lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May play an essential role not only during sporulation, but also during vegetative growth.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTTKKTSPDLLLVIITLLLLTIGLIMVYSASAVWADYKFDDSFFFAKRQLLFAGIGVIAMFFIMNVDYWTWRTWSKLLMVICFFLLVLVLIPGVGMVRNGSRSWIGVGAFSIQPSEFMKLAMIAFLAKFLSEKQKNITSFRRGFVPALGIVFSAFLIIMCQPDLGTGTVMVGTCIVMIFVAGARIAHFVFLGLIGLSGFVGLVLSAPYRIKRITSYLNPWEDPLGSGFQIIQSLYAVGPGGLFGMGLGQSRQKFFYLPEPQTDFIFAILSEELGFIGGTLILLLFSVLLWRGIRIALGAPDLYGSFVAVGIISMIAIQVMINIGVVTGLIPVTGITLPFLSYGGSSLTLMLMAVGVLLNVSRYSRY
The following text describes a protein:
Function:
Plays a role in determining ER morphology.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence:
MGVILSRFRKEKSTFQKLEELEEKIKSLEAYTISTQDRRKRFVGRFLVTSIVLYIVGSLIFYFVFFPPTWNERIVYSVPLLICPILIFVLKRVLAWHYERKLRLNSNKLKDLRADKKKILENVMEKETYKVAVEILDKFGEKSHRIQTQAFAASLTPQRGPKPMPVGQPAAAPRMPTPAMPQRQISPPSVAVRPATPMTPQMRPSGPMHHTPQTAPGMMIRAPPMYGARGSMPYRRTPFPIINQNEKGVLEKMVDYLVGDGPTNRFAMICSECCMHNGMVLKEEYEYTAFRCAFCNALNPAKKQRPVAPRLPYEQEQLDRLSQKPDTSSESEAEEGDDRSSGSSQSGEPRSPGVGEEEPFEPEEQVKQEEMRNLATSETESSADAGEASGEKLLPTDGEPAESSTPDSTEVPSRPETVGSKKVD
The following text describes a protein:
Function:
General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress.
Subcellular Localization:
Nucleus.
Sequence:
MSSASVCTQCGSNNIQLDPHFCLEQQICTDCGFVLEEGSFQNDPTRAFQSQQSQIALPLKYRQHNNFREHVSKARRDGALRVEEISAMLRVTSDVMVEEAKTLFTQAFNLKVLNKAKREKKRVLPGCVVYIVCRQHDWPILLSDMWDLLQCRDSVFYSVYKVILAELDITITVPEIETVVPSVIQKCGFTFDLSDEQMKAVTQIVCLAKNTWITCGRRYDPIIIASVFLVWKAEDYAKRKKTSIPKFCRQIKFGTQVLPMVRSRVQEFEGLFLKLVSEIPWVETGQIDKKNIVCYLSDILRYEKTLLAGKYGDSDLESDDEERELQEKILPPSMTNRKPKSDVRDTDSMTSKVSVAVSYSTELDENDIPDSELHKYIRSTKEVMMVEDAQKSAQEYEEENPLKRKDSSSSRKTRKRKISDVENTP
The following text describes a protein:
Function:
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MSLEERVKEIIAEQLGVEKEKITPEAKFVEDLGADSLDVVELIMAFEEEFGIEIPDEDAEKIQTVGDVINYLKEKVGG
The following text describes a protein:
Function:
Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Miscellaneous:
MISCELLANEOUS: HIU hydrolysis also occurs spontaneously, but more slowly.
Subcellular Localization:
Peroxisome.
Sequence:
MNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS
The following text describes a protein:
Function:
Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite. The products of the cluster lead to a brown coloration and are important for growth and conidiation. The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine-derived dehydroalanine moiety to activated tyrosine but is not essential for the subsequent steps leading to isoquinoline formation. A different enzyme, most likely the ATP-grasp enzyme fsqD, is responsible for activation of tyrosine (Probable). Three additional enzymes encoded by the fsq cluster, the N-methyltransferase fsqC, the phenol 2-monooxygenase fsqG and the FAD-dependent oxidase fsqB, catalyze the formation of the isoquinoline ring system in the fumisoquins. FsqB converts the fspF thiolation domain-bound (2S,4S,5S)-2-amino-6-(3,4-dihydroxyphenyl)-4-hydroxy-5-(methylamino)hexanoyl into isoquinoline. The cyclization most likely proceeds via a two-step mechanism, beginning with FAD-dependent oxidation of the methyl group to an iminium species followed by electrophilic attack on the deprotonated phenol (Probable); Is able to convert N-methyl-3,4-dihydroxy-DL-phenylalanine (N-methyl-DOPA) directly into cyclic isoquinoline, in vitro. The absence of the meta-hydroxyl group, as in L-N-methyl-tyrosine, leads to a 25-fold lower rate of reduction and the formation of the demethylated product L-tyrosine, instead of a cyclic product. Does not accept the D-stereoisomer of N-methyltyrosine, in contrast to N-methyl-DOPA, for which both stereoisomers are oxidized with similar rates.
