lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Sequence:
MPELPEVENVRRTLENLVTGKTIEDVIVTYPKIVKRPDDAEIFKEMLKGEKIENIKRRGKFLLLYVTNYVIVSHLRMEGKFLLHQEDEPIDKHTHVRFLFTDGTELHYKDVRKFGTMHLFKKGEEMNQMPLADLGPEPFDAEMTPQYLQERLQKTNRKIKVVLLDQRLLVGLGNIYVDEVLFRSQIHPEREASSLTVEEIERIYEATVTTLGEAVKRGGSTIRTYINSQGQIGSFQELLNVYGKKGEPCVTCGTILEKTVVGGRGTHYCPICQPRI
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase.
Sequence:
MLPDADSKDQLVTIIQSVKPPTVPPHRSHDPANNLKRTDPYQFGSRYLEEGDDVFEFNAWDHVEPDDEFKAFAEVQYAKQRESPVSDFDKQRFNKDPAKWWNLFYKNNTSNFFKDRKWLRQEFPVLAEVTQKGAGRKVVLEVGAGAGNTAFPLITHNKNEELMVHACDFSKTAVQVMRESEHYNPKFISADVWDVTAVPDEENNGLPPGLTEGSVDVVILIFIFSALAPSQWDQAIRNVYRVLKPGGLVLFRDYGRGDLAQVRFKKGRYMDENFYVRGDGTRVYFFEKEQLEKMWGTWTPEKGLQMAEDNSIVAESEGAFDVEKIGVDRRLIVNRQRKLKMYRCWIQAHYRKRETPAAVEAEKADS
The following text describes a protein:
Function:
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Nucleus.
Sequence:
MSWSVHSAKPYRLCIIHIFCLDKMAATMWTEIIENYVRGEQKEGVTSITAEITNGQQTVENFVDSMGTYLMSTETRIRAKGVELMSEVLTSLPRAFLNQQQIQVLIEFLCARLLDHHSITQHTLKGLLAMSSQSSFPPSSSVQVMTAIFKEVQVQTMLQVDRRTVYNIVVNLLRISLTELQGMGSEFVLGLLHAMDGEKDPRNLILLFNILPTVINNFKIDMFIEETFEVVACYYPVDFHPPPNDPYGISREKLALSLKTCLSSTPKFAQFCLPMVMEKLSSDLQTARLDSYQLLQACAPVYSQGDMMSYIEAIWSYCRKELMVGASVELDQEAVKTLGAVVKAVSTGIQSTSSGGGGDGDLNSFLRNILTECRQHLCEPDHRMIHPCSKLLVAVATASYPACIVVLKYSVPILLDQFHIFDQTRERMVLLDIIQRLLHSGHDHIKEADDWRAIHAHHLDTVVTTVLSTLAKDQGVPDLRKAGLGTLGELVQVPVLMDQSRLELVGQELTRILLEEANVDVRCECIKTVSCFASRHTEFVKSTILTTLWTTVQKGESGYQRIVVDMATIVTNTSDDLSRSLTSELMVEIAKTELNSEQHLVYLATLNTLTAHLSSTPSNLESLLSSVVHPLMKMVVSATLQSSVEAGNNPHCCGEVLVAMAEVFRTVVPKLDTSMGSKLCQCAVDVFLHGNLTSLELTNPNTSVPFSPLDPRAPVHQTQLVTVLQPIVCSLRRDIHMPSSKQLMSSLLHIAAHSRAWLASTWAAKGLAGVVNKHPAGSALDEVLVEAEVLVEAESLLGQAMSSGQEGPVKQQALMAWVLLTKALVMRSHPKATTFLTTLLRLLEDAELGAQVPQTLGMLLEDMGDVLSEGLHADVKIMYKQRVFLQALPFVMALFNKDDLQTRAITALCHLLPSIPRPVLLAELPPIIPRLVQSLRVTDPRPTLPILDILESLLEETLPSLVDQADTLLPTLLELSAYQASMKVRIASLKCVGAITSFPHHLVYPHQETVVRSLAPRLDDKKRLVRQEAGKARTKWILLQQDTKG
The following text describes a protein:
Function:
Facilitator of innate immune signaling that acts as a sensor of second messenger signals produced by cyclic GMP-AMP synthase-like receptors (cGLRs) and promotes the production of type I interferon. Innate immune response is triggered in response to nucleotides from viruses and bacteria delivered to the cytoplasm. Acts by binding cyclic dinucleotides: recognizes and binds 2'-3' linked cGAMP (2'-3'-cGAMP), a second messengers produced by cGLRs in response to nucleotides in the cytosol, such as double-stranded RNA (dsRNA). Upon binding to 2'-3'-cGAMP, oligomerizes and promotes the recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon (By similarity).
