lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcription factor required for hyphal growth, biofilm formation, and virulence. Promotes formation of both conventional and pheromone-stimulated biofilms. Binds and recruits HDA1 to promoters of hypha-specific genes in a rapamycin-dependent manner. Involved in the switch between two heritable states, the white and opaque states. These two cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically at low frequency.
Subcellular Localization:
Nucleus.
Sequence:
MSSSSSLSSSTTTATTTSARIRLPSISELTSRSTISGGSNNGNGSALKSQISPRLSDTSRILPSILKNTSGSSTPTSSSTPFKCPPIKSTVGGTLSSGNTQSNYVLGNTKINSLPRLSSPTLPVKVQPQQQPQLPPASSLSPVTRVINTPPQQPQSVSASTSPNTQYQYYQYQQQSSPIQQQQQQQQATPAATPTVMQMAQNQPSHPAPLQYATQQYYPQPVYYQSPAGVPPPPPSVTHQGHIIAVHQHPGHLPQVGVNGMPPNVGYTIVQPEIVNKSTNRCHRCGTTETPEWRRGPKGVRTLCNACGLFHAKLVKRKGAALAAEEVLNNKVTKGKNGRRISMKKHLLNESLKQQQQINGVGIPINGFNHQILPPSFKPQQGGIATLPPLMHGQYPNNVNNLVIHQPPPQQQQQQQQHNNIC
The following text describes a protein:
Function:
Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Plays a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production and via its modulation of the respiratory chain activity can regulate skeletal muscle differentiation and insulin secretion by pancreatic beta-cells. Involved in cytochrome b translation and/or stability.
Subcellular Localization:
Mitochondrion matrix, mitochondrion nucleoid. Mitochondrion. Mitochondrion intermembrane space. Mitochondrion matrix. Mitochondrion inner membrane. Note=Predominantly expressed in the mitochondrial inner membrane.
Sequence:
MAALRYRRFLKLCEEWPVDETKRGRDLGAYLRQRVAQAFREGENTQVAEPEACDQMYESLARLHSNYYKHKYPRPRDTSFSGLSVEEYKLILSTDTLEEFQEMNKSVWRKLQEKFAPTRPEEKHRAWTRVLSRPRT
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MSRGPMLRTEHLNANYGMFQALFGINFSIERGEVVSLIGANGAGKSTLLRAIVGSVPVAAPSVLLDGEPVGGSAEIDQLSRGIALVPEGRRLFPSLTVEENLLLAAKNGRRGPWTPDRLYRELPALQKLRSRPATALSGGQQQLVAVGRALVTNPDFLLCDEISLGLSPVAVETVYELLGTVIEEGMAVILVEQNVRRALSSSSRYYCMLKGNVVLEGISKTADYARVSAAYFGD
The following text describes a protein:
Function:
Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MLGLSAMQPRQLAAQVLNFALVLSTAFMLWKGLSVVADSPSPIVVVLSGSMEPAFQRGDLLFLWNRGLDTQVGEIVVYNVKGKDIPIVHRVVRRYGGGKTPLRLLTKGDNNVADDTELYATGQSFLNRKEDVVGSVVGFIPFVGYVTILLSEYPWLKQVMLGLMDFFHARGLDRQEPDLDVQMGVQAAMAGQVVGIEVQDMAIEEEMESLSLVVQHHLYTWIDTFPLPDNDSTIFPQDVLDEERVALRKSA
The following text describes a protein:
Function:
Accessory 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, an accessory subunit PolA2 and two primase subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2) is recruited to DNA at the replicative forks (By similarity). 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 (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MEEELKQQFDEMGVEPADAVLGRCAELAITYNIHDATEFVEQWMAFSLSHLQGEDPAIENLGDFERKVLQLRKDKAGYKATGQKAKSYGSPSVQDTSSLATYGVMEDDPMLDDYVSESAVDSSALHTPKAKKQSDRTANLKGAALFSPASYTPQSAKRKAGLETPSNSVAGKPGDIVDTFGHPKLLAGSSWQSQMEHTVPVTQKLLHNDAPLTIANLGYMNDLLTDRCHNLRVRFNQTGPALVDKKLGQAGAAECIWYPQDRQVLQSAGGLHAVGMIHSEDDGPLDAHSAFMAVLDDDVEDEMDPTLTLNFSRVKSASIFPGQVVLAKGFIPRGKTFMVEEIHTERKLTPATPLQIDRELQFVVASGPFTDSTDLFYEPLHDLLKYLKDHRPDVLVLTGPFLDADHKMVGELAETFDTFFEKMIGGIMESIGSHTAVLVVTSQKDAMALSVYPTPPPALRRTYPNLYMLPDPSLVDLDGFTLGVTSTDVVDHLLSHEFAVNAGERMHRAINHLFHQGSFYPLYPPADEDMAYDSQLALKYAQLKQLPNVLILPSDQRHFIRLVNDCLVINPGRVADKKGGTFARFLVAPSVPGKAANMFNSVACQVQRI
The following text describes a protein:
Function:
Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (Probable). Can bind to phosphatidylinositol 4-monophosphate (PI-4-P or PtdIns4P), phosphatidylinositol 4,5-bisphosphate (PI-4,5-P2 or PtdIns4,5P2), and phosphatidic acid (PtdOH), but not to 3-phosphoinositides. May function upstream of the cold response phosphoinositide-dependent phospholipase C (PI-PLC) pathway.