Sequence:
MSIPNSFIIVGSGVFGLSLAYALSLDDRFADKKIILVDRWNFEPPNATGSVHNPAAANADTSRVIRRDYPHGPYASLALEAMKHWRGKFGENNRYVNQRLLFSGEGSSLTTPPKALETVNYIKKAYAISCELTPGGRDAVQVLDSLDEVRAFLGNTPSHPPHLPVNKDPAARDLRGYVSNDCGWADAGASIEWLRQEVLRLGRVECVVGEVESLVYSDDQRAVKGVKLVDGKVLTAELTVIAAGARSSHILGIPKLCDVYSEFVAYIQLTKEEADELRRRQWPILVNCHRGVFAVGPDHDNCLKFGHFSYSGIVDVLREASIQVPTRPDGWEAQQKYWSDPRFAFGGEVKVSALGDVDDYENPAAQRALADYRLFLLELLGPTGLQGVDTLGLDQSDNLLNNIANRPFTRVRKCWYNDTPALDFVVDYHPSYGKTLFVATGGCDHAFKFLPIIGEKTLALILRNRGDSAVSLPAGVEPSLEELSELWRFPVELLQDN
The following text describes a protein:
Function:
Has a role in meiosis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MMKLENKLHRVLCSLHQNSISTHKTYVAVAAQDEYVRMGKVSLPRMYAVKPRIQKNFQDNYRFYGTLLCICWLYFFIWYPFALLALMVGVFLSFVMHGLGSLTINQNIRLDPKYSIPGVCAVTLIVIMFLAPVGRLFWSFCIVSSFAGLHCLLTTYENPAGIL
The following text describes a protein:
Function:
Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Subcellular Localization:
Cytoplasm.
Sequence:
MSNLAYINPGGKQARKASALDINMIAARGLQEVLKTNLGPRGTMKMLVSGAGMIKITKDGNTLLGEMQIQHPTAALIARAATAIDDITGDGSTGVVLTIGEMMRQSERYIQEGMHPRTITEGFHIARDEALKFLEGNIIEIPNEERREYLTNVARTALTTKVNPGLSEQLAEAVVDAVYAIAEHGKEVDLHMVEVMHMRHRLSSDTRFVNGIVLDHGGRNSDMPKYLENAYILTCNVSLEYERSELTTGFYYKDPAEKARMVEAERKMTDDRVRQIIELKRRVCTKENGRTFVVINQKGIDPISLEMLAKENILALRRAKRRNMERLVLSCGGEAVNSTDNLTPDVLGEAGLIQEYTLGDDKYTFVENASKGKSCTLLVKGPNDHTIAQIKDAVRDGLRAVKNAFEALAVVAGAGAFEVALHDHLMKFADNVSGKQKIGIRAYADAMLVMPKTLAENSGLDVQECLITLQEASRTARKGGKWVGLRIENGDVIDPIAAGILDNVIVKRSLLESTGDIVAQLLLVDEIMKAGRRGAGGQ
The following text describes a protein:
Function:
Functions as a guanine nucleotide exchange factor (GEF) that promotes the exchange of GDP to GTP, converting inactive GDP-bound small GTPases into their active GTP-bound form. Involved in regulation of adherens junction between cells. Plays a role in cell migration; Has a higher guanine nucleotide exchange factor activity compared to other isoforms.
Subcellular Localization:
Cell membrane. Cytoplasm, cytosol.