Sequence:
MMSNDSQSEKRTAKWTGSGTPIAEGEESSSPSAHQTRQKATAADDDDDQQITDLEQELAELDLEEQRKAKKKRIASLQRQIEEKRNKLATVEISDLNEKENKNVVNVADGLAWSYYSGYLKLVLPRLEQRISESEKFRHKITDKKLYILLPKSCFTCDDIEHADSRVKWAGNLPESKINRGGIKERSYKHAVHEIVMPPFPDGTGEKYHFIVEYATPLMTLYDMSKFADAQLTDPERDHQVLLFMQKLTELLEKSKDCKGQYDCRGKYELVSFDEEEDKIADILIARHNNANKVGEESEELSIPVQ
The following text describes a protein:
Function:
Probable ATP-dependent zinc metallopeptidase.
Subcellular Localization:
Mitochondrion.
Sequence:
MLQAGRRSSSVIYNELTSTSAFRTPANGTGGVLKALQERYRSSYVGSFARRLRDFDTPSDASLLKEIYRSNPERVVQIFESQPSLHNNSSALSQYVKALVALDRLDESPLLKTLQRGIVNSAREEEGLSGIPAFQSVGRTTKDGALGTAGAPIHMVASETGQFKEQLWRTFRSIALTFLVISGIGALIEDRGISKGLGLHEEVQPSLDSSTKFSDVKGVDEAKAELEEIVHYLRDPKRFTRLGGKLPKGVLLVGPPGTGKTMLARAIAGEAGVPFFSCSGSEFEEMFVGVGARRVRDLFSAAKKRSPCIIFIDEIDAIGGSRNPKDQQYMKMTLNQLLVELDGFKQNDGIIVIAATNFPQSLDKALVRPGRFDRHIVVPNPDVEGRRQILETHMSKVLKADDVDLMTIARGTPGFSGADLANLVNVAALKAAMDGAKSVSMTDLEFAKDRIMMGSERKSAVISDESRKMTAYHEGGHALVAIHTAGAHPVHKATIVPRGMALGMVTQLPEKDQTSVSRKQMLARLDVCMGGRVAEELIFGESEVTSGASSDLSQATRLAKAMVTKYGMSKRVGLVAYNYDDDGKTMSTQTRGLVEQEVKELLETAYNNAKTILTTHNKELHALANALIERETLTGAQIKNLLSQVNSSSDTQQPQAAEVPQQTPAAPASPQSPAAAAAAAAAAAAQQAAAQAKGVAGIGS
The following text describes a protein:
Function:
Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners.
Subcellular Localization:
Secreted.
Sequence:
MGRLPAAAPPLTFAQAAVGEGIKWELRAAPTEQRQSTARPAMKVSILLLLICTAILAVGARAEAPDKTEVVVKKVQEYVKQATEAVKTAFTTVHESEAAQQARKWLSDNADLVKQQLAKLKEQLAELWKLTPTA
The following text describes a protein:
Function:
Participates in the catalytic exchange of histone H2A for the H2A variant pht1, an euchromatin-specific factor, leading to chromatin remodeling and changes in transcription of targeted genes.
Subcellular Localization:
Nucleus.
