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stringlengths 6
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Q9A716 | MRKLGLIAGGGALPVELASHCEAAGRAFAVMRLRSFADPSLDRYPGADVGIGEFGKIFKALRAEGCDVVCFAGNVSRPDFSALMPDARGLKVLPSLIVAARKGDDALLRRVLDEFEKEGFEIEGAHEVMGEMTLPRGRLGKVSPAPEHMADIDKALDVAREIGRLDIGQGAVVCEGLVLAVEAQEGTDAMLRRVADLPEAIRGRAERRLGVLAKAPKPIQETRVDLPTIGVATIHRAARAGLAGIVGEAGRLLVVDREAVIAAADDLGLFVLGVDPQERP | Cofactor: To a lesser extent, can also use Mn(2+) or Co(2+).
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to form 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the beta-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Can functionally complement lpxH deficiency in E.coli. Cannot use CDP-diacylglycerol as substrate.
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29634
Sequence Length: 280
Domain: Consists of two domains: an N-terminal lipid X binding domain (LXD) attached by a flexible linker to a C-terminal catalytic domain (ICD). Binding of UDP-2,3-diacylglucosamine by LpxI induces a conformational switch that brings the catalytic domain close to the lipid-binding domain for specific recognition of the substrate and catalysis.
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular Location: Cell inner membrane
EC: 3.6.1.54
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B7J512 | MTLRQTLEQQWQDGGALATALRPLGALTGKVARWRRRHIQGRAASIPTIVVGNLGVGGSGKTPLVAALARQLTVAGWRVAIVSRGYGARPPHWPYRVQRDDSPQQAGDEPLLLAQEQGQTQAVYLCPDRHRAIAAAAADGYNLALLDDGFQHLALQPSLRLLVLSGPRPLGNGHCLPAGPLRECPDAMLHADALLMDAAAAAAIPERNGPPRFLFRIQPKDLVAVNDPCRSRSLDSLQGQHVTAVTGIARPQRFVASLEGLGAIPDPRFFPDHHSFCASDIAHLPRPLVMTAKDAVKCREFAQADDWTLRIEAELEASSQPWLEQSLLPWRS | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36036
Sequence Length: 332
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q8UHI5 | MVSEAPPFWWQKAGWQAWLLSPFSLLYGKVAGRRMRTAKRANVPVPVICIGNFTVGGAGKTPTAIAIARAAVARGMKPGFLSRGYGGTLDVTTLVDAQHHRAAAVGDEPLLLAREAVTVISRRRVEGAHRLVKEGVNLIIMDDGFQSARLTLDYALVVIDTVRGIGNGHLVPGGPVRAPLAEQMRQMTGLLKVGKGHAADPLVRQAAKAAKPVFVAAIMPQEPEDFRGKRVLAFAGIADPAKFYRTVEALGGDIVLSRSFPDHHHFSDDEIDDLLKDARKENLQLVTTAKDAVRLNGHHGRAEELLWNSQVIEIDMVFDDPNAAGTVIETAVVNCRARLLRDNARSST | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 37690
Sequence Length: 348
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q9PPA9 | MNEEKNYELWLDNYFFKPNFWQKCLAFILLPLSVLYAFFAILNTFFRKKIVFKKPVISVGNLSFGGNGKTPLCKAIAREFDGVFIVLRGYKRKSKGLFVVKNQNEILCTLTQSGDEAMEYAFEENIKGVIVSEDRVKGIEKAFELGAKIVVLDDAFSKFHIKKFDILLESKIKPYFNFTLPSGAYRLPKFYEKRADFIALEGRDFVRYSFVKENPKAVLVTAIAKPFRLYEHFIKARACYFFKDHYEFKKEELENLLKKHNCDTLMLTFKDFVKVKDFGFKCQIIELNIELKDSLREKIKTYIKEFEQ | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36228
Sequence Length: 308
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
|
P58184 | MKLGTPRWWYVKSGAPAPVTRALLTPLSWLWADTTRRRIARATPAIVGAPVICVGNVTMGGAGKTPIVRELLLTLTQRGVAAHGLSRGYGGKLKGPVRVDTIRHTAADVGDEPLMLAQDFPMWIAADRVAGAKAAVRAGASAIVMDDGHQNPSVKKALSLVVVDGETRGGEWPFGDGRVFPAGPMREPLKVGLSRADAVIVLLPVDVEQPDFDLLVAFGDMPVLVARLEAAAPVPKGPQVGFAGIAKPWKVEKALTAAGCQLVDFAPFPDHGAYSESTLKMLADRAEVYEAGLVTTEKDWVRLPPAWRERVTPWPVRARFEDPAALEALLKGIGL | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35775
Sequence Length: 335
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
|
Q3J6I0 | MRPPAFWFTPPDSPALAARLLAPLGQAYAAATARRLRAPGHRAGVPVICIGNLNAGGTGKTPTAIALMQRLAARGIEAHVVSRGYGGRLEGPVEVDARRHRAADVGDEPLLLAAFGRAWVARDRAAGVRAAEAAGAQAILLDDGFQNPSVVKDLSLIVVDAAVGFGNGRCLPAGPLREPVEAGLARADLLLSIGGPEAQRRFATDWPALPVPRLTGRLATLQMGMDWQGARVLAFAGIGRPEKFFASLRAEGAELLRAEALDDHQPLGEALMKRLEIEAMALGAQLVTTEKDAVRLPPSFRQKVLTLPVRLEFDDATALDAALDRLGLAARS | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35058
Sequence Length: 332
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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B3EG23 | MSNPLSPLLKPAAALYRTVVRMRNLGFEKKLFKTWKAPLPVVSIGNISAGGTGKTPLADWIINYCLSVGSEPALLSRGYGRTTKGVQLVSDGQRILLDSREAGDETSMLAARNPGIIVVVAEKRKEGVEFILKRFGTRMPSLIILDDAFQHRQIARDLDIVIINAAEPYCNARMLPEGRLREPLGNIRRAGLIVLNKITDRNAADAIACDLKKTGIPVVLAKTEAGELVPFGEDAGERNMNGIRAFAFAGIGSPEGFLGSLKEKGIQVEAHRFFRDHEPYSGDKLLPILLEAEKKGLSLVTTEKDYFRLLGEHELTATLSVLPCYYLKISTRFLEGEEILASMLNKVIFS | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 38464
Sequence Length: 350
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q9ZCL0 | MIKLLYPQFWQERNIIAYLLLPISLIYQFLSYLRASLAYPVILPAQVICVGNCSVGGTGKTQIVIYLAKLLKAKNVPFVIITKAYGSHIKSTTIIQKGHTALEVGDEGIMLARYGTVIAAKYVKDILPLINELKPDVIIVDDFLQNPYLHKDFTIVSVDSQRLFGNRFLIPAGPLRQNPKQVLDAADLIFLVSSNQDQIPNELTPYIDKLINAQIVPSNNIDKNKNYFAFSGIGNPQRFFLTLENYRLNIVGYKIFPDHYNYLQADLENLYSLAKEHNAILITTRKDYVKFNYLNDEIICLDVELSINNPDLLNEKIFKKAKILN | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36971
Sequence Length: 325
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
|
A1AXA3 | MNLNIRGIINYSLLPISGIFYLVSVFRKWLYRVNFFKVQKFKYPVIVVGNITVGGTGKTPIVIALAQYFKQQGKQVGIVSRGYGGAHHQGSLLVNKDTNVYLSGDEPLLIALQTDLPVMINKNRAKAVKDLINQCQVDLIISDDGLQHYKMDRDVEIVVIDGIKRFGNGFFLPLGPLRESITRLKSVDFVINNAGLCAGEFSVKLTLKMFVNVKTGEEKSLNYFKGKYCHGVAGIGHPERFFNALIRLGINLEHHIFADHYIYQQSDLVFEDNHPILMTAKDCVKCTQFENDQMWYLQVEADLSDDFLKKLDAKL | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35640
Sequence Length: 315
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q21J10 | MSAALAKAIERRWYSRPGILWLLYPLALLFRLLSYFRRRSQTQSSVKFAVPVCIVGNIAIGGTGKTPTIIALVHALAEQGITAGVVARGYGASLAKDEVRVLDANATAAMVGDEPLLIYKRTGCVVAVGSNRVAACETLLKSHAVDVILSDDGMQHYKLGRDLELALVDGERVFGNGQLLPVGPLREHPKRLQSVNWLLVNGGSAEHVNARLQALEAINAAELSSKPNKLNKTPAPVFAQLEAVKLVNLATGKTLLLQNITELGAFVAVAGIGNPARFFKTLQSTGITGFDTFSYPDHHKFTSADFRQFDNKAIVMTEKDAVKCTPFATDAMWYVPVDLKLPQTFIADFCAQIRKVIALYN | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 39190
Sequence Length: 361
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q8BZT5 | MKVTRFMFWLFSMLLPSVKSQASETEVPCNFSRRNYTLIPEGISTNVTILDLSYNRITLNAADSRVLQMYSLLTELYLMENNIIALYNSSFRNLLNLEILNICGNSISVIQQGSFVGLNELKQLFLCQNKILQLNPDTFVPLNNLKVLNLQGNLIRLFDAPQLPHLEILTLDGNPWNCTCGLLELHNWLNTSNVTLENENMTMCSYPDELKHDSIKSAPFTTECHSTFISTITEDFQSTRNSSFNSSSHNLTWTSEHEPLGKSWAFLVGVVATVLLTSLLIFIAIKCPVWYNILLSYNHHRLEEHEAETYENGLTRNPSSLSQITDTNSEDTTVIFEQLHAFVVDDDGFIEDRYIDINEVHEEK | Function: Pathogen-recognition receptor which mediates the activation of TRAF2- and TRAF6 NF-kappa-B signaling pathways and induces the expression of pro-inflammatory cytokines . In kidney, prevents infection by uropathogenic bacteria by inducing the production of cytokines, chemokines and antimicrobial substances . In gut, involved in host-microbiota interactions, plays a critical role in promoting the recruitment of immune cells and intestinal inflammation .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41573
Sequence Length: 364
Subcellular Location: Membrane
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Q8MII8 | MGGPLMWALLLPLLLHQAGSQTSSCSVLSGYMDWTKEYFDTCLNFSGKILTQLPQNQSLRARSVQLLDLSANGLQRLPWSFFRDLEQLQLLIVTNNSLDFVDRALXXXGCGLELLADCSCALLDWHTDRQDNCSGPELPRCLDVPTGAWHNLSVFLDVSCPSGLTKIAIGALAASGSLLLVLAIAGPVLAWRFCRHRMDQNLSKTWASQDGSRSGSGRQPRYSSQGRRPKSPANTPPRSSTPDYENVFVGPPAARHQWDELRSPPSEGGDFYMTYDSLQHESQPVYCNLQSLSQVPLDDEEYVVPGR | Function: Plays a role in the inhibition of RLR-mediated type I interferon signaling pathway by targeting RIGI for autophagic degradation. Interacts specifically with ISG15-associated RIGI to promote interaction between RIGI and the autophagic cargo receptor p62/SQSTM1 to mediate RIGI degradation via selective autophagy. Plays also a role in the inhibition of NF-kappa-B signaling pathway and inflammatory response by promoting the degradation of p65/RELA.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 33934
Sequence Length: 307
Subcellular Location: Membrane
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Q8N386 | MGGTLAWTLLLPLLLRESDSLEPSCTVSSADVDWNAEFSATCLNFSGLSLSLPHNQSLRASNVILLDLSGNGLRELPVTFFAHLQKLEVLNVLRNPLSRVDGALAARCDLDLQADCNCALESWHDIRRDNCSGQKPLLCWDTTSSQHNLSAFLEVSCAPGLASATIGAVVVSGCLLLGLAIAGPVLAWRLWRCRVARSRELNKPWAAQDGPKPGLGLQPRYGSRSAPKPQVAVPSCPSTPDYENMFVGQPAAEHQWDEQGAHPSEDNDFYINYKDIDLASQPVYCNLQSLGQAPMDEEEYVIPGH | Function: Plays a role in the inhibition of RLR-mediated type I interferon signaling pathway by targeting RIGI for autophagic degradation. Interacts specifically with ISG15-associated RIGI to promote interaction between RIGI and the autophagic cargo receptor p62/SQSTM1 to mediate RIGI degradation via selective autophagy . Also plays a role in the inhibition of NF-kappa-B signaling pathway and inflammatory response by promoting the degradation of p65/RELA.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 33179
Sequence Length: 305
Subcellular Location: Membrane
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Q2I0M4 | MRGPSWSRPRPLLLLLLLLSPWPVWAQVSATASPSGSLGAPDCPEVCTCVPGGLASCSALSLPAVPPGLSLRLRALLLDHNRVRALPPGAFAGAGALQRLDLRENGLHSVHVRAFWGLGALQLLDLSANQLEALAPGTFAPLRALRNLSLAGNRLARLEPAALGALPLLRSLSLQDNELAALAPGLLGRLPALDALHLRGNPWGCGCALRPLCAWLRRHPLPASEAETVLCVWPGRLTLSPLTAFSDAAFSHCAQPLALRDLAVVYTLGPASFLVSLASCLALGSGLTACRARRRRLRTAALRPPRPPDPNPDPDPHGCASPADPGSPAAAAQA | Function: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Required for the conversion of BK alpha channels from a high-voltage to a low-voltage activated channel type in non-excitable cells. These are characterized by negative membrane voltages and constant low levels of calcium.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 34857
Sequence Length: 334
Domain: The transmembrane domain is necessary for interaction with KCNMA1.
