lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (By similarity). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (By similarity). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (By similarity). Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). May be involved in nuclear remodeling during sperm head formation in spermatogenesis (By similarity). May play a role in DNA repair by suppressing non-homologous end joining repair to facilitate the repair of DNA cross-links.
Subcellular Localization:
Nucleus inner membrane; Single-pass type II membrane protein. Note=At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles.
Domain:
The coiled coil domains differentially mediate trimerization required for binding to nesprins and are proposed to dynamically regulate the oligomeric state by locking the SUN domain in an inactive confirmation. The coiled coil domains are proposed to be involved in load-bearing and force transmission from the cytoskeleton; The SUN domain may play a role in nuclear anchoring and/or migration.
Sequence:
MDFSRLHMYSPPQCVPENTGYTYALSSSYSSDALDFETEHKLDPVFDSPRMSRRSLRLATTACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGVSHGGTVSLQDAVTRRPPVLDESWIREQTTVDHFWGLDDDGDLKGGNKAAIQGNGDVGAAAATAHNGFSCSNCSMLSERKDVLTAHPAAPGPVSRVYSRDRNQKCYFLLQILRRIGAVGQAVSRTAWSALWLAVVAPGKAASGVFWWLGIGWYQFVTLISWLNVFLLTRCLRNICKFLVLLIPLFLLLAGLSLRGQGNFFSFLPVLNWASMHRTQRVDDPQDVFKPTTSRLKQPLQGDSEAFPWHWMSGVEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRDAVGQPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQLLPTVEHLQLELDQLKSELSSWRHVKTGCETVDAVQERVDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQILRNVTHHVSVTKQLPTSEAVVSAVSEAGASGITEAQARAIVNSALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALMSLFGIPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLSPTGNISSAPKDFAVYGLENEYQEEGQLLGQFTYDQDGESLQMFQALKRPDDTAFQIVELRIFSNWGHPEYTCLYRFRVHGEPVK
The following text describes a protein:
Function:
Involved in vesicular recycling, probably as a RAB11B GTPase-activating protein.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MWLKPEEVLLKNALKLWVLERSNQYFVLQRRRGYGEEGGGGLAGLLVGTLDAVLDSTSKVAPFRILHQTPDSQVYWSIACGASREEITEHWDWLEHNVMNILSVFDSNEDITSFVQGKIRGLIAEEGKGSFTKEEDPEKFREGLMKFERCFGLPEQEKLVTYYSCSYWKGRVPCQGWLYLSTNFLSFYSFLLGAEIKLIISWDAISKLEKTSNVILTESIHVCSHGEDHYFSMFLHINETFLLMEQLANYAVRRLFDKETFENDLVLHDPLQITKRGLESRAHSQQFSAFFRLPKEETLKEVHECFLWVPFTHYNAHGKMCISENYICFASQDGSLCSVIIPLREVIGVDKADPANRGVNISTKGKRAFRFTEVRDFEQLVTKLRIKCNATSTSSPQHINTEVASSSASDSPKDFDEVPSKIDLRDNSKTVSTEALMTVYHPQDAENLDPKMLKEKMKEQSWNILFFERGHGVSMFRTKKTRDLVVRGIPEALRGELWLLFSGAVNDMASSPGYYTELVEKSLGTCTLATDEIERDLRRSLPEHPAFQSDTGISALRRVLTAYAYRNPQIGYCQAMNILTSVLLLYAKEEEAFWLLVAVCERMLPDYFNRRIIGALVDQAVFEELIRVHLPQLTDHMMGMTFFSSVSLSWFLTLFISVLPIESAVNVVDCFFYDGIKAILQLGLAVLEYNMDKLLACKDDAEAVTVLNRFFDSVTNKDSPLPPAVQQGSNLSDAKGDHPKVDITDLIRESNERYGDIRYEDVESMRCRNRLYVIQTLETTTKQNVLRVVSQDVKFSPNVLDELYELFKKEHFLSCYWNVNSPVLQHHDASLPYLEQYRIDCQQFRVLCHLLSPWSHCANRDSIALWTFRLLDENCHGLINFKQFSCVLDTMYNGSFTDKLKLLFKLHIPPAFTEVESLSPSKGVALSKEELIHFSQLSVSSAGDSLESDALKSSPEKGKGKVDIQAYLKQWQDELLKKEENIKDLPRMNQSQFIQFSKTLYNLFHGDPEEELLYRAIAVVTSLLLKMEEVGRRLQSPTSPVRSPAATTEVSAESPQKGQEEGSSEQTEGSGAQSLRKNHEWSFAFEQILASLLNEPAFVRFFEKPHEIKTRIESAKNLQLKARTRV
The following text describes a protein:
Function:
Metalloprotease.
