDTLRAVEGSSPADNRYCDYTEEFSKSEPAVVSLEYGVARMTC
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.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MAQYVKKDDDLDEEEYSPFCGIEKGAVLQEARVFNDPQLDSRRCSQVITKLLYLLNQGDTFTKTEATEVFFSVTKLFQARDIGLRRMVYLIIKELSPSSDEVIIVTSSLMKDMNSKTDVYRANAIRVLCRITDGTLLTQIERYLKQAIVDKNPVVASAALVSGIHLLQTNPEIVKRWSNEVQEAVQSRAALVQFHALALLQQIRQNDRLAVSKLVTSLTKGTVRSPLAQCLLIRYTSQVIRESSMNGQTGDRPFYDYLEGCLRHKSEMVIFEAARAITELSGVTSRELTPAITVLQLFLSSSKPVLRFAAVRTLNKVAMTHPMAVTTCNIDMESLISDQNRSIATLAITTLLKTGNESGVDRLMKQITSFMSDIADEFKIVVVDAIRSLCLKFPLKFRTLMNFLSSILREEGGFEYKKAIVDSIVTIITDVPDAKEGGLLHLCEFIEDCEFTYLSTQILHFLGNEGPKTSDPSKYIRYIYNRVILENATVRASAVSTLAKFGAMVDSLKPRIFVLLRRCLYDNDDEVRDRATLYLNTIGGDGSVVETDKDVKGFLFGSLDLPLANLETSLKNYEPSEEPFDISSVSKAIKSQPFAEKKAAAKKPTGLGAPPAGPTSTADTYEKLLLSIPEFSTFGPLFKSSAPVELTESETEYEVNVVKHIFDKHVVFQFNCTNTIPEQLLENVTVVVDASEAEEFEEVATKPLTSLPYGTPGQTFVAFEKPEGVPAVGKFTNVLRFIVKEVDPSTGEAEEEDGVEDEYQLEEFEVVAADYMLKVGVSNFRNAWESLGPDFERVDEYGLGPRESLKEAVSAVINLLGMQPCEGTEVVAANSRSHTCLLSGVYIGNVKVAVRLSFGVDSAKEVAMKLAVRSEDEAVSDAIHELVAN
The following text describes a protein:
Function:
Catalyzes the conversion of L-asparagine to L-aspartate and ammonium.
Miscellaneous:
MISCELLANEOUS: B.subtilis contains two L-asparaginase isoenzymes: L-asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-asparaginase II, a high-affinity secreted enzyme.
Sequence:
MKKQRMLVLFTALLFVFTGCSHSPETKESPKEKAQTQKVSSASASEKKDLPNIRILATGGTIAGADQSKTSTTEYKAGVVGVESLIEAVPEMKDIANVSGEQIVNVGSTNIDNKILLKLAKRINHLLASDDVDGIVVTHGTDTLEETAYFLNLTVKSDKPVVIVGSMRPSTAISADGPSNLYNAVKVAGAPEAKGKGTLVVLNDRIASARYVTKTNTTTTDTFKSEEMGFVGTIADDIYFNNEITRKHTKDTDFSVSNLDELPQVDIIYGYQNDGSYLFDAAVKAGAKGIVFAGSGNGSLSDAAEKGADSAVKKGVTVVRSTRTGNGVVTPNQDYAEKDLLASNSLNPQKARMLLMLALTKTNDPQKIQAYFNEY
The following text describes a protein:
Function:
Involved in telomere capping.
Subcellular Localization:
Cytoplasm.
Sequence:
MAETKEQTDDVETLMASLDQLGMEADPTSKEFNNDDSKIGAPSEVQDEKELLEFLDQLENDEEKNEKNPIEEANEENESVAATSNERQQHDASNQPSQAAQTTINKNTESATPKTVNEINKSQEFQEHVETPKQSNWLGGFWSTASAAVRSAEQRVRSIKGFEENANWDINVRNMVDLNKLGDLSNGIRSKALPTLSNTIHNVLNVVAPPIHDHEVLQVTVFHDLAGFAHLDRIVYESFEKVMFQVEGGELTVLLDKEAKVRPRTNDVYEDFGLCNGYLEAKKLAKANLAEPITEAKKMNKENKQENVGAGDDEDASESPMVRVTHLLLVIQAFTIKNKEVSDDEQLCFLIHLNDTNHNLEFSTTSQPLPLEWQRWAVDPRYIKLFGSNAILPNEWVTEWVEQSISVAAGIVAQMYTSKRMALGDPSLFAGLPEEDVNTGSSETPVPYYDGAMYA
The following text describes a protein:
Function:
Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Hemokinin induces plasma extravasation, mast cell degranulation, muscle contraction, salivary secretion and scratching behavior. Increases sperm motility. Induces potent analgesic effects and may play a role in pain modulation. Promotes survival of bone marrow B lineage cells and of cultured LPS-stimulated pre-B cells and may act as an autocrine factor required for B-cell survival and proliferation. Lowers systemic arterial pressure following intravenous injection. Induces interferon-gamma production and may play a role in the inflammatory response. Shows potent affinity and specificity for the NK-1 receptor.
