lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Localization:
Preautophagosomal structure membrane; Multi-pass membrane protein.
Sequence:
MTAILAHVHYLPSEWRQQAHTTKVRQEFSNFFQFKAGYLLSEIFSPFVTPFVLIFVFRPKAIELVRFFRTFTVSVRGVGNVCSFAQMDVRKHGNPDWQLTSELEEMTRATAQQPQQEPQQQSLAGGKTEMSLLRFTLNNPEWQMPKEAKQFLRGVREHAVGELVQAKTSMVQENPLTNSLISFGTMGADYCSIANSVLTAQVTPQQLEISQSLRPGLGPVSGGFPVAASDFRQMLQQNLSASVGPLDSMRRLRLSRAEGRLEGPTDTLLYGLCGVDPRVGSTPLNVGVADMCLSALYLHELNQQKRQARQSRIDEAEDERPGTSHWPPRPPAAPSADTGFGSRHTVITSKAAESTPLLGSIRS
The following text describes a protein:
Function:
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MAKNVKKLTLANKLAKRGDLIKPTEIKSRPNRADNVRDIEDLVGVSAGAAGSSSSVFFSPVQTRKQRLLNGEAVKKTNIKMEPLSPARVAPKKFRKDDRMVTRVQMGSATVVICKVVPDAVDSPVRVDKIREEVEPQIKQEAPEDSPSFSEVQAPHPLWFNHLENIRIMRNSRTAPVDTMGCHRCADLKADSKTQRFQNLVALMLSSQTKDQTTYEAMNRLKDRGLTPLKVKEMPVTELENLLHPVSFYKNKAKYLKQTVEILTDKYGSDIPDNVKDLVALPGVGPKMAHICMAVAWNKITGIGVDVHVHRLSNRLGWVPKPTKEPEQTRVALEKWLPFSLWSEVNHLFVGFGQTICTPVKPNCGECLNKDICPSAHAETKEKRKKDR
The following text describes a protein:
Function:
Axonemal protein which is implicated in axonemal and/or peri-axonemal structure assembly and regulates flagellum assembly and beating and therefore sperm motility.
Subcellular Localization:
Cytoplasm.
Sequence:
MKTSPKLSRNLKRWNALRDAAGPGSAIWHQKPLEEQQEKLDQLQHFLTRLSQPKEQLPLAQWLSSHFFECCFQTTTKIKMDGGRKEAEAHANLYLVEEEHGQLEKGAKYYEAFYHLTVDRIWKDETSHSHNSLACENLWRIYTLQADKMLVNKQCQKAIKTLVKAFDLAREGDNEKLEGEAAYRLGLAHISSVNPHNIFKYILYMKISKMLEDNVSLGKVYKAIAKGLER
The following text describes a protein:
Function:
ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type.
Sequence:
MTDTVEDVELPYDDSASQQDKLEALEEQLSTLEEENEEMRDRLLDANAENNKYQQKLERLSHENKKLKQSPLFIATVQELTDEGAVIKQHGNNQEALTEVTDELRATLEPGSRVAVNNSLSVVRQLDDEADVRARVMEVDDSPDVGYEDIGGLDDQLREVRETVELPMKDPGLFETVGINPPSGVLLHGPPGTGKTLMAKAVASQTDASFIKMAGSELVHKFIGEGAKLVRDLFQVARDHEPAVVFIDEIDAIASKRTDSKTSGDAEVQRTMMQLLSEMDGFDERGDIRIIAATNRFDMLDRAILRPGRFDRLIEVPHPNVGGREKIFRIHTRAMNVADSVDFGELAADTGDLSGADVKAICTEAGMFAIRDDRTEVRMQDFQSAREKLDQDSEPAAATDVSRTFA
The following text describes a protein:
Function:
Plays an important role in the organization of the cytoskeleton by regulating actin polymerization in two ways. Firstly, by binding to and sequestering actin monomers (G actin) inhibits actin polymerization. Secondly, by binding directly filamentous actin (F actin) promotes actin polymerization. Regulates the formation of cortical actin in oocytes conferring them enough rigidity to sustain the contractions during ovulation.