Subcellular Localization:
Secreted.
Sequence:
MFRSLLISILLIHDIFSENVVLNFGSHNKHSHGSRAKRQVIIRGEDQDQYKWPNNTVHYYFDEENFDFSMKETILQAMKMLSSHTCIKFSTEPSDVIIRMESDSDRNYCFSEIGHVRENQQFSFTSSCYSVGLAVHEIIHSLGFMHAHQRADRDEYLHFVMDLDGMSLQDRQQYAIWEHQILLVPYDYGSVMQYADADDNYFPINKNRFMYQTMGSEVVAFYDYLMINKYYECSCGDDALKCQNFGYPNPSNCSQCNCPYGFGGDDCSQRAEPGTTLQATKGWKNTTISLDAGFKDVNHLRMRQIDYIYSYLWITAPENKTTEIRVLQSESGKCLRGCGRGAIEIKTNEDPRLTSPRFCCNESKTVRSSHTPTVVMAYNSEGLNEYTIAYRYVDTYQ
The following text describes a protein:
Function:
May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling.
Sequence:
MLRMVLEALQAREKRQGTSVVAIKVYIQHKYPTVDTSRFKYLLKQALDTGMRRGLLTRPANSKAKGATGSFKLVPRPKKKRTCTSIARRRATDAKETGPKKPREPKTDHTSKAKVEKVAVKPRPRRKACPCPAATLEKAPKKASKAKLGEVTKDPLKPDKATLPPPTANKIGQNVKHSGNRHESEAHGKTKDVWEKSEPSVCKVPKSAASLTKRKMTAMAHTKTVVQGARMVHKTKAPVPPQDMGHKAQPTSRVRKTKSPEDPKRPGLPPKISSKAPSKKAEPGN
The following text describes a protein:
Function:
Probable RNA-binding protein that plays a role in meiosis and vegetative growth.
Sequence:
MPSQMREPQGLSPSSYFSEDLCFHDERQVGFWKTNSLQNYHGLKGDDALQRAAVRSSPLENHISLGSPMAKHFEHHGSYLKQDKKVNSIIEKQTFGVERASHSLPRALDHNLDVRSILGADLTSIPAEGDRISIMGGQYENGLFSSSLSELFSRKLRLPTNNSPHGHSVGAADSHYEEEEPFESLKELEAHAIGNLLPDDDDLLAGVTDGLDYVGQPNAGDDIEDLDLFSSVGGMDLGEDGSSPGQRNSEFAGNYTLQGGSSAAIGGKHPPGENPSRTLFIRNINSSVEDSELQTLFEQYGDIHMLYTACKHRGFVMISYYDIRASQHAMKALQNKPLRRMKLDIHFSIPKDNPSEKDVNQGTLLVFDLDSSVSNDELRQIFGVYGEIKEIRETPHRSHHKFVEFYDIRAAEAALRALNRSDIAGKQIKVEASHPSGTRRRLLQQFPSELEQDEPGLYLQQNSPSILATGFSGALPHGGHASSIENGSILGRQSASGSAINSYLDNAFDCGFSFSVPNSLLRLESKGNQVNVGETGHLQSRISFEFSGTSGLHPHSLPEYHDGLSNGASSISPGSISATMNIRPVKSENRKFSRVGSNGHSVELNEVFTPNGNVNCPSPGHQYIWSKSHQPQPQGMMWPNSPTFVGGVCATRPQQLHSVPRAPSHMLNALGPINNHHVGSAPSVNPSLSLWDRRHAYAGESPDASGFHPGSLGSMRISGNSPHHLEFIPHNVFPRTGGSCIDLSMSSSNVGLHSHHQRSLMFPGRGQIIPMINSFDSPNERMRSRRNEGSSNQTDNKKQFELDVDRIARGEDKRTTLMIKNIPNKYTSKMLLSAIDERHRGMYDFIYLPIDFKNKCNVGYAFINMTVPSLIVPFYHAFNGKKWEKFNSEKVASLAYARIQGKAALIAHFQNSSLMNEDKRCRPILFHTDGPNAGDQVPFPMGVNIRPRTSKNRAGTSEESYQESQTSLSTSKDFVNEESSSGSVKESN
The following text describes a protein:
Function:
Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP.
