lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the biosynthesis of the siderophore staphyloferrin A. Catalyzes the ATP-dependent condensation of D-ornithine and citrate to form a citryl-D-ornithine intermediate.
Sequence:
MNLNLIFKEQTLKFNKEEQETYLFLQQHNSDWANIFKEMILQGRDKVTQRLVTSMHRENLVKARTQSKKILSRDLIMLDISTTHILEIQFPQAKQTLYAPITGEHAFDRIDVEGPFYIKDDITNTITRVHHPNEILECILIEAPDLKNAASDQFQQDLINSATNMTFAISYQALSMQHDSAPLFNIIENSEDSYLRSEQAVIEGHPLHPGAKLRKGLNALQTFLYSSEFNQPIKLKIVLIHSKLSRTMSLSKDYDTTVHQLFPDLIKQLENEFTPKFNFNDYHIMIVHPWQLDDVLHSDYQAEVDKELIIEAKHTLDYYAGLSFRTLVPKYPAMSPHIKLSTNVHITGEIRTLSEQTTHNGPLMTRILNDILEKDVIFKSYASTIIDEVAGIHFYNEQDEADYQTERSEQLGTLFRKNIYQMIPQEVTPLIPSSLVATYPFNNESPIVTLIKRYQSAASLSDFESSAKSWVETYSKALLGLVIPLVTKYGIALEAHLQNAIATFRKDGLLDTMYIRDFEGLRIDKAQLNEMVYSTSHFHEKSRILTDSKTSVFNKAFYSTVQNHLGELILTISKASNDSNLERHMWYIVRDVLDNIFDQLVLSTHKSNQVNENRINEIKDTMFAPFIDYKCVTTMRLEDEAHHYTYIKVNNPLYRENN
The following text describes a protein:
Function:
Plays a crucial role in the metabolism of thyroid hormones (TH) and has specific roles in TH activation and inactivation by deiodination. Catalyzes the deiodination of L-thyroxine (T4) to 3,3',5'-triiodothyronine (rT3) and 3,5,3'-triiodothyronine (T3) to 3,3'-diiodothyronine (3,3'-T2) via inner-ring deiodination (IRD). Catalyzes the deiodination of rT3 to 3',5'-diiodothyronine (3',5'-T2), 3,3'-T2 to 3'-monoiodothyronine (3'-T1) and 3,5-diiodothyronine (3,5-T2) to 3-monoiodothyronine (3-T1) via IRD (By similarity). Catalyzes the deiodination of 3-T1 to L-thyronine (T0) via outer-ring deiodination (ORD) (By similarity). Catalyzes the tyrosyl ring deiodinations of 3,3',5,5'-tetraiodothyronamine, 3,3',5'-triiodothyronamine, 3,5,3'-triiodothyronamine, 3,5-diiodothyronamine, 3,3'-diiodothyronamine and 3-iodothyronamine (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein.
Sequence:
AACILLFPRFLLTAVMLWLLDFLCIRKKMLTMPTAEEAAGAGEGPPPDDPPVCVSDSNRMFTLESLKAVWHGQKLDFFKSAHVGSPAPNPEVIQLDGQKRLRILDFARGKRPLILNFGSCTUPPFMARLRSFRRLAADFVDIADFLLVYIEEAHPSDGWVSSDAAYSIPKHQCLQDRLRAAQLMREGAPDCPLAVDTMDNASSAAYGAYFERLYVIQEEKVMYQGGRGPEGYKISELRTWLDQYKTRLQSPGAVVIQV
The following text describes a protein:
Function:
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSPPNQDAQEGRPDSPTAEVVDVRRGMFGVSGTGDTSGYGRLVRQVVLPGSSPRPYGGYFDDIVDRLAEALRHERVEFEDAVEKVVVYRDELTLHVRRDLLPRVAQRLRDEPELRFELCLGVSGVHYPHETGRELHAVYPLQSITHNRRLRLEVSAPDSDPHIPSLFAIYPTNDWHERETYDFFGIIFDGHPALTRIEMPDDWQGHPQRKDYPLGGIPVEYKGAQIPPPDERRGYN
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. Endomembrane system; Multi-pass membrane protein.