Sequence:
MSATESLVAGRTRRANAGNKMRELLEKEHLRMTQQNAEIEKEDEEYNIEEEEEAERDIEISSESSDEEAELKKLEEEGEEVEKILRDEERIKKRKIQKNRAANLQRTLQPPKRPTPSAASEVPKKKYKKIKVDPSARRTSSRMHTVLMAQSTETRLQEAKPRRKYTVSASANRQKGTMTQQQRFEEAAKTEAQNLSSLRNYVHLEEQRRLRLKRNAAKHRQLREPILKFISKTISTEDGREASNYYVAPLEHPLCHSAPPLQMPQHRAVECVITGKPAIYLDPVTQLPISNVQAFQQVREVYNQRYSWSAMLNLFH
The following text describes a protein:
Function:
NADPH-dependent oxidoreductase which catalyzes the reduction of some steroids (estrone, androstene-3,17-dione and cortisone) as well as prostaglandin E1, isatin and xenobiotics in vitro. May have a role in steroid and/or xenobiotic metabolism.
Subcellular Localization:
Endoplasmic reticulum. Note=May be attached to the ER membrane by its C-terminus segment.
Domain:
May be attached to the ER membrane by its C-terminus segment.
Sequence:
MVAPMKGQVCVVTGASRGIGRGIALQLCKAGATVYITGRHLDTLRATAQEAQSLGGRCVPVVCDSSQESEVKSLFEQVDREQKGRLDVLVNNAYAGVQAILNTTNKSFWEVPASIWDDINNVGLRGHYLCSVYGARLMVPAGKGLIVIVSSPGGLQHMFNVPYGVGKAACDRLAADCAHELRRHGVSYVSLWPGLVQTEMVKEFMAKEDTPEDPLFKKMKPDFSSAESPEMSGKCVVALATDPNILNLSGKVLPSCDLARRYGLKDIDGRPVKDYFSLGYALSQVSSLGWLNSFLPGFLRVPKWVVTLYNSKF
The following text describes a protein:
Function:
Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Miscellaneous:
MISCELLANEOUS: Present with 3300 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MTTNNDFYFALLRISILQLLKAQGFDRARPSLVDVMTDLYAKFLSLLASEVSSIAQARCDQDDTIALQDITLALENLGIVKPTNVLDVYDENSELSSSRGMEKFKDWCIYSTQLTDARITALPTVELLQSEEKESDPLSAIPDYLNQLLQNKGAKQKLETKNRKTELIEDLINNNGLDDWIKLVIARQRINMIERASKKESQNVPALPHIAGYKSSILSRHHHTTITNEDRMPSAMTPRDEDALTEIQENPFVTSKLPIMRKENRLENITLSFEDEELESLGEVEGPNQKSQENNNEESFKENNKSLTESPHGDDRDISMFQFDSNVDTKWAEQEDMDSTFQRRTSLDYGGYF
The following text describes a protein:
Function:
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MFHFCLHSIKVCDLIGTIGYHRSNCSMILEWMHRMKKRHGKKACATYESGMVSFEDFPTDQGPIWILGKKYDLSQHQLEARLDVLSRLWFTYRKGFSNIGGTGPTTDQGWGCMLRCGQMMLAQALVYKHLGRDWRWRPQEQDETYLKILQLFLDKKDSCFSIHQIAQMGVGEGKKVGDWFGPNTVGQVIRKLSPFDSWSDLAVHVALDNTVVIEDIRKLCTVNSTTEETSSEGSKTGSERRKRTSSSENIRHKMQLSPENTNIQLPNGLMEGACVSPGGVSWRSLFLIIPLRLGLNEINTVYMQRLKRCFTLPQSLGVIGGKPNHAHYFIGVLGDEMVYLDPHTTQPAADIDKWAFLQDESFHCEHASRMPIKNLDPSIGLGFYCHSEDDFNSWCRNIQYVISDGDLSPMFELTETRPKHWPPFEPNSASIEPSFEIRDCEYPDEDFHNNSDEEFEFL
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MENLGDLAQGLALLGKYLGAGLCMGIGAIGPGIGEGNIGAHAMDAMARQPEMVGTITTRMLLADAVAETTGIYSLLIAFMILLVV
The following text describes a protein:
Function:
Extracellular metalloprotease that contributes to pathogenicity; Involved in the digestion of the blood meal.