Subcellular Localization:
Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region.
Sequence:
MEALTELCDIIAKNPKQFSEKLAWICGRCPQTEWLLAESPRVSRSHLNAVLAVARIISKNPESIDNRAKSVVNEFLSAIPASFRRSFWPHSFPSQLISSFYCDFLSYLSCAADLSPEFGTEVARFTGEVVIAAIAPSSGDSDGDPAISKAFLVALSQHFPSILQSDGDKLITMLLDQFVLNRAPASPKEQRQQNSANSETDTSSSQGSPISTNRYPSGKTEMASPGDEVASHGSNLSSKSSSSVVMNGGSIVWKSGVDQLSFGFSEGSGGANPVFRQQVASFEDESIESLEKQEIAFRLITHILDKVKIDSKLQDQVRFIAKRQLQSMSAFLKSRKRDWNEQGQVLKTRVNAKLSVYQAAAKMKIKSLVSLETDGKTSKRLVLETLALLLDAADACLTSVWRKMKACEELFDSLLSGIAKIAVARGGQPLRVLLIRLKPLVLAVCALPDQGAMLESIFKTSCVIIESAWAKDRAPVDNFIMGLASSIRERNDYEEQVDREKQVPAVQLNVIRLLADLNVAVKKPEVADMILPLFIESLEEGDASTPSFLRLQLLDAVSRIATLGFDKSYRETVVLMTRSYLSKLSSVGSVESKTSAPEATTERVETLPAGFLTIASGLMDTKLRSDYRHRLLSLCSDVGLAAESKSGGSGVDFLGPLLPAVAEICSDFDPTMDVEPSLLKLFRNLWFYIALFGLAPPIVKTPTPPLKSTSNSVNSVGSMSATALQAVGGPYMWDNQWALAVQRIAQGTPPLVVSSVKWLEDELELNALHNPGSRRGNGNEKVASTQRLALSTALGGRVDVAAMNTISGVKATYLLAVAFLEIIRFISNGGILNGESSVSASRSAFSCVFEYLKTPNLTPAVSQCLTAIVHRAFETAVSWLEDRISLTGKDARNRELTTYAHACFLIKSMSQRDEHVRDISVNLLTQLRDKFPQVLWHSSCLDSLLFSVHDNTPSTVVNDPAWTAAVRSLYQKVVREWIIISLSYAPCTSQGLLQDKLCKANTWQRAQTTTDVVSLLSEIKIGTGKNELWSGIRTANIPAVMAAAAAASGANLKVSEAFNLEVLGTGVVSATVKCNHAGEIAGMRRLYNSIGGFQSGSTPSGFGGGLQRLISGAFSQAPQPEDDSFNEMLIARFVRLLQQFVNTAEKGGEVEKSQFRETCSQATALLLSNLGGESKTNVEGFSQLLRLLCWCPAYISTPDAMETGIFIWTWLVSAAPQLVSLVLAELVDAWIWTIDTKRGLFASDVRYSGPAAKLRPHLSPGEPEDPPESDPVDQIVAHRLWLGFLIDRFEVVRHNSAEQLLLLGRMLQRSTDLEWCFTRHPAAAGTFFSLMLLGLKFCSCQTQGNMQKFRSGLQLLEDRIYRTSLGWFAHQPEWYDVNIPNFCHSEALSVSVFVHFLSNELSESSQSDSKGKPRESGNLIDVTDQYHPVWGEMDNYTLGKEKRKQLLLMLCQHEADRLDVWAQPISSKDSPYSRLKISSEKWTEYAKTAFSVDPRIALSVASRFPANASVKSEVTQLVQTNIVDLRTIPEALPYFVTPKNVEENSVLLQQLPHWAACSITQALEFLTPAYKGHPRVMAYVLRVLESYPPERVTFFMPQLVQSLRYDDGRLVEGYLLRATQRSDIFAHILIWHLQGEDVQETPKDGSIDKNAAFQEILPQVRQHIIDGFSPNALDMFTREFDFFDKVTSISGVLFPLPKEERRAGIRRELEKIEMQGDDLYLPTAPNKLVRGIRVDSGIPLQSAAKVPIMITFNVIDRDGDHSDVKPQACIFKVGDDCRQDVLALQVISLLRDIFQAAGLNLYLFPYGVLPTGAERGIIEVVPNTRSRSQMGETTDGGLYEIFQQDYGPVGSTTFETARENFLISSAGYAVASLLLQPKDRHNGNLLFDDVGRLVHIDFGFILETSPGGNMRFESAHFKLSHEMTQLLDPSGVMKSKTWHQFVSLCVKGYLAARRQMDGIISTVQMMLESGLPCFSRGDPIGNLRKRFHPEMSEREAAHFMIHVCTDAYNKWTTAGYDLIQYLQQGIEK