Sequence:
MFSPPARELRLCFLDGGEECKAIILSSVLFCKELKPPDLLAGFRGTVQHGLPLEIGDTVQILEKCEGWYRGFVLKNPNAKGIFPCCYIHLKNAHIKNKGQFETVVPSEDSVITEMTSTLRDWGAMWKQLFVKNEGDLFNRLWHVMNEILDLRRQVLVGHLTHDRMRDVKQHITARLDWGNEQLGLDLVPRREFSMVDPDDISVTELYRLMEHRHRKKETPAPVSTHHLFVHLKSLMSSNLGEELEVFFFIYDSRENRPLSERFFVKLNKNGLPKFPEKTERQCTLFVDLGSSDLRKDVYIVVHIIRIGRMGAGEKKNLCNVQYRRPFGCAVVSIADLLTADSKDDHLLKVYACNTESDWSQIHDNIIKKVNSRYNLSGSNTGLAVALQLLHGDIEQLRREYMVLFTRGVSITKKLGFSDVIMPGEMRNDLYMTLEKGEFEKGGKSVARNVEITIYALDADGQILKGFVAVGSGEPGGDEYHTFVLYHNNSPRWAEQIKLPIPVDMFRGSHVRFEFRHCSTKDKGEKKLFGFSFVPLMQEDGRTLPDGTHELIVHKCEENANLQDCSRYLKLPFSKSNLPGNNQTVKGTKESLWITSFLCSTKLTQNGDMLDLLKWRAHPERISDSLSKLKEIDGSEIVKFLQDTLDTLFGILDESSQRYALKVFDCLVHIINLLQDSKFQHFKPVMDTYIESHFAGALSYRDLIKVLKWYVDRIIDADRQEHIQQVLKATEYIFKYIVQSRRLFALATGGQNEEEFRCCMHELFMSIRFFLSQENKSMRPITHTQAVFLQSFPAVYNELLKLFTVREVATFVRETLGSLPTASQPDCPLEAVKLHCIAKTVDSQLYTNPDSRCVLLPVVLRLLQAHMQEQRDLVMCAHILTCMLSLLKKDDTDSSSSEEVDLIVESVLAVLLRTILEVANRPQPAGPTLRPQVQDVTGEFVSCLLALLRHMKDKHYQQLLQRFTSKEDLRDFLLHIFTVFRILIRPEMFPKDWTVMRLVTNNIIITTVLYLSDALRKNFLSEKFDYKVWDSYFCLSVIFINQTCLQLETFSASKKKKILEKYGDMRVMMGCEIFSMWQNLGEHKLNFIPAMIGPFLEVTLVPQPDLRNVMIPIFHDMMDWEQRRSGNFKQVEAKLIDKLDSLMSEGKGDETYRELFNSILLKKIERETWRESGISLIATVTRLMERLLDYRDCMKLGEVDGKKIGCTVSLLNFYKTELNKEEMYIRYIHKLYDLHLKAQNYTEASYTLLLYDELLEWSERPLREFLSYPMQSEWQRKEYLHLTIIQNFDRGKCWENGILLCRELADQYESYYDYRNLSKMRMMEASFYDKIMDQQRLEPEFFRVGFYGKKFPFFLRNKEFVCRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDQTIYQAEAQYLQIYAVTPIPDSQDVLQRDGVPDNIKSFYKVNHIWRFRYDRPFHKGTKDKENEFKSLWVERTTLTLVQSLPGISRWFEVERRELVEVSPLENAIEVIENKNLQLRTLITQCQTRQMQNINPLTMCLNGVIDAAVNGGLARYQEAFFVKDYIMNHPEDGDKIGRLRELMFEQAHILEFGLTVHEKFVPQDMRPLHKKLVDQFHLMKSSLGIQEFPAYVRASPIHFTNGSPRVGRNSAPNIMSPDGGARVVSRRSPLSYPAVNRYSSSSLSSQASNEVSNITGHSESSDEVFNMQPSPSTSSLSSNHSASPNVSSSAPSSARGSPQLSDKHKHPRENCLSPRDRPCSAVYPNPMEPTQRPVPHPAGDSSLPRSDPNISSPDKVVKPAPSSWSLDMPLSEFNGKCPPVPPRPPYSGSPARTTRSQSPVSTSRSPQKTSVPPFTPSPTECQSTGLVSNSPVLSGSYSSGISSLSRCSVSEASGTENTPTDHVLPNSASSGSDELIRRENKTPPPYSIHERNNPRRQVPLPPSLSLPPNVDAPPIPPKPHQIRRQDTEPRRPEQFPRPRPIPRKVSQL
The following text describes a protein:
Function:
Can bind steroids (in vitro), and may also bind other types of hydrophobic ligands.