Subcellular Localization:
Secreted.
Sequence:
MLPLLALFLLIGPAVSTTTRDREDLTFGAEAESWVTVNLKGIPVPSIELKLQELKRSRTRQFYGLMGKRVEGVHPIQSAERTGYQLGRIVQDLLGTRGLSIEGSCRQETNHQSAGPGAVARESLQSQRGRSEPPNHQQHVALSLGTEEDDQSSERAPRDASQMMPRPSRP
The following text describes a protein:
Function:
Magnesium transporter that may mediate the influx of magnesium.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MEKKDPLEACVRCGDREGSGAWRRVKDGGIYQFLCRACTLLYMGCPHCLVVFQENAGSGEDWIACCRCQRSVHARCETEANPASLPLEPPTFVCCECRRGEEQPSVKKPRAIDMIQGHQEQELERSPEDVLAAARDAAAQALKAAVTAKAAAAAKAAAAVKAAMLARNALNNAALAAKEDLLIAKSLGESLRGTLNERSKEQLSRFSILCDSRESFGSTHENHLSGIIGIGVRKRAGSIGSGAGLLAISCRWINGAAGSRFNSDDGGKRYSVIKIDKNGVWETLSLSLTELGIHPRDMDVITGNSFIPSRATLALRYDKVLVRMENVRALVSRDFCLLFDAHRRRQPREAVVPTKKVETDVTHKLAAFYLTTFTRLTVVAERALEDLTLGVSTGRLQRLLPLKRSLTEVEHDIRDTHEVMDQVLNSEEMLRSFCLEVPASCVDVDSEKAKAKVRQLAADMLFTYLREIDDAGAVLEELRKEMDAAQEVWELGLDATRNRIITTNLYISFATLSFSLATLPGSFFGMNVTNGWENDLNMFRLIAGTTLCTATILGVALIVGFRVWPRFVDRRRAQEHAALLDLLQHIDDIEEIFRDIELKAGGRNISKEQFHQILRSHPSSRFMRQASERKFTSQRMPKAG
The following text describes a protein:
Function:
Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.
Sequence:
MWVHPIDSRYGSELMRAIFRQENRIKLMARVEALYARALAERGFIPKEAAEAIERAAEEVTPEDVRAEEALVKHETMALVRAISKRAGRYGEYLHLGLTSNDVLDTVMGVQIRQAGSIILRSSASLLEKIVKRGEESLDIVCLGRTHGVVADPIPLSMKFALWSYYVRRSIARFMDSLNEASVGKLRGAVGTAAASIELGIKDPLEVESEVLAALGLSPPEITTQVVPRDRLAHLILSMSLFSSALDTIANEIRNLHRTEISEVKEHFEERQVGSSTMPHKMNPINSEKVCGLARLMRSLAIAALENVVLEHERDLTNSSVERAILPEAFLILEEQINTLSAVIENLEIDRVRIGENLEKYGDIALSERLMIWLVKKGLGRQEAHEIVRSISLRSHRSGRRFIDEVLADESLSKILRPEEIEAIFSPRSYLGLGRELSIEEFRAAREFLKEVLLNG
The following text describes a protein:
Function:
Transporter, which promotes the endocytosis-mediated degradation of hedgehog-related proteins such as grl-7 in order to establish the capacity of progenitor cells to maintain quiescence in arrested L1 stage larvae.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Note=Localizes to the apical cell membrane during the 3-fold stage during embryogenesis.