Sequence:
MNFLAHLHLAHLADSSLSGNLLADFVRGNPATHYPPDVVEGIYMHRRIDVMTDNLPEVREAREWFRHETRRVAPITLDVMWDHFLSRHWTQISPDFPLQAFVGYAHAQVATILPDSPPRFVNLNDYLWSEKWLERYRDMDFIQNVLNGMANRRPRLDALRDSWYDLDAHYDALEERFWHFYPRMMAQAARKAL
The following text describes a protein:
Function:
Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. This ion efflux may influence the activity of urease, which is essential for the survival of the bacterium in the gastric environment.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MQEYHIHNLDCPDCASKLERDLNELDYVKKAQINFSTSKLFLDTSDFEKVKAFIKQNEPHLSLSFKEATEKPLSFTPLIITIMVFLGAILILHLNPSPLIEKAMFFVLALVYLVSGKDVILGAFRGLRKGQFFDENALMLIATIAAFFVGAYEESVSIMVFYSAGEFLQKLAVSRSKKSLKALVDVAPNLAYLKKGDELVSVAPEDLRVNDIVVVKVGEKVPVDGVVVKGESLLDERALSGESMPVNVSENSKVLGGSLNLKAVLEIQVEKMYKDSSIAKVVDLVQQATNEKSETEKFITKFSRYYTPSVLFIALMIAVLPPLFSMGSFDEWIYRGLVALMVSCPCALVISVPLGYFGGVGAASRKGILMKGVHVLEVLTQAKSIAFDKTGTLTKGVFKVTDIVPQNGHSKEEVLHYASCSQLLSTHPIALSIQKACEEMLKDDKHQHDIKNYEEVSGMGVKAQCHTDLIIAGNEKMLDQFHIAHSPSKENGTIVHVAFNQTYVGYIVISDEIKDDAIECLRDLKVQGIENFCILSGDRKSATESIAQTLGCEYHASLLPEEKTSVFKTFKERYKAPAIFVGDGINDAPTLASADVGIGMGKGSELSKQSADIVITNDSLNSLVKVLAIAKKTKSIIWQNILFALGIKAVFIVLGLMGVASLWEAVFGDVGVTLLALANSMRAMRA
The following text describes a protein:
Function:
Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MQNPLYKTGHRSGLDSTVNSEFDDNVDKYRELRTESFLGYLNRGNPEGLNSPVPSLPDLPDPIPRTENHPVLAYKVETSEALNQPISTHNTSQYSPQTSRNVFQTNLLSDEYRRLSPATPFADTPTQDTRALTPLIIDPPTAISRHSHYTVGSGLGDPSDCDAYRYSGMSFGDQPLKSRVNRTVKPSRRKRAIFIVSVVVVVCTCAIIGLVIGLITKNKGVKPDSDGVTRLPRGDKLWGVGGDTITTDKGNKFLYNNTLGGTWVGIPYNDTARPQANQPALNESWDYSNHKILGVNLGGWLVIEPFIAPGLFDPYVQEQNPPSDEWELSVRLGSSLAKTIEAHYDSFIVEEDFALIASAGLNWVRIPVGWWMIETMGSEPFLAGVSWKYFFRAIVWARKYGLRINLDLHAVPGSQNGWNHSGRLGTIGFLSGAMGIANAQRTLNYIRTLTEFISQPEFKNVVPMFSILNEPDFTLGSTKALVSWYYESYKLIRQIGGIGEGNGPFMVIHDAFQGIGTGGPAKNPWSGFLQGADRMGLDSHTYFAFTTQLSDVNATRPCNAWAARSNQTMEGFGLTMSGEWSLALNDCGLYVNNIGWGERYEGTYPNATRPDRRFPRIGSCDQWLDHRKWSDTQKKAFADTALASQDALINSFFWTWKIGNSLRQDFPPNPMWNYKLGLEAGYIRPDARTSAGRCAAITSEAQVPLTTYDWSGTLASWQTGGAGAGNISQSQIDSVGPFPPAMILGAAPSGQGTYNTQSLPQLAPTGPPIILKPIPIVMDSKTFSGGDGWFNKADKAGFFAPINGCQYLDPWSGVDVPAPSACSSNPSSSKQPKQSNTNTPNSSLKA
The following text describes a protein:
Function:
May be involved in cell survival, proliferation and progression of cancer cells.