Subcellular Location: Cell membrane
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Q91W20 | MRGSFFSRLPPQLSLLLLLSLRRVWTQEDIGTAPSKSPVAPECPEACSCSLGGKANCSALALPAVPADLSWQVRSLLLDHNRVSALPPGAFANAGALLYLDLRENRLRSVHARAFWGLGVLQWLDLSSNQLETLPPGTFAPLRALSFLSLAGNRLALLEPSILGPLPLLRVLSLQDNSLSAIEAGLLNNLPALDVLRLHGNPWTCNCALRPLCTWLRKHPRPASETETLLCVSPRLQTLSLLTAFPDAAFKQCTQSLAARDLAVVYALGPVSFLASLAICLALGSVLTACGARRRRRRRTTVRHLLRRQLDPEGPPSLEDAGSPVTAAIQA | Function: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Required for the conversion of BK alpha channels from a high-voltage to a low-voltage activated channel type in non-excitable cells. These are characterized by negative membrane voltages and constant low levels of calcium (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35696
Sequence Length: 331
Domain: The transmembrane domain is necessary for interaction with KCNMA1.
Subcellular Location: Cell membrane
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Q9JMH2 | MWVALGMLWLLALGGPHQAWSFCPSQCSCSLHILSDGSKARTVVCSDPDLTLPPASIPPDTCKLRLERTAIRRVPGETFRPLSRLEQLWLPYNALSELSTLMLRGLRRLRELRLPGNHLVTFPWAALKDTPQLQLLDLQANRLSTLPPEAVHFLENLTFLDLSNNQLMRLPEELLDTWAHLKTGPYLSSRRTRLVLGLQDNPWVCDCRLYDLVHLLDGWASNLIFIEARLRCGSPRSLAGVAFSQLELRKCQSPELRPGVTSIISPLGSTVLLRCGATGIPGPEMSWRRANGRPLNGTVHQEVSSDGSSWTLLDLPVVSLFDSGDYICQAKNFLGASETLISLIVTEPQTSTEYTGIPGALWARTGEGAEAAAYNNKLVARHVPHVPEPVALATKPSVPSIKEELPLQNFQMDVPGEFSREPSEHQETQMVRSLKVVGDTYHSVSLVWKAPQAGNTTAFSVLYAVFGQRDMRRMTVEAGKTSVTIEGLAPKTKYVACVCVRGLVPTKEQCVIFSTDEVVDAEGTQRLINMVVISVAAIIALPPTLLVCCGALRRRCHKCRAGGSAEASGAYVNLERLGHSEDGSEELSRSSLSEADRLLSARSSLDSQVLGVRGGRRINEYFC | Function: Possible role in phototransduction.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68417
Sequence Length: 623
Subcellular Location: Endoplasmic reticulum membrane
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Q3SXY7 | MHLFACLCIVLSFLEGVGCLCPSQCTCDYHGRNDGSGSRLVLCNDMDMNELPTNLPVDTVKLRIEKTVIRRISAEAFYYLVELQYLWVTYNSVASIDPSSFYNLKQLHELRLDGNSLAAFPWASLLDMPLLRTLDLHNNKITSVPNEALRYLKNLAYLDLSSNRLTTLPPDFLESWTHLVSTPSGVLDLSPSRIILGLQDNPWFCDCHISKMIELSKVVDPAIVLLDPLMTCSEPERLTGILFQRAELEHCLKPSVMTSATKIMSALGSNVLLRCDATGFPTPQITWTRSDSSPVNYTVIQESPEEGVRWSIMSLTGISSKDAGDYKCKAKNLAGMSEAVVTVTVLGITTTPIPPDTSERTGDHPEWDVQPGSGRSTSVSSASSYLWSSSFSPTSSFSASTLSPPSTASFSLSPFSSSTVSSTTTLSTSISASTTMANKRSFQLHQGGKRNLKVAKNGSKLPPASTSKKEELALLDQTMLTETNAAIENLRVVSETKESVTLTWNMINTTHNSAVTVLYSKYGGKDLLLLNADSSKNQVTIDGLEPGGQYMACVCPKGVPPQKDQCITFSTERVEGDDSQWSLLLVVTSTACVVILPLICFLLYKVCKLQCKSEPFWEDDLAKETYIQFETLFPRSQSVGELWTRSHRDDSEKLLLCSRSSVESQVTFKSEGSRPEYYC | Function: Plays a role in the synapse formation and synaptic transmission between cone photoreceptor cells and retinal bipolar cells (By similarity). Required for normal transmission of a light-evoked stimulus from the cone photoreceptor cells to the ON-bipolar cells and ON-ganglion cells in the inner retina . Required in retinal ON-bipolar cells for normal localization of the cation channel TRPM1 at dendrite tips (By similarity). Seems to play a specific role in synaptic contacts made by ON-bipolar cells with cone photoreceptor pedicles (By similarity). May also have a role in cone synapse formation (By similarity). Might facilitate FGFR1 exit from the endoplasmic reticulum to the Golgi . Could be a regulator of the FGFRs .
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 74754
Sequence Length: 679
Subcellular Location: Cell projection
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P93604 | MSKLLVIALLLLPLINHGIYLATAWDDQDFFKYCPPSKCSQHGPMIRYPLCLESSNTSSSSSCGCAGRSIWKLACSGQDTILVHPVLGPYSVSAIDYRRSSMKITPLVDPCLVLQQKLIISRSSSSPQVDVINDEKPSFDENFFESSSATIVHCSREFTPAAAHADSIAGPVSCLSNTTHFFYLVNSDEDMSILPLDCKVVPVSDRGGISLPHMLKDQMFYNFTETAKKIPSFAETAVSWDEGDCRECELSGRRCAFSSQRDREFCMPDPHGSHIKVIAATSSVAAFVALLLTVATVLYLSLKTRYNAEIHMKVEMFLKTYGTSKPTRYTFSEVKKMARRFKEKVGQGGFGSVYKGELPNGVPVAVKMLENSTGEGESFINEVATIGLIHHANIVRLLGFCSEGMRRALIYEFMPNESLEKYIFSDDSNIFQNLLVPEKLLDIALGIARGMEYLHQGCNQRILHFDIKPHNILLDYNFNPKISDFGLAKLCARDQSIVTLTAARGTMGYIAPELYSRNFGGVSYKADVYSFGMLVLEMVSGRRNSDPRIGSQDDVYLPEWIYEKVINGEELALTLETTQEEKDKVRQLAMVALWCIQWNPRNRPSMTKVVNMLTGRLQSLQMPPKPFVSSENELMS | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 71023
Sequence Length: 636
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9M3D8 | MACRLYLALIFSCVYLICLSSQQETGFVYNGFEQADLFIDGIAKILPDGLLQLTNTTELQMGHAFFKKPFDFDPSSSLSFYTHFVCALVPPKLGADGGHGIVFVVSPSIDLSHAYATQYLGVFSNLTNGTSSSHLLAIELDTVKTVEFNELEKPHVGIDLNSPISVESALPSYFSNALGKNISINLLSGEPIQVWVDYDGSFLNVTLAPIEIKKPNQPLISRAINLSEIFQEKMYVGFSSSTGNLLSNHYILGWSFSRRKEQLQSLNLSTLPRVPLPKEEKKKLSPLLIGLVILLVIPVVMVLGGVYWYRRKKYAEVKEWWEKEYGPHRFSYKSLYKATNGFRKDCRVGKGGFGEVYKGTLPGGRHIAVKRLSHDAEQGMKQFVAEVVTMGNLQHRNLVPLLGYCRRKCELLLVSEYMPNGSLDQYLFHEGNPSPSWYQRISILKDIASALSYLHTGTKQVVLHRDIKASNVMLDSEFNGRLGDFGMAKFHDRGTNLSATAAVGTIGYMAPELITMGTSMKTDVYAFGAFLLEVICGRRPVEPELPVGKQYLVKWVYECWKEACLFKTRDPRLGVEFLPEEVEMVLKLGLLCTNAMPESRPAMEQVVQYLNQDLPLPIFSPSTPGIGAFMPVSMEALSAIGVSSVRNSSVSMFVTHTILDGHGR | Function: Involved in resistance response to the pathogenic fungus Alternaria brassicicola.
PTM: Autophosphorylated on Ser and Thr residues.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 73910
Sequence Length: 664
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9LSS0 | MIRGLLLGIIWMIFCVCSSFQQETPFVYNNFGHVDHLHLDGSARIIPSGGILQLTNATNSQIGHVFYEKPIEFKSSESVSFSTYFVCALLPAGDPSGHGMTFFVSHSTDFKGAEATRYFGIFNRNGSTSTRVLAVELDTSLASDVKDISDNHVGIDVNSAESITSANASYFSDKEGKKIDIKLLSGDPIQVWVDYEGTTLNVSLAPLRNKKPSRPLLSSTSINLTDILQGRRMFVGFSGSTGSSMSYQYILGWSFSKSMASLPNIDISKLPKVPHSSTKKKSTSPVLSVLLGLIAFIVLGILVVAYLYRRNLYSEVREEWEKEYGPIRYSYKSLYKATKGFNRSEFLGRGGFGEVYKGTLPRSRELREVAVKRVSHDGEHGMKQFVAEIVSMRSLKHRSLVPLLGYCRRKHELLLVSEYMPNGSLDHYLFNHDRLSLPWWRRLAILRDIASALSYLHTEADQVVIHRDIKAANVMLDAEFNGRLGDFGMSRLYDRGADPSTTAAVGTVGYMAPELTTMGASTGTDVYAFGVFLLEVTCGRRPVEPGLPEAKRFLIKWVSECWKRSSLIDARDPRLTEFSSQEVEKVLKLGLLCANLAPDSRPAMEQVVQYLNGNLALPEFWPNSPGIGVLSPMALSPAPLVIPSLSFSSSSSNNSMFITHSVLYGSGR | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 73955
Sequence Length: 668
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9M021 | MGTQRSMFIVSFLFKLFLFLSVHVRAQRTTTNFAFRGFNGNQSKIRIEGAAMIKPDGLLRLTDRKSNVTGTAFYHKPVRLLNRNSTNVTIRSFSTSFVFVIIPSSSSNKGFGFTFTLSPTPYRLNAGSAQYLGVFNKENNGDPRNHVFAVEFDTVQGSRDDNTDRIGNDIGLNYNSRTSDLQEPVVYYNNDDHNKKEDFQLESGNPIQALLEYDGATQMLNVTVYPARLGFKPTKPLISQHVPKLLEIVQEEMYVGFTASTGKGQSSAHYVMGWSFSSGGERPIADVLILSELPPPPPNKAKKEGLNSQVIVMIVALSAVMLVMLVLLFFFVMYKKRLGQEETLEDWEIDHPRRLRYRDLYVATDGFKKTGIIGTGGFGTVFKGKLPNSDPIAVKKIIPSSRQGVREFVAEIESLGKLRHKNLVNLQGWCKHKNDLLLIYDYIPNGSLDSLLYTVPRRSGAVLSWNARFQIAKGIASGLLYLHEEWEKIVIHRDVKPSNVLIDSKMNPRLGDFGLARLYERGTLSETTALVGTIGYMAPELSRNGNPSSASDVFAFGVLLLEIVCGRKPTDSGTFFLVDWVMELHANGEILSAIDPRLGSGYDGGEARLALAVGLLCCHQKPASRPSMRIVLRYLNGEENVPEIDDEWGYSKSSRSEFGSKLVGYVSSTSITRVSSTSRISQ | Function: Involved in negative regulation of abscisic acid response in seed germination.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75868
Sequence Length: 682
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q66GN2 | MGRAKSMVSLLLVLFLVRAHVATTETTTEFIFHGFKGNQSEIHMQGDSTITSNGLLRLTDRNSDVVGTAFYHKPVRLLDSNSTNTTVRSFSTSFIFIIPSSSTSNGGFGFTFTLSPTPNRTDADPEQYMGLLNERNDGNSSNHVFAVEFDTVQGFKDGTNRIGNHIGLNFNSLSSDVQEPVAYFNNNDSQKEEFQLVSGEPIQVFLDYHGPTKTLNLTVYPTRLGYKPRIPLISREVPKLSDIVVDEMFVGFTAATGRHGQSSAHYVMGWSFASGGEHPLAAMLDISQLPPPPPNKAKKRGYNGKVIALIVALSTVISIMLVLLFLFMMYKKRMQQEEILEDWEIDHPHRFRYRDLYKATEGFKENRVVGTGGFGIVYRGNIRSSSDQIAVKKITPNSMQGVREFVAEIESLGRLRHKNLVNLQGWCKHRNDLLLIYDYIPNGSLDSLLYSKPRRSGAVLSWNARFQIAKGIASGLLYLHEEWEQIVIHRDVKPSNVLIDSDMNPRLGDFGLARLYERGSQSCTTVVVGTIGYMAPELARNGNSSSASDVFAFGVLLLEIVSGRKPTDSGTFFIADWVMELQASGEILSAIDPRLGSGYDEGEARLALAVGLLCCHHKPESRPLMRMVLRYLNRDEDVPEIHDNWGYSDSSRTDLGSKLVGYISSDRASSSHSHTSSSLTRISSTSLISGR | Function: Involved in negative regulation of abscisic acid response in seed germination.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76735
Sequence Length: 691
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9S9U1 | MKALLFLLTLFLILPNPISAIDFIFNGFNDSSSNVSLFGIATIESKILTLTNQTSFATGRALYNRTIRTKDPITSSVLPFSTSFIFTMAPYKNTLPGHGIVFLFAPSTGINGSSSAQHLGLFNLTNNGNPSNHIFGVEFDVFANQEFSDIDANHVGIDVNSLHSVYSNTSGYWSDDGVVFKPLKLNDGRNYQVWIDYRDFVVNVTMQVAGKIRPKIPLLSTSLNLSDVVEDEMFVGFTAATGRLVQSHKILAWSFSNSNFSLSNSLITTGLPSFVLPKDSIVKAKWFVFVLVLICFLVVALVGLVLFAVVRKRLERARKRALMEDWEMEYWPHRIPYEEIESGTKGFDEKNVIGIGGNGKVYKGLLQGGVVEVAVKRISQESSDGMREFVAEISSLGRLKHRNLVSLRGWCKKEVGSFMLVYDYMENGSLDRWIFENDEKITTLSCEERIRILKGVASGILYLHEGWESKVLHRDIKASNVLLDRDMIPRLSDFGLARVHGHEQPVRTTRVVGTAGYLAPEVVKTGRASTQTDVFAYGILVLEVMCGRRPIEEGKKPLMDWVWGLMERGEILNGLDPQMMMTQGVTEVIDEAERVLQLGLLCAHPDPAKRPSMRQVVQVFEGDKAEIFEAESSEDVESWMLMKMGSRGSSREFWYGSSSHPTIEQIRLQSLSVSLSSWNSSILEGR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76693