Subcellular Localization:
Cytoplasm, cell cortex. Cytoplasm. Cell junction. Cytoplasm, cytoskeleton. Note=Localizes to the cell cortex and the cytoplasm in oocytes and at the inside edges of membrane cubicles surrounding germ cell nuclei. Co-localizes with actin at the cell-cell contact in two-cell stage embryo.
Domain:
The 4 repeats act cooperatively in the binding of G actin.
Sequence:
MAAVTELPKMNQELAGAVREGLELKKVETTEKNVLPTKEDVAEEKQHVERIHEIEHFDSTKLHSTPVKEKIVLPSADDIKQEKQHLELTDKINNFPSENLKKTETIEKNVLPSPTDVAREKTLQMAASFDKSALHHVETIVSTDVRVTEAQ
The following text describes a protein:
Function:
May act as a tumor suppressor. Promotes apoptosis of cancer cells.
Sequence:
MARSRLTATSVSQVQENGFVKKLEPKSGWMTFLEVTGKICEMLFCPEAILLTRKDTPYCETGLIFLTLTKTIANTYFYF
The following text describes a protein:
Function:
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Subcellular Localization:
Cytoplasm.
Sequence:
MALSPGELELIRSALGREPTEVEYALFRSHWSEHCSYKSTRMWLRRLPSKAPWVVRGPGTDAPLVEIAEGLYATFKIESHNHPSAVDPYNGAATGVGGIIRDILTVGARPIALLVNLHFGPPSHPHARWIAVNVIRGISDYGNRVGVPVVGGETWFHEDFTYTPIVLATCVGIVEKDGVPPGGAEPGDLIIVAGLGADKSGLGGSAFASKTLSEEAEEDLGAVQVADPLMGKKLIDLVREARSCVKFIKDLGGGGLATALAELAEWFQLGVVAELDKIHMADREMGPAEVLTSETQERMVFVTSPSKLECLERLLEKFEVPYSIVGRFTAEGRVVLKWRGEVVGDLPLSLVAKAPETPWPQEPYAPPPLPHVPEPPIEKAIDAVLSSPNVAFKQAIYERFDFDVGVRTVLKPGEGDAAVLKIYERGNLGLAVKGDANPRFTYLNPRLGAANAFIKAYRNVAVVGGRPLAAVDSINVGSPSRPSAYWQFVEAVEGLREAAEALGVPIVGGKVSLYNEYKGKPVAPTVAVVVLGVVEDVSKVNKAVWKEGDGVYVWGVTKDEVGGSEYLHRVHGLVAGQPPSIDYSVEKELAAVVRKWAGRLTGAKDVGLGGLAAALAKMAAASGIGADIDICKAPSTTARLDYLLFSESNGRFIAAGEEGPGTRVGAAGGDYFTLRCGSTIVYKRKVEELAELMSLKI
The following text describes a protein:
Function:
May play a role as NF-kappa-B regulator.
Sequence:
MAAAGAPDGMEEPGMDTEAETVATEAPARPVNCLEAEAAAGAAAEDSGAARGSLQPAPAQPPGDPAAQASVSNGEDAGGGAGRELVDLKIIWNKTKHDVKFPLDSTGSELKQKIHSITGLPPAMQKVMYKGLVPEDKTLREIKVTSGAKIMVVGSTINDVLAVNTPKDAAQQDAKAEENKKEPLCRQKQHRKVLDKGKPEDVMPSVKGAQERLPTVPLSGMYNKSGGKVRLTFKLEQDQLWIGTKERTEKLPMGSIKNVVSEPIEGHEDYHMMAFQLGPTEASYYWVYWVPTQYVDAIKDTVLGKWQYF
The following text describes a protein:
Function:
Catalyzes the production of nitric oxide. The complex between TrpRS II and nitric oxide synthase oxygenase catalyzes the regioselective nitration of tryptophan at the 4-position.
Miscellaneous:
MISCELLANEOUS: This protein is similar to the oxygenase domain of eukaryotic nitric oxide synthases but lacks the reductase domain which, in eukaryotes, is responsible for transfer of electrons to the ferric heme during nitric oxide synthesis; MISCELLANEOUS: Affinity for substrate L-arginine is increased by TrpRS II.