Subcellular Localization:
Cytoplasm. Microsome membrane. Endoplasmic reticulum membrane.
Sequence:
MGECPHLVDVRLGHRSLATGPEQSDICHTGSEARWTTTWYGSLSFSRHKYKMLADLTPGVEMSCRHWARWLTPVIPALWKAEAGGLPELRSSRPAWTTW
The following text describes a protein:
Function:
Involved in providing solanesyl diphosphate for plastoquinone-9 (PQ-9) formation in plastids. Catalyzes the elongation of the prenyl side chain of PQ-9 in plastids. Contributes to the biosynthesis of plastochromanol-8 (PC-8) in plastids. Does not contribute to the synthesis of tocopherol or ubiquinone. PQ-9 and PC-8 are lipophilic antioxidants that act as protectant against photooxidative stress under high light stress conditions. Prefers geranylgeranyl diphosphate to farnesyl diphosphate as substrate. No activity with geranyl diphosphate or dimethylallyl diphosphate as substrate.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MMSVTCHNLDFGTRVLDLVTCGTSSNASIERHSVKNYGKTISNASCKGCGGRRMVYCRQNTTGSRVFPTKAPEPLLDAYFFKYRIEFSTWNYIAFSTFNFNIGVGRSTAPVLDLKKELRSPISLANLFKVVADDLQILNQNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAELVGLKELTTKHRRLAEIIEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAILAGDFMFAQSSWYLANLENLEVIKLISQVIKDFASGEIKQASSLFDCDLELEEYLLKSYYKTASLIAASTKGAAIFSGADRSVTGQMYEFGKNLGLSFQVVDDILDFTQSAEQLGKPAGSDLAKGNLTAPVIFALEKEPKLREIIESEFCETGSLDEAIELVKKCGGIERAQVLAKERADLAIKNLQCLPQSAFRLALEDMVMFNLERID
The following text describes a protein:
Function:
Catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P. Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc. Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc. Is not able to use GlcNAc-alpha-1P and GalNAc-alpha-1P as substrates. Cannot accept other nucleotide triphosphates (ATP, CTP, TTP, or GTP) than UTP.
Sequence:
MKAMILAAGKGERMRPLTLHTPKPLVPVAGQPLIEYHLRALAAAGVTEVVINHAWLGQQIEDHLGDGSRFGLSIRYSPEGEPLETGGGIFKALPLLGDAPFLLVNGDVWTDYDFARLQAPLQGLAHLVLVDNPGHHGRGDFRLVGEQVVDGDDAPGTLTFSGISVLHPALFEGCQAGAFKLAPLLRQAMAAGKVSGEHYRGHWVDVGTLERLAEAESLIGERA
The following text describes a protein:
Function:
Regulates COPI-mediated retrograde protein traffic at the interface between the Golgi apparatus and the endoplasmic reticulum. Involved in the maintenance of the Golgi apparatus morphology.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, cis-Golgi network.