Sequence:
MKSISQCLGNVSLWIEQQTHDMFYWVGLKIADYPKWTLFITTIWALLMAGGVVRFKEVNNVRDHFSATNSPSRYEYRVAREFFQELGSPFHVVVAMQAADGGSLLRPKYIDKALEIEDFLQYKLKGSFGNQSYSYSDFCGTQCETSDAVSIFLSMFRDQQIKKTAHVKLTYPSMDVFGHRVYLANNIFQVKINNRSSIIEESKLVAINFHAIYNNETMYEIMKEWEQKLFAYTLSTENDPLIRVYVTSEGLVSEEVRRTGILAMPLMGVTFLIILAFTILTTLKRDPVKSKPFEAFLGVICPILSLCASFGHLFWMGFEYLPIVTVVPFLILSIGVDDVFIFIHAWHRTPYKHSVRDRMAETLADAGPSISITSLTNLLSFAIGIFTPTPAIYTFCVFISTAVIYDYIYQIFFFSAVLVLSGEREEQRKNAYLWWKDVPLPEEPTGKQKKETIVSRVLGKVLDFWVDFIMAKWSKFLIGAIMITYWIFMARGVMEIAVGLSSEKLFLDDSPLLPLVRLQTNVIFKEGGQVAVFVNNPGNMSEPDAVPEIMRILRRFEVANNSVGAASTHMWLLPYLPYVGEQEHGSIEFKYRYLPEFFKLTEFRRWSHFVNLGNHQDCLSEKPSCLQKFVFSTGFHDAVSWSDRLALLENWREMASEYQHLNLTIYEDFSMYSDQLLTIVPVTQSTVFCALICMIMILTLFTPSPVTIVTSTAAVLSINLGVFGCLVYMNIDLDPISMTTLLMAIGFSVDFVAHITWHYYKGDFHSKRARIRHALAGIAWPMFQAGTSTMLAITVLALVHAYMVQVFVKVVVLVIFLGMFHGLVVLPIVFSALPFTKTSGPQKKKVAPLQMHEAGPIPKKEEPKVIKVNGEEDEEDEKTTKEEPVEKSVRSAERA
The following text describes a protein:
Function:
Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MYRLLSVASVPLLASLVHGYADPGACSGVCTTHDPGLIRRESDGTYFLFSTGNKISYVSASSIEGPWTSVGSMLPDGSSIDLDGNDDLWAPDVSYVDGLYYVYYAVSTFGSQDSAIGLATSETMEYGSWTDHGSTGIASSSAKIYNAIDPNLIYADGTYYINFGSFWDDIYQVPMKSTPTAAASSSYNLAYDPSGTHAEEGSYMFQYGDYYYLFYSAGICCGYDTSMPASGEEYHIKVCRSTSPTGDFVDSDGTACTDGGGTMVLESHGEVYGPGGQGVYDDPNLGPVLYYHYMNTTIGYADSDAQFGWNTIDFSSGWPVV
The following text describes a protein:
Function:
Regulator of red blood cell formation.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Domain:
The extracellular domain carries the Vel antigen.
Sequence:
MQPQESHVHYSRWEDGSRDGVSLGAVSSTEEASRCRRISQRLCTGKLGIAMKVLGGVALFWIIFILGYLTGYYVHKCK
The following text describes a protein:
Function:
Involved in cardiac morphogenesis, including heart midline formation, cardiac tubule looping, myocardial formation and maintenance of heart beat speed and rhythm. May protect actin filaments from depolymerization (By similarity). May play a role in development of normal skeletal muscle morphology, muscle fiber type composition and regulation of muscle satellite cell activation and survival (By similarity).
Subcellular Localization:
Cell junction, adherens junction. Cell junction, desmosome. Note=Colocalizes with actin stress fibers.
Domain:
Xin repeats bind F-actin.