Sequence:
MSCPAAAVLTPDMRAFLRRFHEEMGEPGLPARLRAVEEAGLWWPTSAELTWGAKVAWRNSTRCVGRLYWEALSVRDLRELNTAQAVYEALLQHLDDAFCGGHIRPVISVFGPGVRLHNPQLIRYADDPINADFVDKLRRFGWQPRGERFEVLPLLIEVNGRAELFSLPPQAVQEVAITHPVCLGIGELGLRWHALPVISDMHLDIGGLHLPCAFSGWYVQTEIAARDLADVGRYDQLPAVARALGLDTSRERTLWRDRALVELNVAVLHSFDAAGVKLADHHTVTAHHVRFEEREARAGREVRGKWSWLVPPLSPATTPLWSRRYRAREESPRFVRARCPFHTPTVHASTGHAPTG
The following text describes a protein:
Function:
Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine-dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.
Subcellular Localization:
Nucleus.
Sequence:
MAAAGADPGSEPAGGAQFFCTAGRGLEPFLMREVRARLEATQVEYISGKVFFTTCSDLPSMKKLKSAERLFLLIKKQLPITVSSLHRGRLLNEMQRFINDDPGSWLKAISLWRKLLDHDTNGEKVSQGDANPLKRKAGENDSITPKKLKLEEMQVVDKSHGESQQDQPQGPLEQGETLARTDELQEQRLHRASETAAHAQSPEDLTFRISCRCSGSIRKVVTGQIFMHLSDAYSVVGIPLLRVPLASRTYLQTAGLRSTIAWAMASIAEIKAGALVLDPMCGLGTILVEAAEEWPDVFYVGADVSDSQLLGACDNLKAAGLAHRIELLKGSVADLPLPAQSVDVIISDIPFGKKFKLGKDIKSILQEMERVLHVDGVMILLLSEDHHRRLTDCGGSSMPPTSQGNVSDPEMKMLLNPDRTGAPDTASPSQKASSLQSLGRPLPCGSLVPVESFKVSLGKTDAFICKYKKASASGLSPSRCHEPGAHPEVAAMQGSPGLQDSICPGAPSAQPLPVGMAKNTAVR
The following text describes a protein:
Function:
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). Required for lipid droplet accumulation in liver and intestine during embryogenesis. May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). May play a role in the regulation of cell morphology, ER morphology and cytoskeletal organization (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAAAVAGSLVDKLVCLWRQPYTRIYLPHLFFCISLVGSVLKNAELVPESYFSSSRNVLNLYFVKVSWGWTIVLLLPFIAYSNFYIKSHMFALRRLTSLLVATLVWYICTETFFYIEDITGSCYESNTMVVIRGEFDTKAACRKAGFFWDGFDISGHSFILSYSSLVIMEEMVPMLHIQPAYRNPPLDCLYLALNVIVAIWIWMFGCTSVYFHDIIDKILGTSCGILGWYMTYKVWYVKLFSPGLPPQPKQHT
The following text describes a protein:
Function:
Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo. Plays a key role in innate and adaptive immune response triggered by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides from pathogens, and mediated by the nucleotide-sensing receptor TLR9. It is necessary for the translocation of CpG dinucleotides from early endosomes to late endosomes and lysosomes, where TLR9 is located.
Subcellular Localization:
Cytoplasm, perinuclear region. Lysosome.