Sequence:
MWFFARDPVRDFPFELIPEPPEGGLPGPWALHRGRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVTPLGIYLKARVEAGGLKELEISWGLHQIVKALSFLVNDCSLIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQGNGGGPPRKGIPELEQYDPPELADSSGRVVREKWSADMWRLGCLIWEVFNGPLPRAAALRNPGKIPKTLVPHYCELVGANPKVRPNPARFLQNCRAPGGFMSNRFVETNLFLEEIQIKEPAEKQKFFQELSKSLDAFPEDFCRHKVLPQLLTAFEFGNAGAVVLTPLFKVGKFLSAEEYQQKIIPVVVKMFSSTDRAMRIRLLQQMEQFIQYLDEPTVNTQIFPHVVHGFLDTNPAIREQTVKSMLLLAPKLNEANLNVELMKHFARLQAKDEQGPIRCNTTVCLGKIGSYLSASTRHRVLTSAFSRATRDPFAPSRVAGVLGFAATHNLYSMNDCAQKILPVLCGLTVDPEKSVRDQAFKAIRSFLSKLESVSEDPTQLEEVEKDVHAASSPGMGGAAASWAGWAVTGVSSLTSKLIRSHPTTAPTETNIPQRPTPEGVPAPAPTPVPATPTTSGHWETQEEDKDTAEDSSTADRWDDEDWGSLEQEAESVLAQQDDWSTGGQVSRASQVSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDGTRLASEYNWGGPESSDKGDPFATLSARPSTQPRPDSWGEDNWEGLETDSRKCFPWVG
The following text describes a protein:
Function:
Pectin methylesterase (PME) inhibitor involved in the maintenance of cell wall integrity in response to necrotrophic pathogens. Modulates PME activity and pectin methylesterification during infection by Botrytis cinerea and contributes to resistance against the pathogen.
Subcellular Localization:
Secreted, extracellular space, apoplast.
Sequence:
MAKQIFYTLFLFLLSTAILTASSSAPRAAITSKRAINFIQASCKATTYPTVCVNSLTGYANSIQTSPRRLAETALNVTVTQAQSTKVFVWRLGRFTSLKKREIQAVKDCIEEIHDAVDRLTMSIHEVKMCGSAKGRDQFWFHMSNAQTWTSAALTNANTCSDGFAGRVMDGRVKNSVRARILNLGRGTSNALALINAFAKKY
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MPKMSLSCALKASPIFFLLLISTLVSAKSKDVTELQIGVKHKPDSCDIQARKGDRIKVHYRGTLTDGTVFDSSFERDSPIEFELGTGQVIKGWDQGLLGACVGEKRKLKIPSKLGYGDQGSPPTIPGGATLIFETEVVAVNGKTSSEGKTKDAEL
The following text describes a protein:
Function:
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAQESSMFRGHPTVGRVLCCKCGIPIVPNAASMCVKCLSSEVDITEATQSLDPSPIGVDTALDLMLDDAEELELRLIHAEFVWTEPHSKRIKVKLRVQKEVLNGAILEQVYIVEYVQKEHMCESCCRAQGNPDQWVASVQVRQHVPLRRTLFHLEQLILRYFVLPDAILIKKIYVENCQRKGGKPPELSLPATSSGGHFICSSSPSIFFLGSASSPAVSTGSDLSTEQETAAIVRHSPARTQAVGHLHHGSVEATLQRPLTPRSCRSHYDDLKRRFQRIVGGDGGGAVVSFLFSFYALLRIGLASSFLMPLLCGSCIFFSDSIPHVENNHRSQLQKIKIQFTNCLEILRERRIVSSSAIASDDALNRRLKSS
The following text describes a protein:
Function:
Apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors. Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis (By similarity). Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation (By similarity). Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner (By similarity). Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I. Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia. Inhibits too myoblast differentiation through caspase inhibition (By similarity).
