entry
stringlengths 6
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stringlengths 5
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| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
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stringlengths 7
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D2IYS2
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TORSO_BOMMO
|
Tyrosine-protein kinase receptor torso (EC 2.7.10.1)
|
MYSEGKLLKVFLIFAGFIIFSLCGEVVSQRYPPAPGLLKYLEQDVCYSLYYYLNWTSLADCKTNFEETGISDVPSTVKVRCQSKNSIRFETEPSEHWQLFILMEHDNFDPIPFTLIEPNNVFGELITTANKEYQIWSTYLDEYGTLQDWMEGPIVLKFDQRNQQPDDIKYNVTQEFKYIILGNDSYTINGKFVWNTTGDRDLCFDIANICQNTNMKHAKIWPTAHPSFDVENLVLNDECEIHVKGIHGTTKHKYKTPSCFELPECFLNNMEPEIPQDVAIAADQDLRGWWNINVAWAKPHFQPEIYNVTVRANMIRSIILPGNATETTFRNIPNTFLSAGKIYNVSVYAIIGQKASHTSRRAFTPGMLRWVWAGATAGAGCAAGGLLAATLLCCGHRRATSRVSQEDPDEKTPKEDDVEIIGIESGSADDHWEVRSDRVLLHEVIGEGAFGVVRRGTLAPGGKSVAVKMLKEFPSQEEVRSFRSEMELMKSVGAHPHVVSLVGCCSGRKPLIVAEYCSRGDLLSYLRSSWDIIVSKHTAKYYNNNMDSMDTSKLKVHKEHTKLVVNKLYELQGPCETELTPLDLLSFCRQIAMGMEFLASNRIVHRDLAARNVLVTEDKTLKIADFGLSRDIYEENQYKQKGNGKMPVKWMALESLTRRVYTTQSDVWSFGVVIWEIVTVGGSPYPEVPAARLVRSLRSGYRMPKPVNCSKPLYDIMRACWNASPRDRPTFPELHQKLDDLLHSACANEYITLEVDVDEAPSTPKPQRYIKMLIRGKLPWSRESYERPVNPTSNLYSSPPVIQTKTA
|
Probable receptor tyrosine kinase. During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone (PTTH) (By similarity). Binding to PTTH stimulates activation of canonical MAPK signaling leading to ERK phosphorylation.
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D2J0Y4
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CJ090_MOUSE
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(E2-independent) E3 ubiquitin-conjugating enzyme FATS (EC 2.3.2.-) (Centrosomal protein C10orf90 homolog) (E2/E3 hybrid ubiquitin-protein ligase FATS) (Fragile-site associated tumor suppressor homolog) (FATS)
|
MISPVVISRLIDEKKSMENGAILPQAIAQPQLCPTKPALARRDGVSMHRRFALSPDRLGILTPSDDQGLETEPLSTGDNLGKGSHSGFSSITITARRVGPPASSLVWDTFRDPLCPKCKAKDALFQEPPVLAGDAHLCQHNRPFTCTESPSNGSVEGMKVFQAHSRLSARQDYWVTHTNDNEDSFSSDNSPSRKVPLVFSSCVHFRVSQQCPNAIYYLDKSLSVPLERPQIASPKMHRSVLSLSLRCSSHQLTADGVDSSANGEPISTALSQELSEGKQDLLGPQWGQPQGGHWKESPALVPVHLGSGTCPRTGSPPLENVKFADVGRNQVPVRKEKEDHATCTSSSHTNQLSIHIPGWSYRAETKVLSGSKKQQQEAQRTLPAFPVGQKTIKHFPPEGDSSPSSDGQPSILSESNERQHPYFMIPRVPLPGFYCPLQTGCASLQEDGAVQIETHFPKDYTCCDLVVKLKECEKNEDPTVTPEPSPATPSPSTPEGAQSSDPSEDSYEPLLASSMTLQEALEVHRPQFISRSQERLQKLKRMVQQRKTQQKESLGQKQSLLPVRANKKQFTIPHPLSDNLFKPKERCISEKEMHMRSKRIYNNLPEVKKKKEEQKKRMILQSNRLRAEVFKKQLLDQLLQRNAV
|
Tumor suppressor that is required to sustain G2/M checkpoint after DNA damage. Acts as a p53/TP53 activator by inhibiting MDM2 binding to p53/TP53 and stimulating non-proteolytic polyubiquitination of p53/TP53. Exhibits ubiquitin ligase (E3) activity and assemble ubiquitin polymers through 'Lys-11'- (K11-), 'Lys-29'- (K29-) and 'Lys-63'- (K63)-linkages, independently of the ubiquitin-conjugating enzyme (E2). Promotes p53/TP53-dependent transcription of CDKN1A/p21, leading to robust checkpoint response. Mediates CDKN1A/p21 protein stability in a ubiquitin-independent manner. Interacts with HDAC1 and prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. May have a role in the assembly of primary cilia (By similarity).
|
D2KC46
|
PKHA8_CANLF
|
Pleckstrin homology domain-containing family A member 8 (PH domain-containing family A member 8) (Phosphatidylinositol-four-phosphate adapter protein 2) (FAPP-2) (Phosphoinositol 4-phosphate adapter protein 2)
|
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTRMDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSELRLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSELLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELNSCENGSLHMEINDGEEILMKNKSSLYLKPEIDCSISSEENTDDNITVQGEIMKEEGEDNLGNHDSSLAQPASDSSSSPPESHWEEGQEIIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMDLVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRAAPSYEDFVAALTIKEGDHQKAAFSVGMQRDLSLYLPAMEKQLAILDTLYEVHGLESDEVV
|
Cargo transport protein that is required for apical transport from the trans-Golgi network (TGN). Transports AQP2 from the trans-Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi network (TGN) to the plasma membrane and plays a pivotal role in the synthesis of complex glycosphingolipids. Binding of both phosphatidylinositol 4-phosphate (PIP) and ARF1 are essential for the GlcCer transfer ability. Also required for primary cilium formation, possibly by being involved in the transport of raft lipids to the apical membrane, and for membrane tubulation.
|
D2KX21
|
PLAT1_RAT
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Phospholipase A and acyltransferase 1 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (HRAS-like suppressor 1) (HRSL1) (Phospholipid-metabolizing enzyme A-C1) (Rat LRAT-like protein-2) (RLP-2)
|
MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPVDGIPSSFSSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFAIGQEVTYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQGAKS
|
Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity).
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D2W6T1
|
TET1_NAEGR
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Tet-like dioxygenase 1 (EC 1.14.11.80) (NgTet1)
|
MTTFKQQTIKEKETKRKYCIKGTTANLTQTHPNGPVCVNRGEEVANTTTLLDSGGGINKKSLLQNLLSKCKTTFQQSFTNANITLKDEKWLKNVRTAYFVCDHDGSVELAYLPNVLPKELVEEFTEKFESIQTGRKKDTGYSGILDNSMPFNYVTADLSQELGQYLSEIVNPQINYYISKLLTCVSSRTINYLVSLNDSYYALNNCLYPSTAFNSLKPSNDGHRIRKPHKDNLDITPSSLFYFGNFQNTEGYLELTDKNCKVFVQPGDVLFFKGNEYKHVVANITSGWRIGLVYFAHKGSKTKPYYEDTQKNSLKIHKETK
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Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), and thereby plays a role in active DNA demethylation. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC).
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D2WL32
|
GLGB3_ARATH
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1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic (AtSBE III) (EC 2.4.1.18) (Branching enzyme 1) (AtBE1) (Protein EMBRYO DEFECTIVE 2729) (Starch-branching enzyme 3)
|
MVSLSNQTRFSFHPNNLVVSEKRRLGISGVNFPRKIKLKITCFAAERPRQEKQKKKSQSQSTSDAEAGVDPVGFLTRLGIADRIFAQFLRERHKALKDLKDEIFKRHFDFRDFASGFELLGMHRHMEHRVDFMDWGPGSRYGAIIGDFNGWSPTENAAREGLFGHDDYGYWFIILEDKLREGEEPDELYFQQYNYVDDYDKGDSGVSAEEIFQKANDEYWEPGEDRFIKNRFEVPAKLYEQMFGPNSPQTLEELGDIPDAETRYKQWKEEHKDDPPSNLPPCDIIDKGQGKPYDIFNVVTSPEWTKKFYEKEPPIPYWLETRKGRKAWLQKYIPAVPHGSKYRLYFNTPDGPLERVPAWATYVQPEDEGKQAYAIHWEPSPEAAYKWKYSKPKVPESLRIYECHVGISGSEPKVSTFEEFTKKVLPHVKRAGYNAIQLIGVPEHKDYFTVGYRVTNFFAASSRYGTPDDFKRLVDEAHGLGLLVFLDIVHSYAAADQMVGLSLFDGSNDCYFHYGKRGHHKHWGTRMFKYGDLDVLHFLISNLNWWITEYQVDGYQFHSLASMIYTHNGFASFNNDLDDYCNQYVDRDALMYLILANEILHVQHPNIITIAEDATYYPGLCEPVSQGGLGFDYYVNLSASEMWVSLLDNVPDNEWSMSKIVSTLVANKEYADKMLSYAENHNQSISGGRSFAEILFGGVDNGSPGGKELLDRGISLHKMIRLITFTSGGRAYLNFMGNEFGHPERVEFPTQSNNFSFSLANRRWDLLESGVHHHLFSFDKELMDLDKSKGILSRGLPSIHHVNDANMVISFSRGPFLFIFNFHPSNSYEKYDVGVEEAGEYTMILNSDEVKYGGQGIVTEDHYLQRSISKRIDGQRNCLEVFLPSRTAQVYKLTRILRI
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Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Essential during embryogenesis.
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D2X8K2
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PA2_CONGI
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Phospholipase A2 A2-actitoxin-Cgg2a (A2-AITX-Cgg2a) (EC 3.1.1.4) (CgPLA2) (Phosphatidylcholine 2-acylhydrolase)
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GVWQFAYMIAKYTGRNPLDYWGYGCWCGLGGKGNPVDAVDRCCYVHDVCYNSITQGPRPTCSRIAPYHKNYYFTGKKCSTGWLTSKCGRAICACDIAAVKCFRRNHFNKKYRLYKKNIC
|
Sea anemone phospholipase A2 (PLA2). When incubated with plasma, this protein shows a moderate anticoagulant activity (0.15 ug of enzyme/200 uL of plasma), inhibiting clotting induced by thrombin. This enzyme also induces myotoxicity, and edema. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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D2XV59
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GTPB1_RAT
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GTP-binding protein 1
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MAAERSRSPVDSPVPASMFAPEPSSPGAARAAAAAARLHGGFDSDCSEDGEALNGEPELDLTSKLVLVSPTSEQYDSLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQESGGRVRDYLVRKRVGDNDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQRLVFREGRTKAVGTITKLLQTTNNSPMNSKPQQIKMQSTKKGPLSKREEGGPSGVPAAGPPSTGDEASSLGTTQAATSSGLQPQPKPSSGGRRRGGQRHKVKSQGACVTPASGC
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Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity.
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D2Y1X6
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H1A01_CYRHA
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Mu-theraphotoxin-Hhn2b 1 (Mu-TRTX-Hhn2b) (Hainantoxin-I) (HnTx-I) (Peptide F5-19.03)
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MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFAVDDFKGEERECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK
|
Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin).
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D2Y1X7
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H1A02_CYRHA
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Mu-theraphotoxin-Hhn2b 2 (Mu-TRTX-Hhn2b) (Hainantoxin-I) (HnTx-I) (Peptide F5-19.03)
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MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFTVDDFKGEERECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK
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Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin).
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D2Y1X8
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H1A03_CYRHA
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Mu-theraphotoxin-Hhn2b 3 (Mu-TRTX-Hhn2b) (Hainantoxin-I) (HnTx-I) (Peptide F5-19.03)
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MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFAVDDFKGEVRECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK
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Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin).
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D2Y1X9
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H3A01_CYRHA
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Hainantoxin-III 1 (HnTx-III) (Hainantoxin-3) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
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Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y1Y0
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H3A02_CYRHA
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Hainantoxin-III 2 (HnTx-III) (Hainantoxin-3.2) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMYLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
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Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y1Y1
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H3A03_CYRHA
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Hainantoxin-III (HnTx-III) (Hainantoxin-3.3) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFALDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
|
Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y1Y2
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H3A04_CYRHA
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Hainantoxin-III 4 (HnTx-III) (Hainantoxin-3.4) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMYLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGKERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
|
Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y1Y3
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H3A05_CYRHA
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Hainantoxin-III 5 (HnTx-III) (Hainantoxin-3.5) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASRFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
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Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y1Z4
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H3A06_CYRHA
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Hainantoxin-III 6 (HnTx-III) (Hainantoxin-3.6) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMFLALAGLVLLFVVGYASESEEKESPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
|
Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y1Z7
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H3A07_CYRHA
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Hainantoxin-III 7 (HnTx-III) (Hainantoxin-3.7) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
|
MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKVFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
|
Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y1Z8
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H3A08_CYRHA
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Hainantoxin-III 8 (HnTx-III) (Hainantoxin-3.8) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFTGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
|
Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y232
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H4A01_CYRHA
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Mu-theraphotoxin-Hhn1b 1 (Mu-TRTX-Hhn1b) (Hainantoxin-4) (Hainantoxin-IV) (HnTx-IV) (Peptide F8-18.88)
|
MKASMFLALAGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK
|
Neurotoxin that selectively inhibits neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) (IC(50)=44.6 nM). It is active on Nav1.2/SCN2A (IC(50)=22.4 nM), Nav1.6/SCN8A (IC(50)=50.1 nM) and Nav1.7/SCN9A (IC(50)=48.9 nM). It shows low affinity for lipid bilayers.
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D2Y233
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H4A02_CYRHA
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Mu-theraphotoxin-Hhn1b 2 (Mu-TRTX-Hhn1b) (Hainantoxin-4.2) (Hainantoxin-IV.2) (HnTx-IV.2) (Peptide F8-18.88)
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MKASMFLALAGLDLLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK
|
Neurotoxin. Selectively blocks neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) with an IC(50) of 44.6 nM. Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels.
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D2Y2D1
|
H3A09_CYRHA
|
Hainantoxin-III 9 (HnTx-III) (Hainantoxin-3.9) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
|
MKASMFLALAGLALLFVVCYASESEEKEFPIELLSKIFAVDVFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
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Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y2D2
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H3A10_CYRHA
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Hainantoxin-III 10 (HnTx-III) (Hainantoxin-3.10) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMFLALAGLVRLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
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Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y2D3
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H3A11_CYRHA
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Hainantoxin-III 11 (HnTx-III) (Hainantoxin-3.11) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMFLALAGLVLLFVVGYASESEEKDFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
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Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Y2D7
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H4A03_CYRHA
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Mu-theraphotoxin-Hhn1b 3 (Mu-TRTX-Hhn1b) (Hainantoxin-4.3) (Hainantoxin-IV.3) (HnTx-IV.3) (Peptide F8-18.88)
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MKASMFLALTGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK
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Neurotoxin. Selectively blocks neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) with an IC(50) of 44.6 nM. Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels.
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D2Y2I3
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H3A12_CYRHA
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Hainantoxin-III 12 (HnTx-III.12) (Hainantoxin-3.12) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
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MKASMFLALAGLVLLFVVGYASGSEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
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Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state.
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D2Z026
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DCSC_STRLA
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O-ureido-serine racemase (EC 5.1.1.19)
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MIRMRTPSTLPFTKMHGAGNDFVVLDLRDGPDPSPELCRALADRHKGVGCDLVLGIREPRSARAVAAFDIWTADGSRSAQCGNGARCVAAWAVRAGLARGPRFALDSPSGTHEVDVLDADTFRVALAVPRFAPESIPLFGHDGEQDLYEADLGDGTRVRFAAVSMGNPHAVIEVDDTATAPVARVGRAVQASGLFLPTVNVGFARVESRDRVHLRVHEYGAGETLACGSGACAAAAVLMRRGRVDRNVSVVLPGGELRISWPDDAADVLMTGPAAFVYEGTFLHASV
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Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the stereoinversion of O-ureido-L-serine to O-ureido-D-serine.
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D2Z027
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DCSD_STRLA
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O-ureido-L-serine synthase (EC 2.6.99.3) (Cysteine synthase homolog DscD) (EC 2.5.1.47) (O-acetylserine sulfhydrylase)
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MPLFNSILDTIGRTPIVRLQRMAPEHTSVYVKVESFNPGGSVKDRLALSVVLDAEAKGLLKPGDTIVECTSGNVGIALAMVAAARGYRFVAVMGDTYSVERRKLIRAYGGKLVLFPGHLGSKGGNLIADELAEKYGWFRARQFDNPANPSYHRETTASEILADFAGKRLDHFVTGFGTTGTLTGVGQMLRVARPEVRVVALEPSNAAMLARGEWSPHQIQGLAPNFVPGVLDRSVIDDLVTMDEVTARDTSRRLAAEEGIFAGISAGATVATALSIAEHAPEGTVLLAMLPDTGERYLSTFLFDGVDEGSDDAWLASLDTGSGL
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Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the addition of hydroxyurea on O-acetyl-L-serine (OAS) to yield O-ureido-L-serine. It prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate.
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D2Z028
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DCSE_STRLA
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L-serine/homoserine O-acetyltransferase (EC 2.3.1.30) (EC 2.3.1.31) (Homoserine O-trans-acetylase)
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MREFIPPASRFIELPDGFAMRRGGALYGARIAYETFGSLNAARDNAVLVLTGLSPDAHAASRPDDPTPGWWEAMVGPGKPVDTDLWHVICVNSLGSCKGSTGPASTDPRTGEPYRLSFPELSIEDIADAAAHTVRALGISRLACVVGASMGGMSALALLARHPELARTHISLSGAVHALPFSIAVRSLQREAIRSDPGWLQGHYDEGEGPRRGMLTARKLGMMTYRSAQEWDCRFGRTRIGERRRADQGRFGPEFEVESYLDFHAQRFADRFDPNSYLYLSHAMDQFDLGDGGGGGGGAPGALSRMRVERALVMGARTDILFPLSQQQEIADGLSAGGADVSFLPVDTPAGHDAFLVDIERFGPPVAKFLAIVA
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Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over L-homoserine.
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D2Z030
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DCSG_STRLA
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Cycloserine biosynthesis protein DcsG (EC 6.3.3.5)
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MGILALVTDAVSLPIDYDMPPLLEACRTVGITAEVCDWEDGTVDWSRFEAVVFRSPWTWAERQAEFLAFCERVSHVTRLITPMPLVRWALDKRYLADLAAHGVPVIPTTVVAPGSDALAAVRDFLAARPEAREFVVKPTDGCYSKDVQRYQRSLAEPASRHVARLLANGSHVILQPYVESVDRHGETDLTFFDGVYSHAIHKGAMLMPDGTVHVPTLDFRQARDADEDQRAVAAAALAASVAHLGLDLPLVCGRVDLVRGADGSPMVLEMELCEPSLNLTFSEDGALRFAQALAERLKP
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Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the synthesis of D-cycloserine from O-ureido-D-serine (D-OUS). It reacts with D-OUS, D-homocysteine and beta-aminooxy-D-alanine.