The following text describes a protein:
Function:
Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity.
Subcellular Localization:
Nucleus.
Sequence:
MKFVIPGVNVKIFGKAVHALSKIGEELYLIADDESLSLKVFSMSMSCYACFRLLKSFFSVYEASGEGFKGKLSMRSILLAFRTVNGMEKTVEECLLEVSETCDDAVVTLKHRKGMTKRFRLPLIEYETLLFSFQTEGYSNEISGQSKLLTDVLVNFPMSVQEVTLRLSPTKLDVCNHVDDTSDPLKTVNTSVSIESSEFDEFRAAGDGGEVTFCLREFRALLGFCEGLCLNATLHFDGAGKPLLASFEGVPGLESSFVTATLADGPQSLPTTRSGSVATHRHKVPQRRPGRPDPPEPSESGAGPSGEPSIAAKKKKAMLLGLTTPDLDHFTSQLPQDDPVLVEASDDEGD
The following text describes a protein:
Function:
Probable factor involved in nitrate and phosphate signaling in roots. Integrates nitrate and phosphate starvation responses and adaptation of root architecture, depending on nutrient availabilities. Acts downstream of the nitrate sensor and transporter NPF6.3/NRT1.1. Represses primary root development in response to phosphate deficiency conditions, only when nitrate is present.
Subcellular Localization:
Nucleus.
Sequence:
MIKNLSNMKNDNQKREKCCEYIEALEEERRKINVFQRELPLCVELVTQAIEAYKREISGTSTDNLYGQSECSEQTTGECGRILDLFIPIKHSSTSIEEEVDDKDDDDEEHQSHETDIDFDDKNMKSEWLKSVQLWNQSDAVVSNNRQDRSQEKTETLVELIKINDEAAKKNNNIKSPVTTSDGGSGGGGGRRGQRKNRRCWSQELHRRFLNALKQLGGPHVATPKQIRDIMKVDGLTNDEVKSHLQKYRLHARRPSQTTPNNRNSQTQHFVVVGGIWVPQTNHSTANAVNAVASGETTGIYGPMVSSLPSEWPRHSNFGRKISEDRSRCSNNGFFRCSSPAMSCSTRTKTKDAKIIS
The following text describes a protein:
Function:
Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins. Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. Required for normal induction of p53/TP53 in response to DNA damage. Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (By similarity).
Miscellaneous:
MISCELLANEOUS: Interaction with THAP5 has been shown in human, but rodents lack a THAP5 homolog.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. Co-localizes with NUMA1 at mitotic spindle poles.