Sequence Length: 686
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
O49445 | MFSKVSILLFSLASLLLFRSTTGIEFIYNSNFTTTNTLLLGNATVKSPPSILTLTNQTTFSIGRGLYPSRINASSSSASPLPFATSFIFSMAPFKHLSPGHGFAFVFLPFSETSAASSSQHLGLFNFTNNGDPNSRIFAVEFDVFANQEFNDINDNHVGVDVNSLTSVASETAGFYGGRDGQRFTELKLNSGENYQAWIEFNGSAINVTMARASSRKPIRPLISIPLNLTGVLLDDMFVGFTASTGQLVQSHRILSWSFSNSNFSIGDALITRNLPSFKLSGDSVLKSKGFIAGVSSGVVLLVSVIGLLCFYVVRRRRQRLEGDVEDWETEYWPHRVQYKDVLEATKGFSDENMIGYGGNSKVYRGVLEGKEVAVKRIMMSPRESVGATSEFLAEVSSLGRLRHKNIVGLKGWSKKGGESLILIYEYMENGSVDKRIFDCNEMLNWEERMRVIRDLASGMLYLHEGWETKVLHRDIKSSNVLLDKDMNARVGDFGLAKLQNTSKEMVSTTHVVGTAGYMAPELVKTGRASAQTDVYSFGVFVLEVVCGRRPIEEGREGIVEWIWGLMEKDKVVDGLDERIKANGVFVVEEVEMALRIGLLCVHPDPRVRPKMRQVVQILEQGRLVEDGGEREISLLERVKSSYLLETGEGSRQQHPTFQDVWNSSSYSNSFQTYDSILHGR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75711
Sequence Length: 681
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9LYX1 | MLKLPPRFFSVYSTLIHILASFLCSSDVRGDFPATRFDLGTLTLSSLKLLGDAHLNNGTIKLTRELSVPTSTAGKALYGKPVKFRHPETKSPASFTTYFSFSVTNLNPSSIGGGLAFVISPDEDYLGSTGGFLGLTEETGSGSGFVAVEFDTLMDVQFKDVNGNHVGLDLNAVVSAAVADLGNVDIDLKSGNAVNSWITYDGSGRVLTVYVSYSNLKPKSPILSVPLDLDRYVSDSMFVGFSGSTQGSTEIHSVDWWSFSSSFEESSESPPPMPNSPPPSSPSSSITPSLSTVRRKTADPSSSCRNKLCKKSPAAVAGVVTAGAFFLALFAGVIIWVYSKKIKYTRKSESLASEIMKSPREFTYKELKLATDCFSSSRVIGNGAFGTVYKGILQDSGEIIAIKRCSHISQGNTEFLSELSLIGTLRHRNLLRLQGYCREKGEILLIYDLMPNGSLDKALYESPTTLPWPHRRKILLGVASALAYLHQECENQIIHRDVKTSNIMLDANFNPKLGDFGLARQTEHDKSPDATAAAGTMGYLAPEYLLTGRATEKTDVFSYGAVVLEVCTGRRPITRPEPEPGLRPGLRSSLVDWVWGLYREGKLLTAVDERLSEFNPEEMSRVMMVGLACSQPDPVTRPTMRSVVQILVGEADVPEVPIAKPSSSMSFSTSELLLTLQDSVSDCNEVLAPISTTSCSSSEHDIFIVGKDRSV | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 77120
Sequence Length: 711
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9LSL5 | MLYFIFCQNLSSSSSMSNSILFLSLFLFLPFVVDSLYFNFTSFRQGDPGDIFYHGDATPDEDGTVNFNNAEQTSQVGWITYSKKVPIWSHKTGKASDFSTSFSFKIDARNLSADGHGICFFLAPMGAQLPAYSVGGFLNLFTRKNNYSSSFPLVHVEFDTFNNPGWDPNDVGSHVGINNNSLVSSNYTSWNASSHSQDICHAKISYDSVTKNLSVTWAYELTATSDPKESSSLSYIIDLAKVLPSDVMFGFIAAAGTNTEEHRLLSWELSSSLDSDKADSRIGLVIGISASGFVFLTFMVITTVVVWSRKQRKKKERDIENMISINKDLEREAGPRKFSYKDLVSATNRFSSHRKLGEGGFGAVYEGNLKEINTMVAVKKLSGDSRQGKNEFLNEVKIISKLRHRNLVQLIGWCNEKNEFLLIYELVPNGSLNSHLFGKRPNLLSWDIRYKIGLGLASALLYLHEEWDQCVLHRDIKASNIMLDSEFNVKLGDFGLARLMNHELGSHTTGLAGTFGYMAPEYVMKGSASKESDIYSFGIVLLEIVTGRKSLERTQEDNSDTESDDEKSLVEKVWELYGKQELITSCVDDKLGEDFDKKEAECLLVLGLWCAHPDKNSRPSIKQGIQVMNFESPLPDLPLKRPVAMYYISTTTSSSSPSVNSNGVSVTFSGIEYGR | Function: Promotes hydrogen peroxide H(2)O(2) production and cell death.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75295
Sequence Length: 675
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9M9E0 | MSWQWRRRQWPSPLLLILIVLHLVSSSSAIDFLYNSFSSVTNRTDVILIEDSRVESTVISLINDSDPLSFGRVFYPQKLTIIPDPTRNPTRLSSFSTSFVFSILPDISTSPGFGLCFVLSNSTSPPNAISSQYFGLFTNATVRFNAPLLAVEFDTGRNSEVNDIDDNHVGIDLNNIESTTSVTAGYYDSVNGSFVRFNMRNGNNVRAWIDFDGPNFQINVSVAPVGVLRPRRPTLTFRDPVIANYVSADMYAGFSASKTNWNEARRILAWSLSDTGALREINTTNLPVFFLENSSSSLSTGAIAGIVIGCVVFVALIGFGGYLIWKKLMREEEEEEIEEWELEFWPHRFSYEELAAATEVFSNDRLLGSGGFGKVYRGILSNNSEIAVKCVNHDSKQGLREFMAEISSMGRLQHKNLVQMRGWCRRKNELMLVYDYMPNGSLNQWIFDNPKEPMPWRRRRQVINDVAEGLNYLHHGWDQVVIHRDIKSSNILLDSEMRGRLGDFGLAKLYEHGGAPNTTRVVGTLGYLAPELASASAPTEASDVYSFGVVVLEVVSGRRPIEYAEEEDMVLVDWVRDLYGGGRVVDAADERVRSECETMEEVELLLKLGLACCHPDPAKRPNMREIVSLLLGSPQEDLLTGLTPAAAAADSTAAHA | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 73146
Sequence Length: 656
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9M2S4 | MSQTFAVILLLLIFLTHLVSSLIQDFSFIGFKKASPNLTLNGVAEIAPTGAIRLTTETQRVIGHAFYSLPIRFKPIGVNRALSFSTSFAIAMVPEFVTLGGHGLAFAITPTPDLRGSLPSQYLGLLNSSRVNFSSHFFAVEFDTVRDLEFEDINDNHVGIDINSMESSISTPAGYFLANSTKKELFLDGGRVIQAWIDYDSNKKRLDVKLSPFSEKPKLSLLSYDVDLSSVLGDEMYVGFSASTGLLASSHYILGWNFNMSGEAFSLSLPSLPRIPSSIKKRKKKRQSLILGVSLLCSLLIFAVLVAASLFVVRKVKDEDRVEEWELDFGPHRFSYRELKKATNGFGDKELLGSGGFGKVYKGKLPGSDEFVAVKRISHESRQGVREFMSEVSSIGHLRHRNLVQLLGWCRRRDDLLLVYDFMPNGSLDMYLFDENPEVILTWKQRFKIIKGVASGLLYLHEGWEQTVIHRDIKAANVLLDSEMNGRVGDFGLAKLYEHGSDPGATRVVGTFGYLAPELTKSGKLTTSTDVYAFGAVLLEVACGRRPIETSALPEELVMVDWVWSRWQSGDIRDVVDRRLNGEFDEEEVVMVIKLGLLCSNNSPEVRPTMRQVVMYLEKQFPSPEVVPAPDFLDANDSMCLDERSGSAGEFEDFVDSARFYSGPNETTTSSIFSFSGKTRTDPR | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76182
Sequence Length: 684
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9FG33 | MRFSLAWKLLFLILTCKIETQVKCLKFDFPGFNVSNELELIRDNSYIVFGAIQVTPDVTGGPGGTIANQAGRALYKKPFRLWSKHKSATFNTTFVINISNKTDPGGEGLAFVLTPEETAPQNSSGMWLGMVNERTNRNNESRIVSVEFDTRKSHSDDLDGNHVALNVNNINSVVQESLSGRGIKIDSGLDLTAHVRYDGKNLSVYVSRNLDVFEQRNLVFSRAIDLSAYLPETVYVGFTASTSNFTELNCVRSWSFEGLKIDGDGNMLWLWITIPIVFIVGIGAFLGALYLRSRSKAGETNPDIEAELDNCAANPQKFKLRELKRATGNFGAENKLGQGGFGMVFKGKWQGRDIAVKRVSEKSHQGKQEFIAEITTIGNLNHRNLVKLLGWCYERKEYLLVYEYMPNGSLDKYLFLEDKSRSNLTWETRKNIITGLSQALEYLHNGCEKRILHRDIKASNVMLDSDFNAKLGDFGLARMIQQSEMTHHSTKEIAGTPGYMAPETFLNGRATVETDVYAFGVLMLEVVSGKKPSYVLVKDNQNNYNNSIVNWLWELYRNGTITDAADPGMGNLFDKEEMKSVLLLGLACCHPNPNQRPSMKTVLKVLTGETSPPDVPTERPAFVWPAMPPSFSDIDYSLTGSQINSLTELTGR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72868
Sequence Length: 652
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9FHX3 | MNHHHYSLVIFHLILFLSLDFPTLSHRFSPPLQNLTLYGDAFFRDRTISLTQQQPCFPSVTTPPSKPSSSGIGRALYVYPIKFLEPSTNTTASFSCRFSFSIIASPSCPFGDGFAFLITSNADSFVFSNGFLGLPNPDDSFIAVEFDTRFDPVHGDINDNHVGIDVSSIFSVSSVDAISKGFDLKSGKKMMAWIEYSDVLKLIRVWVGYSRVKPTSPVLSTQIDLSGKVKEYMHVGFSASNAGIGSALHIVERWKFRTFGSHSDAIQEEEEEKDEECLVCSGEVSENPKEIHRKGFNFRVTVVGLKIPVWSLLPGLAAIVILVAFIVFSLICGKKRISEEADSNSGLVRMPGRLSLAEIKSATSGFNENAIVGQGASATVYRGSIPSIGSVAVKRFDREHWPQCNRNPFTTEFTTMTGYLRHKNLVQFQGWCSEGTETALVFEYLPNGSLSEFLHKKPSSDPSEEIIVLSWKQRVNIILGVASALTYLHEECERQIIHRDVKTCNIMLDAEFNAKLGDFGLAEIYEHSALLAGRAATLPAGTMGYLAPEYVYTGVPSEKTDVYSFGVVVLEVCTGRRPVGDDGAVLVDLMWSHWETGKVLDGADIMLREEFDAEEMERVLMVGMVCAHPDSEKRPRVKDAVRIIRGEAPLPVLPARRPLLRIRPANEAEEMIVDGLVGEDLPWMTPKSHFS | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76556
Sequence Length: 691
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9FHG4 | MSLSRKLLVIFFTWITALSMSKPIFVSSDNMNFTFKSFTIRNLTFLGDSHLRNGVVGLTRELGVPDTSSGTVIYNNPIRFYDPDSNTTASFSTHFSFTVQNLNPDPTSAGDGLAFFLSHDNDTLGSPGGYLGLVNSSQPMKNRFVAIEFDTKLDPHFNDPNGNHIGLDVDSLNSISTSDPLLSSQIDLKSGKSITSWIDYKNDLRLLNVFLSYTDPVTTTKKPEKPLLSVNIDLSPFLNGEMYVGFSGSTEGSTEIHLIENWSFKTSGFLPVRSKSNHLHNVSDSSVVNDDPVVIPSKKRRHRHNLAIGLGISCPVLICLALFVFGYFTLKKWKSVKAEKELKTELITGLREFSYKELYTATKGFHSSRVIGRGAFGNVYRAMFVSSGTISAVKRSRHNSTEGKTEFLAELSIIACLRHKNLVQLQGWCNEKGELLLVYEFMPNGSLDKILYQESQTGAVALDWSHRLNIAIGLASALSYLHHECEQQVVHRDIKTSNIMLDINFNARLGDFGLARLTEHDKSPVSTLTAGTMGYLAPEYLQYGTATEKTDAFSYGVVILEVACGRRPIDKEPESQKTVNLVDWVWRLHSEGRVLEAVDERLKGEFDEEMMKKLLLVGLKCAHPDSNERPSMRRVLQILNNEIEPSPVPKMKPTLSFSCGLSLDDIVSEDEEGDSIVYVVS | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75842
Sequence Length: 681
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9C6K9 | METVSVLLFFFLFLLAAEARSTKRTGCKDFTCGEHDFKFPFFRTDMPSRCGLFKLNCSANIPEIQLEKDGKWYTVKSVSQANTITIIDPRLNQSLTTGGCSDLSSFSLPDSPWLKLNTLYKCNNSSRKNGFSYANCRGEGSSLYYNLGDDHDVSGCSPIKTPESWVTPKNGNLSDVNATFSLHIELPGNCFRCHNNGGECTKVKNNYRCVGANTEPNNYHAEMRLGLGIGGSVILIIILVALFAVIHRNYRRKDGSELSRDNSKSDVEFSQVFFKIPIFSYKELQAATDNFSKDRLLGDGGFGTVYYGKVRDGREVAVKRLYEHNYRRLEQFMNEIEILTRLHHKNLVSLYGCTSRRSRELLLVYEFIPNGTVADHLYGENTPHQGFLTWSMRLSIAIETASALAYLHASDIIHRDVKTTNILLDRNFGVKVADFGLSRLLPSDVTHVSTAPQGTPGYVDPEYHRCYHLTDKSDVYSFGVVLVELISSKPAVDISRCKSEINLSSLAINKIQNHATHELIDQNLGYATNEGVRKMTTMVAELAFQCLQQDNTMRPTMEQVVHELKGIQNEEQKCPTYDYREETIIPHPSPPDWGEAALLKNMKFPRSPVSVTDQWTSKSTTPNTSAYEF | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70856
Sequence Length: 629
Subcellular Location: Cell membrane
EC: 2.7.11.1