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D3DJG4
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SOXA1_HYDTT
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L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit diheme) (Protein SoxA1) (SoxAX cytochrome complex subunit A1) (Sulfur oxidizing protein A1) (Thiosulfate-oxidizing multienzyme system protein SoxA1) (TOMES protein SoxA1)
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MGKWVTIIFVLFLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDSEAGKRVFLQTVVAVKEDKVATHWPAYRFSNDQLWTMEDRIRGCFGDMRVAPPEHFHWAVVALNLYLSYKAKGGVVRVPGFIY
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C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
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D3DJG5
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SOXA2_HYDTT
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L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit diheme) (Protein SoxA2) (SoxAX cytochrome complex subunit A2) (Sulfur oxidizing protein A2) (Thiosulfate-oxidizing multienzyme system protein SoxA2) (TOMES protein SoxA2)
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MRKLWFLPILLGAVGGVSLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDTFGGQRIRLQTLAKVKEDKVATHWPAYRFSNDQLWTMEDRIRGCYNQIRVTPPPHFSWPQIALSLYMAYESKGGTIETPGFVR
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C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
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D3DKC4
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GLYA_HYDTT
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Serine hydroxymethyltransferase (SHMT) (Serine methylase) (EC 2.1.2.1) (L-threonine/L-allo-threonine aldolase) (EC 4.1.2.48)
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MRHLFNTDAEIYEAIVKEYERQFYHLELIASENFTSLAVMEAQGSVMTNKYAEGLPHKRYYGGCEFVDIAEDLAIERAKALFDAEHANVQPHSGTQANMAVYMAVLKPGDTIMGMDLSHGGHLTHGAKVNFSGKIYNAVYYGVHPETHLIDYDQLYRLAKEHKPKLIVGGASAYPRVIDWAKLREIADSVGAYLMVDMAHYAGLIAGGVYPNPVPYAHFVTSTTHKTLRGPRSGFILCKKEFAKDIDKSVFPGIQGGPLMHVIAAKAVAFKEAMSQEFKEYARQVVANARVLAEEFIKEGFKVVSGGTDSHIVLLDLRDTGLTGREVEEALGKANITVNKNAVPFDPLPPVKTSGIRLGTPAMTTRGMKEDQMRIIARLISKVIKNIGDEKVIEYVRQEVIEMCEQFPLYPELREEINHLAKIKATY
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Its primary function is to catalyze the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-threonine, L-allo-threonine, L-threo-beta-phenylserine and L-erythro-beta-phenylserine. This second activity is likely to be physiological in H.thermophilus, which is an organism that lacks the ortholog gene for the 'real' threonine aldolase characterized in mesophilic bacteria (LtaE), yeast and plants.
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D3GDK4
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GUN_CRYAT
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Endoglucanase (EC 3.2.1.4) (CaCel) (Cellulase) (Endo-beta-1,4-glucanase)
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MKVFVVLAAIVAIANGLTSGSGVTTRYWDCCKPSCSWGGKASVTKPVRTCKANGNTTIDSNTQSGCNGGSSYVCNDQQPFTQGNVGYGFAAASISGQPESQTCCACYEMTFTNTAISGQKMIVQVTNTGSDLNGNHFDLMIPGGGVGIFNGCQSQWGAPSNGWGQRYGGISSQSECNQLPTSLRAGCNWRFGWFKNADNPSMKFTQVRCPTILTQKSQCVRTPGP
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Hydrolyzes carboxymethylcellulose (CMC). Hydrolyzes also lichenan and barley beta-1,4-D-glucan. CMC is hydrolyzed majorily to cellobiose (G2), cellotriose (G3) and cellotetraose (G4). Cellohexaose (G6) is hydrolyzed to G4 and G2 with traces of G3. Cellopentaose (G5) is completely hydrolyzed to G2 and G3, and G4 is partially hydrolyzed to G2. Does not hydrolyze G2 or G3. Does not hydrolyze crystalline cellulose, soluble starch, xylan, mannan or laminarin.
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D3GE74
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STR1_MEDTR
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ABC transporter G family member STR (EC 7.6.2.-) (Protein STUNTED ARBUSCULE)
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MARLERDGTNKSLESLMDSHKPGGTTTNLNQLRTQKSIPGYGLEFTNLSYSIIKKQKKDGVWINKETYLLHDISGQAIKGEIMAIMGPSGAGKSTFLDALAGRIAKGSLQGSVRIDGKPVTTSYMKMVSSYVMQDDQLFPMLTVFETFMFAAEVRLPPSISRDEKKKRVHELLNKLGLQSATHTYIGDEGRRGVSGGERRRVSIGIEIIHKPSLLFLDEPTSGLDSTSAYSVVEKIKDIAQGGSIVLMTIHQPSFRIQMLLDKITILARGRLIYMGRPDALHTHLSGFGRPVPDGENNIEYLLDVITEYDQATVGLDPLVQYQHDGHKPDPAAMTPVPKPPRTPYRRNTPASKHMISLRSQGFTAGTPQPDSSQFGLDDDDNDDDENFDNSLERRSVQTSRNIVTSGVYPRLASQFYQDFSAKDFSVWLYNGVVGTPRRPPSWTPARTPGWTPGKTPLSGPRSFVSNQHSASYQDPYYIQKTNTVVGQSMDYSATSYAPSYEEFEIEEVLDEPDLGPKYANPWLREVAVLSWRTVLNVIRTPELFASREIVLTVMALVLSTIFKNLGDTTFIDINRLLNFYIFAVCLVFFSSNDAVPSFIMERFIFIRETSHNAYRASSYVISSLIVYLPFFAVQGLTFAVITKLMLHLKSNLFNFWMILFASLITTNAYVMLVSALVPSYITGYAVVIATTALFFLTCGFFLKRTQIPAYWKWLHYISAIKYPFEGLLINEFKNNRGCYSGNKADLSPGPLGDVKPSKHHNASLPLNCLLGEDVLSTMDITMESLWYDILILLAWGVLYRFFFYLVLRFYSKNERK
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Together with STR2, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis.
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D3J162
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VPY_MEDTR
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Protein VAPYRIN (MtVpy) (Protein HERMES)
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MDRLIKLDPSNIVLIRVEEGQKCLGKITLNNVMYTMPVAFRIQPLIKTRYTIKPQSGIISPLASLVIEITYHPPQQQGSNNLPHSFPFSDDSFLLHSVLAPGAAIKEPSSMFDSVPSDWFTTKKKQVFIDSAIKVMFVGSQILTQLVEDGNSMDDIREVLEKSDPLWESVNSKDSQGQTLLHLAISKTRPDLVQLILEFKPDIEAINSVGSTPLEAASSSGESLIVELLLAHKANTEGSESSVFRPIHHASREGHMEILRLLLLKGARVDSLTKDGNTSLHLAVEEKRRDCARLLLANGARTDVRNMREGDTPLHIAAANGDENMVKLLLHKGATKYVRNKLGKTAFDVAAENGHSRLFDALRLGDNLCAAARKGEVRTIQKVLESGGVINGRDQNGWTSLHRAAFKGRMDAVRFLVEKGIDLDAKDEDGYTALHCAAESGHADVTEFLVKKGADVEARTNKGVSALQIVESLNYVGITRILVNGGASREGLGEKPPSAPSKIPFGRKVESGSVMTMKKKMSSRTRALRGSFDHSMPLAVL
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Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme and Gigaspora gigantea) both during fungal passage across root epidermis and for arbuscule formation in cortical cells this symbiosis promotes phosphorus (P) and copper (Cu) uptake. Essential for infection by symbiotic nitrogen-fixing rhizobial bacteria (e.g. Sinorhizobium meliloti) leading to the formation of root nodules.
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D3K0R6
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AT2B4_BOVIN
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Plasma membrane calcium-transporting ATPase 4 (PMCA4) (EC 7.2.2.10)
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MTNPTEHTLPSNSILESREGEFGCTVMDLRKLMELRSSDAIDQINVHYGGVMNLCSRLKTNPVEGLSGNPADLEKRKQVFGQNLIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPPGGENEQCGLAVTSPEDEGEAEAGWIEGAAILFSVIIVVLVTAFNDWSKEKQFRGLQNRIEKEQKFSVIRNGHIIQLPVAEIVVGDIAQIKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLERDPMLLSGTHVMEGSGRMVVTAVGINSQTGIIFTLLGASEGEEEEKKKKGKKQGVPENRNKAKTQDGVALEIQPLNSQEGIDSEEKEKKAAKLPKKEKSVLQGKLTRLAVQIGKAGLIMSAITVLILILYFVIDNFVIQRRPWLAECTPIYVQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMSVVQAYIGDTRYHQIPSPDDLVPKVLDLIVNGISINSAYTSKILPPEKEGGLPRQVGNKTECALLGFVSDLKQDYHAVRSEVPEEKLYKVYTFNSVRKSMSTVIEKPGGGYRMYSKGASEIILRKCNRILDKKGEAVPFKNKDRDEMVRTVIEPMACEGLRTLCIAYRDFNDGEPPWDNESEILTELTCIAVVGIEDPVRPEVPEAIAKCKRAGITVRMVTGDNINTARAIATKCGIVTPGDDFLCLEGKEFNRLIRNEKGEVEQEKLDKIWPKLRVLARSSPTDKHTLVKGIIDSTVGDQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTDSLLKRRPYGRNKPLISRTMMKNILGHAVYQLTVIFFLVFAGEKFFDIDSGRRAPLHSPPSQHYTIIFNTFVLMQLFNEINSRKIHGERNVFSGIFRNLIFCSVVLGTFISQIIIVEFGGKPFSCTKLTLSQWFWCLFIGIGELLWGQVISTIPTQSLKFLKEAGHGTTKEEITKDAEGLDEIDHAEMELRRGQILWFRGLNRIQTQIKVVKAFHSSLHESIQKPKNQNSIHNFMTHPEFTIDEEGPRTPLLDEQEEEIFEKVSKPGTKTSSLDGEVTPQTNKNNNTVDCCQVQIVASHSDSPLHSLETSV
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Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (By similarity). By regulating sperm cells calcium homeostasis, may play a role in sperm motility (By similarity).
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D3K5I7
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NCAP_RVFV
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Nucleoprotein (Nucleocapsid protein) (Protein N)
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MDNYQELAIQFAAQAVDRNEIEQWVREFAYQGFDARRVIELLKQYGGADWEKDAKKMIVLALTRGNKPRRMMMKMSKEGKATVEALINKYKLKEGNPSRDELTLSRVAAALAGRTCQALVVLSEWLPVTGTTMDGLSPAYPRHMMHPSFAGMVDPSLPGDYLRAILDAHSLYLLQFSRVINPNLRGRTKEEVAATFTQPMNAAVNSNFISHEKRREFLKAFGLVDSNGKPSAAVMAAAQAYKTAA
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Encapsidates the genomic RNA, protecting it from nucleases (Probable). Displays high affinity for single-stranded nucleic acid. The encapsidated genomic RNA is termed the nucleocapsid (NC) or ribonucleoprotein. The ribonucleoprotein has a non-helical structure. Serves as template for viral transcription and replication (By similarity). After replication, the nucleocapsid is recruited to the host Golgi apparatus by glycoprotein Gn for packaging into virus particles (By similarity).
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D3KCC4
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CRNS1_CHICK
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Carnosine synthase 1 (EC 6.3.2.11) (ATP-grasp domain-containing protein 1)
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MISVDRLSEEQALGMKEQEWAGPEALCPGWQEEEVSDGEGPEDSGHPDPTAHAYEVLQHTLRLEGMPLTIDRTGQPRTGSGPLDMTVCVLGSPTAFLPVLLEGGTRYPGAMVLCLAPAWASRVPSETSPGSWSLLLSRGVSFEAGGCTALEEFVPPRRATYVTGTFGSEGSWEGELARDLDCPTGGSALLTRWLEDPLLSRWLLSARAGLPVPPTLAFITGLWETLPEEPEPPGVHLVRLQDPQGQESLVRDEVGAFLEGSSMQPYDQVAVRLSGWRWRGTDPHSTHRKVEGEAVAQAVAALLKGLREEESILLEALVPTARLPTLPPRSAAPRLPMALRICTVVCRSWGDRPQLCQVACTAGRAEVPVRHGSALPLGLDSSLRQWGLADAAQRQALAGQLREAAEAAMAALLAAEGELSPAQRGGARAHTDVLGVDFLLACVDGTLELVALSANCLRCLETCLLAEGMGHDVGQPAGDVPRLLAECLLHRAQCHLVEGKDILLIGAGGVSKSFVWEAAREYGLRIHLVESDPEHFAAGLVETFLPYDSREHRRDEEHAERVLEMLRARGLRPDACLSYWDDCVVLTALLCQRLGLPGCPPAAVRLAKQKSRTHQHLQRCRRGRPPPAAFSVPCRRLRSHGDVERAAGAVPFPAVAKLEFGAGAVGVRLVENAGQCHAHAAQLWHDLRADADHPGIGLGWGNAMLLMEYVPGTEHDVDLVLFEGRLLGAWVSDNGPTRVPTFLETAATLPSCLPADRQAQLVRAALRCCRACGLRHGVFNVELKLSPAGPRLLEINPRMGGFYLRDWMRAVYGPDLLLAAVLLALGLPPVLPSRPAPRQQLAGVMCLASEHGRALRGGVMAALQGLQRRGLVRLNPLFEEAGGRYEEPCLSVACAGDGPAEACGRLLGLCQALGIDSPQYPVGHFLSHFK
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Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine.
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D3KU66
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ASMT_MOUSE
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Acetylserotonin O-methyltransferase (EC 2.1.1.4) (Hydroxyindole O-methyltransferase)
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MHRGRSASARQERDFRALMDLAHGFMASQVLFAGCALRVFDAAALGPVDAAALARSSGLSPRGTRLLLDACAGLGLLRRRRGAGPRGPAYTNSPLASTFLVAGSPLSQRSLLLYLAGTTYLCWGHLADGVREGRSQYARAVGVDADDPFTAIYRSEAERLLFMRGLQETWSLCGGRVLTAFDLSPFRVICDLGGGSGALARMAARLYPGSEVTVFETPDVVAAARAHFPPPADEDGAEPRVRFLSGDFFRSPLPPADLYVLARVLHDWADAACVELLRRVRGALRPGGAVLLVESVLSPGGAGPTRTLLLSLTMLLQARGRERTEAEYRALTARAGFSRLRLRRPRGPYHAMMAARGGGAGARSDGGGGDATSQTGSGTGSEVGAQD
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Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
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D3KZG3
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TMC1_CAEEL
|
Transmembrane channel-like protein 1
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MQEAARRASLRKEHTPTNEKFGDLSKQDSLGERASSKLTLDDELYDILYAFGETDAFINKGDKQRETDEDGNPLTRQALLERIRQKKEVIGKLRCQAWSMTRKRRTLKLAQKYLEQHESKVSRSHLYMEEMRKRARLMKRSFSNFKTYLIPWESKIKRIESHFGSVVSSYFTFLRWIVFVNIMITLIALVFVVLPETLADSVANEGRFNRTKTRKQIPANERVHADELAVVWHYDGYLRYSPLFYGYYSDDPFLGNKIKYALPLAYFMVTLTIFAYSFFAILRKMAANARMSKLSGSKAEQYIFNWKLFTGWDYTIGNSETASNTVMAVVIKLRESIADIKKDAHGKFRLLQFSLRVFANIIICAMLGFSIYCIIFAVQKSQVQDDGNLFTKNQVPSVVSTITHVFPMIFDLIGKMENYHPRTALRAHLGRVLILYTVNYITLIFALFEKMTALRDRVNSTSTSSSHRTKRQQGGWNPNMQRPPPYASRAEVRQMSDFLAANTRRFQTVSQRTTRSVTTPFTVAPQFGPFNVNNPNAVFHNGTHSTSFESQILGPKALPIFTPPPRKYPGFTPGNVGQQFGGPDFPRNQVYTKSTPLPRVRTKPPWVYTTTHPPLVQNRAMTTTMSKSAKKGNSKNLDDDILLSNETIQMSEAALRRNHDGHNNDICWETIIGQEIVKLVTMDLIFTILSILVIDLFRGLWIKYCSSWWCWDIETTFPEYGEFKVAENVLHIINNQGMIWLGLFFAPLLPAINNIKLIILMYIRGWAVMTCNVPAREIFRASRSSNFYLGILLIWLLLCTLPVGFVIASMSPSRSCGPFARYQHFYTVVTREIEKRVDQTVLSYIRHIASPGVVIPIILFLILIIYFLFSLVRGLREANTDLQAQLVHERTEEKKKIFELAGGKKNKFEKDRDKKRSNDYIPLIEQRRREPWRQYHEMEADHALASDSSEESDINEDEDDERQPLTAYPLRAIETPPETLQVTAFHPSLGSLIENREMEDEESASGDQLPMIHKSVSFQGPSHMQMRQSISTESCSQISRSAIQVATPEEIRALLRPYLEAKYGIPYQHGIKSFPIDVHTPPNNTPSRRSSKYNSFVSLYEHTRDDHKNFVASTIKETDEDPGKSDKKQTSSKDVAPDFMPWPSADEARALREKMKSKTPLMLTKTTVEEKPKGGKSSESEFRPPVPIHRKYNIQTTEEENEEEETDSAPESSKKRFRISVSPTKTIAPASASRAQHKIVSQASSSSSIPHGRQPDPNKKASLVLPPLRAPRVQFDEDDSPRQID
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Sodium-sensor ion channel that acts specifically in salt taste chemosensation. Required for salt-evoked neuronal activity and behavioral avoidance of high concentrations of NaCl.
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D3RVD4
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TSDA_ALLVD
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Thiosulfate dehydrogenase (EC 1.8.2.2) (Tetrathionate synthase)
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MRGDVRVHTASPIAAAWLLAVGLVAHAEEPPTVALTVPAAALLPDGALGESIVRGRRYLSDTPAQLPDFVGNGLACRHCHPGRDGEVGTEANAAPFVGVVGRFPQYSARHGRLITLEQRIGDCFERSLNGRALALDHPALIDMLAYMSWLSQGVPVGAVVAGHGIPTLTLEREPDGVHGEALYQARCLACHGADGSGTLDADGRYLFPPLWGPRSFNTGAGMNRQATAAGFIKHKMPLGADDSLSDEEAWDVAGFVLTHPRPLFQEPTGD
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Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.
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D3TTC1
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VM3KL_NAJAT
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Zinc metalloproteinase-disintegrin-like kaouthiagin-like (K-like) (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP)
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MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQFTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNESVAIVQDYNRRISLVASTITHELGHNLGIHHDKASCICIPGPCIMLKKRTAPAFQFSSCSIREYREYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPQACQSACCNAATCQFKGAETECRVAKDDCDLPELCTGQSAECPTDSLQRNGHPCQNNQSYCYNGTCPTLTNQCITLLGPHFTVSPKGCFDLNMRGDDGSFCRMEDGTKIPCAAKDVKCGRLYCTEKNTMSCLIPPNPDGIMAEPGTKCGDGMVCSKGQCVDVQTAY
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Snake venom zinc metalloproteinase that cleaves the membrane-bound precursor of TNF-alpha (TNF) into its mature soluble form showing the same digestion pattern than ADAM17.
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D3TTC2
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VM3H_NAJAT
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Zinc metalloproteinase-disintegrin-like atragin (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP)
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MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQAKKYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKKLLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDRGFCTCGFNKCVMSTRRTKPAYQFSSCSVREHQRYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPADCQSACCNATTCKLQHEAQCDSEECCEKCKFKGARAECRAAKDDCDLPELCTGQSAECPTDVFQRNGLPCQNNQGYCYNGKCPIMTNQCIALRGPGVKVSRDSCFTLNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFCKRRNSMICNCSISPRDPNYGMVEPGTKCGDGMVCSNRQCVDVKTAY
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Snake venom zinc metalloproteinase that seems to inhibit cell migration. This activity is dominated by the local structure of the hyper-variable region.