Subcellular Localization:
Secreted.
Sequence:
LLHRDKVIRVIPKTDDEVRILADLEHDPTVSFWKEAHAPGMAADIHVPARYYGDVARHLDKNGLKFAIQIIDLQSEVDNEKLTLGRSEGFFSGYKPLDKIEDEMRRLAGVQTLAQVTMNTVGSTYEGPNLVFQIKGRSLPEKPVFFMNCGIHAREWITPATCMYIITQFITKYRSDKSVTEVLDKMDFIIMPVLNADGYVYTWTGNRMWRKTRKPNIQSWWGQKTCYGTDPNRNWGYKWGLPGASSNPCSDTFRGKTAQSEVEVDNVAKFLKGLGPRVKGYMDIHAYSQFWMIPWGYTTANAKDHKELMRVSKIGVDAIRQTYGTAYRYGSSSNIIYKNSGSSKDYTYGHLNIKYSFALELRDTGRYGFLLPPGQILPTALETFNGIIAMAKAMEI
The following text describes a protein:
Function:
Transcription factor that participates in the transcriptional activation of glucose-repressed genes during exponential growth in non-fermentable carbon conditions. Also involved in salt-stress response.
Subcellular Localization:
Nucleus. Note=Found in the nucleus in conditions under which NSF1 is actively transcribed, such as growth with non-fermentable carbon sources or salt stress.
Sequence:
MENTTNRNTAGVLTSSNGNFATNSVAASTPKRSKSARRKTFKCTGYDGCTMSFTRAEHLARHIRKHTGEKPFQCPACLKFFSRVDNLKQHRESVHAHKNHHSTSSHQRKPSSSSLSSSSSASSSSSASSSTSYSDPYRKTNINSGNMPMMAENEKAPQIIHSSPEFITSTRSIPPISPRSIYNTQRQQQHQQQQHQQAPYYFPSHPITDSYYQYPLPSNNNTINYLPSVDVQYPLNVSPSSTSHPASEVIISSFPPRSMPSTSFKYKDSADFQARTTMNKYNIRPSNINVNTSNINNHLDSFSPPFSPSTTVAEAKPIILPQYQQAFSQPPNGNKNNNMSSSKNGGKGGENFKNTDDRNDNNNKKRSETLSESDISVNTNKKRLSVDYILT
The following text describes a protein:
Function:
Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C).
Subcellular Localization:
Cytoplasm.
Sequence:
MELEQLKKSVEENPDDSSLQFELGLYLWDNGGDSEKAAEHFVLSAKSDPNNAVAFKYLGHYYSRVTLDLNRAAKCYQRAVLINPNDSDSGEALCDLFDRQGKEILEIAVCRDASEKSPKAFWAFCRLGYIQLHQKKWSEAVQSLQHAIRGYPTMSDLWEALGLAYQRLGMFTAAIKAYGRAIELDETKIFALVESANIFLMLGSYRKGVELFEQALKISPQNISVLYGLASGLLSWSKECINLGAFGWAASLLEDARKAAKASSELASSMSCIWKLHGDIQLTYARCFPWSGGTENSEFTLKTFSDSILSWRSICYSAALSAKASYQRALHLAPWQANVYTDIAITCDLVSSLSDDSDTSSSWKLPEKMVLGALLLECENSEFWVALGCMSDNSALKLHALIRALHLDVSLAVAWAFMGQIFRESDEMKFAKQAFDCARSIDPTLALPWAGSADTYARESTSDEAFESCLRAAQISPLAEFQVGLAWLALLQGNISSPQIFACIEQAVQRSPYYPEPHNLHGLVCEARHNYHTAIASYRLALAAMSIYPESSVKSHAGKVSINLVRSLSKAGRFKESVMECANLKSKGLLDAGGLQIYAFSLWRTGQNDSALSVIRDLAGRISTREKTSIAFPISFICSLLYCISGLDSAITSIQKMPKDFFQSSKISFIVSAIHSLDQSDRLQSIVASTRSYITSQEEIVAMHYLIALSKLLKTGAGDFLGYEKGIAHLSKAIHMYPHSNLIRNLLGYILLAGEGMKDACTASRCCIINVSECANKEGLKSALEVLGGGSVACNVIGNTAPRFSFPTCHCQYLNAPVVVVELQRFLHQEPSNSSVRYLLILNLVQKAREQRFPRQLCRAIERLISVALSDETCSKEGEYKKFQLLLCASEISLQMGNIAESINHARKASSLSLPSSYLFLGHLQLCRAYAANGSTKNMQEEYRACLELKTDSNIGWICLKLIESQYNLEPDANLLEMSLQECSSQKKNSWKEWMAVYSLARGLDSTGKKDFFSAEEFLAQACSLLNSESCLLLCHGAVCMELARQSNDSQFLSLAVKSLSKVQASSLFPLPIVYTLLAQAHGSLGSKEKWEKNLRLEWFCWPPEMRPAEVYFQMHILARQSEDRPETTSGIENYQSPEKWVIRAIHTDPSCRRYWKVLDKLVQHPMS
The following text describes a protein:
Function:
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular Localization:
Mitochondrion.