Sequence:
MAEAVKPQRRAKAKASRTKTKEKKKYETPQREESSEVSLPKTSREQEIPSLACEFKGDHLKVVTDSQLQDDASGQNESEMFDVPLTSLTISNEESLTCNTEPPKEGGEARPCVGDSAVTPKVHPGDNVGTKVETPKNFTEVEENMSVQGGLSESAPQSNFSYTQPAMENIQVRETQNSKEDKQGLVCSSEVPQNVGLQSSCPAKHGFQTPRVKKLYPQLPAEIAGEAPALVAVKPLLRSERLYPELPSQLELVPFTKEQLKILEPGSWLENVESYLEEFDSMAHQDRHEFYELLLNYSRCRKQLLLAEAELLTLTSDCQNAKSRLWQFKEEQMSVQGICADQVKVFSYHRYQRVEMNENALVELKKLFDAKSEHLHQTLALHSYTSVLSRLQVESYIYALLSSSAVLRSSAIHQQGRASKQTESIPSDLCQLKECISVLFMFTRRVNEDTQFHDDILLWLQKLVSVLQRVGCPGDHLFLLNHILRCPAGVSKWAVPFIQIKVLHNPSGVFHFMQSLALLMSPVKNRAEFMCHMKPSERKPSSSGPGSGTWTLVDEGGEEDEDPETSWILLNEDDLVTILAQFPFHELFQHLLGFKAKGDYLPETTRPQEMMKIFAFANSLVELLAVGLETFNRARYRQFVKRIGYMIRMTLGYVSDHWAQYVSHNQGSGLAQQPYSMEKLQVEFDELFLRAVLHVLKAKRLGIWLFMSEMPFGTLSVQMLWKLFYLMHQVESENLQQLSSSLQPAQCKQQLQDPEHFTNFEKCLSSMNSSEEICLLTTFAQMAQARRTNVDEDFIKIIVLEIYEVSYVTLSTRETFSKVGRELLGTITAVHPEIISVLLDRVQETIDQVGMVSLYLFKELPLYLWQPSASEIAVIRDWLLNYNLTVVKNKLACVILEGLNWGFAKQATLHLDQAVHAEVALMVLEAYQKYLAQKPYAGILSESMKQVSYLASIVRYGETPETSFNQWAWNLILRLKLHKNDYGIQPNCPAVPFSVTVPDMTESPTFHPLLKAVKAGMPIGCYLALSMTAVGHSIEKFCAEGIPLLGILVQSRHLRTVVHVLDKILPLFYPCQYYLLKNEQFLSHLLLFLHLDSGVPQGVTQQVTHKVAQHLTGASHGDNVKLLNSMIQAHISVSTQPNEVGPVAVLEFWVQALISQHLWYREQPILFLMDHLCKAAFQLMQEDCIQKLLYQQHKNALGYHCDRSLLSSLVSWIVAGNITPSFVEGLATPTQVWFAWTVLNMESIFEEDSQLRRVIEGELVINSAFTPDQALKKAQTQLKLPIVPSLQRLLIYRWAHQALVTPSDHPLLPLIWQKFFLLYLHRPGPQYGLPIDGCIGRRFFQSPAHINLLKEMKRRLTEVADFHHAASKALRVPAEGSEGLPESHSGTPGYLTSPELHKELVRLFNVYILWLEDENFQKGDTYIPSLPKHYDIHRLAKVMQNQQDLWMEYLNMERIYHEFQETVGLWTQAKLESHSTPCSLSVQLDFTDPLLAKERVLSNLRKHEAPQPPLALHPTKPPVPVISSAVLLSQKDATQLVCTDLNLLQQQARTAALRESQQVALDGELLDTMPKQYVNREEQTTLHLECRGSSGKKCQGAAVVTVQFEGMHKNEAISQQLHVLRKEVKQLQAEAAKPPSLNIVEAAVHAENLITALVNAYKLQPTPGIQKVGISLFFTIVDYVSDETQRHPPTRQFFTSCIEILGQVFISGIKSECRKVLETILKNSRLCSLLSPFFTPNAAPAEFIQLYEQVVKFLSEDNSDMIFMLLTKFDLKQWLSATKPPLSDRTRLLESIHLALTAWGLEPDEDILMPFNLFCKHWTYLLLYQFPDQYSDILRLLMQSSAEQLLSPECWKATLRALGCCAPSCQQGAASTEGAVLPSSSDALLSDKQVMETIQWLSDFFYKLRLSKMDFKSFGLFSKWSPYMADVKTFLGYLVKRLIDLEMTCLAQDPTASRKTVLKSLHSVIIQLFKPWILVLEDNESSQQRHYPWLESDTVVASSIVQLFTDCIDSLHESFKDKLLPGDAGALWLHLMHYCEACTAPKMPEFILYAFHSTYRKLPWKDLHPDQMLMEAFFKVERGSPKSCFLFLGSVLCEVNWVSVLSDAWNSSPHPETRSMIVCLLFMMILLAKEVQLVDQTDSPLLSLLGQTSSLSWHLVDIVSYQSVLSYFSSHYPPSIILAKESYAELIMKLLKVSAGLSIPTDSQKHLDAVPKCQAFTHQMVQFLSTLEQNGKITLAVLEQEMSKLLDDIIVFNPPDMDSQTRHMALSSLFMEVLMMMNNATIPTAEFLRGSIRTWIGQKMHGLVVLPLLTAACQSLASVRHMAETTEACITAYFKESPLNQNSGWGPILVSLQVPELTMEEFLQECLTLGSYLTLYVYLLQCLNSEQTLRNEMKVLLILSKWLEQVYPSSVEEEAKLFLWWHQVLQLSLIQTEQNDSVLTESVIRILLLVQSRQNLVAEERLSSGILGAIGFGRKSPLSNRFRVVARSMAAFLSVQVPMEDQIRLRPGSELHLTPKAQQALNALESMASSKQYVEYQDQILQATQFIRHPGHCLQDGKSFLALLVNCLYPEVHYLDHIR
The following text describes a protein:
Function:
Activates an alternative mTOR signaling to regulate cell proliferation and migration.