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D3UW23
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AMPE_BITRH
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Glutamyl aminopeptidase (EAP) (EC 3.4.11.7) (Aminopeptidase A) (AP-A) (Rhiminopeptidase A)
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MDIEDKTSKMHCMKGKHVVIICGVVIAVGLILGLGLGLGLDTKACNPPEVNGQVSTKSPISNTPDVTSPSGSSVFCSAKNDENGPWTHFRLPNYVHPVHYDLHLTPEMEAEVYTGMVNISIRLEEQTTKHLWLHLRETKITEMPQLWTSSGQVIEIKRCFGYEPQEYVVIEAEEDLRPSNYFLSMRFKGYLNGSLVGFYSTTYGENGKIKYIAATDHEPTDARKSFPCFDEPNKKATYTISITHEHDYEAISNMPVEKTISLDNKWTKTIFKKSVPMSTYLVAWAVHQFKYEERISSRGIPLRIYAQPQQINTAIYAANVTKVVFDYFENYFNMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDSQESAASNKQRVAAVIAHELVHQWFGNIVTMDWWDDLWLNEGFASFFEFMGVNAKEEKWQMLDQILISDLLPVLKEDSLVSSHPITVNVSSPDEITSVFDGISYSKGASILRMLEDWISPECFRAGCEKYLKEHYFKNAKTDDFWKAMEEVSGKPVKEVMDTWTRQMGYPVLKVDLNSTVTQQRFLLDPKADPSKPSSQFSYKWNIPVKWKEGNTSNIIFYNKSELAGITITRPSDLPLNSFLKVNKDHVGFYRVNYEPQVWRALTDIMMKDHQNFNLADRAGFIDDAFALARAGLLKYADALNLTRYLQNEAEYIPWQRAVVAISYIRNMFEDDKALYPKFQRYFGSLVKPIASELKWEXDEDHIKSLLRTTVLEFACKMEDPEALGNASLLFKKWMSGISLDVNLRLLVYRFGMQNSGDEQAWNYMFQKYRTATLAQEKEKLLYGLASVKNITLLNRFLSCIKNTSLIRSQDVFTVLGYISLNSYGKTMAWDWVRLNWEYLVKRYTLNDRNLGRLISRLSGTFNTELQLWQMENFFERYPDAGAGEASRKQALETTKSNIEWLKQYRDDVATWLENSEHSNFA
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Venom protein that cleaves N-terminal acidic residues from peptides with high potency in presence of calcium. It may have several roles in venom including alteration of blood pressure by cleaving circulating angiotensin-2, general degradation of host tissue, increase of permeability to other venom components, and/or processing of other toxins in the venom (By similarity).
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D3UW26
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IF4EA_SOLTU
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Eukaryotic translation initiation factor 4E allele A (eIF4E-A) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
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MAAAEMERTTSFDAAEKLKAADAGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDSPIAKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVMGADFHCFKHKIEPKWEDPVCANGGTWKMSFLKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRSKGEKIALWTKNAANETAQVSIGKQWKQFLDHSDSVGFIFHDDAKRLDRSAKNRYTV
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Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses.
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D3VML5
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PZNA_BACVZ
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Plantazolicin (PZN) (Plantazolicin A) (Plantazolicin B) (cpd1335)
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MTQIKVPTALIASVHGEGQHLFEPMAARCTCTTIISSSSTF
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Peptide antibiotic inhibiting growth of Gram-positive bacteria in the dimethylated form plantazolicin A. The desmethyl form plantazolicin B has no antibiotic activity. The mode of action appears to be disruption of cell walls and lysis of cells. Inhibits B.subtilis strain HB0042, B.megaterium strain 7A1 and B.anthracis (MIC=2-4 ug/ml). Weakly inhibits Gram-positive bacteria B.brevis strain ATCC 8246, B.subtilis strain 168, B.cereus strain ATCC 14579 and strain CU1065, B.licheniformis strain ATCC 9789, M.luteus, B.sphaericus, P.granivorans and S.pyogenes (MIC=128 ug/ml). Does not inhibit B.pumilus, P.polymyxa, Arthrobacter sp., S.aureus, vancomycin-resistant E.faecalis, L.monocytogenes, methicillin-resistant S.aureus or Gram-negative bacteria E.coli strain K12, K.terrigena, Pseudomonas sp. and E.carotovora.
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D3W0D1
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KLRF2_HUMAN
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Killer cell lectin-like receptor subfamily F member 2 (Lectin-like receptor F2) (Activating coreceptor NKp65)
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MENEDGYMTLSFKNRCKSKQKSKDFSLYPQYYCLLLIFGCIVILIFIMTGIDLKFWHKKMDFSQNVNVSSLSGHNYLCPNDWLLNEGKCYWFSTSFKTWKESQRDCTQLQAHLLVIQNLDELEFIQNSLKPGHFGWIGLYVTFQGNLWMWIDEHFLVPELFSVIGPTDDRSCAVITGNWVYSEDCSSTFKGICQRDAILTHNGTSGV
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C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A.
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D3WYW0
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LEVS_LACGS
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Levansucrase (EC 2.4.1.10)
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MLENKKHKKMSLSGKSLLMGTLSTAAIVLSASTVNAATNTDTVDNANASQVTTVKASASVNKNDNSGLKENATNDKVAGTETNLNSSLNSGKETSSQVNDSKEDSSSTQVGSTPISSAIINNGKASSDLNQDSDNISDHFKDNNSQGQSSTSSEKTELKGKIKEIVNNSGIDVTKLTNDQINNLNKVNFDNDPQDGTKLTLNDLDAIGQALIRRDPKYAVPYFNAKEIKNMDAAETKDAQTGKTETLEIWDSWPVQDPITGYVSNYKGYQLVIAMMGMPKKNDNHIYLLYNKYNDNEFSHWRNAGSIFGYNETPDLQEWSGSAIVNKDGSVQLFYTKNDTSNGKLNDQQLATANLKLNVDNNGVSIASVDNDHVIFIGDGKHYQTYDQFSNGKNRNRDNYTLRDPHVVEEENGDRYLVFEANTGSNNYQGEDQVYRWANYGGNDKFNVNNFLSYFGNNDDQALASVANGALGILKLSGDQNNPTVKLDDVYSPLVTSLMVSDEMERPDIVKVGNKYYLFSATRLSRGTKGEITRLANKVVGDNVAMIGFVSDSLTHGYVPLNGSGVVLTASVPANWRTATYSYYAVPIEGKENQLLITAYMTNRGEVAGKGNNSTWAPSFILQLNPDNTTTVLAKLTNQGVWVWNGDSENKNMIGSLEKDSPNSAALDGEWGKFIDWDAINSYSLKPHQPVTPNVPTTPEKPENPTTPNTPDTPRTPEVPTTPVKKTTQSELPKAGAKDGIAATILGAISSMLGVIGLAGISKRKRNN
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Fructosyltransferase that catalyzes the polymerization of the fructose moiety of sucrose to produce levan polymer and the fructo-oligosaccharide (FOS) 1-kestose. Is also able to convert raffinose into a fructan polymer and a single oligosaccharide (most likely Gal-Glc-Frc-Frc) in vitro however, L.gasseri strain DSM 20077 is unable to ferment raffinose. Also displays sucrose hydrolase activity.
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D3XDS2
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UL97_MUHVS
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Serine/threonine protein kinase M97 (EC 2.7.11.1)
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MSVELTPPRSDGSVGFAPVVVPPAPRKPLRRRAVSDLEKLYKVKRRLVFGADDGAVDNDTSNNNSGSSSTTSRSRRKTAADVVSDSPKRTDDSSTAGEDGYTHCVHSCACTPGERHLLCCELVSIGDSVSVARCPLCSLGISTTYLSRGCCRGRSKVTGGDEDEEDEDEEENSQDEDRDEEEAASASSSGGLEWSDDSNSALSWSDENIIISPFPGLKCYVTTFEDIRQPVLLETGSAYLPVYVPYDESFCRNRCLERGGDDDDERDATLIGKGSFGQVWRLSDKKTALKAAASESINETLLTVWISGVVRSRAQDAGYRGELDDSVYCNILVATGSCLRHNLVSFASFDRDLYNYRGWHYAGLASYRRAFSGIADALRFLNLRCGVGHFDVTPMNVLINYDRADDRQIARAVICDFSLSQCHTEGTTGHCVVVFQQTKTVRALPKSAYYLTDIYHPAFKPLMLQKLCAIEPRKQFPKPSANRFCVSDLCALGHVAAFCLVRVLDERGQLKVRSTSEDALFGVARKTCDALARHSVDEVANFCSLLITRQLAYTATLLGSDDMREPMARLCDYFETVSDKDAPDRFRSVYKRARREIDGSYMVRLLLAASETEDGRYLLDNIRATCLMVDSEDLDVDPYKIFP
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Serine/threonine protein kinase that plays important roles in several processes including viral morphogenesis, nuclear viral egress, viral replication or regulation of host cell cycle progression. Participates in the acquisition of tegument during virion morphogenesis in the nucleus (By similarity). Phosphorylates host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity. Inhibits host DNA synthesis by cyclin A/CDKN2A sequestration to the cytoplasm.
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D3YN49
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GEMC1_XENLA
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Geminin coiled-coil domain-containing protein 1 (xGEMC1)
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MNTILTCQDEYFAGGLGYDCPYFSSTSASTVDVSKETWVSLWASGLLDNRSSNHGPHTQGQLYNMGNSLQEDYLFGDQLSSQISANKQLQDTLLQKEEELSRLHEENNKLKEFLNSAFVKTLAEKTKKLLHQNGQSSFCTNPNSRVPFSSNSTPGSKAKRARRNLYGELTACEAQSSPVVEKWVLQTLGLKDVDTIDDSALANYSAMSLQPKQDSPSSGYSSAHLTPGHSQAATSCSLSPSQCSSASLPESETASPLSSPTYHTPDVAPNKTEVAFSTSLHPHCNVKTHSFPQGQAFVRRDTQGGWKFTWVPKQSE
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Regulator of DNA replication. Promotes initiation of chromosomal DNA replication by mediating topbp1- and cdk2-dependent recruitment of cdc45l onto replication origins.
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D3YVF0
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AKAP5_MOUSE
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A-kinase anchor protein 5 (AKAP-5) (A-kinase anchor protein 150 kDa) (AKAP 150) (P150) (cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein)
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METSVSEIQVETKDEKGPVAASPQKERQERKTATLCFKRRKKANKTKPKAGSRTAEETKKHTPEAGGSGQRQPAGAWASIKGLVTHRKRSEPAKKQKPPEAEVQPEDGALPKKKAKSRLKFPCLRFSRGAKRSRHSKLTEDSGYVRVQGEADDLEIKAQTQPDDQAIQAGSTQGLQEGVLVRDGKKSQESHISNSVTSGENVIAIELELENKSSAIQMGTPELEKETKVITEKPSVQTQRASLLESSAAGSPRSVTSAAPPSPATTHQHSLEEPSNGIRESAPSGKDDRRKTAAEEKKSGETALGQAEEAAVGQADKRALSQAGEATAGHPEEATVIQAESQAKEGKLSQAEETTVAQAKETVLSQAKEGELSQAKKATVGQAEEATIDHTEKVTVDQAEETTVGQAEEATVGQAGEAILSQAKEATVVGQAEEATVDRAEEATVGQAEEATVGHTEKVTVDQAEEATVGQAEEATVGQAEEATVDWAEKPTVGQAEEATVGQAEEATVGHTEKVTVDQAEEATVGQAEEATVGHTEKVTVDHAEEATVGQAEEATVGQAEKVTVDHAEEATVGQAEEATVGQAEKVTVDHAEEATVGQAEEATVGQAEKVTVDQAEEPTVDQAEEAISSHAPDLKENGIDTEKPRSEESKRMEPIAIIITDTEISEFDVKKSKNVPKQFLISMENEQVGVFANDSDFEGRTSEQYETLLIETASSLVKNAIELSVEQLVNEMVSEDNQINTLFQ
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Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses.
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D3YVL2
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CFA70_MOUSE
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Cilia- and flagella-associated protein 70 (Tetratricopeptide repeat protein 18) (TPR repeat protein 18)
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MDQTSSTTKIVHITVTNGYDLKGFKGDTPVTFVRAEFNQTVLGDSSKVTVSPEGTAKYNFTSNIDLSPDGGGALDDLAHKPLFLTVTEVLPKEKKQKDEKTLILGQAVVDLLPLLEGEESFETTVPLHPVPGSPLETPLPGSKQCSLDVKVFVAEPLLTPAQVSASNLLKVTLEAAYSVPESFIPVGPQQNYMVGLQVPSVGEKDYTMIFKNGNLKLGGEKEPVPRPKKWPIANILAPGASNIPDEFIVGGPYEEEEGELNHPEDREFRNQAECTKKRIVWDLESRCFLHPFAVASFQKRIADCRLWPVEITRVPLVVMPKAKPGKLEKIDDENQLSFHGVAYINMVPLLYPGVKKIRGAFHVYPYLDGTVFEKTKCLFSLFRDTGHHLVQNNKAGGLNSPLSKPLSKNLKEEKPGKDKDTEGRPRLGELQAPSIKSQSSDTPLESEAPLSHNLEGQQYIEAGTYIVLEIQLEKALVPKRMPEELARRVKEMIPPRPPLTRRTGGAQKAVSDYHTQIKSISRAILNEYYRMFGKQGPKLESDIDNETMEERKCQLNYELNCSGKYFAFKEQLKHAVVKIVREKYLKTTAFESQEELQTFISELYVFLVDQMHVALNQAVPDDVPSSTSTIQTSSEQLRLFAFEAEVNEKFEIAAMYYEERLVREPQNLENWLDYGAFCLLTEDNIKAQECFRKALSLNESHVDSLLLCGVLAILLENYEQAEIFFEDATCLEPTNVIAWTLLGLFYEIQNNDIRMEMAFHEAFKQLQARTLQTKLKSTVTIENMEEGVKVEPSFGPWGVVQESTTAIKTEGLSGMRPQSSHQLSPHTNMELHPQPQGPNTALSSLDEFLEESPKAQSESQEPMATGQPLEPSLVQRSSNALLKELTSKKDISKCQDSSAFSPPTQHVIAQPPVTIFMETIRFLMKVNAVQFVHRVLAHELLCPQGGPSCEYYLVLAQTHLLKKDFAKTEEYLQQAAQMDYLNPNVWGVKGHLYFLSGNHAEAKECYERTISFVVDASEMHFIFLRLGHIYLEEKEYENAKRTYMHACKRSPSCLTWLGLGIACYRLEELTEAEDALSEANALNNCNAEVWAYLALVCLKVGRQLEAEQAYKYTIKLKLKDQALLEEIHTVQEMVGFGNPSF
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Axoneme-binding protein that plays a role in the regulation of ciliary motility and cilium length.
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D3YWP0
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EFMT3_MOUSE
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EEF1A lysine methyltransferase 3 (EC 2.1.1.-) (Methyltransferase-like protein 21B) (Protein-lysine methyltransferase METTL21B)
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MASSRTDPETEPESVFPREIRLFTDSYSESSRFCFCGHELSITQNFGSRLGVAARVWDAALSLCDYFESQNVDFRGKKVIELGAGTGIVGILAALQGGDVTITDLPVALEQIQDNVHANVPPGGRARVCALSWGIDQHVFPGNYDLVLGADIVYLEPTFPLLLGTLRHLCGPHGTIYLASKMRAEHGAETFFRRLLPQHFHLELAQRDEDVNVNIYRARHREVAPAGQHPFC
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Protein-lysine methyltransferase that selectively mono-, di- and trimethylates 'Lys-165' of the translation elongation factors EEF1A1 and EEF1A2 in an aminoacyl-tRNA and GTP-dependent manner (By similarity). EEF1A1 methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation.
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D3YWQ0
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DGKI_MOUSE
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Diacylglycerol kinase iota (DAG kinase iota) (EC 2.7.1.107)
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MDAAGRGCHLLPLPAARGPARAPAASSALSPTGLCSGTTSASFAAAGAVAMNPSSSAGEERGATGGSSSSGSGAGSCCLGAEGGADPRGAGAAAAAALEEPAAAGQKEKEEALEEKLRDLTFRKQVSYRKAISRTGLQHLAPAHPLGLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGTEQETKGRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQDLKFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGERLHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDIHQVQAADLRRVSAPPGSFTIPQSVPDRLRIRVNKISLQDYEGLHYDKDKLREASIPLGILVVRGDCDLETCRMYIDRLQEDLQSVSSGSQRVHYQDQETSFPRALSAQRLSPRWCFLDATSADRFYRIDRSQEHLHFVMEISHDEIFILDPDMVVSQQAGTPPGMPDLVVEQASGLSDWWNPALRKRMLSDSGMITPHYEDSDLKDFSHSRVLQSPVSSEDHAILQAVLTGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAELLDMADSETGETALHKAACQRNRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETAV
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Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Has probably no preference for any of the diacylglycerols in terms of the acyl chain composition, especially for the acyl chain at the sn-2 position (By similarity). By controlling the diacylglycerol/DAG-mediated activation of RASGRP3, negatively regulates the Rap1 signaling pathway. May play a role in presynaptic diacylglycerol/DAG signaling and control neurotransmitter release during metabotropic glutamate receptor-dependent long-term depression.