Sequence:
MENGIVLTIIDMENKVQTAVGIAGIISGVFLYLTPMKIVIRIAEERSSEKLSVTPYFLAYLNCVFYMGYTAWSSNWLAVIANALDALIVFHYVMIFMFLSPINLIAYKRVGALLVVFVVLVTFIFVPLSMHEHLGLLFNGLVATAFSIALYITSLFLVIQRKEVEFMSFYTSILMLLNGAFWFVFGLLRQDFFIVLLNGVGCGVGAAQIYLMYPNNKGKTVKQKKTIEGETRNQKNKNKGGENKTKIA
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:
MMEFITETYKELKRMNVRQFLGQALQLGLIVTSALMIWKSLMLVTGSESPVVVVLSGSMEPGFYRGDILFLNMGKAPIRTGEVVVFNLDGRDIPIVHRVIKVHERRNGTHIDVLTKGDNNFGDDRALYNKGQDWLHQHHIMGRAVGFLPKVGMVTIIMNDYPYLKYALIGVLGLLVLTNKDA
The following text describes a protein:
Function:
The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein (By similarity). The carboxylated form binds strongly to apatite and calcium (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MKTLSVLVLCSLAVLCLTSDASFSSQPAVDTPAQEGLFVEQEQASSVVRQAPKELSLSQLESLREVCELNLACEDMMDTSGIIAAYTTYYGPIPF
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. Also acts as an important regulator of the HIF1A-mediated hypoxic response. Required for HIF1A mRNA stability independent of poly(A) tail length regulation (By similarity).
Subcellular Localization:
Cytoplasm, P-body. Nucleus. Note=Shuttles between nucleus and cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MNFEGLDPGLAEFSPAMHSTLDPVLDAHLNPSLLQNVELDPEGVALEALPVQESVHIMEGVYSELHSVVAEVGVPVSVSHFDLHEEMLWVGSHGGHATSFFGPALERYSSFQVNGGDDIRQIQSLENGILFLTKNNLKYMARGGLIIFDYLLDENEDMHSVLLTDNSTLLVGGLQNHVLEIDLNTVQETQKYAVETPGVTIMRQTNRFFFCGHTSGKVSLRDLRSFKVEHEFDAFSGSLSDFDVHGNLLAACGFSSRLTGLACDRFLKVYDLRMMRAITPLQVHVDPAFLRFIPTYTSRLAIISQSGQCQFCEPTGLANPADIFHVNPVGPLLMTFDVSASKQALAFGDSEGCVHLWTDSPEPSFNPYSRETEFALPCLVDSLPPLDWSQDLLPLSLIPVPLTTDALLSDWPAANSAPAPRRAPPVDAEILRTMKKVGFIGYAPNPRTRLRNQIPYRLKESDHEFDNFSQVTESPTGREEEPLHTVSKKYRKVTIKYSKLGLEDFDFKHYNKTLFAGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHLCQKEFCLACELGFLFHMLDLSRGDPCQGSNFLRAFRTIPEASALGLILADSDEASGKGSLARLIQRWNRFILTQLHQDMQELEVPQAYRGAGGSFCSSGDSIIGQLFSCEMENCSLCRCGSETVRASSTLLFTLSYPEDKTGKNYDFAQVLKRSICLEQNTQAWCDNCEKYQPTIQTRNIRHLPDILVINCEVNSSKEADFWRLQAEVAFKIAVKKYGGEMKSKEFALADRKELRSPEGFLCSSIEELKNVWLPFSIRMKMTKNKGLDVCNWADEHELSSLGAPSQWGPARAEEELGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHQRKEGVTHQQWYLFNDFLIEPIDKYEAVQFDMNWKVPAILYYVKRNLNSRYNLNIKNPIEASVLLAEASLARKQRKTHTTFIPLMLNEMPQVGDLVGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKISSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETHDSIEDARTALQLYRKYLELSKNGTEPESFHKVLKGLYEKGRKMDWKVPEPESQTSPKNAAVFSVLAL
The following text describes a protein:
Function:
This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC, interleukin-2 receptor, somatostatin receptor II, and interferon-beta genes. It may act in T-cell activation.
Subcellular Localization:
Nucleus.