Sequence:
MADVATKHPMEDEVKKTEASSLVGKLETDVEIKASADKFHHMFAGKPHHVSKASPGNIQGCDLHEGDWGTVGSIVFWNYVHDGEAKVAKERIEAVEPDKNLITFRVIEGDLMKEYKSFLLTIQVTPKPGGPGSIVHWHLEYEKISEEVAHPETLLQFCVEVSKEIDEHLLAEEEEVKTPETPSLVGKLETDVEIKASAEKFHHMFAGKPHHVSKASPGNIQGCDLHEGDWGQVGSIVFWNYVHDREAKVAKERIEAVEPNKNLITFRVIDGDLMKEYKSFLLTIQVTPKLGGPGSIVHWHLEYEKISEEVAHPETLLQFCVEVSKEIDEHLLAEE
The following text describes a protein:
Function:
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct ATG9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity).
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein.
Domain:
The N-terminus might form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane; The L/FRRG motif is essential for the cytoplasm to vacuole transport (Cvt) pathway, for the recruitment of ATG8 and ATG16 to the PAS in nutrient-rich medium, and for its recruitment to and dissociation from the PAS under starvation conditions.
Sequence:
MLQTSSSSATASLQQQLSKQYANSFSNDGSSFSSKNNQQYSEIVNYISFNQDASCITIGLKNGYKIFNCQPNFGRSFQFKNDESTGIVEMLYCTSLLATVAQGEEIGSSPRKLKIINTKTKSTICDLIFPSTILQVKLTNTRLIVVLEDQIYLYDITTMKLLHTIETSPNLSGLSAISYDDSNSYLAYPSPPKTITHDSLLASGINTNGGSNSTQNNISSVSNTPNRVGDVIIFNLTSLQPISVIEAHKSTIASMAFSNNGLYLATASDKGTIVRIFEVATGTKLYQFRRGTYPTKIYSLRFSADDKYVLATSSSLTVHIFRLGEEEALETKHKKKKIPAVATILEEETEGSQSNEQTKSIKRNSEEFEDIRDDGDDSDVDDEDGDIDDESLEVIPAKQRKLSQGSTNSYTSVNSEDVQSNSPKTEPLIDQNRLSMARIIRRSSQTLGRKAAQKMGDFLPSRFSSILEPTRNFASLKINAHSKDTKSVAVMNNVLQQDLIPQTYLASDNASAKQDFMEVSLFHIYVVTTEGMLYTYGLDPERGGDCILLNSHCILDEY
The following text describes a protein:
Function:
Membrane-bound E3 ubiquitin ligase that plays a role in several processes including apoptosis regulation or reticulum endoplasmic stress. Has anti-apoptotic activity, both for apoptosis triggered via death-receptors and via mitochondrial factors. Contributes to the dynamic control of IRE1/ERN1 signaling during ER stress by inducing BAX inhibitor 1/TMBIM6 proteasomal degradation. Promotes the activation of TGF-beta signaling by mediating the 'Lys-63'-linked ubiquitination of TGFBR1 which is critical to activate the pathway. Together with NGFR, negatively regulates NF-kappa-B and JNK-related signaling pathways (By similarity). Promotes the proteasome-mediated degradation of PNPLA3, a protein involveld in lipid metabolism.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEEPQKNDLSMREQEEEHPVRSSGPQISVSEFSCHCCYDTLVNPTTLNCGHSFCRHCLALWWMSSKKTECPECREKWEGFPKVNILLRDAIEKLFPDAIRMRVEDIQQNNDVVQSLAAFQKYGNDQNPLAPSTGRVNPQRGGGFFSGVLTALTGVAVILLVYHWRSRESEHGLLVHKAVDKWTMEEVVLWLEQLGPWASLYRDRFLSERVNGRLLLTLTEEEFSRAPYTIENSSHRRVILTELERVRALGVKPPQNLWEYKAVNPGRSLFLLYALKSSPRLGLLYLYLFDYTDCFLPFIHTICPLQENSSGEDIFTKLLDLREPTWKQWREFLVKYSFLPYQLIAEFAWDWLEVHYWTSRFLIVNAVLLSVLELFSFWRIWSRSELKTVPQRMWSHFWKVSTQGLFMAMFWPLIPQFVCNCLFYWALYFNPIINIDLVVKEVRRLETQVL