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D3YXG0
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HMCN1_MOUSE
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Hemicentin-1 (Fibulin-6) (FIBL-6)
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MIAQEVVHTVFLVALFRSSLAGDGTPQSESRAEEIPEGASTLAFVFDVTGSMYDDLVQVIEGASKILETSLKRPKRPLYNFALVPFHDPEIGPVTITTDPKKFQYELRELYVQGGGDCPEMSIGAIKIALEISLPGSFIYVFTDARSKDYRLTHEVLQLIQQKQSQVVFVLTGDCDDRNHIGYKVYEEIASTSSGQVFHLDKKQVNEVLKWVEEAVQASKVHLLSTDHLEHAVNTWKIPFDPSLKEVTVSLSGPSPVIEIRNPFGKLIKKGFGLNELLNIHNSAKVVNVKEPEAGMWTVKTSSSGRHSVRITGLSTIDFRAGFSRKPTLDFKKTMSRPVQGIPTYVLLNTSGISSPARVDRLELLSISGGSLKTIPVKHYPDRKPYGIWNISDFIPPDEAFFLKVTGYDKDGYLFQRVSSVSFSSIVPDAPKVTMPTRTLGYYLQPGQILCSVESFLPFTLSFMRDGIALGVDQYLRESASVNWDFTKVTLSDEGFYDCIAVSSAGTGRAQTFFDVSEPPPIIQLPNNVTVTPGERAVLACLVISAVDYNLTWQRSGRDIRLADSARIRTLANLSLELRSVKIGDAGEYRCVVSSEGGSAAASVFLTVQEKPKVTVMPKNQSFTGGSEISIMCSATGYPKPKIVWTMNEMFIMGSHRYRMTSEGTLFIKNAVPKDAGTYACLASNAAGTDKQTSTLRYIEAPKLVVEQSELLVALGDTTVMECKTSGIPPPQVKWFKGDLELRPSTFLSIDPLVGLLKIQETQDLDAGDYTCVAINEAGRATGRLTLDVGSPPVFIQEPSDVAVEIGSNVTLPCYVQGYPEPKIKWRRLDNMPVFSRPFSVSFISQLRTGALFISNLWASDKGTYICEAENQFGKIQSQTTVTVTGLVAPLIGISPSMASVIEGQPLTLPCTLLAGNPIPERRWMKNSAMLVQNPYITVRSDGSLHIERVRLQDGGKYTCVASNVAGTNNKTTSVAVHVLPSIQHGQQILSTIEGVPVTLPCRASGIPKPSITWSKKGELISTSSAKFSAGADGSLYVVSPGSEESGEYICTATNAAGYAKRKVQLTVYVRPRVFGDQRGLSQDKPVEISVLAGEEAILPCEAKSLPPPIITWAKDSQLISPFSPRHTFLPSGSMKITETRVSDSGMYLCVATNIAGNVTQSVKLSVHVPPKIQHGNRHIKVQVGQRVDILCNAHGSPPPVITWFKSGRPFLDGAQHPGSPDGTLSIEQAVISDAGVYTCAATNIAGSDEAEVTLHVQEPPSVEDLQPPFNTPFQERLANQRIEFPCPAKGTPKPTIKWLHNGREVTGQEPGVSILEDGALLVIASVTPHNNGEYICVAVNEAGTTERKYNLKVHVPPVIRDKEHVTNVSVLTSQLASLYCEVEGTPSPVITWYKDDIQVTESSTVQIVNNGKILKLFKVSAEDAGRYSCKAINIAGTSQKDFSVNVLVPPSILGASSPSEVSVVLNHNVTLQCPGTGVPFPAIHWFKDGKPLFLGDPNIELSDRGQSLHLRNARRSDKGRYQCTVSNAAGKQAKDIKLTVYVPPSIKGGNITTEISALLNSIVKLECETRGLPVPAITWYKDGQVVTSSSQALYIDKGQLLHIQRAQVSDSATYTCHAANVAGTAEKSFHVDIYVPPTIEGDLTAPSNKQVIIGQSLILECKAAGNPPPILTWLKDGVPVKASDNIHIEAGGKKLEILSALEVDRGQYICVATSVAGEREIKYEVDVLVPPAVEGGEETSYFIVLANNLLELDCQVSGSPPPTIMWLKGGQLIDERDGFKILLNGRKLVIAQAQVSDTGLYQCVATNIAGDHRKEFEVTVHVPPTIKSSDLPEKTVVRYKPVTLQCIANGIPNPSITWLKDDQPVNTAHGNLKIQSSGRVLQIAKALLEDAGRYTCVATNAAGEAHQHTQLHVHEPPSLDDAGKMRNETVVVNNPIQLECKATGKPLPVITWYKDSHPLSGSASAAFLKRGQVLEIGSAQISDAGIYKCVAINSAGATELFYSLQVHVPPSISGSSSMVEVVVNNLARLECEARGIPAPSLTWLKDGSPVSSFSNGIQILSGGRILALTSAQMSDAGRYTCVAVNAAGEKQRDIDLRVYAPPNIMGEEQNVSVLIGQAVELFCQSDAVPPPTLMWLKDGRPLLKRPGLSISENGSVLKIEDAQAGDTGRYTCEATNVAGKTEKNYNVNVWVPPSIYGSDELVQLTAIEGNLITLLCESSGIPPPDLTWKKKGSLVLADSAGRVHILSGGRRLQISIAEKADAGLYTCVASNVAGVAKKEYNLQVYIRPSITNSGGHRPEITVIRGKSISLECEVQGIPQPTVTWMKDGRPLTKGKGVEILDEGRILQLKNVHVSDTGRYVCVAVNVAGMTDKRYDLSVHAPPSIIGNHGVPENVSVVEKSSVSLTCEASGIPLPSITWLKDGWPVNLGSSVKILSGGRMLRLMQTRPEDAGQYTCIVRNAAGEDRKMFGLSVLVPPHIVGENTLEDVKIKEKQSVTLTCEVRGNPVPQITWHKDGQLLQEDEAHHMMSGGRFLQITNAQVSHTGRYTCLASNIAGDKSKSFRLNVFVSPTIAGVDSDGSPEDVIVILNSPTSLVCEAYSYPPATITWFKDGTPLESNRNIRILPGGRTLQILNAQEDNAGRYSCVATNEAGEKIKHYEVKVYIPPIIKKGDLLGPGLSPKEVKIRVNSSLTLECEAYAIPSASLRWYKDGQPLKSDDHVTIAASGHTLQIKEAQISDTGRYTCVASNLAGEDELDFDVNIQVPPSFQKLWEIGNMLDTGRSGEAKDVIINNPLSLHCETNAAPPPTLTWYKDGRPLTSSDRVLILPGGRVLQIPRAKVEDAGRYTCVAVNEAGEDSLRYDVHVLLPPVIKGANSDLPEEVTVLVNKSTQMECSSSGNPAPRNYWQKDGQILLEDEHHKFQSDGRSLQILNAQITDTGRYVCVAENTAGSAKKYFNLNVHVPPSVIGPNHEHLSVVVNHFISLNCEVSGFPPPDLSWLKNEEPIKPNTNVLTVPGGRTLQIIRAKISDGGDYTCIAINQAGESKKKVSLTVHVPPSIKDHGSQSLSIVNVREGTSVSLECESNAVPPPVITWSKNGRMIPDSTNVEILTGGQTLHIRRAEVSDTGQYVCRAINVAGRDDKNFHLNVYVPPTIEGPETEVIVETISNPVTLTCDATGIPPPTITWLKNHKPIENSDPLEVHILSGGSKLQIARPQRSNSGNYTCVASNMEGKAQKNFILFIQVPPSVAGAEVPSEVSVLLGENVELVCNADGIPTPHLQWLRDGKPIVNGETERVRVTTDGSTLNIYRALTSDMGKYTCVATNPAGEEDRIFNLNVYVPPKIRGNKEEAEKLMALVDTSINIECKATGTPPPQINWLKNGLPLPISSHIRLLSAGQVVRIVRAQVSDIAVYTCVASNRAGVDSKHYSLQVFVPPNMDNAMGTEEITIVKGSSTSMTCFTDGTPAPSMSWLRDGQPLAPDAHLTVSTQGMVLQLIKAETEDTGKYTCVATNEAGEVSKHFVLKVLEPPHINGSEGPGEVSVIVNNPLELSCIASGIPAPKISWMKDGRPFLQTEQVQTLEGGAILRVSSAQVEDTGRYTCLASSPAGDDDKEYLVRVHVPPNIAGMDEAQDFTVLRNRQVTLECKSDAVPPPVIMWLKNREQLQATPRVRILSGGRYLQINNADLGDTANYTCVASNIAGKTTREFNLTVNVPPSIGGGPQSLVTLLNKSIALECRAEGVPAPRITWRKDGVVLAESHARYSILENGFLHIESAHVTDTGRYLCMATNVAGTDRRRIDLQVHVPPSIAMGPTNVTVTVNVQTTLACEATGIPKPSVTWRKNGHLLNVDQNQNSYRLLSSGSLVIISPSVDDTASYECTVTSDAGEDKRAVDLTVQVPPTIADEPMDFLVTRQAPAVMTCSASGVPVPSIHWTKNGLRLLPRGDGYRILSSGAIEIPTTQLNHAGRYTCVARNAAGSAHRHVTLRVQEPPVIQPQPSELDVILNNPILLPCEATGIPTPFITWQKEGINVITSGKSLAILPSGSLQISRAVRGDAGTYMCVAQNPAGTALGKVKLNVQVPPVISSHQKEYVVTMDKPVSLLCETEGSPPPDITWHKDGHALTESIRQRILNSGALQIAFAQPDDAGQYTCMAANMAGSSSVSSTLTVHVPPRIQSTEVHFTVNENSQAVLPCVADGIPTPAIHWEKDGVLIANLLGKYTAQPYGELILENVVLEDSGTYTCVANNAAGEDTRIVTLAVHTLPTFTELPGDLSLNKGEQLRLSCKAVGIPLPKLTWTFNNNIIPAHFDSINGHSELVIEKVSKEDSGTYVCTAENSVGFVKAIGFVYVKEPPVFKGDYPSNWIEPLGGNAILNCEVKGDPAPTIQWSRKGADIEISHRIRQLGNGSLAIYGTVNEDAGDYTCVAANEAGMVERSMSLTLQSSPIITLEPVETVVDAGGRVILDCQAAGEPQPTITWSRQGQPISWDNRLSMLPNSSLYIAAARKEDTSEYECVARNLMGSVLVRVPVIVQVHGGFSLWSAWRPCSVTCGKGIQKRSRLCDNPPPANGGRPCQGADSEARHCHNKLCPVDGHWSEWSFWEDCSRSCGHGNQTRTRTCSNPPAQHGGRPCEGHAVETIMCNIRPCPVHGVWNAWQPWSACSKSCGKGSQTRMRLCNNPPPSFGGAHCSGAETQMQVCNERHCPVDGRWATWSSWSACTVSCGGGARKRTRDCSDPVPQYGGNKCEGTGVQSDFCNSDPCPTHGNWSPWSGWGTCSRTCNGGQMRRYRTCDNPRPSNGGRACGGPDTQIQRCNTDMCPVDGSWGTWHSWSHCSVSCGGGERTRKRLCDNPVPTKGGRSCPGDATQVSRCNMQACPGGPQRARGSVIGNINDIEFGIAFLNATITDSPNTDTRVIQAKITNVPRSLGPAMRKIISILNPIYWTTAKEIGEAVNGFTLTNAVFKRETQVEFATGEVLRMTHVARGLDSDGALLLDVIVSGQVLQLHSPAEVGVKDYTEDYIQTGPGQLYAYSTRLFTIDGISIPYTWNHTIFYDQAWGKMPFLVETLHASSIESDYNQLEETLGFKIHASISKGDRSNQCPSGFILDSVGPFCADEDECTAGNPCSHTCHNAIGAYYCSCPKGLTIAADGRTCQDIDECALGGHTCRAGQDCDNTIGSYRCVVHCGTGFRRTSDGLSCQDINECQESSPCHQRCFNVIGSFHCGCEAGYQLKGRKCIDVNECRQNVCRPDQHCKNTRGGYKCIDLCPSGMTKAENGTCIDIDECKDGTHQCRYNQICENTRGSYRCACPRGYRSQGVGRPCIDINECEQVPKPCAHQCSNSPGSFKCICLPGQQLLGDGKSCAGLERLSNYGTQYSSYTLERFSPVRSDYQPSQHYRQYSQLYSSYSEYRNSRASFSRNRRTIRKTCPEGSEANHETCVDIDECQNRDTCQHECKNTIGSYQCVCPPGYRLMLNGKTCQDVDECLEQNVRCGPNRMCFNMRGSYQCIDTPCPPNYQRDPVLGFCLKNCPPNDLECTLSPYALEYKLVSLPFGIAANQDLIRLVAYTQDGVMHPRTTFLMIDEEPAVPFALRDENLKGVVYTTRPLREAETYRMKVGALSYSANGTIEYQTTFIVYIAVSAYPY
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Involved in transforming growth factor beta-mediated rearrangement of the podocyte cytoskeleton which includes reduction of F-actin fibers and broadening, flattening and elongation of podocytes (By similarity). Plays a role in basement membrane organization. May promote cleavage furrow maturation during cytokinesis in preimplantation embryos. May play a role in the architecture of adhesive and flexible epithelial cell junctions. May play a role during myocardial remodeling by imparting an effect on cardiac fibroblast migration.
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D3YXJ0
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DGKH_MOUSE
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Diacylglycerol kinase eta (DAG kinase eta) (EC 2.7.1.107) (Diglyceride kinase eta) (DGK-eta)
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MAGAGSQHHPQGVAGGAVAGASAVSPTAAGPGEDSSDSEAEQEGPQKLIRKVSTSGQMRTKTSIKEGQLLKQTSSFQRWKKRYFKLRGRTLYYAKDSKSLIFDEVDLSDASVAEASTKNANNSFTIITPFRRLMLCAENRKEMEVWISSLKSVQSREPYEVAQFNVEHFSGMHNWYACSHARPTFCNVCRESLSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDEDGVAMPHQWLEGNLPVSAKCAVCDKTCGSVLRLQDWKCLWCKTMVHTACKDVYHPVCPLGQCKVSIIPPIALNSTDSDGFCRATFSFCVSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPYLGLRLFQKFDNFRILVCGGDGSVGWVLSEIDKLNLHKQCQLGVLPLGTGNDLARVLGWGGSYDDDTQLPQILEKLERASTKMLDRWSIMTYELKLPAKSSLLPEPVAATEEFYMTIYEDSVANHLTKIVNSDEHAVVISSAKILCETVKDFVAKVEKAQDRTLENTVVAEAVASKCSVLNEKLEQLLQALHADSQASRVPPGIGPAIPEEDTVESASDESLGESKDQLVNDIGKPSSQKAVKPREIMLRANSLKKAVRQVIEEAEKVMDEPAVQPSEPVSPSCDYDTETDEAKEDDAKESLSAKTTSQSPDAQASCGHPQTDSVAGPAMATTKENLPVLNTRIICPGLRAGLAASIAGSSIINKMLLANIDPFGATPFIDPDLDSLDGYSEKCVMNNYFGIGLDAKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLPSLQGIAVLNIPSYAGGTNFWGGTKEDDIFAAPSFDDKILEVVAVFDSVQMAVSRVIKLQHHRIAQCRTVKITIFGDEGVPVQVDGEAWVQPPGIIKIVHKNRAQMLTRDRAFESTLKSWEDKQKCDSGKPVLRTNLYIHPAPDLATEEVSQMRLCSQAAEELITRICDAATIHCLLEQELAHAVNACSHALNKANPRFPESLTRDTATEIAINVKALYNETEALLVGRVPLHLESPHEERVSSALHSVEMELQKLTEIPWLYYILRPSEDEEPPLDCTKRNNKSTVFRIVPKFKKEKAQKQKTSSQPVQNWGTEEVAAWLDLLNLGEYKEIFIRHDVRGAELLHLERRDLKDLGIPKVGHMKRILQGIKELERNPPNLV
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Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Plays a key role in promoting cell growth. Activates the Ras/B-Raf/C-Raf/MEK/ERK signaling pathway induced by EGF. Regulates the recruitment of RAF1 and BRAF from cytoplasm to membranes and their heterodimerization (By similarity).
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D3YXK1
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SAMD1_MOUSE
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Sterile alpha motif domain-containing protein 1 (SAM domain-containing protein 1) (Atherin)
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MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRVPRGGPAAPPPTPAPPPAPVAAPTRAPRAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAAAPPAGPRRAPPPAVAAREPPAPPQQQQPPPPQPQPPPEGGAARAGGPARPVSLREVVRYLGGSGGASGRLTRGRVQGLLEEEAARGRLERTRLGALALPRGDRPGRAPPAASARAARSKRGGEERVFEKEEEDEDEDEEEEEEDNVSEGSEVPESDRPAGAQHHQINGERGPQSAKERVKEWSPCGPYQGQDEGRGPAPGSCTRQVFPMTAVNKEGGSACVGAAPDSPSPVPLPPGKPALPGADGTPFGCPPGRKEKPTDPVEWTVMDVVEYFTEAGFPEQATAFQEQEIDGKSLLLMQRTDVLTGLSIRLGPALKIYEHHIKVLQQGHFEDDDPDGLLG
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Unmethylated CpG islands (CGIs)-binding protein which localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional repressor. Tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs. Plays a role in atherogenesis by binding with LDL on cell surface and promoting LDL oxidation which leads to the formation of foam cell.
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D3YXK2
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SAFB1_MOUSE
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Scaffold attachment factor B1 (SAF-B1)
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MAETLSGLGDASAAGAAAVSSAASETGTRRLSDLRVIDLRAELKKRNLDSSGNKSVLMERLKKAIEDEGGNPDEIEVTSECNKKMPKRPSKGRKPEDEGVEDNGLEENSGDGQEDVETSLENLQDMDMMDISVLDEADIDNGSVADCVEEEEEATLPEGLADSTELVEGDLKGLPEQLQEHAIDDKDTVNNVDTSSSDFTMLQEMEEASLEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEDQEEEQEEEGDLALASSSKSESPSTRCQWSEADAPLAVVKREPADAPGGGTGMDREPVGLEEPVEQSSTAAQLPEATSQELVRAPTAALSPEPQDSKEDVKKFAFDACNDVPAPPKESSASEGADQKMSSVEEDSDTKRLSREEKGRSSCGRNFWVSGLSSTTRATDLKNLFSRYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCISHLHKTELHGKMISVEKAKSEPTGKRVPDRRDGDSKKEKASTSDRSANLKREEKGERKDDAKKTDDGSTEKSKDADDQKPGPSERSRTTKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSASREKRSVVSFDKVKESRKSRDSESRRERERSEREQRLQAQWEREERERLEIARERLAFHRHRLERERMERERLERERMHVEQERRREQERIHREREELRRQQELRYEQERRPAVRRPYEVDGRRDDAYWPEAKRAALDDRYHSDFSRQDRFHDFDHRDRGRYPNHSVDRREGSRSMMGDREGQHYPERHGGPERHGRDSRDGWGYGSNKRLSEGRGLPPPPRRDWGEHGRRLEDDRAWQGTADGGMMERDHKRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRGHVIPRGGMQAGFGGQSRGSRPSDARFTRRY
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Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Functions as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription (By similarity). Thereby acts as a negative regulator of cell proliferation (By similarity). When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter.
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D3YYI7
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RN217_MOUSE
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E3 ubiquitin-protein ligase RNF217 (EC 2.3.2.31) (IBR domain-containing protein 1) (RING finger protein 217)
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MGEEQSTVSGSGGARASGGGSAGQPESPRPRGDRVRTAGPRAAASSSRPNGGGGGRDPGCVDASVQEPASNRAPAGQPARLPLSGPLDPQSLELQLEREAEGAGPREAPPGQQPPDGLLLDVLAQRHPPPAKPQVLCSVYCVESDLPEAPSAESPSPSESPPQAPLGPIPASPPPSFPSSPLSLPADPLSPDGGSIELEFYLAPEPFSVPGLLGAPPYSGLGGVGDPYAPLMVLMCRVCLEDKPIKPLPCCKKAVCEECLKIYLSSQVQLGQVEIKCPVTECFEFLEETTVVYNLTHEDSIKYKYFLELGRIDSSTKPCPQCKHFTTFKKKGHIPTPSRSESRYKIQCPTCQLIWCFKCHSPWHEGVNCKEYKKGDKLLRHWASEIEHGQRNAQKCPKCKIHIQRTEGCDHMTCSQCNTNFCYRCGERYRQLRFFGDHTSNLSIFGCKYRYLPERPHLRRLVRGSVCAGKLFIAPLILVLGLALGAIAVVIGLFVFPIYCLCKKQRKRSRTGMHW
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E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the degradation of the iron exporter ferroportin/SLC40A1 and thus regulates iron homeostasis.