Sequence:
MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQPCSQLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVIHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAEVNKLRRQITQKKNEKEQERRLQQALLSRQMPSESLEPAFSPRMSYSGFSAEGRSTLAETEPSDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSSYASTSGGLKFTGSGADLLPSQSAAGDSGEESDDSDYENLIDPAESPHSEYSHSKNSRPSTHPDEDPRNTQTSQI
The following text describes a protein:
Function:
Could act as a receptor for an unknown ligand.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MWQPPRLVMNRCKGSSTRPSVTPVLLLLLLVLCAPASAQGGSLRNSLDVECVLLQTTESSTVALNALDVTAQKASITCARKSLSSPLAWAPTDGSGSTLNVYMSALSDTLLSSVVAASSSTSCTLVTSISEGVLDTRRMSKNVYFTNADPATEMLALLSYVMINGAPPKIGFVYTRTDDEETSAGAAVYKEFVRRMDELAYTGTLVTYEAAEDYDSATFAAFSKKFESGVSVVFFFPSAGKGTNDMFAELLKSSREVKVLMPSWLIRTATSRYLVATKPKVPASSIIVSSTNPHPEDKNFEKSMGQFKKDYGNTKPTLASSSVDGIEAVAGWITARATVATLQYHTLWTESPTQKLYFDMLHKQHVYTIGGDIVLGAYGSSCNVGGRMVLLYSLRAMSSGETGAYYGLASVPGANLMLKSWECHAVDVTLSISKMVRAAYVKYHGIGENSNYMTTQMDNIVPAAMVSATFTEATIGPLDSLADTTWKAALDNSPTIAVFGAASVGVDKSPVEKVLVEPVFLQPTLYQNASNVVYLTATNEQQLGAVATWVAQSAVAPDVHAVLLNSGASATAMQSTLQRIMTHAGVTVESVKTLGVGEKLSSKDLPKSGLVLLTGIMQNDIYTLQKHIQNNQNARVILLFDEVTQWYRQIKQAFAASPSSGKRLVFVTNLPPWTPKKQDISRISAEFLATAIGPDYHSPASMRGFLAVRALSMLSYNAANPSTSALLDALYTQQVLQIKDLTLGPFKRTGCAYSTGSNQVECTGVLNGGAGGIYIWSYSDMEGGTNGPIAGPYVVNLFGYVDANDEGSSSSGKAHSSSSKSTIIASVVVCVIVMGVVVAAVIICVLCTRDSRDNRNAPKDENEHVTLIFTDIESSTALWATAPQAMSSAVALHHKLIRQLVIKYKCYEVKTIGDSFMIACKQPFAAVQLARDIQVALHQADWGSTAIDDAYELIGKPSGGTDPGECGSRPWSGLRVRAGVHYGLVEVRFDNVTKGYDYYGNVVNTAARTESVSCGGQVICTSSVVKALTEEEQGMVQFVALGPHQLRGVAEPIEMYELRTVPGRVFPSKGSDVSANPLASLTAGAEADAAPNGEEVDPMLTQEDTFAEVATGVEPVAEVLDVYFSAYTNNQKIKFLQKTCKCFCLPSPPRRMFASNDAYLNSLMLTVATRTSAVINFRHRKLENDTLRPAAESQANAPALELVAHRDAAAELRRHSSVFFSGVDSPVAGESKRRRSVVIDRPGASLSKHGNSDSTMMLVLDNGELLTLCSSAGQSCTEKLPEVREATKVYQNGAPSISGDEVTPCFEGGNGLLFRIIDKATKRWAFYNDTVDFVMHVYFSVGRTSAVKWGPSVAGKVTQAEETSRYEGELIVPPLSTEVLMTGRVNGYTMRYCAMPSSGGE
The following text describes a protein:
Function:
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Miscellaneous:
MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.