Subcellular Localization:
Membrane. Cytoplasm. Lysosome.
Sequence:
MGNTESGSHQKGLSRILPEEKAEIEQFFENMCRMQSGPKKSVGLQYFQDALRNSLPCSISQRIFDGIQSVRTNSKSSTMSAEISKEQFLVFYVDLLRGTAEEKSQVICDMISCNNSEHMKGHQVQKFLEDIIAAVIYVLKQQSLLKGWNLENMRDCTLGTQGLAMQLLSQLQSIDGQKFERQELLDSPCSKSCIEDWLYKIPMISLFVRVMLTVGLSILKHHTEHQKDMKTLLPKCTGMKNTSFVSLLDLPAVMHLNYYLPYEVQHKWRLLFSSQIHGESFSQLCGHILDQGPCLLIVKDSDGFVFGGFASQSWKVKPQFQGDSRCFLFSISPRLDVYTYTGYNDHYMYLNRAQQSLPNGLGMGGQHEYFGFWIDSNFGIGHSKAKPSCTTYNSPQLSAKEEFSIHTVEVWAVGDVPEHLLAKNPRSILDSDTEARALLEMAGQTRQSDGLREVTEEDES
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively. Involved in the biosynthesis of sphingolipids and ceramides. Required with LCB3 for an effective incorporation of DHS into ceramides through a phosphorylation-dephosphorylation cycle. Involved in heat-induced transient cell cycle arrest. Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling. Involved in heat-stress resistance.
Miscellaneous:
MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Late endosome membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Note=LCB4 is synthesized in the cytosol, palmitoylated at the Golgi apparatus by AKR1, and then transported to the plasma membrane (PM) via the late Sec pathway. Most of the LCB4 is delivered further to the cortical ER (cER), which is closely adjacent to the PM. In stationary phase, G1 cell cycle arrest causes ER-localized LCB4 to be transported to the Golgi apparatus via the early Sec pathway, and finally to the vacuole via the MVB pathway, where it is degraded.
Sequence:
MVVQKKLRAILTDEGVLIKSQSHHMFNKHGQLRSGDSLSLLSCLSCLDDGTLSSDGGSFDEDDSLELLPLNTTIPFNRILNAKYVNVGQKGFNNGKISSNPFQTENLSSSSENDDVENHSLSNDKAPVSESQSFPKKDKWDTKTNTVKVSPDDSQDNSPSLGIKDNQQLIELTFAVPKGHDVIPQKLTLLIDHVSRKSRANTGEENISSGTVEEILEKSYENSKRNRSILVIINPHGGKGTAKNLFLTKARPILVESGCKIEIAYTKYARHAIDIAKDLDISKYDTIACASGDGIPYEVINGLYRRPDRVDAFNKLAVTQLPCGSGNAMSISCHWTNNPSYAALCLVKSIETRIDLMCCSQPSYMNEWPRLSFLSQTYGVIAESDINTEFIRWMGPVRFNLGVAFNIIQGKKYPCEVFVKYAAKSKKELKVHFLENKDKNKGCLTFEPNPSPNSSPDLLSKNNINNSTKDELSPNFLNEDNFKLKYPMTEPVPRDWEKMDSELTDNLTIFYTGKMPYIAKDTKFFPAALPADGTIDLVITDARIPVTRMTPILLSLDKGSHVLEPEVIHSKILAYKIIPKVESGLFSVDGEKFPLEPLQVEIMPMLCKTLLRNGRYIDTEFESM
The following text describes a protein:
Function:
Essential regulator of neutrophil polarity. Regulates neutrophil polarization by regulating AKT1 phosphorylation through a mechanism that is independent of PIK3CG activity.