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D3YZU1
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SHAN1_MOUSE
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SH3 and multiple ankyrin repeat domains protein 1 (Shank1)
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MTHSPATSEDEERHSASECPEGGSESDSSPDGPGRGPQGTRGRGSGAPGNLASTRGLQGRSMSVPDDAHFSMMVFRIGIPDLHQTKCLRFNPDATIWTAKQQVLCALSESLQDVLNYGLFQPATSGRDANFLEEERLLREYPQSFEKGVPYLEFRYKTRVYKQTNLDEKQLAKLHTKTGLKKFLEYVQLGTSDKVARLLDKGLDPNYHDSDSGETPLTLAAQTEGSVEVIRTLCLGGAHIDFRARDGMTALHKAACARHCLALTALLDLGGSPNYKDRRGLTPLFHTAMVGGDPRCCELLLYNRAQLGIADENGWQEIHQACQRGHSQHLEHLLFYGAEPGAQNASGNTALHICALYNKETCARILLYRGANKDVKNNNGQTPFQVAVIAGNFELGELIRNHREQDVVPFQESPKYAARRRGPPGAGLTVPPALLRANSDTSMALPDWMVFSAPGASSSGTPGPTSGSQGQSQPSAPSTKLSSGTLRSASSPRGARARSPSRGRHPEDAKRQPRGRPSSSGTPRDGPAGGTGGSGGPGGSLGSRGRRRKLYSAVPGRSFMAVKSYQAQGEGEISLSKGEKIKVLSIGEGGFWEGQVKGRVGWFPSDCLEEVANRSQEGRQESRSDKAKRLFRHYTVGSYDSFDAPSLIDGIDSGSDYIIKEKTVLLQKKDSEGFGFVLRGAKAQTPIEEFTPTPAFPALQYLESVDEGGVAWRAGLRMGDFLIEVNGQNVVKVGHRQVVNMIRQGGNTLMVKVVMVTRHPDMDEAVHKKASQQAKRLPPPAISLRSKSMTSELEEMVSPWKKKIEYEQQPAAVPSMEKKRTVYQMALNKLDEILAAAQQTISASESPGPGGLASLGKHRPKGFFATESSFDPHHRSQPSYDRPSFLPPGPGLMLRQKSIGAAEDDRPYLAPPAMKFSRSLSVPGSEDIPPPPTTSPPEPPYSTPPAPSSSGRLTPSPRGGPFNPGSGGPLPASSPSSFDGPSPPDPRSGGREKSLYHSGALPPAHHHPPHHHHHHAPPPQPHHHHAHPPHPPEMETGGSPDDPPPRLALGPQPSLRGWRGGGPSPTSGAPSPSHHSSSGGSSGPAQAPALRYFQLPPRAASAAMYVPARSGRGRKGPLVKQTKVEGEPQKGSLPPASSPTSPALPRSEPPPAGPSEKNSIPIPTIIIKAPSTSSSGRSSQGSSTEAEPPTQPDGAGGGGSSPSPAPATSPVPPSPSPVPTPASPSGPATLDFTSQFGAALVGAARREGGWQNEARRRSTLFLSTDAGDEDGGDSGLGPGAPPGPRLRHSKSIDEGMFSAEPYLRLESGGSSGGYGAYAAGSRAYGGSGSSSAFTSFLPPRPLVHPLTGKALDPASPLGLALAARERALKESSEGGVTPQPPPRPPSPRYDAPPPTLHHHSPHSPHSPHARHEPVLRLWGDPARRELGYRAGLGSQEKALTASPPAARRSLLHRLPPTAPGVGPLLLQLGPEPPTPHPGVSKAWRTAAPEEPERLPLHVRFLENCQARPPPAGTRGSSTEDGPGVPPPSPRRVLPTSPTSPRGNEENGLPLLVLPPPAPSVDVDDGEFLFAEPLPPPLEFSNSFEKPESPLTPGPPHPLPDPPSPATPLPAAPPPAVAAAPPTLDSTASSLTSYDSEVATLTQGAPAAPGDPPAPGPPAPAAPAPPAPQPGPDPPPGTDSGIEEVDSRSSSDHPLETISSASTLSSLSAEGGGNTGGVAGGGAGVASGTELLDTYVAYLDGQAFGGSGTPGPPYPPQLMTPSKLRGRALGTSGNLRPGPSGGLRDPVTPTSPTVSVTGAGTDGLLALSACSGPSTAGVAGGPVAVEPEVPPVPLPTASSLPRKLLPWEEGPGPPPPPLPGPLSQPQASALATVKASIISELSSKLQQFGGASTAGGALPWARGGSGGSTDSHHGGASYIPERTSSLQRQRLSEDSQTSLLSKPSSSIFQNWPKPPLPPLPTGSGVSSSTAAAPGATSPSASSASASTRHLQGVEFEMRPPLLRRAPSPSLLPASDHKVSPAPRPSSLPILPSGPLYPGLFDIRSSPTGGAGGSADPFAPVFVPPHPGISGGLGGALSGASRSLSPTRLLSLPPDKPFGAKPLGFWTKFDVADWLEWLGLSEHRAQFLDHEIDGSHLPALTKEDYVDLGVTRVGHRMNIDRALKFFLER
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Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction. Overexpression promotes maturation of dendritic spines and the enlargement of spine heads via its ability to recruit Homer to postsynaptic sites, and enhances presynaptic function (By similarity).
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D3Z120
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FOXI3_MOUSE
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Forkhead box protein I3
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MALYCGDNFVYSQPAAAPGAPPTSRAPYGLSDYAAPPAAAANPYLWLNGPGVGGPASAASYLGAPPPPPGAAPGPFLQPPAAPGTFAGAQRGFAQPSASAPASPAGSAAPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADNFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRRRRAEASSNLTVPSGTSKSEGQSSRLRVSGKLEGDSPSSILRPSQSPEPPEGTKSTASSPGASTLTSTPCLNTFLSTFNTLNVNSSSSMGNQRTLPGSRRHLGGTQLPSSTFPNTSVPDSSPDSMQLSTVGGSNQLSSYYNPFSGGSSGDQSSPFSSPFYNFSMVNSLIYPRDGSDI
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Transcription factor required for pharyngeal arch development, which is involved in hair, ear, jaw and dental development. May act as a pioneer transcription factor during pharyngeal arch development. Required for epithelial cell differentiation within the epidermis. Acts at multiple stages of otic placode induction: necessary for preplacodal ectoderm to execute an inner ear program. Required for hair follicle stem cell specification. Acts downstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch.
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D3Z1Q2
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MRAP2_MOUSE
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Melanocortin-2 receptor accessory protein 2
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MEMSAQRLASNRTSPQSPSNSDYTWEYEYYEIGPVSFEGLKAHKYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHQDNAESSERRFRMNSFVSDFGKPLESDKVFSRQGNEESRSLFHCYINEVEHLDRVKVCHQTTAIDSDVHLQEASRSSGRPEEELARFMKFDIPNFVNTEQSSFGEDDLLISEAPVLLENKPVSQTSRIDLD
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Modulator of melanocortin receptor 4 (MC4R), a receptor involved in energy homeostasis. Plays a central role in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of MC4R and MC4R-mediated generation of cAMP. May also act as a negative regulator of MC2R: competes with MRAP for binding to MC2R and impairs the binding of corticotropin (ACTH) to MC2R. May also regulate activity of other melanocortin receptors (MC1R, MC3R and MC5R) however, additional evidence is required in vivo.
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D3Z291
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CAHM1_MOUSE
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Calcium homeostasis modulator protein 1
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MDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNVVYSLGILLTPPLVLFLLGLVMNNNISMLAEEWKRPAGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVATLGNGSLVPGLPAPELARLLARVPCPEIYDGNWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQVAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGVLATATATATATEAVQSPSDRTEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQEAPLMSNGWAGGEPRPPRKEVATYFSKV
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Pore-forming subunit of a voltage-gated ion channel, also permeable to larger molecules including ATP, required for sensory perception of sweet, bitter and umami tastes. Specifically present in type II taste bud cells, where it plays a central role in sweet, bitter and umami taste perception by inducing ATP release from the cell, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways. Together with CALHM3, forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells (TBCs). Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to changes in extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of Ca(2+), Na(+) and K(+), as well as permeation of monovalent anions. Acts as an activator of the ERK1 and ERK2 cascade (By similarity). Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum (By similarity). May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner (By similarity).
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D3Z2R5
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SELN_MOUSE
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Selenoprotein N (SelN)
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MGQARPAARRPHSPDPGAQPAPPRRRARALALLGALLAAAAAVAAARACALLADAQAAARQESALKVLGTDGLFLFSSLDTDQDMYISPEEFKPIAEKLTGSVPVANYEEEELPHDPSEETLTIEARFQPLLMETMTKSKDGFLGVSRLALSGLRNWTTAASPSAAFAARHFRPFLPPPGQELGQPWWIIPGELSVFTGYLSNNRFYPPPPKGKEVIIHRLLSMFHPRPFVKTRFAPQGTVACLTAISDSYYTVMFRIHAEFQLSEPPDFPFWFSPGQFTGHIILSKDATHIRDFRLFVPNHRSLNVDMEWLYGASETSNMEVDIGYVPQMELEAVGPSVPSVILDEDGNMIDSRLPSGEPLQFVFEEIKWHQELSWEEAARRLEVAMYPFKKVNYLPFTEAFDRARAEKKLVHSILLWGALDDQSCUGSGRTLRETVLESPPILTLLNESFISTWSLVKELEDLQTQQENPLHRQLAGLHLEKYSFPVEMMICLPNGTVVHHINANYFLDITSMKPEDMENNNVFSFSSSFEDPSTATYMQFLREGLRRGLPLLQP
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Plays an important role in cell protection against oxidative stress and in the regulation of redox-related calcium homeostasis. Regulates the calcium level of the ER by protecting the calcium pump ATP2A2 against the oxidoreductase ERO1A-mediated oxidative damage. Within the ER, ERO1A activity increases the concentration of H(2)O(2), which attacks the luminal thiols in ATP2A2 and thus leads to cysteinyl sulfenic acid formation (-SOH) and SEPN1 reduces the SOH back to free thiol (-SH), thus restoring ATP2A2 activity. Acts as a modulator of ryanodine receptor (RyR) activity: protects RyR from oxidation due to increased oxidative stress, or directly controls the RyR redox state, regulating the RyR-mediated calcium mobilization required for normal muscle development and differentiation (By similarity). Essential for muscle regeneration and satellite cell maintenance in skeletal muscle.
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D3Z2X2
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DNHD1_MOUSE
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Dynein heavy chain domain-containing protein 1 (Coiled-coil domain-containing protein 35) (Dynein heavy chain domain 1-like protein)
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MKPHSQTSPPSLPMPSTSCRPGQTQKPKAWNWHLDPELWARSVRQQLNTCLHFILEEKKNPWFYTLQSGLVGCSCSGQEHSWDCQMKQEDLKAVVESEQRTLLKLLLSELQSLFSAVMQDGSCEAWRYLHAVLGLLPPYREMLAGQLELLPFLEQLYCWAPKVQARLELDLLDAIDKAFPPDSSLLHSSSHVDCGLWMKRFHRGPPCSACPFVKAQWDRQQKKELATWLRPLTLPELQHCLGIVGAEVALEETPWLDSLSLLPLALATDIPVQYESSDTEQAEGEPAGRKLQVASEAPEEKALKKKSSRTPVLRSQVKSLLERDWTQKKIHFLYLNVVSDRHFNPYKLVAVPPDKVNPEHYIFSPFGILHIHPVEGSEAMTLGTWHRDCALWRELQRIPFFKNCLLRKALTCWKKNVRLCGLHRIQTFLKTHLLSAIPHFGAGMLHINRLLQEFRSVSWLPKEPDRSYELVDLQKAIAKENHKALRVLCHFLNLCTSILQLIHEDTYQMQQGLQERVQNWNRIRKGQGSIYLQRTLCRHLEKKLKQAETWLLKLGKFARLIDYMICQNLVSILEDEISSFIANTLQAPRQNPFLLSQLVFDDNGQLSPMPRVESIIQGLIKSLQSIKTSALKVLQSTDLRTSRDLLYSEDNKDQDSNAEFLMPKFHGKASDAVRLFCGPNVGYVWPWKSHAITDVLEVRGHKLRGQFLHPNYDHVQEDLDKNAGIQQALAVQQSLLEDMRQEVQEFCNKHKWVEGIYEFLKAWSSQKLEDLRGSPINNYVNLVIQLKKWQERVSNMSVELLTKGKLLFLSGHDVQEELGSKLNNMRKNILEQAQNECWSRNQQLMTELTEFLRVFQTISSDIHAIAQCSQKLSEANEQYCQLEERVEYVRSLHDLIRNHCALFIAENETLDIALLDLWEAFQFERSQVSEFLLSKQHAIVPRLQQLMAAALAELEGLLAKALSGPFMDPSQEQRSTEQQLGALEHQFLNILNNFNALCNAYCTFTGYKKPMSPPASGNRPIVLQQRIWRLYRIISENLGEWKCVAFSKFNLSMAREKTDAWLTEAVRLSTALGLQSPVLQRCMRMLEEFRAYLPLLIKLGNLQLQDLNTQSLLRALGLGSLRSLDLLTLGQMLNYPLLEFAERINQVWQYDKERIHAQEILQQMQQYWEGRQLRLLNFILHVPYKPPTSERSKRPALRSPQWELVGKDSGTFLLSDYSSLQDAIQNSLQALFKILAIQKSGQLHKIALEWVAIMYGLGALLEVWVAFQQKWIFLNKVLHEMKIEFPAPELNARFKAMDDQYRTLMRISVADPMVLSLILPNTKRSPYFQGQHLQQMLKAGSGELEAIIMALEDVLYGVCANFPRLFFLSDSELVALLAAPLDTREAQLWAQRCFPHIKAVNFRSKSTKKKINQDSSSSTESAETIAVLAAGGEEVKLQEPLPLHTDLPKWLASLEKCLRFIIVNLLQSCVATRLAQGPSLIKALKAMPQQRQMPMQVYVQHWLDAVQVFPWQCILVAEEVVWRAEMEEALLESRTMHMRSVHVHNLEVLVQFIRSQRSSQDGKSLPSVRQTSLFSTLLVKAVTHRDIAQLLEKNQVSDLTDFHWVRQLKYHLGSSHLNLKSPVQCLTTIASTEPSVSPAACWIDVLGRSFMYNYEYMGPKLGPLPSLMHERQVFILLMALDEVAYGAILGRDGLGKAETVNSLAWTLGRQLVIMPCLPQIEFQCLRNYLNGALQSGAWLLLENVNQLPSSLLSALGQRLDELHYLYAPLYQKASKNISTINPTKPLLLGGGFFEKHQVSMRLGFGCFLTLHSLGPDIPANLHLLLRPVALALPDLQRVAELNLLGAGVQDASQMASRLSKLFSLERELVSGNLPCRLPLLKQVLEHTIQTLNTSQEKKSQQPYDPAASEEAALLRALLHSPLFSILDGLRLQKLQELLCGIFPNASHVLAEPVSHRLIKSVVVEELQQLGLFPASNTVTSLEQLSQALSRASGILLLGPAGSGKSTCWRSLFKIQNRLAAMEHTSTKGFQSVEIVHLYPSVLNSKEYLGWSEGPSWHYGIFPKLLHAAPYCKSVGSEEPSEKFTGIQQWIICDGAPNHAWTDSVTCLLRDPPQLSLPNGQQIARPLGTFFLIEVAEAAGMSPTVLGRCALVWCSGEQTWHSMLSVLMASLPHEYHLQQETITEFNYLAEVLVPSVLRFLTRIGASSQLQVHGHQAVCPGVAEVTSLVRILRALLDPLLHLFEEEKSYTKEDFSGSDLVTQNFKSSKTRVQSDRVNVNKKQRRHLLAISSFLFAIIWSFGAHLPSRHWPLFDDFMKKSISSLPNYPEPPPSALVFDLHVNFEDGTLVPFTGQYLSTHVKGNLGSFQPSSQTEQLLYVVDLLLSNGQPVLLAGEIATGKSAFVEVLVKPNYPVIHSPIHPALNSTHLRHLLSRGVHGQTQASSIPGHHQDSKGSILFLMEDLHLATFDPEKNCQPVLETLRQAMEGTIYAHNTLELQTLQTTVNFLATATVPGYSERPLCPRLYRLFTVLALNSMTQDTLLSRHVPSIQAWLERFPSVEREHTLARALVRASVEAWEAVCKCFMPSPLRPHYRFSPHSVSHILGSLQLLPTRMGSRGFAETFHHQEYLRRVSGLRGTRLTIMMSMRVMVRLWLHEAQRTFCDRLDSDRERSHCAKLLLEVAQNVFCGGPGSESLAKDCEEEEVEEEKVPEVESEEEIAQWETLSNSDSGSEEEEDPYGLQATTGSFLSENSLAPFPRKSVNKENTENVSQMAEQEEDIRDSSSKLQSKTPKHEWQMAPQMDLSLPLLLPVLLFYPQESPSDLVFSLELTLGSNFESPNLYLERQWENLEKQLVATAVRLKMNSGFSQCPVMVQHVAHLVRVLARPQQHALLLSEFRGTGRYTAIILASSICQAHLHYLSVESEEAIFQCLRDASWHAGLLNQPVALLVPEGVNVAIFCRLLALATSGSFPDQYTEADLDNIEEHFPKENIANKHAIKRDTILNRFYQQVCNNLHMFFMVGDNQAQNQLAPTLFLNLLQLTIASVERYEPWDQASLVRIAQFCLENDHSLPLDDGSLKYPDFKHLIPNVANIMARIHVSSACYHKHMCPALPLVTPKTFQDFLDMFLQQQQQMVLQMRMRASRIQTALKTLRLMVERHSTQTSLLTDLEAQLKGSYKSVGICQGQLEQSKIMYRQKMIECQHQESLIENLVRQHDALKAQQEVFLEQMGKAFVGPLSQLRVADFEEIRSYRAPPESVVKVTDALCDLFHQETGWSSAKQLLCTEDFYQELVFFPKEKLTDSELVKLNEALRAPGMSDAALRSVSIPAANLAVWLWAVLRYGLAQRRGLPTGLLLRQVDATLAREQARLGQFQFQAHDLLEQTRSLTKKLEDAQVSHNHVMETLNQAQCGNFQKWPMESALLTPMHMWTTQLQKLQEQAKTVFGDALLCSAAIIYLGPFPPQRRQELLEKWLSLCQGSEEALDPDDVARALRQKSVGVPKNPLLPTRTPFSILTLLSYGSELHQWDRDLKPQAKSARLLGLLLRSHIHFSSSRWPLLIDPSNQAIMWLNPLPPKQNRSLEPSPKESKEKFHVTKQDSGDNTEDELEDENNEEEDEANEQRKEQKAEENKIQGENEQEVQETEKENEPESSGSHSSLPSETQSLPSCLTVLSGTDPELGPQLLEAAANGLPVLLTNVELSLGCQELQWLLSKKNLSPPSVQPGFCLFLSTTFPIHALSRVLGFEMLKGLNVLDLGLNMEILEEQMLHEILCRERPELETRWQDLKIRAADTYEAMKADEEQLLVTLLRQNQKRQKPSKFLRKMVRTQAKICQLNAQMEELEDQKQEVVALWAPYRPVAYHGMAMVEALSPLQNLLPSFCMTSENWLAVIRRAIDSMKSYDSYRGEDLPSHLLRLKIHLARQLLTNTVVALGLIQTPLVGAFGALAMLQVTTKTPKLERLALWPGLSASPSSGHNMQIPGVIRPAWLSSKAWEECGALELLPPFAGLCESLAGHSGVWQDYLSLSSTVLGPAPGPNSEPLSLFQKLILWRVLRPDCLAGALADLTTSLLGRPLDENLGAPTMIFEHIQPTQPILILLPPPGHPTATLHPVTVIRKLAANHEKPQHLHVIALGSEDWDPVSTVVNTLCQAMLQGHWLVLDNCHLMPFWPRELLQPLQGLLDRARVVSDSELLAEPESRSVVTVHRDFRLWLIVPTEASTSLPGMLTQSSMPVFWNQSLELGRILIDSLDSQQGLCTQPLTQTLPLFFLHGLLLHRQLYGLKLQAHRGRWSQVTLTRALQIQEQLWASLGNPSAALLELTASVLYGGSLGDLEDREALVSLTRTCLNPRNMNWDQPHTPQYLLATLMPSPELGELDARTDCKAQMHLLPTPPEPRTCGLNEAPQAWLMRRQSRVLLNALQKCSSTWVPTVCGGIAQRKERQLQQRLAQAKKRLVALQALLTNNRIRSGQCVTPWAVLGPNARRPLEGFLETEVLELKHLVGTLLCDLDCLLQQLKGGTPCTSSRCAKVAQALWAGHLPQPWRSHALAGSQLPWLWLRQLSRRGHLLIRYLDSGMSENANKPERIFHLSAFRHPGRLLLALRWEAVLENSVHNPNLPGHQDSISGSLPPKWQELSNHPLHIWVENGPNPKVPKMGLLLTGLQLQHAEWDQTDGALQDSFSSQPCPLPPVSISTQARRGKDAPVSAGLGMYSCPVYMTGPFGTTKLHSKNILMHLPLPTRLSPDTCIQRRVHVCSPTLT
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Essential for the normal function of sperm flagella axonemes.