Sequence:
MAEPQKSSKVAIKKMEDDLPPPPIPDSIQVIAPASQDPNPLPVPPPKQAFSKFYQQRQVNELKRLYRHMHPELRKNLEEAVTEDLAEMLNTEDPNAQGSVNLDKVLPGEVQSMRWIFENWALDSIGDHQATKKMMEDEIIPGGDVKSTSLRFENQSVNGDYLSTTAKVSETDLARGDVHTARWLFETQPLDSLNKLYSDETEMQEAVLKEPVQGGDVKGAKELFEAQSLDAIGRCCSVEEKSILQLKSEIQELKGDVKKTIRLFQTEPLCAIRDKTGNIHEIKSVCREEIQSNAVRTARWLFETQPLDTINKDTSKVQIIRGISLEEIGRPDVSGARWIFETQPLDAIREITVEEQDFKASTDFVTGADVTKQRLLFGTQALDSLKGEASESVAAKEQVIGGDVKSTLWLFETQPMETLKDNVEVGHLKKVELSAEEKGDVKQRKHVFETCPLGSISKAFEEEISAASTEEVVKGDVKSFKTLFETLPLDSIKEVDAEPITKEEEKIPPGNVKANQILFETTPLYAIKDSFGNFHEVTSVSREQVISGDVKKYKWMFETRPLDQFDESTKKVDIIRGITKQEVVAGDVRTAKWLFETQPMDVIHHQATQGEEHPSMKREISQRGDVKTCRWLFETQPMHTLYEKAEKKQEEDVSVPQADVKSYTWMFETQPLDSLKGQEEQYLRVSKAYSQDELQGVDVKTVRHLFETEPLGSSVVSEADQKKTLRYSSRVEIQSGEVSRVKEFFEAKPLDTTTKPTAVIKDDGTIEAGSVHKFTWLFENYPMDTLKDSSEGIQEIPPEKDIKGGDVGGKRFIFETYSLDQIHDKVDETELHKIQKDTMSKANVKSCTMLFESQPLYAIQDKEGGYHEVTSVQKEEIMKGDVKGARWLFETKPLDQIKKEEEVFVIRAVTQEDIKKGDVQAARWRFETEPLDSFPGGKISVPRTVDDVQKGDVQSNKQLFESQQVGQKKYVRMVSVSDVQRGDVRTSTWLFENQPVDSLYGDADRSSSISTVQREDSQKGDVKRCTWLFETQPMDTLKDPEVTVSTGTQEPIPRADVKSTTWLFESTPLDKFSASECSRETELKERTMRETLETLCTCQAIQHDGILIEANDTESVKMVKYQLSSPGAPEILKEEIVRGHLQGIMLQLLHRTNVEPQSVLVEEDREGKIKVSSLQLLDQSEAIKGKEDLSGNVAKALQSLLSQDASIKKGMVIQETKSESVKMTLYSLLFHSVQQKVVKGDVKSTIGNLMASSQEQRATVTVKREDNEKGNVQLFASCIEKGDLDYLKNLQQESEIQSLISAQAEQGAAESAPRALQSTNTHVLANKEQVEKVMAEAKSGALEGAKMVFACESTGKEGALEREVVHAVGVTGTTVQCLGKPQNLPTGMEKEEIMSGGLKVTTKSIQRVADVSKNTEKEESISACLKEPKATMQGIAQAKVTAERNEVVGEQQSLVTEQASQKQSEEKVLGNDLQAAMQSLRLATAEARNIQHHVQSKLQRNREEVHMACRQQVASKQETKTLQSTIHQQESASTMRENTSTAIRTSTTRVQEASRTHTSVSQKSIASHKKVSASEEVQGGQLLSQENQVVPSRDVSIKDGLYTATPVKTYINPFVESDYKEQSVQEERDVIIRGDVQTAIRALQSAATEQRLVEKEDIVRGNLKATLQSLEKSNVNVSKGDFKAAMIYRNAGQSYSVCKKKSETQVNNNQTAVVASGSQADNDFPPPPPVAVMKAEHCPPSTKATREGAPPLLTSKDEAPGCFSPLQTPLPPPPSLSCKPSDQNSTEKPKIPPKPEITAPLRKKPVPPPKPEHLLHEAYSASTNNSTNRSTKSVPPPVPPKPPGLREISMPKPPPAELQLSCTEVCEQSDHRESQDKCCTLESSMDKSITVHGPERKLPKYTAKTPLQMAEERYKARKGGQGKFELDRAKPSKPVKNGEVG
The following text describes a protein:
Function:
This enzyme is required for electron transfer from NADP to cytochrome P450.
Subcellular Localization:
Endoplasmic reticulum membrane.