Sequence:
MLLWQYIVLRGQLAALLSSPCNLDNLTHRATLATVQQREDMRQCIRRLAESSRALPQLTTKELLAQGRVPSFSVTYRDFMEWNNIQVARHGRFFEKRNAASLSQLHSLGRAEPLLCHALARWMHVDYKLNSYPYYDLNVLLVYTDWDQAQRVAGALVAFLERVQAASGQRVNCFLAPLHDAPAPARRRAAVPPGVRVLDSGLLLGPEPCRMEDPVYVVLMNDVVRYLSCDLVRMGNGGDWQQMHLDVEKRSTQRVWFDTMDHWCHAATTLHVPQGMEFRPGTRMFVPTRLTQLLHCLCEYMPEHRLFALDMPQQRQWWYWLYYNNQRTVTDAIQVHQLHDVFTKSEVETVFAADFASLKRLYALVSDGLKLAHTEPAADFASHWTDLRESEELLGRDLSAEYASLQACMLSVMRAL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I, CD4 and ICAM1, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein.
Domain:
The RING-CH-type zinc finger domain is required for E3 ligase activity.
Sequence:
MLKSRLRMFLNELKLLVLTGGGRPRAEPQPRGGGGGGCGWAPFAGCSARDGDGDEEEYYGSEPRARGLAGDKEPRAGPPPPPAPPPPPPGALDALSLSSSLDSGLRTPQCRICFQGPEQGELLSPCRCDGSVRCTHQPCLIRWISERGSWSCELCYFKYQVLAISTKNPLQWQAISLTVIEKVQIAAIVLGSLFLVASISWLIWSSLSPSAKWQRQDLLFQICYGMYGFMDVVCIGLIVHEGSSVYRIFKRWQAVNQQWKVLNYDKTKDVGGDTGGGAAGKPGPRTSRTSPPAGAPTRPPAAQRMRMRTLLPQRCGYTILHLLGQLRPPDARSSSHSGREVVMRVTTV
The following text describes a protein:
Function:
May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MHTFAGFANYLYYLLLNFIVITLLGLWMNEYSLTEFLIEALMYVWGRKNEQRPLLFLFFIQIQAQYMVWFLLFLNLISGKSIQSNLVGVMIGHTFYYFAFIVPNLPRFKGLQLLSTPKFLINICKYFERQNQLQ
The following text describes a protein:
Function:
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNLRIAMAIALGGAFGAVARFYISGLLPVYRDFPVGTLMVNSIASLILGYLYGLLFWGFDVPPDWRAFFGTGFCGALSTFSTFSYETFSLLREREYLIATLNILANVIITIALVFAGFMLARR
The following text describes a protein:
Function:
Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA.
Subcellular Localization:
Mitochondrion.