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D3Z3K2
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CIP1_MOUSE
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E3 ubiquitin-protein ligase CCNB1IP1 (EC 2.3.2.27) (Cyclin-B1-interacting protein 1) (RING-type E3 ubiquitin transferase CCNB1IP1)
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MSLCEDMLLCNYRKCRIKLSGYAWVTACSHIFCDQHGSGEFSRSPAICPACNSTLSGKLDIVRTELSPSEEYKAMVLAGLRPEVVLDISSRALAFWTYQVHQERLYQEYNFSKAENHLKQMEKMYMQQIQSKNIELTSMKGEVISMKKVLEEYKKKFSDISEKLMERNRQYQKLQGLYDSLRLRNITIASQEGSLEPGMIPQSGVFGFPPGNNSKFSLDHIPVGNQGGGDEDVQFRPFFVCSPTAPEPINNFFSFASPSHEAEQQVCSRAFKAKRI
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Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over. Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis.
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D3Z4I3
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RBM24_MOUSE
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RNA-binding protein 24 (RNA-binding motif protein 24)
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MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAAAGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ
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Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation. Plays a major role in pre-mRNA alternative splicing regulation. Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation. Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing. Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes. Plays a role in the regulation of mRNA stability. Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities. Involved in myogenic differentiation by regulating MYOG levels. Binds to multiple regions in the mRNA 3'-UTR of TP63, hence inducing its destabilization. Promotes also the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence. Plays a role in the regulation of mRNA translation. Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation. Binds to a huge amount of mRNAs (By similarity). Required for embryonic heart development, sarcomer and M-band formation in striated muscles. Together with RBM20, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity).
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D3Z5L6
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S18B1_MOUSE
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MFS-type transporter SLC18B1 (Solute carrier family 18 member B1) (Vesicular polyamine transporter) (VPAT)
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MDEAGSPAPAGTGGGDDPGGSTRETSRRLSREQIFVLVSAASMNLGCMMTYSILGPFFPKEAEKKGASNTMIGMIFGCYALFELLASLVFGKYLVHIGAKFMFIAGMFVSGGVTILFGVLDQLPEGPIFIAMCFLVRIVDAIGFGAAITASSSILAKAFPNNVATVMGSLEVFSGLGLVAGPPLGGLLYQSFGYEVPFIFLGCIVLLMIPLNLYILPSYAQESDPGKQSFWKLVTLPKMGLLAFVIISLSSCFGFLDPTLSLFVMEKFSLSTGYVGLVFLGLSLSYAISSPLFGLLSDKMPTLRKWLLVFGNLITAGCYMLLGPVPLLHIKSQLWLLVLVLVVNGISAGMSIIPTFPEMLSCAYANGFEDSISTLGLVSGLFGAMWSVGAFMGPILGGFLCEKIGFEWAAAMQGLWTLLSGVSMALFYLWEDSTARRRSKAQNSLGTEEERAALLPNDT
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Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecule (By similarity). Facilitates vesicular storage of spermine and spermidine in astrocytes with an impact on glutamatergic neuronal transmission and memory formation (By similarity). Upon antigen stimulation, regulates polyamine accumulation and release in mast cell secretory granules, which in turn potentiates mast cell degranulation and histamine secretion.
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D3Z5S8
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TET5A_MOUSE
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Terminal nucleotidyltransferase 5A (EC 2.7.7.19)
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MHQRYFWTDQGQVAFGGHYMAEGEGYFAMAEDELTGGPYIPLGGDFGGGGSSFGDRCSDYCESPTAHCNVLNWEQVQRLDGILSETIPIHGRGNFPTLELQPSLIVKVVRRRLEEKGIGVRDVRLNGSAASHVLHQDSGLGYKDLDLIFCADLRGEEEFQTVKDVVLDCLLDFLPEGVNKEKITPLTLKEAYVQKMVKVCNDSDRWSLISLSNNSGKNVELKFVDSLRRQFEFSVDSFQIKLDSLLLFYECSENPMTETFHPTIIGESVYGDFHEAFDHLCNKIIATRNPEEIRGGGLLKYCNLLVRGFRPASEEIKTLQRYMCSRFFIDFSDIGEQQRKLESYLQNHFVGLEDRKYDYLMTLHGVVNESTVCLMGHERRQTLNLITMLAIRVLADQNVIPNVANVTCYYQPAPYVADANFSNYYIAQVQPVFTCQQQTYSTWLPCN
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Cytoplasmic non-canonical poly(A) RNA polymerase that catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group and participates in the cytoplasmic polyadenylation. Polyadenylates mRNA encoding extracellular matrix constituents and other genes crucial for bone mineralization and during osteoblast mineralization, mainly focuses on ER-targeted mRNAs.
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D3Z6P0
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PDIA2_MOUSE
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Protein disulfide-isomerase A2 (EC 5.3.4.1) (PDIp)
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MDKQLLPVLLLLLGVSGSWGQGEEPGGPSEVLPEEPTGEEVPKEDGILVLNHRTLSLALQEHSALMVEFYAPWCGHCKELAPEYSKAAALLAAESAVVTLAKVDGPAEPELTKEFEVVGYPTLKFFQNGNRTNPEEYAGPKTAEGIAEWLRRRVGPSATHLEDEEGVQALMAKWDMVVIGFFQDLQGKDMATFLALAKDALDMTFGFTDQPQLFEKFGLTKDTVVLFKKFDEGRADFPVDKETGLDLGDLSRFLVIHSMHLVTEFNSQTSPKIFAAKILNHLLLFVNQTLAQHRELLTDFREAAPPFRGQVLFVMVDVAADNSHVLNYFGLKAEEAPTLRLINVETTKKYAPTGVIAITAASVAAFCQAVLHGEIKHYLLSQEIPPDWDQGPVKTLVSKNFEQVAFDETKNVFVKFYAPWCSHCKEMAPAWEALAEKYKDREDIVIAELDATANELEAFSVLGYPTLKFFPAGPDRKVIDYKSTRDLETFSKFLDSGGHLPKEEPKEPAASAPEAQANSTLGPKEEL
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Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (By similarity).
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D3Z752
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SPXN_MOUSE
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Spexin (NPQ) (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1; Spexin-2]
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MKGPSVLAVTAVVLLLVLSALENSSGAPQRLSEKRNWTPQAMLYLKGAQGRRFLSDQSRRKELADRPPPERRNPDLELLTLPEAAALFLASLEKSQKDEGGNFDKSELLEDRLFNW
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Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (By similarity). [Spexin-1]: Acts as a ligand for galanin receptors GALR2 and GALR3. Intracerebroventricular administration of the peptide induces an increase in arterial blood pressure, a decrease in both heart rate and renal excretion and delayed natriuresis. Intraventricular administration of the peptide induces antinociceptive activity. Also induces contraction of muscarinic-like stomach smooth muscles (By similarity). Intraperitoneal administration of the peptide induces a reduction in food consumption and body weight. Inhibits long chain fatty acid uptake into adipocytes. {ECO:0000250, ECO:0000269|PubMed:24550067}. [Spexin-2]: Intracerebroventricular administration of the peptide induces a decrease in heart rate, but no change in arterial pressure, and an increase in urine flow rate. Intraventricular administration of the peptide induces antinociceptive activity (By similarity).
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D3Z7P3
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GLSK_MOUSE
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Glutaminase kidney isoform, mitochondrial (GLS) (EC 3.5.1.2) [Cleaved into: Glutaminase kidney isoform, mitochondrial 68 kDa chain; Glutaminase kidney isoform, mitochondrial 65 kDa chain]
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MMRLRGSAMLRELLLRPPAAVGAVLRRAQPLGTLCRRPRGGSRPTAGLVAAARLHPWWGGGGRAKGPGAGGLSSSPSEILQELGKGGTPPQQQQQQQQQPGASPPAAPGPKDSPGETDAFGNSEGKEMVAAGDNKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDDGKGNQTVHKNLDGLL
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Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain.
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D3Z8D9
|
MD2L2_RAT
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Mitotic spindle assembly checkpoint protein MAD2B (Mitotic arrest deficient 2-like protein 2) (MAD2-like protein 2)
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MTTLTRQDLNFGQVVADVLSEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSINSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKNS
|
Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.
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D3Z8E6
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CAMP1_RAT
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Calmodulin-regulated spectrin-associated protein 1
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MVDAGGRSAAEGWRRMEAPPEGADLVPLDRYDAARAKIAANLQWICAKAYGLDNIPEDLRDPFYIDQYEQEHIKPPVIKLLLSSELYCRVCSLILKGDQAATLQGHQSVIQALSRKGIYVMESDDTPVTDADLSQAPIKMSGHMAMVDALMMAYTVEMISIEKVVASVKRFSTFSASKELPYDLEDAMVFWINKVNLKMREITEKEVKLKQQPLESPAHQKPGLEHAVMHCMLEPVDFARVVRYRREHLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHLNKCFYLTLEDMLYAPLVLKPNVMVFIAELFWWFENVKPDFVQPRDIQELKDAKTVLQQKSSRPPVPISNATKRSFLGSPAAMSPADLPPSTQPLTEGSHRYHLHSEEPECLGKGASTFSPSHPLLPLRQKQQKVSQAEEIPDQRHRSNSLTRADGQPRGAAIAWPDKKNRPVSQPTSFALHHAASCDVDPSSGDSISLARSISKDSLASNIIHLTPQNQPHPSAGKTNGKSLLSNVNIEDDEEEELVAIIRTDVSPHSPEIPRTSPQAPGLVASIRSPQRQADTLESKPDSFYLEPLMPAVLRPAKEKQIITKEDERGEGRPRTIMAKRPSEGSQPLVRKKVTGSHGSRDLNRTFTPIPCSEFAASIDPTEVGPQSTEATGEGQPLALGRFDPVPQGQVADGFFLHVGRAEEDEGRWYVGSQSPSSHDSEPWTILRQDSDSDVVDVEDAEQDFIGEDHPVVIPRYAGEEESAKLQEDMKVKEHEDKDDASGRSSPCLSTTSQLSSMSMASGSVKMTSFAERKLQRLNSCETKSSTSSSQKTTPDASESCPAPLTTWRQKREQSPSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKKGKADGAPQPLRPEHFTKEFTQHNGEDLDDGTCKTEGFLVKEEQRDLSDSQDVAFVQLHKPRDPATLHDGEKHRVISAALLEDSVGEVDVNECDLSIEKLNETISTLQQAILKISQQQEQLLMKSPTVPTSGTKNNCQDQKVKAPVHFVEPLSPTGVPGHRKPPRLGQGRNSRSGRPAELKVPKDRQQGCSRSKTPTPSVETLPHSRSLPPSTHPRSPLDPGGELPEKCLFDSYRLHDESNHRTFGLSSCKDANIVSEQMNFKEGLDTSVQEAELSSSAITGKEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLELGGESDQKPGVGFFFKDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEEQGLGKPKSKPKKPRPKSVHREESCSDSGTKCSSTPDNLSQTHSGSSLSLASAATTEPESVHSGGTPSHRVESLEALPILSRNPSRSTDRDWETASAASSLASVAEYTGPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTGPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKRPTVPKKTQTRK
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Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. Specifically recognizes growing microtubule minus-ends and stabilizes microtubules (By similarity). Acts on free microtubule minus-ends that are not capped by microtubule-nucleating proteins or other factors and protects microtubule minus-ends from depolymerization (By similarity). In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of minus-end microtubules without significantly affecting the polymerization rate: binds at the very tip of the microtubules minus-end and acts as a minus-end tracking protein (-TIP) that dissociates from microtubules after allowing tubulin incorporation (By similarity). Through interaction with spectrin may regulate neurite outgrowth.
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D3Z8K2
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CCD39_RAT
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Coiled-coil domain-containing protein 39
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MSSEFLSELHWEDGFAIPVANQENKILEDQLAKLHKEKSNLQDQLRDYEDRINSMSSHLKNVNQEFLFTQSLYKARECEIESEEHFKAIAERELGRVKDEIQQLEKEMAIILERKNDKENAIFKATQKLDGLKCQMNWDQQALEAWLEESAHKDSDSLTLQKYSQQDNNKIRALTLKLEKLTMECNEKRKLLDNELTETLSAQLELDKAAQDFRKIHVERQELIQQWENTIEQMQRRDQEIDNCALALARIKQEAREKEGVVREKIKFLENEVGNNVEYERRISIAERKVSKCRMEYQRQEANRNQLKDELDTLKTTLNRTSSDLEALRKNISKVKKDILDETGRLQKLKHHNEIVKHKLKMITEKTISIEEKATNMEDMLKEEEKNLKEVEVQLNIVKGVLFKKVQELQSAITKEKALGSEIEGTRSSLKHLNQRLHKLDFETLKQQEIMYSQDFYIQQVERRMSRLKGEINSEEKQALEVKIVELRKTMEERKSTLSLLEEQIKKLHNDLYFIKKSNGKNKDEKESLMNKIGELHLFVDRSEKELNKAKAVKEDLMIEDNLLKLQVKRARELLYSKAEEVLSLEKRKQQLCTAMEERVEEIKVHKAMLTSQIRYVDQQRQTVSSEFHERLSKIDKLKNRYEILTVVMLPPEGEEEKTQSYYVIKAAQEKEELQREGDSLDAKISKAEKEIYALQNTLQVLSSCNNNYKQSFKKVTPSSDEYGIKIQLEEQKRSADEKYRCKQRQIRELQEDIQSMENTFEVIEHLANNAREKLSEKQTLSFQLRKETEEQKPKIQRVTKQCGRLRREIRILRQTNDETLEEQDIQLREIIQFHKDIDQMLVNAMENAEIHVIFQTYFQQNGLELPTAKGPSSRSSSQSSLSSIRSLEDSIPISPPTAKVIELRFPGPPARSDSSRSSSGSNSNIPKGKKLNK
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Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Not required for outer dynein arm complexes assembly.
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D3Z8L7
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RRAS_RAT
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Ras-related protein R-Ras (EC 3.6.5.-) (p23)
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MSSGAASGTGRGRPRGGGPGPRDPPPGETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPTIEDSYTKICTVDGIPARLDILDTAGQEEFGAMREQYMRAGNGFLLVFAINDRQSFIEVSKLFTQILRVKDRDDFPIVLVGNKADLETQRQVLRSEASSFSASHHMTYFEASAKLRLNVDEAFEQLVRTVRKYQEQELPPSPPSAPRKKDGRCPCVLL
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Regulates the organization of the actin cytoskeleton. With OSPBL3, modulates integrin beta-1 (ITGB1) activity.
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D3Z902
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FBXW7_RAT
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F-box/WD repeat-containing protein 7
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MNQELLSVGSKRRRTGGSLRGNASSSQVDEEQMNRVVEEDPQQQPRHQEEEHTARNGELVGADPRPGAQNDSQQGQVEENNNRFVSVDEDSSGNQEEQEEDEEHAGEQEEEEEEEEEEEEEEEMDQESDDFDQSDDSSREDEHTHNSNVTNCTSVVDLPINQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSDYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKIIKPGFIHSPWKSAYIRQHRIDTNWRRGELRSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPSKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK
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Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the SCF complex for ubiquitination (By similarity). Identified substrates include cyclin-E (CCNE1 or CCNE2), JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, RICTOR and probably PSEN1 (By similarity). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (By similarity). SCF(FBXW7) complex mediates the ubiquitination and subsequent degradation of NFE2L1 (By similarity). Involved in bone homeostasis and negative regulation of osteoclast differentiation (By similarity). Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1 CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination (By similarity). Also able to promote 'Lys-63'-linked ubiquitination in response to DNA damage (By similarity). The SCF(FBXW7) complex facilitates double-strand break repair following phosphorylation by ATM: phosphorylation promotes localization to sites of double-strand breaks and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4, enhancing DNA non-homologous end joining (By similarity).
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D3Z9H7
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NFAC4_RAT
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Nuclear factor of activated T-cells, cytoplasmic 4 (NF-ATc4) (NFATc4) (T-cell transcription factor NFAT3) (NF-AT3)
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MGAASCEDEELEFKLVFGEEKEAPPLGPGGPGEELDSEDAPPCCRLALGEPLPYGAAPIGIPRPPPPRPGMHSPPPRPAPSPGTWESQPPRSVRLGGPGGTAGGTGGGRVLECPSIRITSISPTPDPPTSLEDAPETWGDGSPRDYPPPEGFGGYREAGGQGGGAFFSPSPGSSSLSSWSFFSDASDEAALYAACDEVESELNEAASRFGLSSPLPSPRASPRPWTPEDPWSLYGPSSGGRAPEDSWLLLSAPGPIPASPRPASPCGKRRYSSSGTPSSASPALSRRGSLGEEGPEPPPPPPLPLVRDPSSSGPFDYVGAPPTESVPQKTRRTSSEQAVALPRSEEPASCNGKLPSGTEDSVAAPGALRKEMAGMDYLAVPSPLAWSKARIGGHSPIFRTSALPPLDWPLPSQYEQLELRIEVQPRAHHRAHYETEGSRGAVKAAPGGHPVVKLLGYNEKPLTLQMFIGTADERSLRPHAFYQVHRITGKMVATASYEAVVSGTKVLEMTLLPENNMAANIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQGGGKVVSVQAASVPIECSQRSAQELPQVEAYSPSACSVRGGEELVLTGSNFLPDSKVVFIERGPDGKLQWEEEAAVNRLQSSEVTLTLTIPEYSNKRVSRPVQVYFYVSNGRRKRSPTQSFKFLPVIFKEEPLPDSSLRGFPSTSGPPFGPDMDFSPPRPPYPSYPHEDPAYETPYLSEGFGYSTPALYPQTGPPPSYRSGLRMFPETGGTTGCARLPSVSFLPRPFPGDQYGGQGSSFPLGLPFSPPAPFRPPLPSSPPLEDPFNPQSAVHPLPAEGYNEVGPGYTPGEGASEQEKSRGGYGSGFRDNVPIQGITLEEVSEIIGRDLSGFPARPGEEPPA
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Ca(2+)-regulated transcription factor that is involved in several processes, including the development and function of the immune, cardiovascular, musculoskeletal, and nervous systems. Involved in T-cell activation, stimulating the transcription of cytokine genes, including that of IL2 and IL4. Along with NFATC3, involved in embryonic heart development. Involved in mitochondrial energy metabolism required for cardiac morphogenesis and function. Transactivates many genes involved in heart physiology. Along with GATA4, binds to and activates NPPB/BNP promoter. Activates NPPA/ANP/ANF and MYH7/beta-MHC transcription. Binds to and transactivates AGTR2 gene promoter. Involved in the regulation of adult hippocampal neurogenesis. Involved in BDNF-driven pro-survival signaling in hippocampal adult-born neurons. Involved in the formation of long-term spatial memory and long-term potentiation. In cochlear nucleus neurons, may play a role in deafferentation-induced apoptosis during a developmental critical period when auditory neurons depend on afferent input for survival (By similarity). Binds to and activates the BACE1/Beta-secretase 1 promoter, hence may regulate the proteolytic processing of the amyloid precursor protein (APP). Plays a role in adipocyte differentiation. May be involved in myoblast differentiation into myotubes (By similarity). Binds the consensus DNA sequence 5'-GGAAAAT-3' (By similarity). In the presence of CREBBP, activates TNF transcription. Binds to PPARG gene promoter and regulates its activity (By similarity). Binds to PPARG and REG3G gene promoters (By similarity).