The following text describes a protein:
Function:
May transport inorganic phosphate (Pi).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKFGKEFSSQMVPEWQQAYMDYDYLKTLLKEIIRFKLRTNNAPTRGGAKNHHGGGLNRKMTLYRAFSGLVSTPGRHRRGNPHDVEEGIQLTGTTTTTSGPILVNNTADRGYETTFLMAAEEGGEYELVFFRRLDDEFNKVNKFYKEKVEEVLKEAMVLNKQMDALIAFRVKVENPDGWGWDERAVEITRLASDISTSAAAISASTPAGAKSISILETRFRFIQIRIVIVPPTYRTDISNLLVKVRSQAHMEAIQEGGSSKAGQLEDDDEEEEAEAQAEIVASVSTGASTTRMRAARPAPLDVLDRVTINNTKETPRSTIKRVLQVSKQTDLKFSRENLMKVEEKLRSAFIVFYQKLRLLKSYSFLNVLAFSKVLKKYDKITSRDATKPYMKVVDSSYLGSSDEVVRLMERVEATFIKHFANANRTKGMNILRPKAKRERHRLTFSTGFTAGCVFSLIVALAAIIRTRNLLQEEGQKQYMNTMFPLYSFFGFIVLHMIMYAANIYYWRRYKVNYSFIFGFKQGTELGYRQVLLVGFSIGVFALLCVLANLDMEANPKTKDYKTFTELLPLFLLLAMFVVLILPFNFFYRSSRFFFLTCLFHCLAAPLYKVTLPDFFLGDQLTSQVQALRSIEFYICYYGWGDFRHRQNTCNKSSVYNTFLFIVAVIPYASRLLQCLRRLFEEKNPEQGIQKGQIAWRVLAAISSAAAAIFSTYWDFIHDWGLLNRTSKNRWLRDKLLIPQKKVYFIAMILNVLLRFAWIQTILDFNFSFMHRQTMVTVVASLEIIRRGIWNFFRLENEHLNNVGKYRAFKSVPLPFNYDEDEDKDD
The following text describes a protein:
Function:
Potent inhibitor of hemorrhagic activity but also proteolytic activities of atrolysin C and jararhagin. Inhibition occurs by formation of a non-covalent complex between BJ46a and the proteinases at their metalloproteinase domains.
Subcellular Localization:
Secreted.
Sequence:
MNSLVALVLLGQIIGSTLSSQVRGDLECDEKDAKEWTDTGVRYINEHKLHGYKYALNVIKNIVVVPWDGDWVAVFLKLNLLETECHVLDPTPVKNCTVRPQHNHAVEMDCDVKIMFNVDTFKEDVFAKCHSTPDSVENVRRNCPKCPILLPSNNPQVVDSVEYVLNKHNEKLSDHVYEVLEISRGQHKYEPEAYYVEFAIVEVNCTAQELHDDHHHCHPNTAGEDHIGFCRATVFRSHASLEKPKDEQFESDCVILHVKEGHAHSHLIQQHVEKDSISPEHNNTALNFVHPHNDTSTSHESHEHLAEVPVAFVKKELPKDISDRHTTPVKGCPGKVHHFEL
The following text describes a protein:
Function:
May be involved in several stages of intracellular trafficking. Overexpression of SNX15 disrupts the normal trafficking of proteins from the plasma membrane to recycling endosomes or the TGN.
Sequence:
MSRQAKDDFLRHYTVSDPRTHPKGYTEYKVTAQFISKKDPEDVKEVVVWKRYSDFRKLHGDLAYTHRNLFRRLEEFPAFPRAQVFGRFEASVIEERRKGAEDLLRFTVHIPALNNSPQLKEFFRGGEVTRPLEVSRDLHILPPPLIPTPPPDDPRLSQLLPAERRGLEELEVPVDPPPSSPAQEALDLLFNCESTEEASGSPARGPLTEAELALFDPFSKEEGAAPSPTHVAELATMEVESARLDQEPWEPGGQEEEEDGEGGPTPAYLSQATELITQALRDEKAGAYAAALQGYRDGVHVLLQGVPSDPLPARQEGVKKKAAEYLKRAEEILRLHLSQLPP
The following text describes a protein:
Function:
Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decrease in cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MAGPRGLLPLCLLAFCLAGFSFVRGQVLFKGCDVKTTFVTHVPCTSCAAIKKQTCPSGWLRELPDQITQDCRYEVQLGGSMVSMSGCRRKCRKQVVQKACCPGYWGSRCHECPGGAETPCNGHGTCLDGMDRNGTCVCQENFRGSACQECQDPNRFGPDCQSVCSCVHGVCNHGPRGDGSCLCFAGYTGPHCDQELPVCQELRCPQNTQCSAEAPSCRCLPGYTQQGSECRAPNPCWPSPCSLLAQCSVSPKGQAQCHCPENYHGDGMVCLPKDPCTDNLGGCPSNSTLCVYQKPGQAFCTCRPGLVSINSNASAGCFAFCSPFSCDRSATCQVTADGKTSCVCRESEVGDGRACYGHLLHEVQKATQTGRVFLQLRVAVAMMDQGCREILTTAGPFTVLVPSVSSFSSRTMNASLAQQLCRQHIIAGQHILEDTRTQQTRRWWTLAGQEITVTFNQFTKYSYKYKDQPQQTFNIYKANNIAANGVFHVVTGLRWQAPSGTPGDPKRTIGQILASTEAFSRFETILENCGLPSILDGPGPFTVFAPSNEAVDSLRDGRLIYLFTAGLSKLQELVRYHIYNHGQLTVEKLISKGRILTMANQVLAVNISEEGRILLGPEGVPLQRVDVMAANGVIHMLDGILLPPTILPILPKHCSEEQHKIVAGSCVDCQALNTSTCPPNSVKLDIFPKECVYIHDPTGLNVLKKGCASYCNQTIMEQGCCKGFFGPDCTQCPGGFSNPCYGKGNCSDGIQGNGACLCFPDYKGIACHICSNPNKHGEQCQEDCGCVHGLCDNRPGSGGVCQQGTCAPGFSGRFCNESMGDCGPTGLAQHCHLHARCVSQEGVARCRCLDGFEGDGFSCTPSNPCSHPDRGGCSENAECVPGSLGTHHCTCHKGWSGDGRVCVAIDECELDMRGGCHTDALCSYVGPGQSRCTCKLGFAGDGYQCSPIDPCRAGNGGCHGLATCRAVGGGQRVCTCPPGFGGDGFSCYGDIFRELEANAHFSIFYQWLKSAGITLPADRRVTALVPSEAAVRQLSPEDRAFWLQPRTLPNLVRAHFLQGALFEEELARLGGQEVATLNPTTRWEIRNISGRVWVQNASVDVADLLATNGVLHILSQVLLPPRGDVPGGQGLLQQLDLVPAFSLFRELLQHHGLVPQIEAATAYTIFVPTNRSLEAQGNSSHLDADTVRHHVVLGEALSMETLRKGGHRNSLLGPAHWIVFYNHSGQPEVNHVPLEGPMLEAPGRSLIGLSGVLTVGSSRCLHSHAEALREKCVNCTRRFRCTQGFQLQDTPRKSCVYRSGFSFSRGCSYTCAKKIQVPDCCPGFFGTLCEPCPGGLGGVCSGHGQCQDRFLGSGECHCHEGFHGTACEVCELGRYGPNCTGVCDCAHGLCQEGLQGDGSCVCNVGWQGLRCDQKITSPQCPRKCDPNANCVQDSAGASTCACAAGYSGNGIFCSEVDPCAHGHGGCSPHANCTKVAPGQRTCTCQDGYMGDGELCQEINSCLIHHGGCHIHAECIPTGPQQVSCSCREGYSGDGIRTCELLDPCSKNNGGCSPYATCKSTGDGQRTCTCDTAHTVGDGLTCRARVGLELLRDKHASFFSLRLLEYKELKGDGPFTIFVPHADLMSNLSQDELARIRAHRQLVFRYHVVGCRRLRSEDLLEQGYATALSGHPLRFSEREGSIYLNDFARVVSSDHEAVNGILHFIDRVLLPPEALHWEPDDAPIPRRNVTAAAQGFGYKIFSGLLKVAGLLPLLREASHRPFTMLWPTDAAFRALPPDRQAWLYHEDHRDKLAAILRGHMIRNVEALASDLPNLGPLRTMHGTPISFSCSRTRAGELMVGEDDARIVQRHLPFEGGLAYGIDQLLEPPGLGARCDHFETRPLRLNTCSICGLEPPCPEGSQEQGSPEACWRFYPKFWTSPPLHSLGLRSVWVHPSLWGRPQGLGRGCHRNCVTTTWKPSCCPGHYGSECQACPGGPSSPCSDRGVCMDGMSGSGQCLCRSGFAGTACELCAPGAFGPHCQACRCTVHGRCDEGLGGSGSCFCDEGWTGPRCEVQLELQPVCTPPCAPEAVCRAGNSCECSLGYEGDGRVCTVADLCQDGHGGCSEHANCSQVGTMVTCTCLPDYEGDGWSCRARNPCTDGHRGGCSEHANCLSTGLNTRRCECHAGYVGDGLQCLEESEPPVDRCLGQPPPCHSDAMCTDLHFQEKRAGVFHLQATSGPYGLNFSEAEAACEAQGAVLASFPQLSAAQQLGFHLCLMGWLANGSTAHPVVFPVADCGNGRVGIVSLGARKNLSERWDAYCFRVQDVACRCRNGFVGDGISTCNGKLLDVLAATANFSTFYGMLLGYANATQRGLDFLDFLDDELTYKTLFVPVNEGFVDNMTLSGPDLELHASNATLLSANASQGKLLPAHSGLSLIISDAGPDNSSWAPVAPGTVVVSRIIVWDIMAFNGIIHALASPLLAPPQPQAVLAPEAPPVAAGVGAVLAAGALLGLVAGALYLRARGKPMGFGFSAFQAEDDADDDFSPWQEGTNPTLVSVPNPVFGSDTFCEPFDDSLLEEDFPDTQRILTVK
The following text describes a protein:
Function:
May be required for lysis of autophagic vesicles after delivery to the vacuole.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Note=Vacuole and punctate structures.