Sequence:
MRLKELGEFGLIDLIKKTLESKVIGDDTAPVEYCSKKLLLTTDVLNEGVHFLRSYIPEAVGWKAISVNVSDVIANGGLPKWALISLNLPEDLEVSYVERFYIGVKRACEFYKCEVVGGNISKSEKIGISVFLVGETERFVGRDGARLGDSVFVSGTLGDSRAGLELLLMEKEEYEPFELALIQRHLRPTARIDYVKHIQKYANASMDISDGLVADANHLAQRSGVKIEILSEKLPLSNELKMYCEKYGKNPIEYALFGGEDYQLLFTHPKERWNPFLDMTEIGRVEEGEGVFVDGKKVEPKGWKHF
The following text describes a protein:
Function:
Possible sulfate transporter.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTSNNSLLGRGRMSYSSTAPPRFKRSVDQRDTFSDNFDYDKDSSNRGRTYIAASNSTTGVPPPNNSRSGCTNNTNNTNNTSNTSNTNNNDSVDENTVFETLPYYLPCFSWLPEYTFNKLWGDVIAGISVASFQIPLALSYTTSIAHVPPLCGLYSLAISPFVYGILGSVPQMIVGPESAISLVVGQAVESITLHKENVSLIDISTVITFVSGTILLFSGISRFGFLGNVLSKALLRGFISSVGLVMIINSLISELKLDKFLVSLPQHYHTPFEKILFLIDYAPAQYHIPTAIFSGCCLIVLFLTRLLKRKLMKYHKSAIFFPDILLVVIVTILISMKFNLKHRYGISIIGDFSMDNFDELKNPLTRPRRKLIPDLFSASLIVAMLGFFESTTASKSLGTTYNLTVSSNRELVALGFMNIVISLFGALPAFGGYGRSKINALSGAQSVMSGVFMGVITLITMNLLLQFVHYIPNCVLSVITTIIGISLLEEVPGDIKFHLRCGGFSELFVFAVTFCTTIFYSIEAGICIGCVYSIINIIKHSAKSRIQILARVAGTSNFTNLDDYMMNMKRNSLDVEGTEEIEGCMIVRIPEPLTFTNSEDLKQRLDRIERYGSSKIHPGRKSLRSKDSIKYVIFDLGGMTSIDSSAAQVLEEIITSYKRRNVFIYLVNVSINDKVRRRLFKAGVAASVERAQANNNENNTSNTFSDAGETYSPYFDSIDAALYEIEKMKIKGNNVPNNDSESFMSNTLFNSSLV
The following text describes a protein:
Function:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER), probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA.
Subcellular Localization:
Nucleus.
Sequence:
MEDIMQLPKARVNASMLPQYIDRPVCFVGKLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGKVTAKATVLCASYTLFKEDTNRFDLELYNEAVKIINELPQFFPVGLPQHE
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Sequence:
MYTYMEYLQKCFYKSTNWNEDNIYSNITATSQALLDFPIPNGFKIDSSSKTTDYSASSFTLSNHHQINGSLAYLYSSIPLTNTMGTKDVSLQDAIAGFRIIEPSVGLRSKLKNNIMSNRSSLLYGRMYFPGSALEAMIIKRLTKNSQLLIKCVNNPHLEKNGTMIVYLQNNTAKYSRELIYSTNEALIGLRCLYNLGDATSHNFTNINPAVIPKFDNSVVSIGTEIWYAARTMSPGLSAALRYSTRSTSTGKPLTMTLAINPIVGHVSSTYTVKTSVASTFCSKYDFNVFSYASNLSLGFELYSYANKKKNSFPSFEHHEIHSSSEENKYLKKHPELQRHHNLHHNLHHQRVPIKSHKYEGNRTIINPIQNLDNVYHINPTLLSSNGSTSTTTNNENTNTSETVTAAFQNLVNESDFSSVFKFSTSLNDKVVKILWEGRLKEFLVSTGVKLSLNPITNTPEFNKLGISFSYAL
The following text describes a protein:
Function:
Component of light signal transduction machinery. Involved in fruit pigmentation and fruit nutritional quality. Acts as a negative regulator of fruit pigmentation. Probably acts by participating in the CDD complex, a complex probably required to regulate the activity of ubiquitin conjugating enzymes. Repression of photomorphogenesis is probably mediated by ubiquitination and subsequent degradation of photomorphogenesis-promoting factors such as HY5.
Subcellular Localization:
Nucleus.