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P0C5E2 | MNPSTPSLLYTSIFFYFTIIATQTLSLDPKFKACEPKSCGKGPQISYPFYLSGKQESFCGYPSFELTCDDEEKLPVLGISGEEYVIKNISYLTQSFQVVNSKASHDPCPRPLNNLTLHRTPFFVNPSHINFTILYNCSDHLLEDFRTYPLTCARNTSLLRSFGVFDRKKLGKEKQIASMSCQKLVDVPVLASNESDVMGMTYVEILKRGFVLNWTANSCFRCITSGGRCGTDQQEFVCLCPDGPKLHDTCTNGKNDKRRRVIVKVLIGASAAVVGLIAASIFWYVYHRRKTKSYRNSSALLPRNISSDPSAKSFDIEKAEELLVGVHIFSYEELEEATNNFDPSKELGDGGFGTVYYGKLKDGRSVAVKRLYDNNFKRAEQFRNEVEILTGLRHPNLVALFGCSSKQSRDLLLVYEYVANGTLADHLHGPQANPSSLPWSIRLKIAVETASALKYLHASKIIHRDVKSNNILLDQNFNVKVADFGLSRLFPMDKTHVSTAPQGTPGYVDPDYHLCYQLSNKSDVYSFAVVLMELISSLPAVDITRPRQEINLSNMAVVKIQNHELRDMVDPSLGFDTDTRVRQTVIAVAELAFQCLQSDKDLRPCMSHVQDTLTRIQNNGFGSEMDVVDVNKSGPLVAQSPDSVIVKWDSK | Function: Probable receptor-like serine/threonine-protein kinase involved in abscisic acid (ABA) signaling. Acts as a positive regulator of abiotic stress response.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72862
Sequence Length: 651
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q8VYG0 | MFSPVLFRFSKPNSFLVLLFFLSYIHFLPCAQSQREPCDTLFRCGDLTAGFPFWGVARPQPCGHPSLGLHCQKQTNSTSLIISSLMYRVLEVNTTTSTLKLVRQDFSGPFCSASFSGATLTPELFELLPDYKTLSAYYLCNPSLHYPAKFICPNKGVGSIHQDDLYHNHCGGIFNITVPIGYAPEEGALNVTNLESVLKKGFEVKLSIDERPCQECKTNGGICAYHVATPVCCKTNSSSEVNCTPMMPSGSSAHAGLSKKGKIGIGFASGFLGATLIGGCLLCIFIRRRKKLATQYTNKGLSTTTPYSSNYTMSNTPTSTTISGSNHSLVPSISNLGNGSVYSGIQVFSYEELEEATENFSKELGDGGFGTVYYGTLKDGRAVAVKRLFERSLKRVEQFKNEIDILKSLKHPNLVILYGCTTRHSRELLLVYEYISNGTLAEHLHGNQAQSRPICWPARLQIAIETASALSYLHASGIIHRDVKTTNILLDSNYQVKVADFGLSRLFPMDQTHISTAPQGTPGYVDPEYYQCYRLNEKSDVYSFGVVLSELISSKEAVDITRHRHDINLANMAISKIQNDAVHELADLSLGFARDPSVKKMMSSVAELAFRCLQQERDVRPSMDEIVEVLRVIQKDGISDSKDVVVEIDVNGGDDVGLLKHGVPPPLSPETDKTTASSSNTTASSF | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75294
Sequence Length: 686
Subcellular Location: Cell membrane
EC: 2.7.11.1
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O75074 | MEKRAAAGLEGAPGARAQLAVVCLVNIFLTGRLSSAVPALAACSGKLEQHTERRGVIYSPAWPLNYPPGTNCSWYIQGDRGDMITISFRNFDVEESHQCSLDWLLLGPAAPPRQEAFRLCGSAIPPAFISARDHVWIFFHSDASSSGQAQGFRLSYIRGKLGQASCQADEFRCDNGKCLPGPWQCNTVDECGDGSDEGNCSAPASEPPGSLCPGGTFPCSGARSTRCLPVERRCDGLQDCGDGSDEAGCPDLACGRRLGSFYGSFASPDLFGAARGPSDLHCTWLVDTQDSRRVLLQLELRLGYDDYVQVYEGLGERGDRLLQTLSYRSNHRPVSLEAAQGRLTVAYHARARSAGHGFNATYQVKGYCLPWEQPCGSSSDSDGGSLGDQGCFSEPQRCDGWWHCASGRDEQGCPACPPDQYPCEGGSGLCYTPADRCNNQKSCPDGADEKNCFSCQPGTFHCGTNLCIFETWRCDGQEDCQDGSDEHGCLAAVPRKVITAALIGSLVCGLLLVIALGCAFKLYSLRTQEYRAFETQMTRLEAEFVRREAPPSYGQLIAQGLIPPVEDFPVYSASQASVLQNLRTAMRRQMRRHASRRGPSRRRLGRLWNRLFHRPRAPRGQIPLLTAARPSQTVLGDGFLQPAPGAAPDPPAPLMDTGSTRAAGDRPPSAPGRAPEVGPSGPPLPSGLRDPECRPVDKDRKVCREPLVDGPAPADAPREPCSAQDPHPQVSTASSTLGPHSPEPLGVCRNPPPPCSPMLEASDDEALLVC | Function: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. Its precise role is however unclear, since it does not bind to very low density lipoprotein (VLDL) or to LRPAP1 in vitro.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 82884
Sequence Length: 770
Subcellular Location: Membrane
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Q98931 | MCRPALARLLLLQLLLLKLYLGKGAMKECDKDQFQCRNERCIPAVWACDEDNDCSDNSDEADCPKKTCAETDFACDNGHCIPDRWKCDGEEECSDGSDESEAACTKQVCPAEKISCGDLSNKCIPSSWRCDGQKDCESGIDEAGCAPACSPDEFQCSNKTCISINFVCDGYNNCGDGSDEKKCSPLTCSPNEFQCNNSVCIPQLWVCDNQADCEDHSDESIERCGYDAKAFNTCAAHEFQCGNGECILLNWKCDGDEDCKDKSDEQDCPLVTCRPDEFQCGDGTCIHGAKQCDKVHDCPDNSDEAGCVQESACESPSKFQCKSGECIDGGKVCDLHRDCRDWSDEPLKECGINECSLNNGGCSHICKDLKIGYECECPPGYKLLDKKTCGDIDECENPDACSQICINYKGDYKCECYEGYEMDTLSKNCKAVGKSPYLIFTNRHEVRKIDLVKRDYSRIIPMLKNVVALDVEVATNRIYWCDLFYRKIYSAYIDKASDTAEQVILIDSQLNSPEGVAIDWVHKNIYWTDSGNKTISVATADGSRRRTVFNSDLSEPRAIAVDPTRRFMYWSDWGDKAKIEKAGLNGVGRQVLVSDNIEWPNGITLDLLNQRLYWVDSKLHSLSCIDFNGSNREVLISSIDDLSHPFGLAVFEDRVFWTDLENEAIFSANRLSGLDISVLAENLNNPHDIVVFHELKQPKAPDSCELSPQPNGGCEYLCLPAPHISPRSPKFTCACPDNMWLGPDMKKCYKELPTTPATVEVPTTTTSHPAATSTVTVTGSANTTTAVIPRAVSEATTAIPSSHSTTSLLIDSEMTTGNSNLSQHYSNNGQGFDSTVTAAVIGIVIPVVVIGLLCMGGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEDEDEIHIGRTAQIGHVYPARVALSLEDDGLP | Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. Also binds alpha2-macroglobulin. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity).
PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 101379
Sequence Length: 917
Subcellular Location: Membrane
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Q14114 | MGLPEPGPLRLLALLLLLLLLLLLQLQHLAAAAADPLLGGQGPAKDCEKDQFQCRNERCIPSVWRCDEDDDCLDHSDEDDCPKKTCADSDFTCDNGHCIHERWKCDGEEECPDGSDESEATCTKQVCPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCATLCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPACGPREFRCGGDGGGACIPERWVCDRQFDCEDRSDEAAELCGRPGPGATSAPAACATASQFACRSGECVHLGWRCDGDRDCKDKSDEADCPLGTCRGDEFQCGDGTCVLAIKHCNQEQDCPDGSDEAGCLQGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECKDPDACSQICVNYKGYFKCECYPGYEMDLLTKNCKAAAGKSPSLIFTNRHEVRRIDLVKRNYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAYMDKASDPKEQEVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATVDGGRRRTLFSRNLSEPRAIAVDPLRGFMYWSDWGDQAKIEKSGLNGVDRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFSGGNRKTLISSTDFLSHPFGIAVFEDKVFWTDLENEAIFSANRLNGLEISILAENLNNPHDIVIFHELKQPRAPDACELSVQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASTMTRTVPATTRAPGTTVHRSTYQNHSTETPSLTAAVPSSVSVPRAPSISPSTLSPATSNHSQHYANEDSKMGSTVTAAVIGIIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEDEDELHIGRTAQIGHVYPAAISSFDRPLWAEPCLGETREPEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKSKRVALSLEDDGLP | Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands . LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity). Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells (By similarity).
PTM: O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 105634
Sequence Length: 963
Domain: The cytoplasmic domain is involved in the binding of DAB1 and in the recruitment of JNK-interacting proteins. Isoforms, which lack part of the cytoplasmic domain, are unable to recruit members of the family of JNK interacting proteins (JIP) to the cytoplasmic tail (By similarity).
Subcellular Location: Cell membrane
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Q924X6 | MGRPELGALRPLALLLLLLLQLQHLSAADPLPGGQGPVKECEEDQFRCRNERCIPLVWRCDEDNDCSDNSDEDDCPKRTCADSDFTCDNGHCIPERWKCDGEEECPDGSDESKATCSSEECPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCPTLCAPHEFQCSNRSCLASVFVCDGDDDCGDGSDERGCSDPACPPREFRCGGGGTCIPERWVCDRQFDCEDRSDEAAELCGRAGQGTTATPAACAPTAQFTCRSGECIHLGWRCDGDRDCKDKSDEADCSPGPCRENEFQCGDGTCVLAIKRCNQERDCPDGSDEAGCLQESTCEGPRRFQCKSGECVDGGKVCDDQRDCRDWSDEPQKVCGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECQDPDACSQICVNYKGYFKCECHPGYEMDTLTKNCKAVAGKSPSLIFTNRHEVRRIDLVKRDYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAHMDKASIPDEQVVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATTDGRRRCTLFSRELSEPRAIAVDPLRGFMYWSDWGFQAKIEKAGLNGADRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFNGGNRKMLIFSTDFLSHPFGVAVFEDKVFWTDLENEAIFSANRLNGLEIAILAENLNNPHDIVIFHELKQPKAADACDLSAQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASAMTRTVPATTRAPGTTIHDPTYQNHSTETPSQTAAAPHSVNVPRAPSTSPSTPSPATSNHSQHYGNEGSQMGSTVTAAVIGVIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEEEDELHIGRTAQIGHVYPAAISNYDRPLWAEPCLGETRDLEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKCKRVALSLEDDGLP | Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation . May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 . Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells .
PTM: O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 109818
Sequence Length: 996
Domain: The cytoplasmic domain is involved in the binding of DAB1 and in the recruitment of JNK-interacting proteins. Isoforms, which lack part of the cytoplasmic domain, are unable to recruit members of the family of JNK interacting proteins (JIP) to the cytoplasmic tail.
Subcellular Location: Cell membrane
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D4A7P2 | MGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATDKGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNKIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDCRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNKISNLTCGMEWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILSSLRSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTAMATTYRDPTTEYTKISSSSYHVGDKEIPTTAGIAVTTEEHFPEPDNAIFTQRVITGTMALLFSFFFIIFIVFISRKCCPPTLRRIRQCSMIQNHRQLRSQTRLHMSNMSDQGPYSEYEPTHEGPFIIINGYGQCKCQQLPYKECEV | Function: Involved in the development and maintenance of excitatory synapses in the nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58804
Sequence Length: 515
Domain: Synaptogenic effects are mediated by the extracellular LRR region.