Subcellular Localization:
Cytoplasm. Mitochondrion. Sarcoplasmic reticulum. Membrane; Lipid-anchor. Note=Phosphorylation at Thr-149 results in translocation to mitochondria. Colocalized with mitochondria in response to oxidative stress.
Domain:
CARD is critical for both extrinsic and intrinsic apoptotic pathways (By similarity). CARD domain mediates a protective effect against myocardial ischemia/reperfusion, oxidative stress and TNF-induced necrosis. The C-terminal domain (amino acids 99 to 220) is involved in calcium binding and plays a protective role in calcium-mediated cell death (By similarity).
Sequence:
MGNVQERPSETIDRERKRLVETLQADSGLLLDALVARGVLTGPEYEALDALPDAERRVRRLLLLVQSKGEAACQELLRCAQQTVRMPDPAWDWQHVGPGYRNRSYDPSCPGHWTPEAPSSGTTCPELPRASEQEEVGGPEGSEALQPRTPEEPELEAEATEGDEPDLEQEMNPEQEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPDFQEEDESEDS
The following text describes a protein:
Function:
Catalyzes the production of 7-dehydrocholesterol (7-DHC or cholesta-5,7-dien-3beta-ol) by inserting a double bond (desaturating) at the C7-C8 single bond of cholesterol. Essential regulator of steroid biosynthesis, as this reaction is the first step in the synthesis of the steroid hormone Delta(7)-dafachronic acid. Required for insect molting, metamorphosis and body growth throughout development via the regulation of ecdysteroid biosynthesis in the prothoracic gland.
Miscellaneous:
MISCELLANEOUS: Nvd_Dm plays a pivotal role in larval development in Drosophila. On this basis of the prolonged first instar larval phenotype, the gene was named 'neverland', which is the fictional island featured in J. M. Barrie's play Peter Pan, where children cease to age.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MTSYSLFWMSLLKNNWKPISNDFVICLWTLAVTFIRIYWIFFVPLEWKKDLDNEKWSFLRKTENVVCYNHKRDTINRLRKLKIQKIIELPPPYPNGWYGILKSSQLKAGEATCVSCLGEDLVIFRSKKDIVFILDAYCPHLGANLGIGGSVADDCVICPFHQWKFRGTDGLCINIPYSTSVPKGSKLKKWISQEVDGFIFIWYHAEQTELPWDLPVPMGEIDDTFVYHGHNEFYINCHIQEIPENGADIAHFNAIHKKNFINGSWAQKKRLFGLGSHHWKARWSPFTGKLKYLAEVNLSHTFKLFGKFGCFRMEVSGKQIGPSIVCLEVNSYTFGKIKVFQYITPIEPMLQKVVHEFYGPRWIAPLMKIFIYGESLMFERDIKIWNHKVFNRNPILAKEDASIKKFRLWFSQFYSSNSKIYSEATNIGW
The following text describes a protein:
Function:
Involved in pheromone-induced morphogenesis and efficient mating, perhaps as a cytoskeletal protein.
Miscellaneous:
MISCELLANEOUS: Present with 274 molecules/cell in log phase SD medium.
Subcellular Localization:
Cell tip. Note=Localizes to a sharp patch at the shmoo tip (mating projection) which corresponds to the site of polarized cell growth.