Sequence:
VAVKYFIDNQRKIELKELQRARRQQQQTKTSFAGDDVLFERIGGAGIITLNRPSALNALNLSMIKKIFPKIKEWEEDPATTMIIMKGAGGKAFCAGGDILSITEEGKKGNYEAGQEFFRSEYQLNYRIATCLVPYIAFIDGITMGGGVGLSVHGENRICTERTLFAMPETAIGLFPDVGGSYFLPRLSKHLGMYLALTGFRLKGRDVYKAGVATRMVHSTVLPQLEQDLVAMENPSTQDITDLLRKYHEECQTGRERDYLILRDKEEDIKRMFCADSVEEIFENLRNDGSEWALEQLSVMEKMSPTSLKITHRQLSLGESLDLSECLEMEYRMGSQCLRHPDFYEGVRSVLIDKDKSPKWNPATLSGVTEGIVDKHFILPSDGEELQL
The following text describes a protein:
Function:
In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7. Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5; Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle.
Subcellular Localization:
Cytoplasm, cytosol. Peroxisome matrix.
Sequence:
MAMRELVEAECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGTPASEAVSKPLGVASEDELVAEFLQDHNAPLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPAVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFISEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGTAASDRWNDEYHPEEDLQHTASDFVAKVDDPKLANSEFLKFVRQIGEGQVSLESGAGSGRAQAEQWAAEFIQQQGTSDAWVDQFTRPVNTSALDMEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLMSASYDKGYQFEEENPLRDHPQPFEEGLRRLQEGDLPNAVLLFEAAVQQDPKHVEAWQYLGTTQAENEQELLAISALRKCLELKPDNRTALMALAVSFTNESLQRQACETLRDWLRYTPAYAHLVVPGEEGAGGVALGHSKRVLGSLLSDSLFLEVKELFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPDDYLLWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLSLSMLGQSDAYGAADARDLSTLLAMFGLPQ
The following text describes a protein:
Function:
Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.
Subcellular Localization:
Host nucleus inner membrane. Note=Remains attached to the nucleus inner membrane through interaction with NEC2.
Sequence:
MAPVTPDAVNARQQRPADPALRRLMHPHHRNYTASKASAHSVKSVSRCGKSRSELGRMERVGSVARSICSRHTRHGVDRSHFSLRDFFRGISANFELGKDFLREMNTPIHVSEAVFLPLSLCTLSPGRCLRLSPFGHSLTLGSHCEICINRSQVHVPQEFSSTQLSFFNNVHKIIPNKTFYVSLLSSSPSAVKAGLSQPSLLYAYLVTGHFCGTICPIFSTNGKGRLIMHLLLQGTSLHIPETCLKLLCENIGPTYELAVDLVGDAFCIKVSPRDTVYEKAVNVDEDAIYEAIKDLECGDELRLQIINYTQLILENKQ
The following text describes a protein:
Function:
Binds all-trans retinoic acid and may act as a retinoid carrier protein within the epididymis. May play a role in male fertility.
Subcellular Localization:
Secreted.
Sequence:
MRLLCGLWLWLSLLKVLQAQTPTPPPLPPPMQSFQGNQFQGEWFVLGLAGNSFRPEHRALLNAFTATFELSDDGRFEVWNAMTRGQHCDTWSYVLIPAAQPGQFTVDHGVEPGADREETRVVDSNYTQFALMLSRRHTSRLAVLRISLLGSSLLPPGTLDQFICLGRAQGLSDDNIVFPDVTGWSPQASVC
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Catalyzes with a lower efficiency the sulfation of Gal residues of keratan sulfate, another glycosaminoglycan. Can also catalyze the sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May play a role in the maintenance of naive T-lymphocytes in the spleen.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MEKGLALPQDFRDLVHSLKIRGRYVLFLAFVVIVFIFIEKENKIISRVSDKLKQIPHFVADANSTDPALLLSENASLLSLSELDSTFSHLRSRLHNLSLQLGVEPAMESQEAGAEKPSQQAGAGTRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVFFQQRGASAAGSALVYRDVLKQLLLCDLYVLEPFISPPPEDHLTQFLFRRGSSRSLCEDPVCTPFVKKVFEKYHCRNRRCGPLNVTLAGEACRRKDHVALKAVRIRQLEFLQPLVEDPRLDLRVIQLVRDPRAVLASRIVAFAGKYENWKKWLSEGQDQLSEDEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARRPLQKAREMYSFAGIPLTPQVEDWIQKNTQATRDSSDVYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPTMHLFGYKLARDAASLTNRSISLLEERGTFWVT
The following text describes a protein:
Function:
Acts as a glycogen-targeting subunit for PP1. PP1 is involved in glycogen metabolism and contributes to the activation of glycogen synthase leading to an increase in glycogen synthesis.