Subcellular Localization:
Cell projection, stereocilium. Membrane.
Sequence:
MVGGQQLGSRRPASVGCRCAWTGWRELLGVLGHRGPGCGPRAGRGLRGSGRPRLCSARGRVNDRAPAAPEPSGRFRNAVARRELWVKRGPGGRLPCGGRRGARAVAAPGTRGGRSLGARGPPSPPGAAAGPGRGRGPGAGPSRGGRGRGGAPPVPAQRAAGGRRQAAPRRLRRLRRPAGLGARSPGSAPLAAGGPALGSRRMTLKASEGEGGGSMRTALSDLYLEHLLQKRSRPEAASHQVNAVTEDMYTNGSAAPGSPTQAKGQEVRKVRLIQFEKVTEEPMGITLKLNEKQSCTVARILHGGMIHRQGSLHVGDEILEINGTNVTNHSVDQLQKAMKETKGMISLKVIPNQQNRLPALQMFMRAQFDYDPRKDHLIPCKEAGLKFVTGDIIKIINKDDSNWWQGRVEGSSKESAGLIPSPELQEWRVASAAQSAPSEAPSCSPFGKKKKYKDKYLAKHSSIFDQLDVVSYEEVVRLPAFKRKTLVLIGASGVGRSHIKNALLTQNPDKFAYPAPYTTRPPKKGEEDGKEYHFISTEEMTKNISANEFLEFGSYQGNMFGTKFETVHQIHEQDKIAILDIEPQTLKIVRTAELSPFIVFIAPTDQGAQTEALQQLQKDSEAIRSQYAHYFDLSLVNNGVEETLTKLQEAFEQACSSPHPWGRRCSSSAPAHPPIGVSEGAMRHPEAEAPSARTARRRRGTGRGRAPAAPR
The following text describes a protein:
Function:
Required for the formation of functionally normal spores. Could be involved in the establishment of normal spore coat structure and/or permeability, which allows the access of germinants to their receptor (By similarity).
Sequence:
MPAMVGHIRIVNIGSSGIFHIGDVFAIRPISYSRAFAGAGSFNVGDNVSVYNYQSATTVNDSDVVDQAIIGST
The following text describes a protein:
Function:
Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MVSTGLFRPTKAIPLLFLLFSLYKTEKIDDSIHYYVSFTSDSVTIKDPPTLETGNTELSDDYVRIMSKNNERFLCKLPQIDVEVKKNVEYSGATAGKLLETMLYKDKMCSYLIDVYWTYQVCHGRYVIQYHEDKMLTGQVSRTEFYLGNFDSALTASTNEQVKPATRRIENEDYPYYSVSYNHGTSCDVTGGKPRTTDVVYICVEKVQHKILSVTEISSCHYEIVIMTDLLCKHPEYQLSEKKDHKIVCWNEDAKNENEAKPQTLQRLDDFHDSTFKREYTVFTDQDPQYSENTEEEDGGLIDEKDFEKLKETRQAGYILGGVKRFNTKESLANNPAVVHHTVNRILTGEDCIVGGTGWWKYEFCYGKHVIQFHEDANGQRSDILLGVFDEVVHKEWVKLDRHARGAIQGNNQIDQISQIYAKGDICDETGAHRDVEVRIRCATADHSALSFSMHLTEPRTCQYVLTIDSERFCEPLQFADDYGLIELTQVASSSQSAAAAAAAPVELSIDEEEEDEAHEQSDEDDHDVKIHEDL
The following text describes a protein:
Function:
Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin-arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export.
Subcellular Localization:
Cytoplasm.
Sequence:
MNQEFHITSLVIHATSKSVEDIKQRLSALVGAEIHAVTDEGKFVVTLEGETQRSILDNVEAINAFEGVINSSLIYHQVDPVEQKSEEHHEH
The following text describes a protein:
Function:
Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.