Sequence:
MDTGDTALGQKATSRSGETDKASGRWRQEQSAVIKMSTFGSHEGQRQPQIEPEQIGNTASAQLFGSGKLASPSEVVQQVAEKQYPPHRPSPYSCQHSLSFPQHSLPQGVMHSTKPHQSLEGPPWLFPGPLPSVASEDLFPFPIHGHSGGYPRKKISSLNPAYSQYSQKSIEQAEEAHKKEHKPKKPGKYICPYCSRACAKPSVLKKHIRSHTGERPYPCIPCGFSFKTKSNLYKHRKSHAHAIKAGLVPFTESAVSKLDLEAGFIDVEAEIHSDGEQSTDTDEESSLFAEASDKMSPGPPIPLDIASRGGYHGSLEESLGGPMKVPILIIPKSGIPLPNESSQYIGPDMLPNPSLNTKADDSHTVKQKLALRLSEKKGQDSEPSLNLLSPHSKGSTDSGYFSRSESAEQQISPPNTNAKSYEEIIFGKYCRLSPRNALSVTTTSQERAAMGRKGIMEPLPHVNTRLDVKMFEDPVSQLIPSKGDVDPSQTSMLKSTKFNSESRQPQIIPSSIRNEGKLYPANFQGSNPVLLEAPVDSSPLIRSNSVPTSSATNLTIPPSLRGSHSFDERMTGSDDVFYPGTVGIPPQRMLRRQAAFELPSVQEGHVEVEHHGRMLKGISSSSLKEKKLSPGDRVGYDYDVCRKPYKKWEDSETPKQNYRDISCLSSLKHGGEYFMDPVVPLQGVPSMFGTTCENRKRRKEKSVGDEEDTPMICSSIVSTPVGIMASDYDPKLQMQEGVRSGFAMAGHENLSHGHTERFDPCRPQLQPGSPSLVSEESPSAIDSDKMSDLGGRKPPGNVISVIQHTNSLSRPNSFERSESAELVACTQDKAPSPSETCDSEISEAPVSPEWAPPGDGAESGGKPSPSQQVQQQSYHTQPRLVRQHNIQVPEIRVTEEPDKPEKEKEAQSKEPEKPVEEFQWPQRSETLSQLPAEKLPPKKKRLRLADMEHSSGESSFESTGTGLSRSPSQESNLSHSSSFSMSFEREETSKLSALPKQDEFGKHSEFLTVPAGSYSLSVPGHHHQKEMRRCSSEQMPCPHPAEVPEVRSKSFDYGNLSHAPVSGAAASTVSPSRERKKCFLVRQASFSGSPEISQGEVGMDQSVKQEQLEHLHAGLRSGWHHGPPAVLPPLQQEDPGKQVAGPCPPLSSGPLHLAQPQIMHMDSQESLRNPLIQPTSYMTSKHLPEQPHLFPHQETIPFSPIQNALFQFQYPTVCMVHLPAQQPPWWQAHFPHPFAQHPQKSYGKPSFQTEIHSSYPLEHVAEHTGKKPAEYAHTKEQTYPCYSGASGLHPKNLLPKFPSDQSSKSTETPSEQVLQEDFASANAGSLQSLPGTVVPVRIQTHVPSYGSVMYTSISQILGQNSPAIVICKVDENMTQRTLVTNAAMQGIGFNIAQVLGQHAGLEKYPIWKAPQTLPLGLESSIPLCLPSTSDSVATLGGSKRMLSPASSLELFMETKQQKRVKEEKMYGQIVEELSAVELTNSDIKKDLSRPQKPQLVRQGCASEPKDGLQSGSSSFSSLSPSSSQDYPSVSPSSREPFLPSKEMLSGSRAPLPGQKSSGPSESKESSDELDIDETASDMSMSPQSSSLPAGDGQLEEEGKGHKRPVGMLVRMASAPSGNVADSTLLLTDMADFQQILQFPSLRTTTTVSWCFLNYTKPNYVQQATFKSSVYASWCISSCNPNPSGLNTKTTLALLRSKQKITAEIYTLAAMHRPGTGKLTSSSAWKQFTQMKPDASFLFGSKLERKLVGNILKERGKGDIHGDKDIGSKQTEPIRIKIFEGGYKSNEDYVYVRGRGRGKYICEECGIRCKKPSMLKKHIRTHTDVRPYVCKLCNFAFKTKGNLTKHMKSKAHMKKCLELGVSMTSVDDTETEEAENLEDLHKAAEKHSMSSISTDHQFSDAEESDGEDGDDNDDDDEDEDDFDDQGDLTPKTRSRSTSPQPPRFSSLPVNVGAVPHGVPSDSSLGHSSLISYLVTLPSIRVTQLMTPSDSCEDTQMTEYQRLFQSKSTDSEPDKDRLDIPSCMDEECMLPSEPSSSPRDFSPSSHHSSPGYDSSPCRDNSPKRYLIPKGDLSPRRHLSPRRDLSPMRHLSPRKEAALRREMSQRDVSPRRHLSPRRPVSPGKDITARRDLSPRRERRYMTTIRAPSPRRALYHNPPLSMGQYLQAEPIVLGPPNLRRGLPQVPYFSLYGDQEGAYEHPGSSLFPEGPNDYVFSHLPLHSQQQVRAPIPMVPVGGIQMVHSMPPALSSLHPSPTLPLPMEGFEEKKGASGESFSKDPYVLSKQHEKRGPHALQSSGPPSTPSSPRLLMKQSTSEDSLNATEREQEENIQTCTKAIASLRIATEEAALLGPDQPARVQEPHQNPLGSAHVSIRHFSRPEPGQPCTSATHPDLHDGEKDNFGTSQTPLAHSTFYSKSCVDDKQLDFHSSKELSSSTEESKDPSSEKSQLH
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.