Subcellular Location: Cell membrane
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Q86VH5 | MGFNVIRLLSGSAVALVIAPTVLLTMLSSAERGCPKGCRCEGKMVYCESQKLQEIPSSISAGCLGLSLRYNSLQKLKYNQFKGLNQLTWLYLDHNHISNIDENAFNGIRRLKELILSSNRISYFLNNTFRPVTNLRNLDLSYNQLHSLGSEQFRGLRKLLSLHLRSNSLRTIPVRIFQDCRNLELLDLGYNRIRSLARNVFAGMIRLKELHLEHNQFSKLNLALFPRLVSLQNLYLQWNKISVIGQTMSWTWSSLQRLDLSGNEIEAFSGPSVFQCVPNLQRLNLDSNKLTFIGQEILDSWISLNDISLAGNIWECSRNICSLVNWLKSFKGLRENTIICASPKELQGVNVIDAVKNYSICGKSTTERFDLARALPKPTFKPKLPRPKHESKPPLPPTVGATEPGPETDADAEHISFHKIIAGSVALFLSVLVILLVIYVSWKRYPASMKQLQQRSLMRRHRKKKRQSLKQMTPSTQEFYVDYKPTNTETSEMLLNGTGPCTYNKSGSRECEIPLSMNVSTFLAYDQPTISYCGVHHELLSHKSFETNAQEDTMETHLETELDLSTITTAGRISDHKQQLA | Function: Exhibits a limited synaptogenic activity in vitro, restricted to excitatory presynaptic differentiation (By similarity). May play a role in the development and maintenance of the vertebrate nervous system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65896
Sequence Length: 581
Subcellular Location: Cell membrane
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Q80XG9 | MGFRLITQLKGMSVFLVLFPTLLLVMLTGAQRACPKNCRCDGKIVYCESHAFADIPENISGGSQGLSLRFNSIQKLKSNQFAGLNQLIWLYLDHNYISSVDEDAFQGIRRLKELILSSNKITYLHNKTFHPVPNLRNLDLSYNKLQTLQSEQFKGLRKLIILHLRSNSLKTVPIRVFQDCRNLDFLDLGYNRLRSLSRNAFAGLLKLKELHLEHNQFSKINFAHFPRLFNLRSIYLQWNRIRSVSQGLTWTWSSLHTLDLSGNDIQAIEPGTFKCLPNLQKLNLDSNKLTNVSQETVNAWISLISITLSGNMWECSRSICPLFYWLKNFKGNKESTMICAGPKHIQGEKVSDAVETYNICSDVQVVNTERSHLAPQTPQKPPFIPKPTIFKPDAVPATLEAVSPSPGFQIPGTDHEYEHVSFHKIIAGSVALFLSVAMILLVIYVSWKRYPASMKQLQQHSLMKRRRKKARESERQMNSPLQEYYVDYKPTNSETMDISVNGSGPCTYTISGSRECEIPHHVKPLPYYSYDQPVIGYCQAHQPLHINKAYEAVSIEQDDSPSLELGRDHSFIATIARSAAPAIYLERITN | Function: May play a role in the development and maintenance of the vertebrate nervous system. Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 67148
Sequence Length: 590
Subcellular Location: Cell membrane
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Q04087 | MTTLLQLLSNYYKAKLDSERIYNEYVQSQYEFASLDKLNNNKGDPKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQKALYQSKLSSKDAFIDDLKLKLKVEQISVDKHNKERTPSTGRDEQQRNSKAAHTSKPTIHLLSPIVNRDKPNNQTNDRGGNDPDSPTSQRRSRGLRSLLSSGKNTIFDSISKNLDDEINENAHIRNDTTSSKIAGKSPSRLSALQKSPELRKERNNMILKEHILRSKDDQNITSSRKLDNIELSSIGDSTAMTSRSSTVNANDILGNEENDGITKLKRVNKLTSSPVKRDCSTNKKRKLTKQRIATLPNSDEELSNNLNVDEFV | Function: Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Involved in rDNA silencing.
PTM: Phosphorylated by CDC5. This phosphorylation is required for the location to the kinetochores during late pachytene.
Sequence Mass (Da): 39354
Sequence Length: 347
Subcellular Location: Nucleus
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A0A0P0VIP0 | MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPHPNHRRRHLFYKVLGGVLGGMVLLGLVVVGSAVLLGRSVRRKNQEHAVASEDMGEATLSMEVARAATKGFDSGNVIGVGGSGATVYEGVLPSGSRVAVKRFQAIGSCTKAFDSELKAMLNCPHHPNLVPLAGWCRSKDELVLVYEFMPNGNLDSALHTLGGATLPWEARFRAVYGVASALAYLHDECENRIIHRDVKSSNVMLDAEFNARLGDFGLARTVSHGGLPLTTQPAGTLGYLAPEYVHTGVATERSDVYSFGVLALEVATGRRPAERGISVVNWVWTLWGRRRLVDAADRRLQGRFVADEMRRVLLVGLCCVHPDCRKRPGMRRVVSMLDGTAPLILVPDKMPPVLLQPVPNASSMNSADTANTAFFSCR | Function: Legume-lectin receptor-like kinase required for normal pollen development and male fertility . Regulates pollen exine assembly and aperture development . Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum . May function by regulating the expression of genes involved in pollen exine development . Kinase activity is required for its function in pollen development .
PTM: Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-657.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 74135
Sequence Length: 695
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q6UWE0 | MPLFFRKRKPSEEARKRLEYQMCLAKEAGADDILDISKCELSEIPFGAFATCKVLQKKVLIVHTNHLTSLLPKSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLDASAMVYPPREVCGAGTAAILQFLCKESGLEYYPPSQYLLPILEQDGIENSRDSPDGPTDRFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLTESCKNRLIQMAYESQRQNLVQQACSSMAEMDERFQQILSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQIKLIETELLQLTQLELKRKSLDTESLQEMISEQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQYQRLLNQKPLSLKLQEEGMERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLDAARIQPELKPPMGEVVTPTAPQEPPESVRPSAPPAELEVQASECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIYHSS | Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos . Bacterial recognition protein that defends the cytoplasm from invasive pathogens . Localizes to several intracellular bacterial pathogens and generates the bacteria-associated ubiquitin signal leading to autophagy-mediated intracellular bacteria degradation (xenophagy) .
PTM: Ubiquitination promoted by PHF23 leads to proteasomal degradation.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 83594
Sequence Length: 723
Domain: The coiled coil domains interact with the SB domain of TSG101.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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B0R160 | MEKITEKILLEKSSTKTNKLDQIKTLNLSRMSLKSEDLPVPLLSKLCRLEKLDLSGNMLQKIPKGLRLPCLKILNCSNNDMEDVLSLEALTNLEELRLEDNLYLTVNDEHKVIFLLPNLRMFNGKDISSTAHHIRHGSTEILRKRVIGVWERDFSLPDPISAKSLAAVEKSFVNAACTQVKYGPNSLSDYTKWRVEKIAKEYLKSLTSSEEEERVADTTPTKENKTKACDVGGNSITSPQKRTRNNTDVVAEASPRKSSRLVSAAPVEASPRKSARVLNTPQKTQPVVSSPRKHARLTSAETPESSPRKSSRLENVTQKAASQTESPRKPGMSTPTSKQAKCESPRKQSKQSTAKMEKSTPRKTTKAKLQVPQEPVSLTPLHVLQCHSRQNDPDDFSTQLWACAFEPQQDDSIDISGGSQTIATCGGETLCVINCESGLVLKKYKVPGEDFFSLAWSTVLMSRTGGSARPCNILAAGGKRGCVKLIHPRVNLAFGEFRVSRRAISIMRFNPRKPTFLFTGTYDKKIFLWDIGGLDQDYNFKISKLLTLETSSTPLHLALLPSSPDTHLLSGCDEGLYCFDVQLSKNTLKRNEEIEIVFPIYKKNDKKNNYRTIDGLSFLSDDVVASKSHMQGSIYLWSWSATRASWNSRKKEVPAVILAELQWSSTDIPYLSLGTCPGYGYVVCGDEQGRLWMYHITDTMMENFKSGKTISATEVLQWPSPIRAGKGALEGPSINSTAMDPGLHYLVALTDKNMVVVWKRESH | Function: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability (By similarity).
Sequence Mass (Da): 85048
Sequence Length: 763
Domain: The entire WD repeat region is required for the interaction with ORC complex components, as well as for association with chromatin and for binding to histone H3 and H4 trimethylation marks H3K9me3 and H4K20me3.
Subcellular Location: Nucleus
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Q9UFC0 | MGPLSARLLMQRGRPKSDRLGKIRSLDLSGLELLSEHLDPKLLCRLTQLQELDLSNNHLETLPDNLGLSHLRVLRCANNQLGDVTALCQFPKLEELSLEGNPFLTVNDNLKVSFLLPTLRKVNGKDASSTYSQVENLNRELTSRVTAHWEKFMATLGPEEEAEKAQADFVKSAVRDVRYGPESLSEFTQWRVRMISEELVAASRTQVQKANSPEKPPEAGAAHKPRARLAALKRPDDVPLSLSPSKRACASPSAQVEGSPVAGSDGSQPAVKLEPLHFLQCHSKNNSPQDLETQLWACAFEPAWEEGATSQTVATCGGEAVCVIDCQTGIVLHKYKAPGEEFFSVAWTALMVVTQAGHKKRWSVLAAAGLRGLVRLLHVRAGFCCGVIRAHKKAIATLCFSPAHETHLFTASYDKRIILWDIGVPNQDYEFQASQLLTLDTTSIPLRLCPVASCPDARLLAGCEGGCCCWDVRLDQPQKRRVCEVEFVFSEGSEASGRRVDGLAFVNEDIVASKGSGLGTICLWSWRQTWGGRGSQSTVAVVVLARLQWSSTELAYFSLSACPDKGIVLCGDEEGNVWLYDVSNILKQPPLLPAALQAPTQILKWPQPWALGQVVTKTMVNTVVANASFTYLTALTDSNIVAIWGRM | Function: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability.
PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination leading to proteasomal degradation. Ubiquitination occurs within the WD repeats at the end of the G1 phase. Ubiquitination may be catalyzed by the CUL4-DDB1 E3 ubiquitin-protein ligase complex and other E3 ligases.
Sequence Mass (Da): 70861
Sequence Length: 647
Domain: The entire WD repeat region is required for the interaction with ORC, CDT1 and GMNN, as well as for association with chromatin and for binding to histone H3 and H4 trimethylation marks H3K9me3 and H4K20me3.
Subcellular Location: Nucleus
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B0JZ65 | MSKITADVLLKEGLPKSIHLKDLKKLNLSKMHLEMKDIDPKLFSQMVNLDELDISHNTLSELPDNLGLHNLRILNFADNHVEDVTVLKQFPNLEEVIYEDNIYLTVSDNYKVFCLLPKLRRLNNKDITSLANHVRFVNHRELSNRVEAHWDSKFKDNLPDKPSSQKINAVAKDFIKSVVNNIKYGPSSLKEFVRWKALGCSGKKRDSADDCTEGSPTKRTRIQHELQSIPLSPRKSNRLQNSPLSLTPIKRKQETSTQGTPSKSTETKSPKVALKSTPSKKQSNESSAKINGKQKLSLTPKIIQKALDNIEPLHFLQCHSKNNSCEDFKTQLWACAFEPILDSSSPKAVATCGGDSVCIIDCETGKVMKKYKVTGEEFFTLVWTTLTMIGKDEQKRKINVLAAGGKHGVVRIIHAKVSLCYGEIKAHKKAISIMCFSPKQDTFLFTGSYDKRIILWDIGVPDCDYNFRPSQLLTLDTTSVPLRMCLVPSCPDEFLVAACEDGCFAWDIRLDKKQGRRSYEVELNFPIYKEERKDNDFHVIDSLAFLNEDIIASKSVMQGSIYLWSWEKTLKTRKTKNVKKLDAVILAQMKWSSSETPYLVLSTSPERYCVFCGDEDGKIWIYDLDSCKADLQRGKLCSVVKEPTKILSWPILFSPKEKVEKTLINVVTVDPTMEYLVALTDINIVSIWKIK | Function: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability (By similarity).
Sequence Mass (Da): 78447
Sequence Length: 691
Domain: The entire WD repeat region is required for the interaction with ORC complex components, as well as for association with chromatin and for binding to histone methylation marks.