Sequence:
MEMVLEYVDLIESLIIDNLGAIIIVVVIVGTYLYMNKPPPPPPIPQNKKAPIKPQRTESNKGGKKENKEKEKVMKIFFGTQTRTAEDFSRIIEKESKKIGIPCEVVDLESYDVEDLANEWFVMFLVSTHGEGDPTDNAKEFYLWLTNDERPTDLLTGVPFTVFGLGNKTYEHYNAVARVIDRRMEELGAKRAFERGEGDDDATLEEDFNHWKKRMWPVICPFLGYELKATDEDKFVPRFRMVTLDSENKDITNPFLKVVPTISKPKTSVDGKTIYDIKNPYYATITENRELHSSESDRSCRHIEFALGGAVTYQTGDHLGIYPINDGELVEKLIQRLGVNGEEIISLIPADQEGNIIKASFGPMSIRKALSEHFDITNPPRKSVLRTLSEYTTDEQEKKKLLRLASEEASEEYNQFIKHDFRSIGELLDNFPNLKPNIAHFLEFIPRLPARYYSISSSPNHKKDTVSITSVVVNFTTPTSRFHNGVASTWLSNLKVGDKVPLFVRESHFRLPSNTNKPVIMVGPGTGLAPFRGFLQEMQHKSVNSSESLLFFGCRSDTIDYLYKEELEQYKSTGVIGDLIVAFSRKTNEKVYVQNKIMEHKHKVWDLIHNKGAHFYICGDARNMAKSVQQSLVSLIKELGSKDDNSAQQYIEDMESVKKIINISSIVGFYSRQCGFSIYSSTKFAVEAITEGLQEDVIHVSSILPGYF
The following text describes a protein:
Function:
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Miscellaneous:
MISCELLANEOUS: This protein is not essential for chromate resistance, however it may contribute to resistance under certain environmental conditions.
Sequence:
MLYEMKPLGCEPAKLTGLSEKLIFSHYENNYGGAVKRLNAITATLAELDMATAPVFTLNGLKREELIATNSMILHEVYFDSLGDGGSLDGALKTAIERDFGSVERWQAEFTAMGKALGGGSGWVLLTYSPRDGRLVNQWASDHAHTLAGGTPVLALDMYEHSYHMDYGAKAAAYVDAFMQNIHWQRAATRFAAAVRD
The following text describes a protein:
Function:
Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules. Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle. During spindle-kinetochore attachment, kinetochores first attach to the lateral surface of spindle microtubules, which supports the congression of chromosomes toward the middle of the dividing cell; they then slide along towards the spindle pole, a process independent of the DASH complex but requiring the NDC80 complex. When the end of a disassembling microtubule reaches the laterally attached kinetochore, the DASH complex together with the NDC80 complex and STU2 convert lateral attachment to end-on capture to produce a structure that can track with microtubule shortening and sustain attachment when tension is applied across sister kinetochores upon their biorientation. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached DASH complex to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. Incorrect microtubule attachments are corrected by releasing microubules from the kinetochore through phosphorylation by IPL1 of kinetochore components. Links the microtubule cytoskeleton to chromosomes during interphase. Also contributes to the poleward transport of kinetochores on microtubules following centromeric DNA replication in S-phase.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Note=Associates with the mitotic spindle and the kinetochore. Localizes to microtubule plus-ends.
Sequence:
MSEDKAKLGTTRSATEYRLSIGSAPTSRRSSMGESSSLMKFADQEGLTSSVGEYNENTIQQLLLPKIRELSDSIITLDSNFTRLNFIHESLADLNESLGSLLYGIMSNSWCVEFSQAPHDIQDDLIAIKQLKSLEDEKNNLVMELSNMERGIKRKKDEQGENDLAKASQNKQFNQPLFPSSQVRKYRSYDNRDKRKPSKIGNNLQVENEEDYEDDTSSEASFVLNPTNIGMSKSSQGHVTKTTRLNNNTNSKLRRKSILHTIRNSIASGADLPIENDNVVNLGDLHPNNRISLGSGAARVVNGPVTKNRNSMFSGRAERKPTESRHSVAKKTEKKINTRPPFR
The following text describes a protein:
Function:
Phosphorylates the antibiotic amicoumacin A (Ami), leading to its inactivation. Mediates natural B.subtilis resistance to the drug.
Sequence:
MLDVHKDIKKIFHEEQVLAEAAARYGFSKDQVRFLADAENYVYECMKDNQPYILKITHTIRRSSDYMMGEMEWLRHLAIGGISVAKPLPSLNGKDVEAVPDGNGGSFLLRVYEKAPGQKVDESDWNETLFYELGRYTGSMHSLTKSYKLSNPAFKRQEWDEEEQLKLRKYVPEDQIKVFQQADSLMNELRRLPKSQDNYGLVHADLHHGNFNWDHGKITAFDFDDIGYNWFVNDISILLYNVLWYPVVPYDDKAAFTEEFMTHFMKGYWEENELDPAWLMIIPDFLRLRHMLIYGLLHQMFDLNTIGEEEKEMLAGFRRDIENGTPITAFDFSALV