Sequence:
MGLIVQKYGGTSVGSAERMRSVAERIARTHRQGHDLVVVVSAMGHTTDALVKMACEMHGEPDPREMDMLLTTGEQQSVALLTMALHALGCKAISLTGAQVGVVTEPNHTRARIRRVQTGRINELLAAGYVLVVAGFQGICHSRFWEITTLGRGGSDTSAVALAAVLKANRCEIYTDVPGVLTTDPRLVGDAALLEEITSEEMLELASLGAQVLHPRAVEIARNYAVPLVVRSSWSDAPGTIVLSPRLPVDRAIDNLETERPVDAVYIDNHQAKIALLRVPDRPGVAAALFGHLAKAGIDVDLIIQSIHHPNAPEPTNDIAFTVQRSDLAAAVATSETAAAALGGCAVVVDPVPTKVSIRGAGIIGRPGVVAQMFKALAEARINIQMISTSETSLSCVIAGEQAEKAGEVLCGQFGLRAPVYEEPPVVSGARPVAQAVRGVALDTNQAQVAILQIPDRPGVAAEIFQCLAQEGIAVDMIVQSQRGADTNDIGFTVSRSAVRAAQRALASLCMGFAGCGGVVVRESVAKLSLVGAGIVGTPGVAARMFETLASLGTNIEMISTSTIKVSCIVEAACCEASLQAVHRAFGLGSGAMVAVEGRSS
The following text describes a protein:
Function:
Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex. Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.
Subcellular Localization:
Nucleus.
Sequence:
MSDKELEEQLASAGTKLLEPPSSVDELMPLLEELENYLSRVEQSPTTSMQDALSPSLKALVADQLFRHSDADVRVAIASCISEITRITAPEAPYDDDLMKEVFQLIVSSFENLHDKSSRSYTRRASILETVAKVRSCVVMLDLECDAMVVEMFQHLLNSIRDHHPEHIFQSMETIMTLIIDESEDVSPELLSPVLDSVKSDNKEVLPIARKLGETVLKNCASKLQPYFCQALKALGTSIDEYTNVITSIYQEASAAVEGNNNHAASEHKVNKEKASHQDSPAAARSPKSVIGNGATQKAELDSVSNRKPEDARHGSPPKVTKALSNDNIVKLNTANVAKKESKLGKKKKGRGRKPVSSTRSNATPDGSQTIPDSPHDNSPVEYSPSESEKETAANPSSPKPAGDESMSVASLSQNEGQPDESRPRKGGRRKKQELAKEVMGHAADISKNEATSDKEVKPHTSTGRNTSLVSSEDVKTGITLKISRKENAATSDVEAKSLKNSSRKVSVGTDTEDGSSTKRSGDKKGVARVKVASEKDLRKSTEAAASPKSAMKAGGGDEKSHETPKESLKRKRTPGKEASDAKEYGEDLVGSKIKVWWPQDRAFYKGVVDSFDPIRKRHKVLYTDGDQEILNLKKQKWELVEGNSVSYRGQEGDSRSPDASPELPLKKRAKMKEGRTETSAKKGNASSSKSNAGSAKSGKKFRGGNKSDGKFEKDGIGKSKDRTSENGSKSGSVALNKMTKTGKPKDEDPSTPHVASKSGEESSVTTKSKKGSKIASKGSDLKSSGKPEKLKSNGSDKLKSGLLKAKERIMDNDSVDSAETETNEERLDPSKVLGSGSKSGKKRQRA
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
Subcellular Localization:
Nucleus.