Sequence:
MGTSSEVSLAHHRDIFHYYVSLKTFFEVTGENRDRSNSTRAQKARAKLLKLSSSQFYELSTDVSDELQRRIGEDANQPDYLLPKANFHMKRNQARQKLANLSQTRFNDLLDDILFEIKRRGFDKDLDAPRPPLPQPMKQEVSKDSDDTARTSTNSSSVTQVAPNVSVQPSLVIPKMASIDWSSEEEEEEQVKEKPNEPEGKQTSMDEKKEAKPALNPIVTDSDLPDSQVLARDITSMARTPTTTHKNYWDVNDSPIIKVDKDIDNEKGPEQLKSPEVQRAENNNPNSEMEDKVKELTDLNSDLHLQIEDLNAKLASLTSEKEKEKKEEKEEKEKEKNLKINYTIDESFQKELLSLNSQIGELSIENENLKQKISEFELHQKKNDNHNDLKITDGFISKYSSADGLIPAQYILNANNLIIQFTTRLSAVPIGDSTAISHQIGEELFQILSQLSNLISQLLLSADLLQYKDQVILLKASLSHAITSIRYFSVYGPVLIPKITVQAAVSEVCFAMCNLIDSAKIKSDSNGESTTSNEGNRQVLEYSSPTATTPMTPTFPSTSGINMKKGFINPRKPASFLNDVEEEESPVKPLKITQKAINSPIIRPSSSNGVPTTSRKPSGTGLFSLMIDSSIAKNSSHKEDNDKYVSPIKAVTSASNSASSNISEIPKLTLPPQAKIGTVIPPSENQVPNIKIENTEEDNKRSDITNEISVKPTSSIADKLKQFEQSSEKKSSPKENPIAKEEMDSKPKLSNKFITSMNDVSTDDSSSDGNENDDADDDDDFTYMALKQTMKREGSKIEKNNDSKLPANIVELDLHESPESVKIESPESIKEITSSEMSSEMPSSSLPKRLVEDVEPSEMPEKGASVESVRKKNFQEPLGNVESPDMTQKVKSLGMTGKAVGPESDSRVESPGMTGQIKSLNMAGKVVGPEADSRVESPGMKEQIKSLGMTGKITAQESIKSPEAARKLASSGEVDKIESPRMVRESESLEAVGNTIPSNMTVKMESPNLKGNTVSEPQEIRRDIASSEPIENVDPPKVLKKIVFPKAVNRTGSPKSVEKTPSSATLKKSGLPEPNSQIVSPELAKNSPLAPIKKNVELRETNKPHTETITSVEPTNKDANTSWRDADLNRTIKREEEDEDFDRVNHNIQITGAYTKTGKIDYHKIPVDRKAKSEAEVHTSEEDIDESNNVNGKRADAQIHITERKHAFVNPTENSQVKKTSHSPFLNSKPVQYENSESNGGINNHIKIKNTGETTAHDEKHYSDDDDSSYQFVPMKHEEQEQEQNRSEEEESEDDDEEEEDSDFDVDTFDIENPDNTLSELLLYLEHQTMDVISTIQSLLTSIKKPQVTKGNLRGESNAINQVIGQMVDATSISMEQSRNANLKKHGDWVVQSLRDCSRRMTILCQLTGDGILAKEKSDQDYADKNFKQRLAGIAFDVAKCTKELVKTVEEASLKDEINYLNSKLK
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIIAILLFTTVFAFPKYKQNIFVTKPDSLKKLAYQLSIASDLQVDVDQDQVCTWLKEYTLTTAQDAYYAKLASSFLDECQADYNIDFPKIDSDDFESIYYNSLFNGLCPKLDQFITAGGAAKPQLKKQDDSYRTAAQAYHLATFCNHSKVHQAIQEAIFNFQEIYEGVSAVLDRDNSATATAQILFSFFTFNITNLHPKLQDLLQNQIYQQTIINFLYQRTQVLGSIEEQYWITKLFQLDQVNSIIYPIFQDHYQLNKGKTQINVKFVNFRGEKIQPTEVYALINNQKEHYTYTPIKSKEFSGYFEISAVGSVPFELHFPHYILKYTIKVLQEVEIEEVIFDIVDSKTSKPNFHHSVENGEVYPVILSANEKCFLHVIIKVRILFQQTKNQIKQQVAIRLIHPQYSSASTQVFAEYDKKKKIYYGIIDFGDPDHITPLNAIYSVELLIADSNVVPKRLSFVKIDTKFQAQTTFQNDSTYKLPQEIVHQFNQEQPEVPFFFVSFFVMIILIAFLFFLSIISNLNLSFERLPKDNSTIVYLFLALIIGLFFVLTLFWIKLNLIETIAVLGILSVPQVVVGNYALLALRKSEKLD
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MGGDVKAHGDHAVHGIPKIPDYRIYKVEDVPRLVRAQKLLAAKGLRDPWLRNEVWKFCLEKESTTMQRFWRFWRRGMMPGLALAVAAVGLEQAWKFASGGDIKHHGEHH
The following text describes a protein:
Function:
Cysteine protease inhibitor that likely functions in defense against insects by inhibiting cysteine proteases in the midgut of herbivore insects such as C.maculatus. Selectively inhibits cathepsin L, as well as papain, ficin and bromelain with lower efficiency. Shows antitumor activity, inhibiting the growth of prostate cancer cell lines PC3 and DU145, and the gastric cancer cell line Hs746T. No activity against cathepsin B or serine proteases (trypsin, human plasma kallikrein and elastase).