Sequence:
MEAAESGRSRWAAPTKVDGLYDPALEKEACGVGFVVQIDGIRSNKILKDARTLASRLDHRGACSCDNDTGDGAGVLTAIPHQLYSSIIREEADIELPPIGHYATGICFVDRENHAESEAMFQEIAKECSLQVLYWRTVPTDRSVIGQVARNGEPFMRQVFVTWDNPAFTSPEDERIFLEKVFVLRKKVTHRIPRPGARFYICSLSPDVIVYKGQLTSTQVWTYFSDLDRPEYETYLALVHTRFSTNTFPSWERAHPLRMLAHNGEINTLRGNVNYMKAREGLMSSERFGKRALAELYPVVEPNLSDSGSADCVLEFLVRAGGRSLPEAIMTMIPEAWEQDPLMDQEKKDFYRWAGCSMEPWDGPALMAFTDGRYIGAVLDRNGLRPSRYYVTKDNVVVMASEGRLEPSRMLLIDTANRVIIGDDEIKMSIARSRPHSEWLAQLVTLDDIRKTSAVISSQNGQPPSIEPQLKSAEEIRKILSLFNYTLETLSLLLVPMFTNKKEALGSMGNDAPLACISDFQPLLYEYFKQLFAQVTNPPIDPFRERIVMSLACPIGPEANILEPSDQQCRRLYLEQPILSPDDLKLIVNCSANDWKSKIIDITVDANVPLVYITQLDRICEEVTEAVKSDFQFIILSDRKAGKERIPLSALLTLGAVHHHLIEERLRMKVGLIVETGEAREVHHMCVLLGFGADAICPYLIMEATRRLRCEGVLNDKLNDKQVFDNYIEAMENGIAKVMAKMGISTLQSYKGAQIFEAIGLSDEIIDKCFKGTSSRVGGVTFKEVAQETVERHIISFQKMECDTYVLRDPGNYHWRRGGEKHLNDPDSIGVLQEAAKNNSRDAFNRFQQSTMKSLRQCTLRGQLEIIASSQPVSIEDVEPASEIVKRFVTGAMSFGSISKEAHTTLATAMNRIGAKSNTGEGGEDPERYLNQDPSNSQRSAIKQVASGRFGVTAAYLANADELQIKMAQGAKPGEGGELPGYKVTVDIARTRHSVAGVGLISPPPHHDIYSIEDLAELIYDLKCANPLARISVKLVSVVGVGVVAVGVAKGKAEHITISGHDGGTGASSWTGIKNAGLPWELGIAETHQTLVLNDLRSRVVLQVLIKFPLGRTNTILIADGQIRTAFDVIVAAVLGADEFGFSTAPLIALGCTMMRKCHLNTCPVGIATQDPVLREKFAGQPEHVINYFFLLAEEVRKEMAKLGLVKFQQLIGRTDFVRVRDAQDHTSPKKSKLLYFGAVLRSALSMRPGVNIIGGSVAQDFGLENHLDQKLIKESASVLNGTCQKVSFAVNVVNSNRAVGTILSYTIAKRYGEKGLPDGSINVFMRGSAGQSFGAFLARGISITLAGDANDYVGKGLSGGEIVIYPPRTSTFQSEKNIIVGNACLYGATSGRAFFRGVAGERFCVRNSGAIAVVEGVGNHGCEYMTGGTVLILGPTGRNFAAGMSGGIAYVLDTKGIFPTFCNTTTVQLLPLVTVEDAVIVHSLLEEYYEKTASDYAKVLLDEWPKARYKFVKVFPYDYQKALLAQEAEAKKQKKAKGKSPKVNVKTNGFQTKLNDIADIEDAAGPSQPVDKARGFMKYKREVVSYRPAEKRMNDWEEIYDFDHVKKGLKVQASRCMDCGVPFCQSSFGCPLGNIIPKWNDLVSQDKWKEALDQLLQTNNFPEFTGRVCPAPCESACVLGINNLPVTIKSIECSIIDYAFEQGWMKAEPPLIRTGKKVAVVGSGPAGLACAHQLNKAGHLVTVFERDDAIGGLLQYGIPTMKLSRDVIERRVELLQQEGIAFLTGVDIGKDVSAEDLRKQYDAIVLCIGSTRPRDIAIPGRMLDGILQAVSYLGTWQKKQMHPDNNLGNPCYSAKDRDVIILGGGDTGNDCIGTSLRQGARSITTFEILPPPPTSRASDNPWPQWGRVFKVDYGHEEVKIKYGKDPRLYNTMSKEFVSDGKGGVAGIKAVQVEWKKDAESGKWVMTEVPNSEKLYKCDMVLLAMGFLGPEPAIMNQLKLQVDPYSNVSTPSDEYSTNVSGVYAAGDCRRGQSLVVWAIAEGRQAARQVDEMLMGSSSLSGPGGIIQLDSSVGGAP
The following text describes a protein:
Function:
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Sequence:
MSVIWEEPIYRFVVGPHKGNGGAICGNDGGVWGRSETLDISFEEARACSRIFYHPTTALPFSLSGVSFEVKSISEDETVNWITAKSPKYKCGCTLVETGTGYVIGYYDSPITEEENLKATLQLARHVTERGY