Sequence:
MPKETASRWSESRYTNLQVPSYVPSEALMHEDGQFLRAFLLRVLANDMQRMLATNTCATYFRNIPLEPEYDASGNRTNTPENVVMEKRLRVMDDISKLLRTYVERAEYAANKSKDINRRIYFTAEQIETGDYGALIGPRGLVHQQLEKETNCHIVLVGRGITNPLKDTNPNAASMALEDPHVRITATTEEDLQTAAERIEWILSDEPEAVEFRENNRRRMAQVDGRYDPRTWMTAAEKRKKAAAEKAAAAGGAAAGEDETKAEKGRKREREEAPVEEEDTELNEFLEDL
The following text describes a protein:
Function:
Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.
Subcellular Localization:
Nucleus.
Sequence:
MGSRLDKNSESIRKRIESHTFQNEGGEEYEGSKFGGFSDYFRRKRIKLQNLDAEVRSTSTGNPNIFRGVVAHVNGYTQPSLNDLHHLIVTHGGGFMQYLDGKTTVTHIIASTLTPRKAIEFKRYRIVKPAWVVDSVKAGKCLPWDSYRVLDEGVGQRLLGFSDGKVVSHSNTPQRGYRDQTNASWYTSQVKTVAGNIDDDDGPQFPSSQVQRIMPHKTGAFAPSPTDQLVESLEEVDQIPVDDPISSTGSFEVTSSLEEALKHAADIPTPTSREALKSTRTAKDSFLMNNSPSPSPALQTSSSPAQVTPKRPEFLLGNTKILHDVEASRYAEEVPVERRLFSNAKKRPHNEETYNSPKKAQVETAEEHNAMLLADPHTRKSSTANPDFIKQYYSESRLHHLSAWKADLKSKFQQMASEKSASQKQSMKWKPGSRRYIMHVDFDSFFCAVSLKSAPEYFDKPAVVAHGNGTGSEIASCNYPARVFGVKNGMWMKNAIKLCPDIKVLPYDFPAYEEASKAFYEAILDVGGIFQSVSVDEAFVDITSLCLAAGGTDGVGIREGSIWREQERAEEIGNALRKVIREKTGCNVSVGIGGNILLAKVALRKAKPAGQYQIKPEEVLDFVGELDVQNLPGVAYSIGGKLEEIGVKFVKDVRQLSKDRLMTVLGPKTGEKIWDYSRGIDRAEVGEQVVRKSVSAEVNWGIRFISQVEAEEFVQNLCIELQRRLIDQRVKGRQMTMKIMRKAADAPLDPPKFLGHGNCDTFNKSIVLGVATNDATIIGREAVSILRSYGFSPGELRGLGVQMTKLEPVKSSNGTPFDGSQRKINFGAPVVSKPVKQVVEDPIVDDPETPTKRRTTPRAQPTNPLSEGIHDPVTPTKPKSIMKSIHTEDPIDESSPLKAKPTPAHPATFIARTNAGDQSARKLNLTGTQFIIPSQIDPEVLKELPQNIRSKLMAQSKSVPVSREQTPVTAMPESLSKSPSRLKTSHMPSQLDPEVFDALPEEMKAEILASYKPQIANSIPGAQSILPQSPRRNRTITGKKPPTPVKKRGRGRPPGPRIKSEPPHGPLQSKFVANPRAREVSVDATDDTEVLDPEFLAALPEDMREEIMAEHRRKRLQKRGNLMTSTVKKVKKPDPPPLGPRKIRLPPRPIKPTFTTQELSTLEELRETLTIWFREFESEGPHPDDVAAMERYLRRVILDERDLAKVVGVVKWLEWLKDDSEIVGKGKELWENAFEDVKSKVQEAVKERGLGILDI
The following text describes a protein:
Function:
Involved in vesicular protein trafficking.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MLSHYIFLAFVLLPFRVSAFYFYGYGGDRKCFLKELSKDTLLKGSYNLEVYDDKLADYALPSYNDYGIVIDVEEVFDNNHRVVHQQGSPSGDFSFLALESGEYKICLQSRVNNWVGKTKTKLEIEFEVGFEAMLDMQRKETLESLHGKVSILNSKIVDIRREQQLMREREESFRDISESVNSRAMWWTVTQVTLLIIICVWQMKSLRSFFVKQKVL
The following text describes a protein:
Function:
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTKLAQWLWALALLGSAWAALTLGPGSRALPPPWHQVLGPLPAYLLVVAGCYALGTVGYRVARFNDCEDAARELQAQIRQARADLGRKGLRF
The following text describes a protein:
Function:
Nuclear receptor that lacks a DNA-binding domain and acts as a corepressor that inhibits the transcriptional activity of other nuclear receptors through heterodimeric interactions. Component of a cascade required for the development of the hypothalamic-pituitary-adrenal-gonadal axis (By similarity). May also have a role in the development of the embryo and in the maintenance of embryonic stem cell pluripotency (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Note=Shuttles between the cytoplasm and nucleus. Homodimers exits in the cytoplasm and in the nucleus.