Sequence:
MFKTNNVTARLFERQICTPAPGTSIHRARRFYENVVPSYTIYDVECPDHSFRKFTDDGLYFVSFSRNHQDLVVYRPTWLTFSCKEEDCDTHDLPLKARKFESFFTQLYSVTLASSGELICKDFFLYMESNQFGLFATSTAQIHDAPPTGGAIQGVPSVEKITFHLLRLVDGAILDERVFHNDYVNLAHSIGAFLYDDLLAIVSLRYQRIHILQIRDSGDLVDVRAIGEFCREDDELFLNSNSQVLVNHVGNGFHHSLPQSETSFLSGIKQRLLSYIFRGIWNEADQTMRVQCLKKKFYFHFQDYIDLIIWKVQFLDRHHLLIKFGSVDGGVSRNADIHPSFFAVYNMETTEIVAFYQNSADELYFLFELFSDHFHVSSKSSLHMNFMSSHSNNIHALEQLRCTKNKATNFSQFVKKMMASLPCSCQSQSPSPYFDQSLFRFDEKLISAIDRHRQSTDHPIKFISRRQPNILKFKMKPGPEAGSTDGRTKKICSFLFHPILPLALSVQQTLFLQASVVNIHFRR
The following text describes a protein:
Function:
Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition.
Subcellular Localization:
Secreted.
Sequence:
MRWPCSSWFRGLWPEAAPWAVLLALGVPGWVLAVSATVAAVVPEQHVSSAGQAPLDWLLTDRGPFHRAQEYADFMERYRQGFTTRYRIYREFARWKVNNLALERRDFFSLPLPLAPEFVRNIRLLGRRPNLQQVTENLIKKYGTHFLLSATLGGEESLTIFVDKRKLSRKSETTGGIPVVGGTGNSSAVSLETLHQLAASYFIDRESTLRRLHHIQIATGAIKVTETRTGPLGCSNYDNLDSVSSVLVQSPENKVQLLGLQVLLPEHLRERFVAAALSYITCSSEGELVCRENDCWCKCSPTFPECNCPDADIQAMEDSLLQIQDSWATHNRQFEESEEFQTLLKRLPSDRFLNSTAISQYWTMDSNLQHRYQQLGASLKVLLKKMHRIVRRLFNLCKRCHRQPRFRLPKERSLSFWWNRIQSLLYCGESTFPGTFLEQSHSCTCPYDQSSCQGPIPCALGEGPACAHCASDNSTRCGSCNPGYVLAQGLCRPEVAESLENFLGLETDLQDLELKYLLQKRDSRIEVHSIFISNDMRLGSWFDPSWRKRMLLTLKSNKYKPGLVHVMLALSLQICLTKNSTLEPVMAIYVNPFGGSHSESWFMPVNEGNFPDWERTNVDAAAQCQNWTITLGNRWKTFFETVHVYLRSRIKSLDDSSNETIYYEPLEMTDPSKNLGYMKINTLQVFGYSLPFDPDAIRDLILQLDYPYTQGSQDSALLQLIELRDRVNQLSPPGKVRLDLFSCLLRHRLKLANNEVGRIQSSLRAFNSKLPNPVEYETGKLCS
The following text describes a protein:
Function:
Plays a crucial role in homologous chromosome pairing and synapsis in meiosis. Does not seem required for cytokinesis. Is essential for meiotic bouquet formation, homologous chromosome pairing and normal recombination, and synaptonemal complex (SC) assembly. Required for the proper association of PAIR2 with chromosomes.
Subcellular Localization:
Chromosome. Nucleus. Note=During interphase-early leptotene, distributed as numerous punctuate foci throughout the chromatin. Associates with chromosomal axes at leptotene, zygotene and pachytene. Associates with chromosomal axes at zygotene.