Sequence:
MKVNHNHISNTGVNDSEDILEAQDEISIDNNKNQENIWNKKSIFHTWLLLCYSTGPVASMSRTYIPASIQSIAKNVGKTKMNQPCGTQGNDCYVKFGFMTVHHTSYVLYLRAVSTAIEGVVAIFLMGIADYSNYRKSFLIFSILVYGFLALPFIGLTNNDYQTLVLASILYSLLIIDDSIYQILEGSYIPLFMRADKKNPMQRGSVVAVLGLFLGNLGGITALVIGIIISYLSGTPESKGYHNFLLAITIAGCLTIGLSLFSALYIPNVQGKQRIDNFLVLPFKRFFNLLKDIQKYPMAFLYCISWVIWNVSFNNFMSMFLLLFRSTLGLGNSDAEYTVYTFMSYICSSWGSLVWMFLYQKWNSNIKYWGYSFLSVSLLANFWGCLGIHKLTPLGYQNRWEFWVFEVFYSATSSAMRSLNRCVYSSLLPEGNEAQYFGLEVTLGIASGWIGGLVNAVIQDRTNDDRFPFLPNMFLVVVSLIVYYYVDLQKGKNDVNNGNS
The following text describes a protein:
Function:
Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Binds to and phosphorylates CDC25. This leads to negative regulation of CDC25 and prevents mitotic entry.
Subcellular Localization:
Nucleus.
Sequence:
MAQKLDNFPYHIGREIGTGAFASVRLCYDDNAKIYAVKFVNKKHATSCMNAGVWARRMASEIQLHKLCNGHKNIIHFYNTAENPQWRWVVLEFAQGGDLFDKIEPDVGIDEDVAQFYFAQLMEGISFMHSKGVAHRDLKPENILLDYNGNLKISDFGFASLFSYKGKSRLLNSPVGSPPYAAPEITQQYDGSKVDVWSCGIILFALLLGNTPWDEAISNTGDYLLYKKQCERPSYHPWNLLSPGAYSIITGMLRSDPFKRYSVKHVVQHPWLTSSTPFRTKNGNCADPVALASRLMLKLRIDLDKPRLASSRASQNDSGFSMTQPAFKKNDQKELDRVEVYGALSQPVQLNKNIDVTEILEKDPSLSQFCENEGFIKRLAKKAKNFYEICPPERLTRFYSRASRETIIDHLYDSLRLLAISVTMKYVRNQTILYVNLHDKRKCLLQGVIELTNLGHNLELINFIKRNGDPLEWRKFFKNVVSSIGKPIVLTDVSQN
The following text describes a protein:
Function:
Endoplasmic reticulum (ER)-shaping membrane protein that plays a role in determining ER morphology. Involved in the stabilization of nascent three-way ER tubular junctions within the ER network. May also play a role as a curvature-stabilizing protein within three-way ER tubular junction network (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein; Cytoplasmic side. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions, which represent crossing-points at which the tubules build a polygonal network.