Sequence:
ERRCDPRRLSDCEDFVRGRSKGGRGEKECRLSERCCTELQKMPRECRCEAVEGMYKEAERKERGEGEQRQRLERARALPGLCSIEPSYCEIRPS
The following text describes a protein:
Function:
A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Subcellular Localization:
Cell junction, desmosome. Cell membrane; Single-pass type I membrane protein.
Sequence:
MDWLFFRNICLLIILMVVMEVNSEFIVEVKEFDIENGTTKWQTVRRQKREWIKFAAACREGEDNSKRNPIAKIRSDCELNQKITYRISGVGIDRPPYGVFTINPRTGEINITSVVDREITPLFLIYCRALNSRGEDLERPLELRVKVMDINDNAPVFSQSVYTASIEENSDANTLVVKLCATDADEENHLNSKIAYKIVSQEPSGAPMFILNRYTGEVCTMSSFLDREQHSMYNLVVRGSDRDGAADGLSSECDCRIKVLDVNDNFPTLEKTSYSASIEENCLSSELIRLQAIDLDEEGTDNWLAQYLILSGNDGNWFDIQTDPQTNEGILKVVKMLDYEQAPNIQLSIGVKNQADFHYSVASQFQMHPTPVRIKVVNVREGPAFHPSTMAFSVREGIKGSSLLNYVLGTYTALDLDTGNPATDVRYIIGHDAGSWLKIDSRTGEIQFSREFDKKSKYIINGIYTAEILAIDDGSGKTATGTICIEVPDINDYCPNIFPERRTICIDSPSVLISVNEHSYGSPFTFCVVDEPPGTADMWDVRSTNATSAILMAKQVLSPGFYEIPILVKDSYNRACELAQMVQLYACDCDDNHMCLDSGAVGIYTEDITGDTYGPVTEDQAGVSNVGLGPAGIGMMVLGILLLLLAPLLLLLCCCKQRQPEGLGTRFAPVPEGGEGVMQSWRIEGAHPEDRDVSNICAPMTASNTQDRMDSSEIYTNTYAAGGTVEGGVSGVELNTGMGTAVGLMATGAAGASGAARKRSSTMGTLRDYADADINMAFLDSYFSEKAYAYADEDEGRPANDCLLIYDHEGVGSPVGSIGCCSWIVDDLDESCMETLDPKFRTLAEICLNTEIEPFPSHQACIPISTDLPLLGPNYFVNESSGLTPSEVEFQEEMAASEPVVHGDIIVTETYGNADQCVQPTTIIFDPQLAPNVVVAEAVMAPVYDIQGNICVPAELADYNNVIYAERVLASPGVPDMSNSSTTDGCMGPVMSGNILVGPEIQVMQMMSPDLPISQTVGSTSPMTSRHRVTRYSNIHYTQQ