Sequence:
MSKGPDSALLPSTPGPRKLAPRSLSCLSDMDGRSCRPPGCDPRLRPIIQRRSRSLPTSPERRAKAAGAQGAACGAGCNRQVRVRFADALGLELAQVKVFNAGDDPSVPLHVLSRLAINSDLCCSSQDLEFTLQCLVPDFQPPIEVPGFGDRLARQLVCLERVTCSDLGISGTVRVRNVAFEKQVTVRYTFSGWRSAHEAVARWRGPAGGEGTEDIFAFGFPVPPFLLELGSQVHFALRYGVAGAEYWDNNDGQDYSLTCRSHALHMPRGECEESWIHFI
The following text describes a protein:
Function:
Involved in cytokinesis and septation where it has a role in the localization of F-actin.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSWIPFKIGQPKKQIVPKTVERDFEREYGKLQQLEDQTKKLQKDLKKSTDADLAMSKSAVKISSDLLSNPLCEQDQEFLNLVTALDTAMKRMDAFNQEKVNQIQKTVIEPLKKFGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGPVLAKLHQVREELRPVKDDFEAKNRQLLEEMPRFYNSRLDYFQPSFESLIRAQVVYYTEMHKIFRDLTQQLDQPGHTDEQREQENETKLSELRALSIVADD
The following text describes a protein:
Function:
NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde.
Sequence:
MTIHRLKDIVVCLTGASSGIGASIAEHLLREGANVMMAARRVEKLHDVQQACLTKHPDSPGKLLYKECDVTQRESLADLVKEAEEKLGGVDVIINCAGVMYFTEMKSCLQDQWEQTVDVNCKGVLNGIGAVLPKFIARGKGKILTISSDAGMRQFQSLAVYCASKTFVETLCEITRRELVGTGVTLTTICPGDVKGTELVMKNTDQSAAENLGVEIGKPVGEGFSRTQLLDTSDVAEAVIYALTAPPHVAINTVLIEPRDQE
The following text describes a protein:
Function:
Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Has a promiscuous chemokine-binding profile, interacting with inflammatory chemokines of both the CXC and the CC subfamilies but not with homeostatic chemokines. Acts as a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13, CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1 and TARC. May regulate chemokine bioavailability and, consequently, leukocyte recruitment through two distinct mechanisms: when expressed in endothelial cells, it sustains the abluminal to luminal transcytosis of tissue-derived chemokines and their subsequent presentation to circulating leukocytes; when expressed in erythrocytes, serves as blood reservoir of cognate chemokines but also as a chemokine sink, buffering potential surges in plasma chemokine levels.
Subcellular Localization:
Early endosome. Membrane; Multi-pass membrane protein. Recycling endosome.
Sequence:
MVGPGPRALRKTQVVPSAGWGLGPLWGGEGGGFLTVGGSPRPPGSSPGARPGDLPRPCGLRHRNPASYLPSAAAPTGPPPAHRPPPAALPGAMGNCLYSEASLPYNSTQTGSLRVDVDDLPMLNYSYSEEDEDFYRDLDLNLVAPCRSCHLLGPSSLPFFALVSALGLLASAALLYALLGGPARRRPPPRARALLVQQAGACALCAAVLPFLAPGPTWPPALCQPAVGAWYAGAFAQALLVAGGAWPRPDPGRCRPAVLSAAAWAGSALLALPAAGSARASPGLCAVRPSGQQPGWAWALAVTCAAAFLLLPLGLGVGWAVRRARADPLWAWFALWAPHGAAVGADVLVRLGVVLPSCRAQQALDVAGDLAQALAALHCPAAPLGALLLLRRRQRRSARNPARAPAAVHPEEGAWTLHPK