Domain:
The transmembrane domain 1 and 2 function as a signal-anchor and stop-transfer sequence, respectively, generating a double-spanning integral membrane protein with a N- and C-terminal cytoplasmic orientation. Transmembrane domain 1 and 2 are probably sufficient to mediate membrane translocation and topology formation in a N-myristoylation-independent manner. Transmembrane domain 2 is sufficient to block the protein secretion pathway. The two coiled-coil domains are necessary for its endoplasmic reticulum (ER) three-way tubular junction localization. The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence:
MGAIISRWKTKPSTVELLESLDKDIKDLEEFRAKNQRLLKLWVGRLLFYSSALYLLTCLCVYYLYFPQQWGARLITALPLLAFPALVLLLRKMLIFLFSKRTERNNDKLEDLKTQKRKILEEVMETETYKNAKLILERFDPESKKKAEAEATPVRPHMTPRPGQELRQRHIAMATPGPVLGPMSPGTTPLRTAPGGPPEKGLAGSASTPAGASQAETPQQMMRRSMNPYSPGPGSGMRPPGPPLARPILPRERGAVDRVIEYLVGDGPQNRYALICQQCFSHNGMALKEEFEFVAFRCAYCYFMNPARKTRPQAPRLPEFSFERRLRSESPETQSSAATETPEDSDAPEDDMERTTSADPQNPAADEAPVLQESETEESQPQDVPHAEAEALEEQKKEDESN
The following text describes a protein:
Function:
May function in the transport of nucleosides and/or nucleoside derivatives between the cytosol and the lumen of an intracellular membrane-bound compartment.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MAVPAGPQEEAPQAPATDNTAPTATAGCLSAEVRAGSSSPRWRTPDSPYRTSPQVVNLLMGILLTVEVTHPNVVPTVNIQYEVIGNYYASERMAENACVLFAISLLMFTISAMMVYGAIAHRVGWLIPFFCYQLFDFVVSCLVAISSLTYLPRIKDYLDQLPDFPYKDDLLSLDSSCLLFIVLVFFALFIILKAYLINCVWNCYKYISNRNLPEIAVYPAFEAPPQYVLPTYEMAVKMPEKEPPPPYIPA
The following text describes a protein:
Function:
Involved in the final steps of polyacyltrehalose (PAT) biosynthesis. Catalyzes the transfer of three mycolipenoyl groups onto diacyltrehalose (DAT) to form PAT.
Miscellaneous:
MISCELLANEOUS: The topology of this protein is unsure. According to PubMed:25124040, the C-terminal catalytic site is on the periplasmic side of the inner membrane. However, PubMed:25331437 authors conclude that Chp2 has the opposite topology, and that the C-terminal catalytic site is on the cytoplasmic side of the membrane.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MKRVIAGAFAVWLVGWAGGFGTAIAASEPAYPWAPGPPPSPSPVGDASTAKVVYALGGARMPGIPWYEYTNQAGSQYFPNAKHDLIDYPAGAAFSWWPTMLLPPGSHQDNMTVGVAVKDGTNSLDNAIHHGTDPAAAVGLSQGSLVLDQEQARLANDPTAPAPDKLQFTTFGDPTGRHAFGASFLARIFPPGSHIPIPFIEYTMPQQVDSQYDTNHVVTAYDGFSDFPDRPDNLLAVANAAIGAAIAHTPIGFTGPGDVPPQNIRTTVNSRGATTTTYLVPVNHLPLTLPLRYLGMSDAEVDQIDSVLQPQIDAAYARNDNWFTRPVSVDPVRGLDPLTAPGSIVEGARGLLGSPAFGG
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence:
MESKSVNKFDSDPYKGEKEGKLREVGNQAVWSVSSCKPGFGVEQLRDTSLETYWQSDGPQPHMVNIQFRKKTTVSDIFLYADFKADESYTPNRVSVRVGNHINDLIEIDLVEFIEPTGWVMIPLKNLNETAVRAFMIQIAVLSNHQNGRDTHVRHIKIHSPIQDCSTSKKINLVNKEMLQWQNIR
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular Localization:
Nucleus.
Sequence:
MSGILFEDMFIVDSTDPGRYNKVCRITGHSSTSKDITITLDINKELFPVQNHDSLTITLASSLGNESSMITSNGSWRPPKPDERSLADDYDYVMYGTVYKFEENADNDKMAVYISFGGLLMRLEGGYRSLSNLKQENAYILIRHYKDN
The following text describes a protein:
Function:
Putative odorant or sperm cell receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFSSRDELTARVSNVTEFILLGLTQNPELQKLLFGVLLTTYLITLAGNLLISVTIFISPALASPMYFFLSYLSLIDVFYSSSIAPKMIFDLISGTNTVSFKGCMTQLFAEHFFAGSEIIMLIVMAYDRYVAICKPLHYMTIMSPPVRAFLVGMAGALGFIHGGIQVLFMVQLPFCGPNVIDHFMCDLIPLLELACTDMHTLGPLIAANSGSMCLVIFCMLVASYGVILRSLRTHSSEGRRKALSTCASYIMVVILFFVPCSFLYLRPMTSFPTDKAVTVFCTIVTPMLNPLIYTLRNAEVKDVFKKLWGQIMKTGGK