Subcellular Location: Nucleus
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O65375 | MLFPPLRSLFLFTLLLSSVCFLQIKADHDDESDLGSDIKVDKRLKFENPKLRQAYIALQSWKKAIFSDPFNFTANWNGSDVCSYNGIYCAPSPSYPKTRVVAGIDLNHADMAGYLASELGLLSDLALFHINSNRFCGEVPLTFNRMKLLYELDLSNNRFVGKFPKVVLSLPSLKFLDLRYNEFEGKIPSKLFDRELDAIFLNHNRFRFGIPKNMGNSPVSALVLADNNLGGCIPGSIGQMGKTLNELILSNDNLTGCLPPQIGNLKKVTVFDITSNRLQGPLPSSVGNMKSLEELHVANNAFTGVIPPSICQLSNLENFTYSSNYFSGRPPICAASLLADIVVNGTMNCITGLARQRSDKQCSSLLARPVDCSKFGCYNIFSPPPPTFKMSPEVRTLPPPIYVYSSPPPPPSSKMSPTVRAYSPPPPPSSKMSPSVRAYSPPPPPYSKMSPSVRAYPPPPPPSPSPPPPYVYSSPPPPYVYSSPPPPPYVYSSPPPPPYVYSSPPPPYVYSSPPPPYVYSSPPPPPPSPPPPCPESSPPPPVVYYAPVTQSPPPPSPVYYPPVTQSPPPPSPVYYPPVTNSPPPPSPVYYPPVTYSPPPPSPVYYPQVTPSPPPPSPLYYPPVTPSPPPPSPVYYPPVTPSPPPPSPVYYPPVTPSPPPPSPVYYPSETQSPPPPTEYYYSPSQSPPPTKACKEGHPPQATPSYEPPPEYSYSSSPPPPSPTSYFPPMPSVSYDASPPPPPSYY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization. Together with LRX2, component of the extracellular mechanism regulating root hair morphogenesis and elongation.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 80994
Sequence Length: 744
Subcellular Location: Secreted
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Q9T0K5 | MKKTIQILLFFFFLINLTNALSISSDGGVLSDNEVRHIQRRQLLEFAERSVKITVDPSLNFENPRLRNAYIALQAWKQAILSDPNNFTSNWIGSNVCNYTGVFCSPALDNRKIRTVAGIDLNHADIAGYLPEELGLLSDLALFHVNSNRFCGTVPHRFNRLKLLFELDLSNNRFAGKFPTVVLQLPSLKFLDLRFNEFEGTVPKELFSKDLDAIFINHNRFRFELPENFGDSPVSVIVLANNRFHGCVPSSLVEMKNLNEIIFMNNGLNSCLPSDIGRLKNVTVFDVSFNELVGPLPESVGEMVSVEQLNVAHNMLSGKIPASICQLPKLENFTYSYNFFTGEAPVCLRLPEFDDRRNCLPGRPAQRSPGQCKAFLSRPPVNCGSFSCGRSVSPRPPVVTPLPPPSLPSPPPPAPIFSTPPTLTSPPPPSPPPPVYSPPPPPPPPPPVYSPPPPPPPPPPPPVYSPPPPPPPPPPPPPVYSPPPPSPPPPPPPVYSPPPPPPPPPPPPVYSPPPPPVYSSPPPPPSPAPTPVYCTRPPPPPPHSPPPPQFSPPPPEPYYYSSPPPPHSSPPPHSPPPPHSPPPPIYPYLSPPPPPTPVSSPPPTPVYSPPPPPPCIEPPPPPPCIEYSPPPPPPVVHYSSPPPPPVYYSSPPPPPVYYSSPPPPPPVHYSSPPPPEVHYHSPPPSPVHYSSPPPPPSAPCEESPPPAPVVHHSPPPPMVHHSPPPPVIHQSPPPPSPEYEGPLPPVIGVSYASPPPPPFY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 82246
Sequence Length: 760
Subcellular Location: Secreted
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Q9LHF1 | MKNNTTQSLLLLLLFFFFFFEISHSLSISSNAPLSDTEVRFIQRRQLLYYRDEFGDRGENVTVDPSLIFENPRLRSAYIALQAWKQAILSDPNNITVNWIGSNVCNYTGVFCSKALDNRKIRTVAGIDLNHADIAGYLPEELGLLTDLALFHVNSNRFCGTVPHKFKQLKLLFELDLSNNRFAGKFPTVVLHLPSLKFLDLRFNEFEGTVPKELFSKNLDAIFINHNRFRFELPENFGDSPVSVIVLANNHFHGCIPTSLVEMKNLNEIIFMNNGLNSCLPADIGRLKNVTVFDVSFNELVGPLPESVGGMVEVEQLNVAHNLLSGKIPASICQLPKLENFTYSYNFFTGEAPVCLRLSEFDDRRNCLPGRPAQRSSRQCSAFLSRPSVDCGSFGCGRSVVKPSPPIVALPPPPPPSPPLPPPVYSPPPSPPVFSPPPSPPVYSPPPPPSIHYSSPPPPPVHHSSPPPPSPEFEGPLPPVIGVSYASPPPPPFY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 54703
Sequence Length: 494
Subcellular Location: Secreted
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Q9LUI1 | MREDTFFFQWWFLVSGLSFIFLLPQAFTYHTPPINPCFAHPFLPPITNPRLLKAFTALQAWKFTITSDPNGFTSNWCGPNVCNYTGVFCAPALDNPYVLTVAGIDLNHANIAGYLPLELGLLTDLALFHINSNRFQGQLPKTLKCLHLLHELDVSNNKLSGEFPSVIFSLPSLKFLDIRFNEFQGDVPSQLFDLNLDALFINDNKFQFRLPRNIGNSPVSVLVLANNDLQGSCVPPSFYKMGKTLHEIIITNSQLTGCLNREIGLLNQLTVFDVSYNNLVGSLPETIGDMKSLEQLNIAHNKFSGYIPESICRLPRLENFTYSYNFFSGEPPACLRLQEFDDRRNCLPSRPMQRSLAECKSFSSYPIDCASFGCSPPSPPPPPPPPPPPPPPPPPPPPPPPPPPPPPYVYPSPPPPPPSPPPYVYPPPPPPYVYPPPPSPPYVYPPPPPSPQPYMYPSPPCNDLPTPVHY | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 52335
Sequence Length: 470
Subcellular Location: Secreted
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Q4PSE6 | MRIYQPTLLIFTTVVLLSISAVAPGGSRQLLYTRDDPITIPPYLIFENVRLERAYVALQAWKRAMISDPWNLTTNWFGSRVCDYNGVVCSESLDDPLVKTVSGVDLNQGDIAGHLPEELGLLTDIALFHVNSNRFCGTLPVGFSQLSLLFELDLSNNRFAGKFPEVVIGLPKLKYLDLRYNEFEGELPESLFDKDLDALFLNSNRFRSKIPVNMGNSPVSVLVLASNRFEGCIPPSFGKMGKTLNEIILMDNGLQSCIPNDMGLLQNVTVLDISYNWLVGELPKSMGQMENLEVLNVERNMLSGLIPDELCSLEKLRDFRYGSNYFTGEPATCRYLENYNYTMNCFKDVRDQRSMMECKMFLSKPVDCDSFKCSPGSSCFSPPPSQISPSSQPLAPAPSPTSPPLSTPPPARPCPPVYSPPPPPPLSLAPSMN | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 48088
Sequence Length: 433
Subcellular Location: Secreted
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Q8ND56 | MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEVFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSTSSFQSMGSYGPFGRMPTYSQFSPSSLVGQQFGAVGVAGSSLTSFGTETSNSGTLPQSSAVGSAFTQDTRSLKTQLSQGRSSPQLDPLRKSPTMEQAVQTASAHLPAPAAVGRRSPVSTRPLPSASQKAGENQEHRRAEVHKVSRPENEQLRNDNKRQVAPGAPSAPRRGRGGHRGGRGRFGIRRDGPMKFEKDFDFESANAQFNKEEIDREFHNKLKLKEDKLEKQEKPVNGEDKGDSGVDTQNSEGNADEEDPLGPNCYYDKTKSFFDNISCDDNRERRPTWAEERRLNAETFGIPLRPNRGRGGYRGRGGLGFRGGRGRGGGRGGTFTAPRGFRGGFRGGRGGREFADFEYRKTTAFGP | Function: Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for translationally inactive mRNAs and protect them from degradation . Acts as a repressor of mRNA translation . May play a role in mitotic spindle assembly .
Sequence Mass (Da): 50530
Sequence Length: 463
Domain: The LSM14 domain and the RGG repeats are required for accumulation in P-bodies, and the region containing the FDF motif is responsible for cytoplasmic retention.
Subcellular Location: Cytoplasm
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Q9Y802 | MMDLSSKDALSDVLKDTHAQSSDPSLWAIFGHQSSDNVHEGGNESVSVEQEIFDLSQLSERPVSETVSKASIPTNINGLSQVKPSALEKSQEVLSLQKLPIKGRRPAGRRGRPALNTSNSLERNGTRYVSAEAPISVKSSIPAIPRVTFERLCYESAIASNLPPNALSPLEAEMLSEILENPTWLSLYLSIRNGICYLWHRNPTLYVSFNEALGIVREKKAFPLASLAFEFLSRNGHINYGCIYIISSLKLDESLSQKTVAIIGAGMAGISCARQLTNLFAQYEQDFLSRGEKPPRIVIYEASERLGGHIYTHMVPLSDNEVSEKSSLATTVNATNECMVNLLTDSLIGMPTLDSDPLYIISSQQLSLDAVHTRNREFILHDIENGRIDTEHVQRIFRLFDALLFYFNASASKQPLHSLITPPEQEFIQKLDQIGWYISIEAFPLQIKDTLSEFLGNSANTLTSLLHLTVLDLKIFEWFKEYLSQSLSVSLENVYPGSIPNLNLLLGENVASYSFKHGMADMLNSLASTPSPLPILFDQCVHTVKLEDNTVNLSFVNETTVSVDKVVICIPMDKLNTHLITFEPPLEEKKLKAIDRCHFTNVKKVILIFKTQFWEPNISIFGSLPQDSGRNFIFNDCTRFYEHPTLSVFVKVEGIDFMKDDDIVNGIVSQLKKVYKPKSEAINPIRTIISNWENNSYTNHSSYQISNLFLEEDYAILSEPIDNTVFFASEAISQKNSGSIRGAFDSGILAARDVLASLIGNVVLPNTLVIEENLEQPRKTYGTKRNAQQALGKEGERENKEKRISYHTEYLRLRQKRLDKEQQECDLLIAELLGPSPVPPSRPSANPYLLYQKTQWHVCKTLADQDKQRVTGDPEARATKNEIRAKLGKTWRALDSLGKQPWVDEINARRANYSTRLEEYQRQINSYNVRVAQIKSEHQRRCESQPIPEDEAKLKLLAEQEDEHLHPEKEGMSVENSDDDYHDDLDYEDSISEVFPDNFS | Function: Catalytic component of the SWM histone demethylase complex that specifically demethylates H3K9me2, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Has a role in regulating heterochromatin propagation and euchromatic transcription. Also has a gene activating role.
Sequence Mass (Da): 112829
Sequence Length: 1000
Subcellular Location: Nucleus
EC: 1.-.-.-
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Q9VW97 | MKPTQFGGSSSKMTEPIEYVTLISDDSDGEPTPKRNVNHPPSALSAPNPGQKQKHPDEDSNDAPATSDERRTSRRNRPKVDYSNRPSGSGDTASNDKSGSASMGPNNQQAERRSQSQTRKSEANATSSSVSGPSAGNSRPSQNGDSKDRDAGTPTVLSGQEGAVFQSRLPFNKMTPNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPPFDSEPSLVRRVHSFLERHGFINFGIFKRLKPIPAKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYGNPMTILSKQIGMDLVPIQQTCPLYGPDGKPVPKEKDDVIEREFNRLLESASYLSHRLDFNYAGDCPVSLGDALEWIISMQEMQVMHKRGQHMQEIIATQTKIIEQRRRLKTLRDTIGKLKNEHLAMINQRKPKGTDGDLKYCYQEFNIRNTQIKMEETISTFHDLHAEEKQMLAKLHELEQNRPSDVYLSSRDRLILDWHFANLEFANATRLNNLSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYGTKGVEVVAENLKTSNSQMTYKADLVVCTLTLGVLKVAVAHKESQQSNTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWSISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLKNIFGNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVIPPSSKDAEGLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRIADYYLGYPEGTPPDIGYSVAEAANLVSVGNVVKLRDLSPNLSDSSPSSKKSEENSNSNTADSTELQ | Function: Probable histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for heterochromatic gene silencing. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and tri-methylated 'Lys-4' of histone H3. May also demethylate 'Lys-9' of histone H3, Plays a role in the repression of neuronal genes.
Sequence Mass (Da): 98389
Sequence Length: 890
Subcellular Location: Nucleus
EC: 1.-.-.-
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Q53353 | MAHFPQTPGFSGTLRPLRIEGDILDIEIEGEVPPQLNGTFHRVHPDAQFPPRFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAYRNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEGYTNFDGKLQSQTFCAHPKIDPVTGNLCAFAYGAKGLMTLDMAYIEISPTGKLLKEIPFQNPYYCMMHDFGVTEDYAVFAVMPLLSSWDRLEQRLPFFGFDTTLPCYLGILPRNGDARDLRWFKTGNCFVGHVMNAFNDGTKVHIDMPVSRNNSFPFFDVHGAPFDPVAGQGFLTRWTVDMASNGDSFEKTERLFDRPDEFPRIDERYATRAYRHGWMLILDTEKPYEAPGGAFYALTNTLGHIDLATGKSSSWWAGPRCAIQEPCFIPRSPDAPEGDGYVIALVDDHVANYSDLAIFDAQHVDQGPIARAKLPVRIRQGLHGNWADASRLAVAA | Cofactor: 1 Fe(2+) ion per subunit.
Function: Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene).
Catalytic Activity: 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin
Sequence Mass (Da): 54436
Sequence Length: 485
EC: 1.13.11.43
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F4J117 | MAFLQQISGLGALERSCPSIMIGSSFRSGNGRVFDGRGIAYLGSREKFGFNRRRRVVLRVVAMSSSSTPFKMNLNEYMVTLEKPLGIRFALSADGKIFVHAIKKGSNAEKARIIMVGDTLKKASDSSGGTLVEIKDFGDTKKMLVEKTGSFSLVLERPFSPFPIQYLLHLSDLDLLYNRGRVSFVTWNKNLLSSNLRASSQGSGNSGYAAFSSKFFTPQGWKLLNRQSNSFQSGTKKNILSPPISPLVSVFSEDVPGDGEWGYGNFPLEEYIKALDRSKGELSYNHALGMRYSKITEQIYVGSCIQTEEDVENLSEAGITAILNFQGGTEAQNWGIDSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHACKPDRPAIAWATWDLIAMVDDGKHDGTPTHSVTFVWNGHEGEEVLLVGDFTGNWKEPIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIVVGDVANVRPTIQQPRKDANIIKVIERVLTESERFRLAKAARCIAFSVCPIRLCPKS | Function: Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Participates in the regulation of the initial steps of starch degradation at the granule surface. May release a different set of phosphate groups from those removed by DSP4.
Sequence Mass (Da): 65741
Sequence Length: 591
Subcellular Location: Plastid
EC: 3.1.3.-
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Q9SRK5 | MSVIGSKSCIFSVARYTRENEKSSCFTSINKKSSLDLRFPRNLAGVSCKFSGENPGTNGVSLSSKNKMEDYNTAMKRLMRSPYEYHHDLGMNYTLIRDELIVGSQPQKPEDIDHLKQEQNVAYILNLQQDKDIEYWGIDLDSIVRRCKELGIRHMRRPAKDFDPLSLRSQLPKAVSSLEWAVSEGKGRVYVHCSAGLGRAPGVSIAYMYWFCDMNLNTAYDTLVSKRPCGPNKGAIRGATYDLAKNDPWKEPFESLPENAFEDIADWERKLIQERVRALRGT | Function: Starch-associated phosphoglucan phosphatase that selectively dephosphorylates the glucan C3 position. Probably participates in the regulation of starch degradation.