The following text describes a protein:
Function:
Catalyzes the GDP transfer from GTP to D-glycero-alpha-D-manno-heptose 1-phosphate, yielding GDP-D-alpha-D-heptose. Is able to use ATP, CTP or UTP as substrate in the presence of pyrophosphatase, but at a significantly slower rate. Can also form GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate and GTP.
Sequence:
MQAIILCGGLGTRLKSIIKDIPKPMAPINDKPFLEFIFEYLKKQGIKEVILAVSYKYEVIKEYFKDEFLGIKIKYSIEKEPLGTGGAIKETLKFVKNEAYVLNGDTFFDIDLSKLKLNESKICLALKQMNDFDRYGTVNVDEQDLVISFEEKVFKKQGLINGGIYLLTKDIFNDFALQEKFSFEEFLQENYKKLKARACIFDDYFIDIGVPEDYYHFLINN
The following text describes a protein:
Function:
May play an important role in the progression of epithelial malignancies.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Domain:
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence:
MAPAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPWHAALPSSPAPAPATQEAPRPASSLRPPRCGVPDPSDGLSARNRQKRFVLSGGRWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDDQGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYPLSLSPDDCRGVQHLYGQPWPTVTSRTPALGPQAGIDTNEIAPLEPDAPPDACEASFDAVSTIRGELFFFKAGFVWRLRGGQLQPGYPALASRHWQGLPSPVDAAFEDAQGHIWFFQGAQYWVYDGEKPVLGPAPLTELGLVRFPVHAALVWGPEKNKIYFFRGRDYWRFHPSTRRVDSPVPRRATDWRGVPSEIDAAFQDADGYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGCAEPANTFL
The following text describes a protein:
Function:
May play a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MNKQRGTYSEVSLAQDPKRQQRKLKGNKSSISGTKQEIFQVELNLQNASSDHQGNDKTYHCKGLLPPPERLTAEVLGIICIVLMATVLKTIVLIPCIGVLEQNNFSLNRRMQKACDCGHCPEEWITYSNSCYYIGKERRTWEEGVCWPVLQRTLICFL
The following text describes a protein:
Function:
Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases. Involved in endocytosis and calcium-mediated signaling (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MVHKKKNVDIPSSQKYLGIQHVNFYSNAFGKESLRFQLRELILPIVRKETRLLYKIQSFFRNPWLDVYFMYTATLGTHVFFMLALPIFFWSGCIYYTLDITQLFAAGVYFSGCIKDYFCLPRPRSPPMVRLTLSSDAEYEYGFPSTHTTNAMATGFYSLFLLLSMSDSMSSISYYFLLSLVLLYIASISLGRIYCGMHGFMDVSTGTILGVTLAIFQWKYADFFHNVWSSSSTSVPILSVVLALFFIWFHPQPAERCICLEDSISFISVIMGIDLGTWFASPESLSHLHDNLNSYFLLKFFVRVLFGVCMILIWKSFAKQALLAVLPPIFKSLRLSYLEPKSQSEKGIRAATGSNHSPGNIGTELGVITSHQSHPHPVRFDIETIARIIVYSGIGFLCTYFAPKVFLKWKI