Domain:
Homodimerization involved an interaction between amino and carboxy termini involving LXXLL motifs and steroid binding domain (AF-2 motif). Heterodimerizes with NR5A1 and NROB2 through its N-terminal LXXLL motifs.
Sequence:
MAGEDHQWQGSILYNMLMSAKQTHATREAPEARLRGSCWGCSCGSEPPVGREGQPGGPAVALLYRCCFCGEDHPRQGSILYNMLTSAKQTQETPEAPEARLGGACWGCSCGSEPRVGREELPGGRATVLLYRCCFCGEEHPRQGSILYSLLTSAKQTHVALEAPEARPGGAWWDRSYCAQRLGAREELPGGRPVTLPYRCCFCGEDHPRQSGILCNMPMSAKQTHVAPEAQPGAPWWDPSCAAQRVALKSPQVVCEAASAGLLKTLRFVKYLPCFQVLPLDQQLVLVRSCWAPLLMLELAQDRLNFETVETLEPSLLQMILTTRRQETEGDEPPSPQPPVQPHLVLPSEAEHLPSVAEVQAIKGFLAKCWSLDISTKEYAYLKGTVLFNPDLPGLQCVKYIQGLQWGTQQILSEHIRMTHRGYQARFAELNSALFLLRFINANVLAELFFRPIIGTVSMDDMMLEMLCAKL
The following text describes a protein:
Function:
Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid.
Subcellular Localization:
Secreted.
Sequence:
MKFHLLLVCVAISLGPIPQSEAGVTEEQMWSAGKLMRDVCLPKYPKVSVEVADNIRNGDIPNSKDTNCYINCILEMMQAIKKGKFQLESTLKQMDIMLPDSYKDEYRKGINLCKDSTVGLKNAPNCDPAHALLSCLKNNIKVFVFP
The following text describes a protein:
Function:
Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA. Required for double-strand break repair and V(D)J recombination. Also has a role in chromosome translocation. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection. Binding to DNA may be mediated by XRCC6. The XRCC5-XRRC6 dimer acts as a regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription (By similarity).
Subcellular Localization:
Nucleus. Chromosome.
Sequence:
MEMWVLGEVGMAVLSAAAMADWVSYYRGDGPDEEEDGEQQEEEGPEAVADYRFSGRDSLIFLVDASKAMFEPYENEEAATPFDMTMQCIRNVYTSKIISSDKDLLSVVFYGMENNKNSADFKHIYVLQELDNPGAKRILELDQYRGDEGRVLFRETFGHNADYSLGEALWACSNLFSDVRVRLSHKRIMLFTNEDNPHANDSAKAKLARTRAGDLRDTGIILDLMHLKKPGGFDISLFYRDIINVAEDEDLGIQPDESGKLEHLMKKVRAKETRKRALSRLNLYLNKDLSFSVGVYNLIQKAYKPYPVKLYRETNEPVKTKTRVFNGKTGSLLLPSDTKRAQTYGNRQIAMEKEETEEVKRFDSPGLFLIGFKPLSMLKQHHHIRPSQFMYPEESLVTGSTTLFNALLMKCLEKEVMALCRYIARRNTPPRIVALIPQEEEVDEQKVQIAPPGFHIIFLPYADDKRNVDFTEKVPANREQVDKMKGIIQKLRFKYRTDSFENPVLQQHFRNLEALALDMLEPEQAEDLTMPKTEEMSRRLGNLVEEFKQLVYPPDYSPEGKAAKRKQAGDAQAEKRPKIEISEDSLRSYVQNGTLGKLTVSALKDTCRHYGLRSGGKKQELIDALTEYFSGR
The following text describes a protein:
Function:
tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.