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D3Z9Z9
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SMRCD_RAT
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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (EC 3.6.4.12)
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MNLFNLDRFRFEKRSKIEEAPEAAPQPSQPGPSSPISLSAEEENAEGEVSRANTPDSDVTEKTEDSSVPEPPDNESKASLSCFQNQRTIQEYIDLSSDSEDVSPNCSSTVQEKKFSKDTVIIVSEPSEDEESHDLPSATRRNDISELEDLSELEDLKDAKLQTLKELFPQRSDSDLLKLIDSTSTMDGAIAAALLKFGDAGGGPRKRKLSSSSEAYEEDEANDDQSLKKPRGDRREESNESAEASSNWEKQESIVLKLQKEFPNFDKQELREVLKEHEWMYTEALESLKVFAEDQDVQCASQSEVTNGKEVARNQNYSKNAAKIKMKQKISMKPQNGFNKKRKKNVFNPKKAVEDSEYDSGSDAGSSLDEDYSSCEEVMEDGYKGKILHFLQDASIGELTLIPKCSQKKAQKIIELRPFNNWETLFTKMSKINGLSEDLIWNCKTVIQERDVVIRLMNKCEDISNKLTKQVTMLTGNGGGWNIEQPSLLNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLFQEGNKGPHLIVVPASTIDNWLREVNLWCPTLNVLCYYGSQEERKQIRFNIHNKYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINARNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTKPADEQSIYEKERIAHAKQIIKPFILRRVKEEVLKLLPPKKDQIELCAMSEKQEQLYSGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQYYTAEKLKEMSQLMLKEPTHCEANPDLIFEDMEVMTDFELHVLCKQYQHINSYQLDMDLILDSGKFRTLGCILSELKQKGDRVVLFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLEQDMTTVDEADEGSMPADIATLLKTSMGL
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DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing (By similarity).
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D3ZA12
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CHD6_RAT
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Chromodomain-helicase-DNA-binding protein 6 (CHD-6) (EC 3.6.4.12) (ATP-dependent helicase CHD6)
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MKMKIQKKEKQLSKLRALNHSPMSDASVNFDYKSPSPFDCSPDQGENIEEAANHCLPQKDFYTTEEEADTLFSRKLMSHNGMEDNGGRGTGVKKKRKKKEPGEQEGTKASKDREPKPKRKREPKEPKEPRRAKEPKRAKEPKEAKQKDGVKKPRKPREASGTKEGKEKRSCTDCGPRTKPKKASKDQGPTPVERKKKGKRKNETTVESLELDQSLPNPSLQSPEEPSESADSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEKDPRIAQKIKRFRNKQAQMKHIFTEPDEDLFNPDYIEIDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQILPEVKPVERPASDAWQKLETSREYKNSNRLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIAFLSEIFVRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVVIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLINGAEEKILEDFRKAHSSEASDFQLQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAILQDINRKGSTNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWAKIAELDTEANNEKESLVIDRPRVRKQTKHYNSFEEDELMEFSELDSDSDERPTRSRRLSDKARRYLRAECFRVEKNLLTFGWGRWKDILTHGRFKWPLNEKDMEVICRALLVYCVKHYKGDEKIKSFIWELITPSKDGQVQTLQNHSGLSAPVPRGRKGKKTKNQLLLPELKTADWLATCNPEVVLHDDGYKKHLKQHCNKVLLRVRMLYYLKAEILGEAADKAFEGTPARELDVLLPDIDYVEIPVDWWDAEADKSLLIGVFKHGYERYNAMRADPALCFLEKVGMPDEKSLSAEQGVTDGTSDIPERGNIDKEDSAEDKVDGLQKQTASPSDGSDGIFGEKKDDSQAVSSALTARLRRLVTIYQRCNRKELCRPEILGPGNQGYWVQEEVFRRTSDMDLINKEAQKRWTRREQADFYRTVSSFGVVYDQEKEAFDWTQFRAISRLDKKSDENLEHYFHSFVAMCRNVCRLPTWKDDGPPDASIYVEPITEERAAKTLYRIELLRKVREQVLTCPQLHERLQLCRPSLYLPVWWECGKHDRDLLIGTAKHGLNRTDYYIMNDPQLSFLDAYRNYAQHKRTDTQAPGSLCCLYQGNSKLYESLTYTPMSRTSESLESEPENLVKMDSRDDHLCLPEAGLPDITCENFVSKVQEVISLDHDESLLPESLENMMYGKTGLSQEPRSFQEAPSTNMQSRKKTVTVSASRDESCQLPGIEAEITSASSLMSSLEAGVAKMNIKNGKHLLVSISEEGEPCCSETGRSPESRGRLEARCLASPTLDTGHESGFVDLCSLSVYDSKRNFSSDQQLIDLLENKSLENKLILNQSDEEEEENEKETLAIVASTTEKPAVLDFTQPTASIPRGKNLSFHQDEAKKGRLEVGSKTPGPQRAFPPSANQCHCKHIERWAHGLGSEESEGEKPKAYEPDPYRSKANNTTVEGEPAIIPTEPFKLKHELLKEPWKESSEGGKSFSMYVPEGSEPKSEEMDFENKDDYEKDGACHSQDYPGKYSEEESKSSASGIAGDLGEEAQEVRAPTIAQLLQEKTLYSFSEWPKDRVIINRLDNICHVVLKGKWPCSHQYEPSGALPTPVLSSSAGSRSSLSEPEATEHSFSNGAALAAQIQKESFLAPVFTKDEQKHRRPYEFEVERDAKARSLEEYSASHGRPPIVLNGWHGESAIDLSCSSEGSPGATSPFPVSASTPKIGAISSLQGALGMDLSGILQAGLIHPVTGQIVNGSLRRDDAAMRRRRGRRKHIEGGMDLIFLKEQTLQAGILEVHEDAGQTTLNTTHPEGPGAASSASEPTAAASSQAEKAVPSKSLLDWLRQQADYSLDVPGFGASFSDKPKQRRPRCKEPGKLDIGSLGGEERVSAVPKEPGLRGFLPESKFNHTLAEPVLRDAGPRRRGRRPRNELLKAPAIVADSPSGMGPLFMNGLIAGMDLVGLQNVRNIPGIPLTGLVGFPAGFATMPTGEDVKNTLSMLPMMLPGMATVPQMFGVGGLLNTPMATTCTTTASASLASTKSGASATEKTTEDELSGRDVKADSLVEDKPGPSPFSDQSEPTITTSSPVAFNPFLIPGVSPGLIYPSMFLSPGMGMALPAMQQGRHSEMAGLETQKRKKKKTKGDNPTPEPASVCEREPGSDQNCTESSVTVSPEREHVAQAREEGLKDSNDDTN
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DNA-dependent ATPase that plays a role in chromatin remodeling. Regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. Activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.
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D3ZAA9
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MPP2_RAT
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MAGUK p55 subfamily member 2 (Protein MPP2)
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MPVAATNSESAMQQVLDNLGSLPNATGAAELDLIFLRGIMESPIVRSLAKAHERLEETKLEAVRDNNLELVQEILRDLAELAEQSSTAAELARILQEPHFQSLLETHDSVASKTYETPPPSPGLDPTFSNQPVPPDAVRMVGIRKTAGEHLGVTFRVEGGELVIARILHGGMVAQQGLLHVGDIIKEVNGQPVGSDPRALQELLRSASGSVILKILPSYQEPHLPRQVFVKCHFDYDPARDSLIPCKEAGLRFNAGDLLQIVNQDDANWWQACHVEGGSAGLIPSQLLEEKRKAFVKRDLELTPTSGTLCGSLSGKKKKRMMYLTTKNAEFDRHELLIYEEVARMPPFRRKTLVLIGAQGVGRRSLKNKLILWDPDRYGTTVPYTSRRPKDSEREGQGYSFVSRGEMEADIRAGRYLEHGEYEGNLYGTRIDSIRGVVASGKVCVLDVNPQAVKVLRTAEFVPYVVFIEAPDFETLRAMNRAALESGVSTKQLTEADLRRTVEESSRIQRGYGHYFDLSLVNSNLERTFRELQTAMEKLRTEPQWVPVSWVY
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Postsynaptic MAGUK scaffold protein that links CADM1 cell adhesion molecules to core components of the postsynaptic density. In CA1 pyramidal neurons, required for synaptic KCNN2-containing channel function and long-term potentiation expression (By similarity). Seems to negatively regulate SRC function in epithelial cells (By similarity).
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D3ZAR1
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ARH_RAT
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Low density lipoprotein receptor adapter protein 1 (Autosomal recessive hypercholesterolemia protein homolog)
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MDALKSAGRALIRSPSLAKQSWAGGRHRKLPENWTDTRETLLEGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTAQMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFEFWQVSKEEKEKREKANQEGGDVPGTRRDSTPSLKTSVATGNLLDLEELAKAPLSTVSANTKNMDDALRPQVLGNNSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDIHYAQCLSPTDWDKPDSSGFDQDDVFSF
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Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytosis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface (By similarity). Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression.
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D3ZAW2
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PISD_RAT
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Phosphatidylserine decarboxylase proenzyme, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase beta chain; Phosphatidylserine decarboxylase alpha chain]
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MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL
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Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).
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D3ZAZ5
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BCAR3_RAT
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Breast cancer anti-estrogen resistance protein 3 homolog (BCAR3 adapter protein, NSP family member) (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B) (p130Cas-binding protein AND-34)
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MAAGKFASLPRHMPVNHQFPLASSMDLLSSKSPLAEHRTEAYPDVSIHGTLPRKKKGPPPIRSCDSASHMGTLPHSKSPRQSSPLTQDLILEKPLPDWKGDSFAFRDPYLLDPTLEYVKFSKERHIMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLWCLEERYGTSPGRGREGSFAEGRPDVVKRLSLTTGGIQARDHSLPRGNLLRNKDKSGSQPACLDHVQDRKAATLKAHQSESHLPIGCKLPPQSPSVDTSPCPNSPVFRTGSEPTLSPALVRRFSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPPSPSPWLNSEANYCELNPAFAVGCDRGAKLLSQALDSHEMLLTAKQNGASGPRNSGINYSILDGDDQGRHWDPLAVQTDEGQEDETKFVPPVMETVSSFRPNDFESKLLPPENKPLETAMLKHAKELFTNHDARVIAQHMLSVDCKVARILEVSEDMKRSMGVSSGLELITLPHGRQLRLDIIERHNTMAIGIAVDILGCTGTLENRAGTLNKIIQVAMELKDTMGDLYSFSAIMKALEMPQITRLEKTWTALRHHYTQTAILYEKQLKPFSKILHEGRESTYVPASSVSVPLLMPLVTLMERQAVTFEGTDMWEKNDESCEIMLSHLATARFMAEASESYRMNAERVLADFQPDEEMTEILKTEFQMRLLWGSKGAEVNQNERYDKFNQILTALSRKLEPPSGKQAEL
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Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis. Promotes insulin-mediated membrane ruffling. In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (By similarity). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB/SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity).
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D3ZB51
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TUTLB_RAT
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Protein turtle homolog B (Immunoglobulin superfamily member 9B)
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MIWYVATLIASVISTRGLVAQVAHGLREEPEFVTARAGEGVVLRCDVIHPVTGQPPPYVVEWFKFGVPIPIFIKFGYYPPHVDPEYAGRASLHDKASLRLEQVRSEDQGWYECKVLMLDQQYDTFHNGSWVHLTINAPPTFTETPPQYIEAKEGGSITMTCTAFGNPKPIVTWLKEGTLLSASGKYQVSDGSLTVTSVSREDRGAYTCRAYSIQGEAVHTTHLLVQGPPFIVSPPENITVNISQDALLTCRAEAYPGNLTYTWYWQDENVYFQNDLKLRVRILIDGTLIIFRVKPEDAGKYTCVPSNSLGRSPSASAYLTVQYPARVLNMPPVIYVPVGIHGYIRCPVDAEPPATVVKWNKDGRPLQVEKNLGWTLMEDGSIRIEEATEEALGTYTCVPYNTLGTMGQSAPARLVLKDPPYFTVLPGWEYRQEAGRELLIPCAAAGDPFPVITWRKVGKPSRSKHNALPSGSLQFRALSKEDHGEWECVATNVVTSITASTHLTVIGTSPHAPGSVRVHVSMTTANVSWEPGYDGGYEQTFSVWMKRAQFGPHDWLSLSVPLGPSWLLVDSLEPETAYQFSVLAQNRLGTSAFSEVVTVNTLAFPVTTPEPLVLVTPPRCLTANRTQQGVLLSWLPPANHSFPIDRYIMEFRVGERWEMLDDAIPGTDGEFFAKDLSQDTWYEFRVLAVMQDLISEPSNIAGVSSTDIFPQPDLTDDGLARPVLAGIVATICFLAAAILFSTLAACFVNKQRKRKLKRKKDPPLSITHCRKSLESPLSSGKVSPESIRTLRAPSESSDDQGQPAAKRMLSPTREKELSLYKKTKRAISSRKYSVAKAEAEAEATTPIELISRGPDGRFVMGPSEMEPSVKGRRIEGFPFAEETDMYPEFRQSDEENEDPLVPTSVAALKPQLTPMSSSQDSYLPPPAYSPRFQPRGLEGPSGLGGRLQATGQARPPAPRPFQHGQYYGYLSSSSPGEVEPPPFYMPEVGSPLSSVMSSPPLHTEGPFGHPTIPEENGENASNSTLPLTQTPTGGRSPEPWGRPEFPFGGLETPAMMFPHQLHPCDVAESLQPKPCLPRGLPPAPLQVPAAYPGMLSLEAPKGWVGKSPGRGPIPAPPATKWQERPMQPLVSQGQLRHTSQGMGIPVLPYPEPAEPGGHGGPSTFGLDTRWYEPQPRPRPSPRQARRAEPSLHQVVLQPSRLSPLTQSPLSSRTGSPELAARARPRPGLLQQAEMSEITLQPPAAVSFSRKSTPSSTGSPSQSSRSGSPSYRPTMGFTTLATGYPSPPPGPAPPAPGDNLDVFGQTPSPRRMGEEPLRPEPPTTLPTSG
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Transmembrane protein which is abundantly expressed in interneurons, where it may regulate inhibitory synapse development. May mediate homophilic cell adhesion (By similarity).
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D3ZBE5
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NEK7_RAT
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Serine/threonine-protein kinase Nek7 (EC 2.7.11.34) (Never in mitosis A-related kinase 7) (NimA-related protein kinase 7)
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MDEQPQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRASCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALDHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNICINPDPEKRPDIAYVYDVAKRMHACTASS
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Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis (By similarity). Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity). Phosphorylates RPS6KB1. Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity (By similarity). Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1 (By similarity). Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis (By similarity).
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D3ZBN0
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H15_RAT
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Histone H1.5
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MSETAPAETTAPAPVEKSPAKKKTKKAGAAKRKATGPPVSELITKAVSASKERGGVSLPALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKVASGEAKPKAKKTGAAKAKKPTGATPKKPKKTAGAKKTVKKTPKKAKKPAAAGVKKVTKSPKKAKAAAKPKKATKSPARPKAVKSKASKPKVTKPKAAKPKAAKVKKAVSKKK
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Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
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D3ZBP4
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MICA1_RAT
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[F-actin]-monooxygenase MICAL1 (EC 1.14.13.225) (EC 1.6.3.1) (Molecule interacting with CasL protein 1) (MICAL-1)
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MASPTSTNPAHDHFETFVQAQLCQDVLSSFQGLCRALGVESGGGLPQYHKIKAQLNYWSAKSLWAKLDKRASQPAYQQGQACTNTKCLVVGAGPCGLRAAVELALLGARVVLVEKRTKFSRHNVLHLWPFTIHDLRALGAKKFYGRFCTGTLDHISIRQLQLLLLKVALLLGVEIHWGFTFTGLQPPPKKGSGWRARIQPSPPAQLASYEFDVLISAGGGKFVPEGFTIREMRGKLAIGITANFVNGRTVEETQVPEISGVARIYNQKFFQSLLKATGIDLENIVYYKDDTHYFVMTAKKQCLLRLGVLRQDLPETDQLLGKANVVPEALQQFARAAADFATQGKLGKLEFAQDARGRPDVAAFDFTSMMRSESSARIQEKHGARLLLGLVGDCLVEPFWPLGTGVARGFLAAFDAAWMVKRWAEGTGPLELLAERESLYQLLSQTSPENMHRNVAQYGLDPATRYPNLNLRAVTPNQVQDLYDIMDKEHARKKSDETDARKTTTGSAGTEELLHWCQEQTAGFPGVSVTDFSSSWADGRALCALVHRLQPGLLEPSELQGMSALEATAWALRVAEYELGIIPVLSAQAVVAGSDPLGLIAYLSHFHSAFKNTPHSSGLVSQPHGTPSAILFLGKLQRSLQRTRTKVEEETPCTEEPPVSEPSVPPALPSEHEEAGAEDVCELCGKRLYILERFCVDGHFFHRGCFCCRTCEATLRPGGYGQYPGDGYFYCLQHLPQEDQKEADNNGSPENQELPTPGDSTTQSGPSSPVPPVTEASPVPSPSQPARRLIRLSSVERLRLSSLNIIPDSGVEPPPKPPRSCLDLAQESLKSSFMGWGVLRAPQVPEAIEKGEEEEEEEEEEEEEEEELPPPLALEVEQSLLTLAKNSGDMTKYPTWRRTLMRRAKEEEMKRFCKAQAIQRRLNEIEAAMRELETEGMKLEVALRKESSSPEKQKKLWLEQLLQLIQKKNSLVTEEAELMITVQELDLEEKQRQLDHEFRGINREETLKTQADRLSEDRVLRKLLDVVNQRDALIQFQEERRLREMPV
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Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L acts by antagonizing STK38 and STK38L activation by MST1/STK4. Involved in regulation of lamina-specific connectivity in the nervous system such as the development of lamina-restricted hippocampal connections. Through redox regulation of the actin cytoskeleton controls the intracellular distribution of secretory vesicles containing L1/neurofascin/NgCAM family proteins in neurons, thereby regulating their cell surface levels. May act as Rab effector protein and play a role in vesicle trafficking.
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D3ZCM3
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ABCG4_RAT
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ATP-binding cassette subfamily G member 4 (EC 7.6.2.-) (ATP-binding cassette, sub-family G (WHITE), member 4)
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MAEKALEAVGCGLGPGAVAMAVALEDGAEPPVLTTHLKKVENHITEAQRFSHLPKRSAVDIEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAHGGRTVICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDLNPMLFRAVQNGLCTMAEKKSSPEKNEVPAHCPTCPPELDPIESHTFATSTLTQFCILFRRTFLSILRDTVLTHLRFMSHVLIGVLIGLLYLHIGDDASKVFNNTGFLFFSMLFLMFAALMPTVLTCELICLAKMAVFMREHLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALSIATALVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGLILTIYGMERGHLTCLEDHCPFRDPQIILHELDVEEAKLYMDFLVLGIFFLALRLLAYLVLRYRVKSER
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ATP-dependent transporter of the ATP-binding cassette (ABC) family that may be involved in the cellular efflux of sterols, in particular cholesterol and desmosterol (a cholesterol precursor), to high-density lipoprotein (HDL) (By similarity). May play an important role in the removal of amyloid-beta peptides from brain,in a process that can be antagonized by desmosterol. However it is unclear whether ABCG4 can directly transport amyloid-beta peptides or whether peptide export may be facilitated due to changes in the membrane lipid environment (By similarity). Induces apoptosis in various cells (By similarity).