Sequence:
MEVELTNIQKATSSDYWSLASNQYPCGKFPKVSVGVTIPRTSSVSRGRDAASTAAFEKNLSQGTDGRSRPPKMDNASLQVSPEAANHGGSAKEVPKPVPAKVSVSQPDDNAIEQTGTFSFGTRREQDSHLDQLDRPPLVSSQGKRQVESADKNKPNSEMLRMKLWEILGGTSQNKEAVASPNPEDIETPCQPKSQIANGPSSGRQKVFTSPVPYNIKTPAQFNSQTANKPSSDPIESDSDSPQVVEVRPITRSLGRKKEPTGSTHQDKSGSAKKPLSTHRSTPKQKILDNVFAFNDKCTPKTVGKSANGESGSLRNLRSLSRRAKVEPKKAHCSDRISHKTTQDDMERKVPSKYIPSEKKGEKTNSFSSLSRTGKTAESCSRSPKRERRVNTMANVGARKMQLSENLLVKTLNDGEHKLSSPQLTSFKSKGKCSSISPQQKENDNTHIPEASDRTAARNSFNSTPSPAANPSPVLRKYSWEHDENPAINGKSGQKDASPLADRFSDMPDDFASPTFAANIKISPHRSKMLDDDLFSSKYPKGVNRSRSTSFTSDPESEPLDKMEKTNELPGSESPNSQEERQNRKQPHLSPLSPIESEGAQISIPSFRKGYKSHKWLSDVDSPDKSSIEHLGRKSHLKEGRKGKRQLTSPTHFATSGTQETMSDKEPEKVPENYLTRAFDQLVVVLGRFQTKIKSETRNKSSKILAATGEIIRQHLEGVEGQMQADVDKLVNAGKSKRKRLESTFEEQQEKLRILHEKFKEEVNQQLLGCKNSVEDFEAYHAELKGVADKQKASHKKLLQNAEKTVGAQLSDAETKIAEVQKRARKRMKGLKFVLKELIAETAE
The following text describes a protein:
Function:
Plus-end directed microtubule motor that may be used for anterograde axonal transport and could conceivably move cargos in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MGENVKVVVRCRPMNKREQQSNCKSVIQIDNSLVNLDNPNDPNASQKSFQFDNAYGYAATTENIYSDICYSLVESVLEGYNATIFAYGQTGCGKSHTMQGTTYNLSAADPNNANNIGIIPRSFEHIFEAISLASEVRYLVLVSYLEIYNETIRDLLQPQSPAATASTLQIKEVPGEGVMVQNLSLHTVHGMKECIELLEAGAKNRMVGATLMNIESSRSHSIFSISLEQMSTSVEADSGVAIKRGKLNLVDLAGSERQSKTGATGDRLKEATKINLSLSALGNVISALVDGKTRHIPYRDSKLTRLLQDSLGGNTKTLMIACISPADYNYDETLSTLRYASRAKNIANKPRVNEDPKDTMLREYQQEIMRLKELLKGEGSTPPAAVNGHHDANGLDAEKQALRSQYDQEVTHLRREYEQQRIAKQELVKDIEKIKAYYEQQMQLLTSSRQQAADAEQHRQSTPAVTLAGRDRKEIYDRIKQIKDALIGGERANDIQLKEKRYRNKLASEKRINALAQALGRIEQSADRDLLQGHYSDIQQELKVRYEQIRALRRRTKLLEQEVSDIQGEFQRERDDYLATIRLLEKKVLFYETVFQKAMPVLRKDGRYWNLECLERESEWNDDLRKWRLPDDTLLRLRLPPAETPPPAPSPPPSDVSSPGKLNGRESQTSLTAPGRLERSSTMFLAKLPEFQQHDRKPPDEQQQRKGDFLSKSTNSNPFPKIEDVAMTYFRPRRAAELVYKSGWRSLQK
The following text describes a protein:
Function:
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MATPMGNSRKTMIAKYAIISRLVVTFLQILLNNLIPDHHADAFHQDPMQNPGFGDLCIDLLLGGFCKWDGAHFLHIAEHGYTTDRMMAFFPLYPGLVRALADTLFSPLQMVMQLRSVLLVAGWLLNVLMFTLAAVVLYELTKRVCKDQRIADIAWILYCFNPASIFMTAMYTEASFLLLSLSGMLFLEKRRYLISTIAFGLGTCARSNGIVSIGFVAYHTVQLSIFVFAKMRSPINLSTLKKVCRIIVVGVTRTFYSAAIILFPCALYQIYCYLRICNKEKVISFQKILEHGMEILFKRANNRTSVLQTTDDVPLWCSKSFVIPYSEVQAEHWNVGLLNYYEFKQLPNFFLALPVIILCLYGVQDYCSLKWDHVKVLGLLQPIRKDVKKTDDPISQSEGFYSSGVFVYLVHLLVLLVFGVCCMHVQVVTRFLFSSSPVPIWIASHIIQSSLKPNGVDTPSPELNGSVQELIPLDIMWRKHLDWKGRLLRGYFLGYCVIGVALHCNFLPWT