Sequence Mass (Da): 32087
Sequence Length: 282
Subcellular Location: Plastid
EC: 3.1.3.-
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Q9SHS8 | MGKNEKTSLGRALVKHHNHMIQETKEKGKSYKDQHKKVLESVTEVSDIDAIIEQAEEAERLFAIHHDSATPVPINMDTGSSSSGITAKEWKEQRMREEALHASSLQVPRRPHWTPKMNVEKLDANEKQAFLTWRRKLASLEENEKLVLTPFEKNLDIWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAKAATATLEGKPLKEQWRAPDTTQKTDNPAVKVYGRDDLLDRLKLEALEIVKMRKSRGVSATSTESHCEQVVVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISEDLMLCDCPGLVFPSFSSSRYEMVASGVLPIDRMTEHLEAIKVVAELVPRHAIEDVYNISLPKPKSYEPQSRPPLASELLRTYCLSRGYVASSGLPDETRAARQILKDYIEGKLPHFAMPPEITRDDENETADDTLGAETREGSQTEKKGEEAPSLGLDQVLDDLSSFDLANGLVSSKTKQHKKSHRKQ | Function: GTPase that might be redundant with LSG1-2 for ribosome biogenesis (Probable). Binds to 23S rRNA .
Sequence Mass (Da): 60758
Sequence Length: 537
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Cytoplasm
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Q9SJF1 | MGKSEKTSLGRSLVKHHNHMIQESKDKGKYYKNLQKKVLESVTEVSDIDAIIEQAEEAERLYTINHSSSTPLSINLDTNSSSSVIAAEEWREQQKIEEALHASSLQVPRRPPWTPEMSVEELDANEKQAFLNWRRMLVSLEENEKLVLTPFEKNLDIWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKIMLLVNKADLLPTDVREKWAEYFRLNNILFVFWSAIAATATLEGKVLKEQWRQPDNLQKTDDPDIMIYGRDELLSRLQFEAQEIVKVRNSRAASVSSQSWTGEYQRDQAVVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISDELMLCDCPGLVFPSFSSSRYEMIASGVLPIDRMTEHREAIQVVADKVPRRVIESVYNISLPKPKTYERQSRPPHAAELLKSYCASRGYVASSGLPDETKAARLILKDYIGGKLPHYAMPPGMPQADEPDIEDTQELEDILEGSESDDSAVGDETENEQVPGIDDVLDDLSSFDLANGLKSSKKVTAKKQTASHKQHKKPQRKKDRTWRVQNTEDGDGMPSVKVFQKPANTGPLTMR | Function: GTPase involved in ribosome biogenesis (Probable). Binds to 23S rRNA and associates with 60S pre-ribosomes . Involved in early cotyledon and leaf development .
Sequence Mass (Da): 66743
Sequence Length: 589
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Cytoplasm
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Q2YDM7 | MGRRRAPEGGTLGRALIRQQVQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLDDFLATAELAGTEFVAEKLNIKFVPPEARTGLLSFEENQRIKKLHEENKQFLCIPRRPKWDQKTSPEELKQAEKDNFLEWRRQLVWLEEEQNLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKTIDDNKENVILINKADLLTAEQRSAWAEFFKKENVKVIFWSALAEAIKLMGNSKGDVNGDTGEAITAEFENSSCDEAEILHKETEHLSLGEAASSEEDESEYEDCQEEEEDWQTCLEDSSSSDEEACGQDCKEGHTVDSEAQGRNTPQKRQIHNFSHLVSKQELLEVFKQLHSGKKVKDGQLTVGLVGYPNVGKSSTINTILGNKKVSVSATPGHTKHFQTLYVEPGLCLCDCPGLVMPSFVSTKAEMICSGILPIDQMRDHVPPVSLVCQNIPRHVLEATYGIDIIKPREDEDPRRPPTSEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVNGKLLYCHPPPGRDPVTFQYQHQRLLEKKVNGGEIKLQVVRNKKVYQIENVVDKAFFHQENVRALTKGVQAVMGYKPGSGLVTAAAVSSERGAGKPWKKHGNRNKKEKSRRLYKHLDM | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity).
Sequence Mass (Da): 74249
Sequence Length: 652
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q5ZJD3 | MGKKRGTGLGRSLQRQRGSERRGASSWLHASEVVGESGPERRSAVEQSPLEEFLATAELAGTRFVAERLNIQFVSAQSRTGLLTAQEAQHVRQLHEENRQFLRIPRRPYWDRTTSSEDLKQAERESFLEWRRQLAHLEEEKKLILTPFERNLEFWRQLWRVIERSDIVVQIVDARNPLLFRCQDLESYVKEVSNDKENMILINKADLLSEEQRAAWAQFFEKEGVKVVFWSALAECRRLSGEVKELDADSVADDLSDSEEESSSQEEDVTAEDSAESTSTGSALQTENQCLLSDDDSSDEYEDCEDEEEDDWQTCSEDEGGDKVNAIAPKSMENRTDIVSMHHVVQEQNRNVKNFSHLVQRNELLEIFKTLHSGPRVKDGEVNVGLVGYPNVGKSSTINTILGDKKVSVSATPGRTKHFQTLYVEPGLCLCDCPGLVMPSFVSTKAEMICSGILPIDQMRDHVPPISLVCQHIPRNILEATYGINIIRPREDEDPDRKPTAEELLTAYGYMRGFMTAHGQPDQPRSARYVLKDYVSGKLLYCHPPPGIDPDGFQHQHERCPESRTVQASGPVKPKKNTKAKQIENVVDKSFFHQENVRALMKGVRATMGYRPGSGLVSVPAPSAGSVVGKPWKKHGNRNKKEKVRRITKHLEN | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity).
Sequence Mass (Da): 73831
Sequence Length: 653
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q9W590 | MGKKNKGGAPNLGRQLIKDRFGHTQRRKVDNDTMLHTTELQDGYDWGRLNLSSVTEESSFQAFLRTAELAGTEFQAEKLNITFVNPKQRVGLLSKTQEQRMHQKHDEHRDQLKIPRRPKWTKETSAEELVRAENEAFLDWRRDLALLQEDEEILMTPYEKNLEFWRQLWRVVERSDVVVQIVDARNPLLFRSADLERYVKEVEPSKMNMILVNKSDLLTEEQRRHWAEYFDSEGIRTAFYSATLVEEELKREAEECLDSFPEVQQLRRAVEEIKQSLDSVEDALNVIEQKYKTIPETQNDELPRLPGDKNSPRLLSRLELIEFLRNIYTGPRHTEQHVTVGMVGYPNVGKSSTINSLMTVKKVSVSATPGKTKRFQTLFLDKDILLCDCPGLVMPSFVLTKADMLLNGILPIDQMRDHVPAVNLLCERIPRHVLEDKYGIVIAKPLEGEDMERPPHSEELLLAYGYNRGFMTSNGQPDQARSARYVLKDYVNGRLLYAMSPPSVPQTEYHTFPERQRRVIEESQLPGQQQRAMRINKSTSKELDNQFFSDKPTHAHVKGRTNFPNVRLANDGSLVAGNDPAAKPWRHVKKERREKLRKKFSHLDEH | Function: GTPase required for the nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of Nmd3 from the 60S ribosomal subunit after export into the cytoplasm. Regulator of body size; acts in serotonergic neurons to regulate insulin signaling and thus exerts global growth control.
Sequence Mass (Da): 70246
Sequence Length: 606
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q9H089 | MGRRRAPAGGSLGRALMRHQTQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLDDFLATAELAGTEFVAEKLNIKFVPAEARTGLLSFEESQRIKKLHEENKQFLCIPRRPNWNQNTTPEELKQAEKDNFLEWRRQLVRLEEEQKLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEMDANKENVILINKADLLTAEQRSAWAMYFEKEDVKVIFWSALAGAIPLNGDSEEEANRDDRQSNTTKFGHSSFDQAEISHSESEHLPARDSPSLSENPTTDEDDSEYEDCPEEEEDDWQTCSEEDGPKEEDCSQDWKESSTADSEARSRKTPQKRQIHNFSHLVSKQELLELFKELHTGRKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYVEPGLCLCDCPGLVMPSFVSTKAEMTCSGILPIDQMRDHVPPVSLVCQNIPRHVLEATYGINIITPREDEDPHRPPTSEELLTAYGYMRGFMTAHGQPDQPRSARYILKDYVSGKLLYCHPPPGRDPVTFQHQHQRLLENKMNSDEIKMQLGRNKKAKQIENIVDKTFFHQENVRALTKGVQAVMGYKPGSGVVTASTASSENGAGKPWKKHGNRNKKEKSRRLYKHLDM | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (Probable).
Sequence Mass (Da): 75225
Sequence Length: 658
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q3UM18 | MGRRRAPGGGSLGRVLIRQQTQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLEDFLATAELAGTEFVAEKLNIKFVPPEARTGLLSFEESQRIKKLHEENRQFLCIPRRPNWDRKTSPEELKQAEKDNFLKWRRQLVRLEEEQKLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSALAETDHLNGDLKEEVDSVAGDTNKTESESSSLDANEIPHRDLISLSEESASDSGDSKYEDCQEDEEEDWQTCSEEDSVPEEEEGCNADSETQNRKNAENQQVNNDSYLVSKQELLELFKKLHTGKKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYVEPGLCLCDCPGLVMPSFVSTKAEMICNGILPIDQMRDHVPPVSLVCQNIPRRVLEVTYGINIIKPREDEDPYRPPTSEELLTAYGCMRGFMTAHGQPDQPRSARYILKDYVGGKLLYCHPPPGKDPVAFQHQHQQLLESKVKGGELRLQPGKGRKAKQIENVVDKTFFHQENVRALTKGVQAVMGYKPGHGLVTAAAASAENVPGKPWKKHGNRNKKEKSRRLYKHLDV | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity).
Sequence Mass (Da): 73157
Sequence Length: 644
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q88W75 | MWIYLILMVALVIIDQVIKAAIVSHIALGASTSIVTGLLSLTNLHNNGAAWSILEGKMWFFYLISVIALIVMGYLLWRLRGKWLYEVGISLMIAGTLGNFIDRLRIGYVVDMFQLDFINFPIFNFADSCLTVGVIFILIGVLRDDSFEK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16765
Sequence Length: 149
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
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Q38X31 | MLLYIILGLLILVGDQLLKGWIVANVSYGALHTVIPNILGLTYVQNDGAAWSMLAGQQWFFYIVTIIAVGVIGYLFYTSERSEKLYRIGLTLMLAGALGNFIDRLHLKYVVDMFQLEFINFPIFNVADTALTCGVICVFIAILLKEKVTHD | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16893
Sequence Length: 151
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
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Q6AE72 | MATSRTAPTRAPSLRSSPALEASPSRTKASVGALVILAVVALCVYLMDQITKALVVSNLSEGQQVAVLGQLLQLHFVKNPGAAFSIGSGSTWIFSLVGVGVLGFVIWYAPRIRSTAWAILFGLLLGGLLGNLTDRLFREPGFGVGHVIDFLQIPLLTAIFNLADVAIVFSMGLFLLLTLRGIGLDGRRQRDEGAGVSSASPAGDESAADKPENLSA | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22631
Sequence Length: 216
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
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Q72PS8 | MKYFEKRFLDVYRPIYLGVIFLGIVLDLVTKFLVILYFQPHRYLEVFGSFFRMTLTFNTGFVFGAFQDNAIPSLIATGVAIVFLIGYRWKNHDLGNPWGWNLVMAGAFGNFLDKFFVKIPGTGFRFGFQPNMGEYIGVVDFLDFDWPDFLLFSRWPAFNVADSCVTIGLTILIFTMKLEEEK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21088
Sequence Length: 182
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q1WTX7 | MWLYIPMIIILIIADQGLKFWISVNIKLGTSQVILPNVLALTNVRNDGAAWSVLSGQQWFFTVITIVALGLMGYFFWKLRSDNLYMLAISLLIAGTLGNFIDRIRLGYVVDMFETLFMNFPIFNVADMCLTFGVIIVIIALIKDEKDE | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16802
Sequence Length: 148
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
|
Q8EWS0 | MIKQFFSNVYEGIKHYSNYLWELSKKQLIKIYLNKKHLIWKISIILICAFIVLLTSFLTRNSILNATQSYWELIPGFLVINITGNTGVSFGTLGDSNPSLVYFVQSIPIVLGFFVLLFSSNYLLDIGVSLVFFGGLSNIIDRSIVDNYKYLSGISTNNAVVDYFQFPFIKNSAIFNFPDTFVIIGMIFVGIQIIISFVKDYKKEKDSEENKKPIKDVVLDEERNKTKKEPIKKPIVIQKS | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27483
Sequence Length: 240
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
|
C6BV90 | MNKYFLAGIISVVTLVLDQVTKIAVREKMVLWTSETVIPGFFNLVHVVNKGAAFGFLNRADITWQRNFFVVVTIIALGAIGMLLKSAEEKDKFQILGLGFVLGGAIGNLIDRILYHQVTDFLDFYYGSHHYPAFNVADIAICLGAFAMIVSFYKNK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17400
Sequence Length: 156
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
C5BQX3 | MHKLNVLAALKWYGVALLVILLDQITKNVASHMLVLHQPEPITSFFNFTLRHNFGAAFSMFHDAGGWQRWFLALLAAGVSVLLIFWIAKLPKQKWMEALALALVLGGALGNLYDRMLLGYVVDFIVVHYKEHEWPAFNIADSAICIGAALLVWDSLFGTKVAKYGDAK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18770
Sequence Length: 168
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
B5YJT2 | MSLKLYKTSISIFLILLIDQITKYLAIKFLSPDGIVKLLPFLNLVYVENTGTAFGMFKFLGSGFFIIIALVVTGFLVYMYFKDTQNWFIYSLIIAGALGNIIDRLIYGYVIDFIDLHLKNLHWPAFNVADSAISIGIVLFVYKNLKK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16734
Sequence Length: 147
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
C4LD11 | MMSLLTGTGLRWMWLAVFAIVLDQAAKLAIMQHIPYGHGVVITPFFNLVHVYNTGAAFSFLADAEGWQRWLFSGLAIVISGVLAVAMAKAPAKCSLSNLAYSLVIGGAIGNLIDRVVYGHVVDFLDFHWQDLYHFAAFNVADMAISCGAVFIILDGFIKKPADK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17850
Sequence Length: 164
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
Q73JG0 | MNNKKDYYLPFLLTAIVIVVDQVTKILVVQYMSVNEVIPVIGDLVNLRFVYNTGAAFSLGAGFGEIARKILLVFLPFLLLIALTGAYLKSAELTRAQRWFICGILGGGFGNLIDRFFRSEGVVDFIDVKFFGILGMERWPTFNAADSFIVCCGIGLGVNLILQGIKQKKLKDS | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19150
Sequence Length: 173
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
O83943 | MKLTRIQKEKWIPLFAAGLVVVLDQCAKLLVGAYVPTNTSGVRVLGDFVRIVHVYNVGAAFSIGHQLNQVLRTLVLGIVPLIIMFLIVFSYFRTDAFCPVQRWAVSGIIGGGIGNLIDRFLRPNGVLDFIDVKFFGIFGFERWPAFNIADAVIMTCGLLLIISFIKQEKEISSQPSCNETGGVFRT | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20596
Sequence Length: 186
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
Q83G22 | MTTRTLRFYALVGFLVFLDQVTKYLAHAYLARDFIVIPNLFRLTLAKNSGAAFSFGTGFSWLFFLLGIIALIFIGWFLPRTTGSIVFLALLQGGIAGNVFDRLFKPPYFGNGEVVDFLNTPLLSGVVFNIADLFILAGVFGTFLFLKGSK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16609
Sequence Length: 150
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
|
Q9KU46 | MSNSSLALKQSGLRWLWLALLVFIADITIKLIVMDNMGYGWANRIEVLPFFNLLYVHNYGAAFSFLSDQEGWQRWLFTGIAFVVTGMLAYWMRRLPASDKWNNIAYALIIGGAVGNVFDRIVHGFVVDYLDFYWGTYHWPAFNLADSTICIGAAMIILDGFRAKKSAPSQS | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19390
Sequence Length: 171
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
Q8D2R1 | MKTKSNLIIISIFLIDFFTKKWILNNYEIFDSIKIFPMIKITYIRNYGIALGLFQSYSNLIRILIIVISIFILLFIFYMKNLCKDLLSNLGYSIIIGGSFGNIFDRIFYGSVIDFIDIYIYKWHFPVFNFADISIFIGFLILIYNKKIFIVNT | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18085
Sequence Length: 153
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
|
Q7M9M1 | MRIALFRSLGLFVLVFAIDQAIKALILGGFRWESEALSITLAFNKGVAFSMFAFLEGWLKYIQLGMLGGILLFLAYDRSFFVAHYLPLSILLAAGFSNILDRFIHGGVVDYVYWHYGFEFAIFNFADVMIDVAVALFLWQTFFKQK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16675
Sequence Length: 146
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
|
Q8ZKP9 | MHVTLVEINVHDDKVEQFIDVFRQNHLGSIKEPGNLRFDVLQDPQVLTRFYIYEAYVDEQAVAFHKTTPHYKTCVEQLEPLMTGPRTKKVFMGLMP | Function: Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-phosphonooxypentane-2,4-dione (P-HPD).