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D3ZD32
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CHD5_RAT
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Chromodomain-helicase-DNA-binding protein 5 (CHD-5) (EC 3.6.4.12) (ATP-dependent helicase CHD5)
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MRGPLGTEEELPRLFAEEMENEEEMSEEEDGGLEGFEDFFPAEPVSLPKKKPKKLKESKSKGKRKKKEGSNDELSENEEDLEEKSESEGSDYSPTKKKKKKLKEKKEKKAKRKKRDEDEEDNEDGGLKEPKSSGQLMAEWGLDDVDYLFSEDDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTIAPPLAISPQQVPQPLPVRKAKTKEGKGPGVRKKNKGAKDSKKKGRGKRVAGLKFRFGGISKRKKGSSSEEDEPEDSDLDNASIHSSSVRSECSAALGKKNKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDEEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPEVEPGMPPPRPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMVHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDEIDIPYYDNLKQTYWGHRELMLGEDARLPKRLVKKGKKLKDDKQEKPPDTPIVDPTVKFDKQPWYIDSTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRGGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPMLPNGSYDGSSLVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTEELFKDDVEGMMSQGQRPTTPIPDVQSTKGGSLAAGAKKKHGGTPPGDNKDVEDSSVIHYDDAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREVIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRWGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLVPEGPEGKKPGEVISSDPNTPVPASPAQLPPAPLGLPDKMEAQLGYTDEKESGTQKPKKSLEIQALPTALDRVEAEDKHQSSDSKDRAREERMEEVEKAQGSPEQPLKEETLPDKEPVPDKLELSLSHSNDFRPDDPKAEEKEPTETQQNGDREEDEEGKKEDKNGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYEIWHRRHDYWLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEVHKGNYLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQGAFGSSQMYNNSFGPNFRGPGPGGIVNYNQMPLGPYVTGR
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Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa.
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D3ZDI6
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MYLIP_RAT
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E3 ubiquitin-protein ligase MYLIP (EC 2.3.2.27) (Inducible degrader of the LDL-receptor) (Idol) (Myosin regulatory light chain interacting protein) (MIR) (RING-type E3 ubiquitin transferase MYLIP)
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MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKESLLAGHLQCSPEQAVELSALLAQTKFGDYNQNTAQYSYEDLCEKELSSSTLNSIVGKHKELEGISQASAEYQVLQIVSAMENYGIEWHAVRDSEGQKLLIGVGPEGISICKEDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRNDQSPPSSPLKSSDSSMSCSSCEGLSCQQTRVLQEKLRKLKEAMLCMVCCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI
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E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR.
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D3ZDK2
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UB2D1_RAT
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Ubiquitin-conjugating enzyme E2 D1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D1) (Ubiquitin carrier protein D1) (Ubiquitin-conjugating enzyme E2(17)KB 1) (Ubiquitin-conjugating enzyme E2-17 kDa 1) (Ubiquitin-protein ligase D1)
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MALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLTVHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDPNPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM
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Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4 (By similarity). Mediates ubiquitination of PEX5.
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D3ZDK7
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PGP_RAT
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Glycerol-3-phosphate phosphatase (G3PP) (EC 3.1.3.21) (Aspartate-based ubiquitous Mg(2+)-dependent phosphatase) (AUM) (EC 3.1.3.48) (Phosphoglycolate phosphatase) (PGP)
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MAEAEAGGDEVRCVRLSAERAKLLLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPMGPEAGLEVFGTAYCSALYLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRYLQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQESDCMFKKKMVPDFYVDSIADLLPALQG
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Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (By similarity). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By similarity).
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D3ZE55
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PCDH8_RAT
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Protocadherin-8 (Activity-regulated cadherin-like protein) (Arcadlin)
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MSPVKRWGSPCLFPLQLFSLCWVLSVAQSKTVRYSTFEEDAPGTVIGTLAEDLHMKVSGDTSFRLMKQFNSSLLRVREGDGQLTVGDAGLDRERLCGQSPQCVLAFDVVSFSQEQFRLVHVEVEVRDVNDHAPRFPRAQIPVEVSESAPVGTRIPLEVPVDEDVGANGLQSVRLAEPHSPFRVELQTRADGAQCADLVLLQELDRESQASYSLELVAQDGGRPPRSATAALSVRVLDANDHSPAFPQGAVAEVELAEDAPVGSLLLDLDAADPDEGPNGDVVFTFGARTPPEARHLFRLDPRSGRLTLAGQVDYERQDTYELDVRAQDRGPGPRTATCKVIVRIRDVNDNAPDISITPLAAPGAPATSPFAAAAAAAALGGADAASSAGSGTQETGVTSLVPEGAARESLVALVSTSDRDSGANGQVRCALYGHEHFRLQPAYAGSYLVVTAASLDRERIAEYNLTLVAEDRGAPPLRTVRPYTVRVGDENDNAPLFTKPVYEVSVRENNPPGAYLATVAARDPDLGRNGQVTYRLVEAEVGRSGEAVSTYVSVDPATGAIYALRSFDYETLRQLDVRVQASDGGSPQLSSNALVQVRVLDQNDHSPVLVHPAPANGSLEVAVPGRSTKDTAVARIQARDADEGANGELAFDLLQQEPREAFSIGRHTGEIVLTGDLSQEPPGRVFKALLVISDGGRPPLTTTATVSFVVTAGGGSAVPASAGSPEHFRPPGSRLAPSGPSLQWDTPLIVIIVLAGSCTLLLAAIIAIATTCNRRKKEVRKGGALREERPGAAGGGASAPGSPDETARGTGPRPNMFDVLTFPGSGKAPFGSPAADAPPPAVAAAEVPGSEGGSATGESACHFEGQQRLRGAHAEPYSASPGFGKEPAPPVAVWKGHSFNTISGREAEKFSGKDSGKGDSDFNDSDSDISGDALKKDLINHMQSGLWACTAECKILGHSDRCWSPSCAGPNTHPPPHPPAQMSTFCKSTSLPRDPLRRDNYYQAQLPKTVGLQSVYEKVLHRDYDRTVTLLSPPRPGRLPDLQEIGVPLYESPPGGRYVSPKKGTNENV
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Calcium-dependent cell-adhesion protein. May play a role in activity-induced synaptic reorganization underlying long term memory. Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its action on CDH2 endocytosis.
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D3ZEF4
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CUL7_RAT
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Cullin-7 (CUL-7)
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MVGELRYREFRVPLGPGLHAYPDELIRQRVGHNGHPEYQIRWLILRRGDDGDSSQVDCKAEHILLWMTDDEIYANCHKMLGEDGQVIRPSQESAEAGALDKSVLGEMETDVKSLIQRALRQLEECVGAVPPAPLLHTVHVLSAYASIEPLTGVFKDRRVLDLVMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLTEHPMSFEGVQLPQVPGRLLFSLVKRYLCVTFLLDRLNGNAEDQDAQNNFIPEELNAGRGRVELEFSMAMGTLISELVQAMRWDWASSRSESSSPIFQPPPTEFFRPRAQRFRRSRRFRPRTAFASVNTYALYVRDTLRPGMRVRMLEDFEEISAGDEGQFRQSNDGMPPVQVLWDSTGHTYWVHWHMLEILGFEEDIEDVVDIDDQGAMVHGGLGVAPPFQHWKPIAQLFAEPYVVPEEEDREEREHLTQAEWWELFFFIKKLNAEERQHVVELLQEFLEGEHVLDFEILPELTVPVELAQDLMLSLPQQLDDSALRDLFNCYVYRKYGPEVLVGKRNRPFVLDDQLNLFRIETDSEAQDPPSQSASPALRQLVEGLGPSGKLLVDLERALSSEAPQENEVKPCLLQLQEEPQPFLTLMRSLDTPASNKALHLTALRILMQLVNFPEALLLPWHEAMDACMTCLRSPNTDREVLQELIFFLHRLTSTSRDYAVILNQLGARDAISKVLEKHRGKLELAQELRDMVFKCEKHAHLYRKLTTNILGGCIQMVLGQIEDHRRTHRPIQIPFFDVFLRYLCQGSSAEVKKNKYWEKVEVSSNPHRASRLTDRNAKTYWESNGTAGSHFITVHMRPGVLIRQLTLLVAGEDSSYMPAWVVVCGGDSISSVNTELNAVNVMPHASRVILLENLTRFWPIVQIRIKRCQQGGINTRIRGLEVLGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDIAEDRRSLLHLSSRLNGALRQEQNFADRFLPDEEAALALSKTCWEALVSPLVQNITSPDEDSTSSLGWLLNQYLECREAAYNPQSRAAAFSSRVRHLTHLLVHVEPCEAAPPVVAISQSKGRNRSHDWSSLTTRGLPSSIMRNLTRCWRSVVEEQVNKFLTSSWKDDDFVPRYCERYYILQKSSSELFGPRAAFLLAMRNGCADALLRLPFLRAAHVSEQFARHIDQRIQGSRMGGARGMEMLAQLQRCLESVLILSPLEIATTFEHYYQHYMADRLLSVGSSWLEGAVLEQIGPCFPGRLPQQMLQTLNISEELQRRFHVYQLQQLDQELLKLEDTEKKIQVAHEDSGKEHKSKKEDAAGETAAVAMADEEEEEGKKEEGEEEEGEGEEELEEEEERYYEGTMPEVCVLVLSPRFWPVASVCHMLNPTTCLPSYLRGTINHYSNFYSKSQSHSGLEKESPRQLQWTWQGRAEVQFGDQILHVSTVQMWLLLHLNHLKAVSVESLQALSELPPEVLNKAIGPLTSSRGPLDLQEQKNIPGGVLKIRDDSEEPRPRRGNVWLIPPQTYLKAEDEEGRNLEKRRNLLNCLVVRILKAHGDEGLHIDQLVHLVLEAWEKGPCPPRGLVSSLGRGAACRSSDVLSCILHLLGKGTLRRHDDRPQMLFYAVPITVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYASCTGTQTFSTFR
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Core component of the 3M and Cul7-RING(FBXW8) complexes, which mediates the ubiquitination of target proteins. Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Interaction with CUL9 is required to inhibit CUL9 activity and ubiquitination of BIRC5. Core component of a Cul7-RING ubiquitin-protein ligase with FBXW8, which mediates ubiquitination and consequent degradation of target proteins such as GORASP1, IRS1 and MAP4K1/HPK1. Ubiquitination of GORASP1 regulates Golgi morphogenesis and dendrite patterning in brain. Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Acts as a regulator in trophoblast cell epithelial-mesenchymal transition and placental development. Does not promote polyubiquitination and proteasomal degradation of p53/TP53. While the Cul7-RING(FBXW8) and the 3M complexes are associated and involved in common processes, CUL7 and the Cul7-RING(FBXW8) complex may be have additional functions (By similarity). {ECO:0000250, ECO:0000269|PubMed:21572988}.
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D3ZEH5
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SIDT2_RAT
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SID1 transmembrane family member 2
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MIAWRLPLCVLLVAAVESHLGALGPKNVSQKDAEFERTYADDVNSELVNIYTFNHTVTRNRTEGVRVSVNVLNKQKGAPLLFVVRQKEAVVSFQVPLILRGLYQRKYLYQKVERTLCQPPTKNESEIQFFYVDVSTLSPVNTTYQLRVNRVDNFVLRTGELFTFNTTAAQPQYFKYEFPDGVDSVIVKVTSKKAFPCSVISIQDVLCPVYDLDNNVAFIGMYQTMTKKAAITVQRKDFPSNSFYVVVVVKTEDQACGGSLPFYPFVEDEPVDQGHRQKTLSVLVSQAVTSEAYVGGMLFCLGIFLSFYLLTVLLACWENWRQRKKTLLVAIDRACPESGHPRVLADSFPGSAPYEGYNYGSFENGSGSTDGLVESTGSGDLSYSYQDRSFDPVGARPRLDSMSSVEEDDYDTLTDIDSDKNVIRTKQYLCVADLARKDKRVLRKKYQIYFWNIATIAVFYALPVVQLVITYQTVVNVTGNQDICYYNFLCAHPLGNLSAFNNILSNLGYILLGLLFLLIILQREINHNRALLRNDLYALECGIPKHFGLFYAMGTALMMEGLLSACYHVCPNYTNFQFDTSFMYMIAGLCMLKLYQKRHPDINASAYSAYACLAIVIFFSVLGVVFGKGNTAFWIVFSVIHIISTLLLSTQLYYMGRWKLDSGIFRRILHVLYTDCIRQCSGPLYTDRMVLLVMGNIINWSLAAYGLIMRPNDFASYLLAIGICNLLLYFAFYIIMKLRSGERIKLIPLLCIVCTSVVWGFALFFFFQGLSTWQKTPAESREHNRDCILLDFFDDHDIWHFLSSIAMFGSFLVLLTLDDDLDTVQRDKIYVF
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Mediates the translocation of RNA and DNA across the lysosomal membrane during RNA and DNA autophagy (RDA), a process in which RNA or DNA is directly imported into lysosomes in an ATP-dependent manner, and degraded. Involved in the uptake of single-stranded oligonucleotides by living cells, a process called gymnosis (By similarity). In vitro, mediates the uptake of linear DNA more efficiently than that of circular DNA, but exhibits similar uptake efficacy toward RNA and DNA. Binds long double-stranded RNA (dsRNA) (500 - 700 base pairs), but not dsRNA shorter than 100 bp (By similarity).
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D3ZEN0
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MILK2_RAT
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MICAL-like protein 2 (Junctional Rab13-binding protein) (Molecule interacting with CasL-like 2) (MICAL-L2)
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MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFNALRKENIYENNKLAFQVAEEQLGIPALLDAEDMVALKIPDRLSILTYVSQYYNYFHGRSPIGGMAGMKRPSSDSTEELSGKKKVPSQPAKLSSPVPTQRLPLSPARTNPVVQRNEGVSERPSPKAAPGTVGSSVSSICGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHHSSEAVSVSPKLSNLASRQPGGGIADTRPIGVSQKVLETNGEATPLRARTAAWEHAGGNRAAKGFVQTELTPPATSRVHVGSPAGPRLPMSTVTTTSANSKATTHVTNSSPVGWSSSAQSSTGTSGSRPVVSPSALGAHLSVPQGQAASKGVKTQLNSSTDSSSTAPTPAWTSSSSRTQQAREKFFHNLSPAPAPAPASSSSSHASRVPTVVTAPSGKVSPLVNTSTSKVPSATVVTVPTSKASTVVTAPTSKAPTVVTVPISKAPTVVTAPTSKVSTVVTVPTSKASTVVTAPTSKASTVVTVPTGRGHVVVNTSASKVSGVVDNPAQESSREQALSVLRKALPGLTRAGSQAPSRSSPATSSVLITLPKNEVPPKVPSAKLSHSTTQAFSPTPKMEPTAPLSVGSTSWTSVSLQAGKKSPGISPGIGKTSAVSRPQAEVKGTSGPGPTSQEGQEEGPEGWRARLKPVDKSIPSARALEQKEPVLAEPRAGDTPRKASSSSDSSIHITLTPIQQKRTPCLADSGSSLAAPSPPSRRKKLVVPPTLDVSADWLQPELKKQDDQTRSCKEKTATWGTRESSAILDNDLVSPDEAVTSPVRLHPNYISQEELQRQLQDIERQLDALELRGVELEKRLRAAEGDASEDGLMVDWFRLIHEKQLLLRRESELMYKSKDQCLEERQLDLQGELRRLMEKPEGLKSPQDRKREQELLNQYVNTVNDRSDIVDNLDEDRLREQEEDQMLESMIQNLGLQRKKSKSFLSKIWSSKSKSGQT
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Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth.
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D3ZER2
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BFSP2_RAT
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Phakinin (49 kDa cytoskeletal protein) (Beaded filament structural protein 2) (Lens fiber cell beaded filament protein CP 47) (CP47) (Lens fiber cell beaded filament protein CP 49) (CP49) (Lens intermediate filament-like light) (LIFL-L)
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MSERRVAMDLPSGSNASMPLQRHRVSSLRGTRSPSSLDSPPASRTSAVGSLVRAPGVYVGVAPSGGIGGLGARVTRRALGISSVFLQGLRSSGLATAPAPGPERNHATAEDLGGCLVEYMTKVHALEQVSQELETQLRAHLESKAKRSGGWDALRASWASSYQQVGEAVLENARLMLQMETIQAGADDFKERYENEQPFRKAAEEEVSSLYKVIDEANLTKTDLEHQIESLKEELGSLSRSYEEDVKVLYKQLAGSELEQTDVPMGTGLDDVLETIRVQWERDVEKNRAEAGAVLQAKQQTEVVHVSQTQEEKLAAALSVELHDTSRQVQSLQAETESLRALKRGLENTLHDAKHWHDMELQNLGAVVGRLEAELAEIHSETEQQQQERAHLLACKGQLQKDVASYHALLDREESN
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Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Plays a role in maintenance of retinal lens optical clarity (By similarity).
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D3ZEY4
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DGKQ_RAT
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Diacylglycerol kinase theta (DAG kinase theta) (DGKtheta) (EC 2.7.1.107)
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MATAAESGARTWPGSGSPRLGSPAGSPVLGISGRARPGSGPERTGRAIGSVAPGHSFRKVTLTKPTFCHLCSDFIWGLAGFLCDVCNFMSHEKCLKQVKTPCTSIAPSLVRVPVAHCFGSLGLYKRKFCVVCRKSLEVPAFRCEVCELHVHPDCVPFACSDCRQCHQDGQHDYDTYHHHWREGNLPSGARCEVCRKTCGSSDVLAGVRCEWCGVQAHSVCSTALTPECTFGRLRSMVLPPSCVRLLSRNFSKMHCFRIPETMVLELGDGDDGLDGSAAVGTGREVSAATESTKQTLKIFDGNDSMRKNQFRLVTVSRLARNEEVMEAALRAYYINEDPKDFQLQALPLTLLSGNAQALGKAGTTEEETSKDSGPGDSVPEAWVIRSLPRTQEILKIYPDWLKVGVAYVSIRVNSQSTARSVVQEVLPLFGRQVEDQERFQLIEVLMSSRQVQRTVLVDEEPLLDRLRDIRQTSVRQASQTRFYVAEARAVTPHVSLFVGGLPPGLSPQDYSNLLHEAMATKAAVVSVSHVYSLQGAVVLDVTCFAEAERLYMLARDTAVHGRPLTALVLPDVLHTKLPPDCCPLLVFVNPKSGGLKGRELLCSFRKLLNPHQVFELTNGGPLPGFHLFSQVPCFRVLVCGGDGTVGWVLAALEETRRHLACPEPSVAILPLGTGNDLGRVLRWGAGYSGEDPFSVLVSVDEADAVLMDRWTILLDAHEIDSTENNVVETEPPKIVQMNNYCGIGIDAELSLDFHQAREEEPGKFTSRFHNKGVYVRVGLQKISHSRSLHKEIRLQVEQQEVELPSIEGLIFINIPSWGSGADLWGSDSDSRFEKPRIDDGLLEVVGVTGVVHMGQVQGGLRSGIRIAQGSYFRVTLLKATPVQVDGEPWIQAPGHMIISATAPKVHMLRKAKQKPRKAGAIRDTRVDTLPAPEGNPL
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Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Within the adrenocorticotropic hormone signaling pathway, produces phosphatidic acid which in turn activates NR5A1 and subsequent steroidogenic gene transcription (By similarity). Also functions downstream of the nerve growth factor signaling pathway being specifically activated in the nucleus by the growth factor. Through its diacylglycerol activity also regulates synaptic vesicle endocytosis (By similarity).
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