Sequence:
MSQQLQQAVEIAYSSTAEPALKKQALEYVQNVKAGAGAAEVFVGYLGDAGTSDVGRFVALQALSELAGEGGPARLAFLKDSAMRALRGETGGVWGAPEYVRNKTAEWVSRLFYAMYGEVNGNMWNSFFEDVAQATGVAGLRGSAAVEYNAAGLDAFLRVCAAINSEIGDQTFVRSKDAQVKNNSLKDAMRVQDVATLTSIWRHALEAMRQDVQRQDVAVLVLQCIGSFISWIDINLIVNSEYISTIYAYLNYPKTRIACAQCLCEILSKKMKPGDKLQLLGMLSLTDKVLQLGDVEVEVHEQLAKLTSSVGLELSVILEQCHDDSSSAGSCSIANSADHQIIHQVAPLVLKFMNHEYDSVTQQTFPFISHYLTFLKRLFALGGKPGSAVALNSKKLPLDDDHRQFLTSLIIVCMNKMKFDETCSYDDEDEVEEFVETVRSKLKVFQDNIAVINPAIYMENISKHIKSLLLGNSWRDLELAIYQMHNFAESIRNNLFGLNKSAISQSQPAQLMTTFMQDILDNSAIFQSSNPLIQISFFELIVRHYNFISHTGKNDISILSIFCTPFSMFNDSEKVRLRSWYLFSRLIKVTKPRLDDESLSQLLSKLAPLLAVKLLPNVANDSEIDTTFDNQLYIFEGVGILIGAKAKEEYSILDGVLSPLFADLESCIAAPVKSPEIVVQAHHILMAIGTIARGVHAGLVPENQLNNPQVNAALVHKSLIEKFSNIAEVILVTFSYFNKYETIRDATRFSFARLTPILKNDIIPFSSRLISIFLESDLKTIEMNDFLGFLGQMVHTFHADDNCYQLFNNLFTPVIKKVFDLVAQVEQEGSLASGANTAPAVSKVANGKNVVITDSFRDKVQLKKAYYSFLQSFVSNNVTSLLLTTANRNILPLILSDLLSYTPAEIHETSSMKLSLNVLINFVKFFGTGRCADFKDRNANTFEPLEGLSEFFITKVVPLVFEIPFKPEYEFNIDDGSCLVLAADLSRLLKALYDVNGDPANNASLKYLTEAYFPQVQFPQELSMEFIQTLATADEKAFEKYFVSFIKRMRS
The following text describes a protein:
Function:
Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end (By similarity). Cooperates with kif10 and dynein to organize interphase microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSSPILNTDDNNCVRVALRVRPLSKKEEAERSMEVVKYVDGEPQVIMGDNNQTFTFDYVFNGKSRQQEIFDDCVANLVDCLFEGYNSTILAYGQTGSGKTFTMGTTSTIGIPTEELGVIPRVIDFIYDKIDRKKDTHQLVLKVSFLELYNEEIRDMLNPYPTAGGLPIREKSNGEVYIPGLVEQIVRSRQQMEEALIRGSQSRTTGSTLMNSHSSRSHAIFSIIVEQTPINSPVTSSSTSSTSTSSSSDDKKQSKGKKKKKSSSPDSLSPNKDDDSSIMIDEDEEDDEEDEDDDIMSMDERNPSIRSMFHFVDLAGSERVKKTKAEGQRLKEGININGGLLALGNVISALGDTRRATTKPKHIPYRDSKLTRMLQSSLGGNSKTLMIACVSPADSNFEETLNTLKYAYRARNIMNKPVVNIDPVTQQILTYKTQIQTLKELLEKCTCRDIGDINSILASIPTVSIPPAPPLSTPTLTNNNNNNSSSNNNNNSNNNKLNVGGNNSGFSRTPSSSSLPPTNSSKSSIVKMNNSRNISSSSSSSSSSSSSSSLTTTPSITNNTATPSPTSVIVTNLSKEKEKEIFDLGMKVSQLEFENNMLQDISNKITSKYKALANRSRQLEEISQNFINNFSPNKDQTYFNELFEQFNSVLNQPTISPITPMMAAVSTQISSSNVIINSNSLLPMAEDNLLPGGKLESINNNNNNNNNSSEGIELFENDSEELSDLNQYISEKEEELELISKTKQQYQQMKEQFDQKVKELQSQLEEVTVEKDQALKELDKDKDKDKDNKDKDQYYEDEKLRLTQHYEKKLNELKQQLDQHAGSNKKDYQRLLDLKRKSEEKIDSLQQDIKDTKRQKSDLLKKMRDELKKRDDAKQTQAKELDALKREARKTEVIIDQLKNQSKKKDLLLQKKTDESESYKKKLKEIEVHKQRVIQPINSKSIPSNNNNNNSSGSVKSSNGSTASSASSANSSSSSSSSSSTNTSTTSTSATNNTTTSTSTSTPTTEQLNRKLLHRKSINVPYWREWLIHQIQKNLEKNELTELLQREFKNKEIFVRQANDLKKAFTSVPSKLSKSEYNEQSQFLETNIKLQNEKILKSQKDLTIISNDCLDSPEILRMVSNTSFDKLPKLIQSSIELCIEYAEINRKNQQIKFINVPTPPTLQSQQQHQKSQHFYIQPPQPLQSQQQQQEKQQKQSNSEQVLEQRSSTSDLLEGIKLAISESNNKNNINNNNNNVNIAKSQPILPSQQQLSSSQELAEEYTSPSTSSLGMKLDQLLDEIKLDKEKREKNKLLNGYPPMSGINYFNPPTPQPLSASSFLTSAAATTTTTTTTTTTTNKQQVPKSFAPLNNTNNNNNNNNSSPLLLISDDKLDHSVFDKDLLDVDILGNDSSNNGFSVININSNNNITIKKPPSSPTRPHRKTTSLQSSPLSLSLESGLATALANNGNNNNNSNNNDVFTRLASQPRPDSRLKKYRDKLNTDDYLMAIKRNMNREDENFMRCNWTFNGHDGGLLTLVLDEQNPSTLYSGGSDKNIKLWDLHTGDNMLDLSSPGPVRSLCINGSSGCMFSGGAERTVKVWDIRSPGNTNLCIFKTPSDVNCLVTYGNYVVSGLENGTFKVWDIRHMQKPLKTPLTTTPHHTGTIFSMSVTSKYLVTGSRDHTINLFHRDSFVLAQKLQPPHHDGVTSIAVLDDVIYSGSRDRTIKRWDVSSINNLINNNGENNSNNLITTQLAQQTVPILSNTPSNSNLIINNNNNIINNNNNNNNSSNNNKSSSAPSSTTSSLSSSLDNSTFSLLNQYQQNRLLNNAHNDWVNCLCIHNGMIFSGGKDSNIKGWDPLLSSNSLLLGHESSISCLTSSKEFLFSGSTDKCIKIWKC
The following text describes a protein:
Function:
Radical SAM enzyme that catalyzes the addition of the adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoate, leading to aminodeoxyfutalosine (AFL), a key intermediate in the formation of menaquinone (MK, vitamin K2) from chorismate.
Sequence:
MDFLEKVLDNQVTESKELVRLYDYDLYTLGEVADRMRQNMHQKIVYFNVNRHLNPSNICADACKFCAFSAHRKNPNPYEMSLEEILEKVKNSYNKGIKEVHIVSAHNPNYSYEWYLKVFETIKQEMPNLHLKAMTAAEVHFLSVKFNKPFELVLEDMLKAGVDSMPGGGAEIFDEEIRRKICNGKVGSSRWLEIHAYWHKLGKMSNATMLFGHIENKIHRIDHMLRIKKIQSPKNQVENKEGGFNAFIPLLYQKENNYLNVEKSPSAIEILKTIAISRILLNNIPHIKAYWATLGLNLALVAQEFGANDLDGTIEIESIQSAAGAKSRHGLEKEDLIFKIKDAGFVAVERDSLYNFIQKF