Catalytic Activity: (2S)-2-hydroxy-3,4-dioxopentyl phosphate = 3-hydroxy-2,4-dioxopentyl phosphate
Sequence Mass (Da): 11234
Sequence Length: 96
Subcellular Location: Cytoplasm
EC: 5.3.1.32
|
A1JJ50 | MHVTLVEINVKEDKVEQFVEVFRANHQGSLLEPGNLRFDVLQDESIPTRFYIYEAYVDEAAVAAHKKTPHYLRCVEELEGLMTGPRKKTTFIGLMP | Function: Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-phosphonooxypentane-2,4-dione (P-HPD).
Catalytic Activity: (2S)-2-hydroxy-3,4-dioxopentyl phosphate = 3-hydroxy-2,4-dioxopentyl phosphate
Sequence Mass (Da): 11050
Sequence Length: 96
Subcellular Location: Cytoplasm
EC: 5.3.1.32
|
Q8GYS8 | MKIGVVLVLLTVFVVVMSSTSVSAQSDEDECLKETGQMQLNCFPYLTDNRIHTPSFACCSEVYTVGKTYVDCFCQFINNGGPSFGIVVSQKLLDLPELCGVYGACGNGKNFKNTSL | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12580
Sequence Length: 116
Subcellular Location: Cell membrane
|
F4HZB9 | MILAILALVIATFLYGGATTVQAGCRDTLTSLSPCLYYLNGGSSSPSWSCCRQFSTVVQSSPECLCSVVNSNESSFYGFKFNRTLALNLPTACNVQTPSPSLCNTGGNVPTTLPANTPVGSPRSAPSPSGTTSPANTPSGSKKFPLSNESSSKSNVIILSFVSIALVLAII | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17664
Sequence Length: 171
Subcellular Location: Cell membrane
|
Q9LJ85 | MSKIISLVVAMIAVLALPIRGQQQPLSQCTPSMMTTVSPCMGFITNSSSNGTSPSSDCCNSLRSLTTGGMGCLCLIVTGTVPFNIPINRTTAVSLPRACNMPRVPLQCQANIAPAAAPGPAATFGPSMSPGPETDPIVPEPTPAAQTPQSDTTRPFTPSVDGGAPTSDDGGSTSRPSETPSSAYALSPSLLFFSIALVALKFY | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20779
Sequence Length: 203
Subcellular Location: Cell membrane
|
Q1G2Y5 | MNSNSFLISAALIFSLLSSNSPTSILAQINTPCSPSMLSSVTGCTSFLTGGGSFPTSDCCGALKSLTGTGMDCLCLIVTAGVPISIPINRTLAISLPRACGIPGVPVQCKASAAPLPTPGPASFGPTTSPTDSQTSDPEGSASFRPPTSPTTSQTPNDKDLSGSGNGGDPMGFAPPPPSSSPSSSHSLKLSYLLFAFAFTIIKFI | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20621
Sequence Length: 205
Subcellular Location: Cell membrane
|
Q9M2G1 | MARFMAYNQNPQMLALCITVAVMFLGVRSELSQDIKGCQDAMSDLYSCLPFVTNKAKAPDSTCCSTLKVKIDKGQTRKCLCTLVKDRDDPGLGFKVDANRAMSLPSACHVPANISQCPDLLHLLPDSPASQIFKQFTESSSQTVGHKAVSTSSSIKGRDNKQFGLMMAGALSIWYIM | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19291
Sequence Length: 177
Subcellular Location: Cell membrane
|
Q2PE60 | MKPSFVLLSIVLLLSSSLSDAADFGSPSQPPSMAPTPQPSNSTDCSSVIYSMVDCLSFLTVGSTDPSPTKTCCVGVKTVLNYSPKCLCSALESSREMGFVLDDTKALAMPKICNVPIDPNCDVSTPAASTPVSPPVESPTTSPSSAKSPAITPSSPAVSHSPPPVRHSSPPVSHSSPPVSHSSPPTSRSSPAVSHSSPVVAASSPVKAVSSSTASSPRAASPSPSPSPSISSSGILLVSKLFIAVVMVSSFLYILA | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25907
Sequence Length: 256
Subcellular Location: Cell membrane
|
Q9STH5 | MAQTTTLILLLATLLVAATTVSGQGPHIPLAPSPSVNEAMNCAAGLAVCLPAITQRGPPSQECCTAVETALTTQLSCLCGFIKSPMLLIPFNVTDFNALFSKTCGLTTDPNLCSETAAQAPLPKTAAPVPGAPKSDKDAASKLAGTGLVGIVVITIAAMFY | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16330
Sequence Length: 161
Subcellular Location: Cell membrane
|
F4JIG1 | MATKITGVFILILTITFSSSSAVTATQQAPSSSPPVLTCTEELVMFSPCLPYVSSPPNNMSETPDPICCSVFTSSVHSSTGNCLCYLLRQPMILGFPLDRSRLISLSQICTDQNSEESFESLCSVSESPELPPLQSIQFTNPFVSGNNVSASPQSVDLAPEVSPSSDLFSPETATLAPPPPPPPLPVLQYFSSDSLKIRNFWFPSTIIMTFATSILARI | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23547
Sequence Length: 219
Subcellular Location: Cell membrane
|
O49644 | MAYTNKVAVAVGAAVVFLAVVMNPRWTEAQTYPKLDRLCVMMIPDILEECFTHDRLKPTEDCCNDLKNATMTQVDCLCDNFLESLSFSDLSRTFSAGVLKKCDVSHKYMCQAAKNRGEAKGGRNSTTTCDNSITNTSVGGKNKVATSMSAFGLVAILLFVMF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17730
Sequence Length: 162
Subcellular Location: Cell membrane
|
Q1G3I0 | MAYTNQISAVVFLAVAIAPLLAEPQSTMFPEMTPECATVMPDLLEKCFATGSVTPTEDCCTDLKSATSTQVTCLCDNYIANPAVSNITGPYSKAITTKCGVFDKYSCDGTSKGGEEKKGGSSSSNGKDNGKSEGNGGRANSVAASMAMFGLLASLVFVMF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16587
Sequence Length: 160
Subcellular Location: Cell membrane
|
Q9FY78 | MAYFSTATSLLLLVLSVSSPYVHGASDCDTLVITLFPCLPFISIGGTADTPTASCCSSLKNILDTKPICLCEGLKKAPLGIKLNVTKSATLPVACKLNAPPVSACDSLPPASPPTANGQAPVWGSGWAPAPSPSKGNSLIPISGFSFVIVTALAMFRI | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16164
Sequence Length: 158
Subcellular Location: Secreted
|
Q9FFY3 | MMMGMKFFSFYVVLLLVAASSGMRINGQSVSCLNQLAPCLNYLNGTKEVPQVCCNPLKSVIRNNPECLCRMISNRWSSQAERAGIDVNDAQMLPARCGEHVNPIACLTRSRGGSTNSDRSSSIGNTFSQSYWMTTLAIAATVLSYCHHIIS | Function: Lipid transfer protein that promotes the number of phloem (pro)cambial and pericycle cells.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16532
Sequence Length: 151
Subcellular Location: Cell membrane
|
Q8VYI9 | MATHSSFTATTPLFLIVLLSLSSVSVLGASHHHATAPAPSVDCSTLILNMADCLSFVSSGGTVAKPEGTCCSGLKTVLKADSQCLCEAFKSSASLGVTLNITKASTLPAACKLHAPSIATCGLSVAPSTAPGLAPGVAAAGPETAGFLAPNPSSGNDGSSLIPTSFTTVLSAVLFVLFFSSA | Function: Probable lipid transfer protein (By similarity). Proteoglycan-like factor that exhibits xylogen activity consisting in mediating local and inductive cell-cell interactions required for xylem differentiation .
Location Topology: Lipid-anchor
Sequence Mass (Da): 17972
Sequence Length: 182
Subcellular Location: Cell membrane
|
O49645 | MAYTNKVTISAAVATMMLFLAVTIVDAQSMPPMPKFNPVCALADLPNIVQLCYFNLDLTPSEECCNDLKSSSTIQVNCLCDNFIAHPSNGNISQARYDLVNSACGVADKFACKGGDASGGSTNKIAASMVLLGLVASLFF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14753
Sequence Length: 140
Subcellular Location: Cell membrane
|
Q9SUV6 | MAVAVTAVLFLAVVIAPQWTETKKPPRPSDTSDTSGTSGRDRRTMCPLSIPGIVQNCYATLNAFPSKECCKDLKTASKREVTCLCNNVIAHPDPLYTNTNQVNKACGVLDKYACDAGNSNGGATKKIVASMGLFGVVASLFF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 15077
Sequence Length: 142
Subcellular Location: Cell membrane
|
A4F2N8 | MQLSSYHDVIKAAERLEGFANRTPVFTSRTLDAETGAQVFIKCENLQRTGSFKFRGAFNALSRFDEAQRKAGVVAFSSGNHAQGIALAARLLQMPATIVMPTDAPAAKVAATREYGATVVFYDRITEDREQIGRTLAEQHGMTLIPSYDHPDVLAGQGTAAKELLEFTGPLDALFVGLGGGGMLSGTALATRALSPDCLLYGVEPEAGNDGQRSFQTGSIVHIDTPATIADGAQTQHLGNHTFPIIRENVNDILTVSDAELVESMRFFMQRMKMVVEPTGCLGLAALRNLKQQFRGQRVGIIVTGGNVDIEKYASLLKG | Cofactor: Requires a divalent metal cation such as Mn(2+), Mg(2+), or Ca(2+).
Function: Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D,L-threo-3-phenylserine, D-serine, and L-serine, are not substrates for this enzyme . Exhibits no detectable serine and aspartate racemase activity . Might play a role in the detoxification of naturally occurring 3-hydroxyaspartate in Pseudomonas sp. T62 cells .
Catalytic Activity: (3S)-3-hydroxy-L-aspartate = NH4(+) + oxaloacetate
Sequence Mass (Da): 34333
Sequence Length: 319
EC: 4.3.1.16
|
P36007 | MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISGKEDGPTI | Cofactor: Requires a divalent metal cation such as Mn(2+), Mg(2+), or Ca(2+).
Function: Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D-serine, and L-serine, are not substrates for this enzyme. Exhibits no detectable serine racemase activity. Is responsible for the 3-hydroxyaspartate resistance of S.cerevisiae, and thus may be involved in the detoxification of naturally occurring 3-hydroxyaspartate.
Catalytic Activity: (3S)-3-hydroxy-L-aspartate = NH4(+) + oxaloacetate
Sequence Mass (Da): 34899
Sequence Length: 326
EC: 4.3.1.16
|
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