UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
P32185 | ASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVF | 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. |
A1L107 | MAASLGFRGAASGLRYWSGRRRPVGSLAAVCSRSMASKTPVGFIGLGNMGNPMAKNLIKHGYPLILYDVFPDVCKEFKEAGEQVASSPADVAEKADRIITMLPSSMNSIEVYSGANGILKKVKKGSLLIDSSTIDPSVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVENEFAAAQELLGCMGSNVLYCGAVGSGQSAKICNNMLLAISMIGTAEAMNLGIRSGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSSNNYQGGFGTTLMAKDLGLAQDSATSTKTPILLGSVAHQIYRMMCSKGYSKKDFSSVFQYLREEETF | 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH Amino-acid degradation; L-valine degradation. Homodimer. Higher level in kidney, liver, and heart than in muscle. Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily. |
A9AKG8 | MKISRSLSTVEVHTGGEAFRIVTSGLPRLPGDTIVRRRAWLKEHADEIRRALMFEPRGHADMYGGYLTEPVSPNADFGVIFVHNEGYSDHCGHGVIALSTAAVELGWVQRTVPETRVGIDAPCGFIEAFVQWDGEHAGPVRFVNVPSFIWQRDVAVDTPSFGTVTGDIAYGGAFYFYVDGAPFDLPVRESAVERLIRFGAEVKAAANAKYPVEHPEIPEINHIYGTIIANAPRDPRSTQANCCVFADREVDRSPTGSGTGGRVAQLYQRGLLAAGDTLVNESIVGTVFKGRVLRETTVGGMPAVIPEVEGSAHICGFANWIVDERDPLTYGFLVR | Catalyzes the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t3LHyp) to cis-4-hydroxy-D-proline (c4DHyp), albeit with 3.6-fold lower efficiency. Displays no proline racemase activity. trans-3-hydroxy-L-proline = cis-3-hydroxy-D-proline trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline kcat is 1.3 sec(-1) for t4LHyp epimerization. kcat is 30 sec(-1) for t3LHyp epimerization. Belongs to the proline racemase family. |
F8J2B3 | MKTLLLTLVVVTIVCLDLAYTRKCYKTHPYKSEPCASGENLCYTKTWCDFRCSQLGKAVELGCAATCPTTKPYEEVTCCSTDDCNRFPNWERPRPRPRGLLSSIMDHP | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
Q53B54 | TKCYITPDVKSETCPDGENICYTKSWCDVFCTSRGKRIDLGCAATCPKVKPGVDIKCCSTDNCNPFTPWKRH | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. LD(50) is 210 ug/kg by intraperitoneal injection into mice. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
Q9YI13 | MKTLLLTLVVVTIVCLDLGYTIVCHTTATSPISAVTCPPGENLCYRKMWCDAFCSSRGKVVELGCAATCPSKKPYEEVTCCSTDKCNPHPKQRPG | Binds with high affinity to muscular (tested on Torpedo marmorata, Kd=0.4 nM) and neuronal (tested on chimeric alpha-7/CHRNA7, Kd=0.95 nM) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission (PubMed:9305882). It also shows an activity on GABA(A) receptors (PubMed:16549768, PubMed:25634239). It antagonises GABA-activated currents with high potency when tested on primary hippocampal neurons (PubMed:25634239). It inhibits recombinantly expressed GABA(A) receptors composed of alpha-2-beta-2-gamma-2 (GABRA2-GABRB2-GABRG2) subunits with high potency (62.3% inhibition at 20 uM of toxin) (PubMed:25634239). It also shows a weaker inhibition on GABA(A) receptors composed of alpha-1-beta-2-gamma-2 (GABRA1-GABRB2-GABRG2) subunits, alpha-4-beta-2-gamma-2 (GABRA4-GABRB2-GABRG2) subunits, and alpha-5-beta-2-gamma-2 (GABRA5-GABRB2-GABRG2) subunits (PubMed:25634239). A very weak inhibition is also observed on GABA(A) receptor composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) (PubMed:26221036). It has also been shown to bind and inhibit recombinant GABA(A) receptor beta-3/GABRB3 subunit (Kd=about 50 nM) (PubMed:16549768). In addition, it blocks the extracellular increase of dopamine evoked by nicotine only at the higher dose (4.2 uM) (PubMed:9840221). In vivo, when intraperitoneally injected into mice, induces flaccid paralysis of the limbs and respiratory distress, and causes death in a dose-dependent manner. Monomer in solution, homodimer in crystal state. Expressed by the venom gland. LD(50) is 0.3 mg/kg by subcutaneous injection. Is identical to Alpha-bungarotoxin (A31) from B.candidus (AC Q7T3J2). Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. PubMed:9837992 indicates that a number of mRNA with sequence conflict(s) are produced by RNA editing. This seems not to be the case as discussed in PubMed:10497260. |
Q9YI08 | MKTLLLTLVVVTIVCLDLGYTIVCHTTATSPISAVTCPPGENLCYRKMWCDVFCSSRGKVVELGCAATCPSKKPYEEVTCCSTDKCNPHPKQRPG | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Monomer in solution, homodimer in crystal state. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. PubMed:9837992 indicates that a number of mRNA with sequence conflict(s) are produced by RNA editing. This seems not to be the case as discussed in PubMed:10497260. |
P01385 | VICYRGYNNPQTCPPGENVCFTRTWCDAFCSSRGKVVELGCAATCPIVKSYNEVKCCSTDKCNPFPVRPRRPP | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. LD(50) is 0.13 mg/kg by intramuscular injection into mice. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
P25670 | RICYIAPYDHKTCAAGENICYLKAWCDAWCSSRGKKLEFGCAATCPTVKPGVDISCCDTDNCNPHPKL | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. LD(50) is 0.13 mg/kg by intravenous injection. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
B2BRQ5 | MKTLLLTLVVVTIVCLDFGGGLICYMGPKTPRTCPPGQNLCYTKTWCDGFCGSRGKVVVLGCAATCPTVKPGVDITCCATDKCNPFPKTKAPWERP | Potent long-chain postsynaptic neurotoxin. Pseudo-irreversibly inhibits the nicotinic acetylcholine receptor through competitive antagonism. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
A8S6A8 | MKTLLLTLVVVTIVCLDVGNSFSCYKTPDVKSEPCAPGENLCYTKTWCDRFCSIRGKVIELGCAATCPPAEPRKDITCCSTDNCNPHPAH | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
P84467 | YTLLCYKTPSPINAETCPPGENLCYTKMWCDAWCSSRGKVIELGCAATCPSKKPYEEVTCCSTDKCNPHPKQRPG | Binds to muscular and neuronal nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission (Ref.2, PubMed:30944155). Reversibly blocks chick and mouse muscle nicotinic acetylcholine receptors (Ref.2, PubMed:30944155). Blocks muscle type nAChR with an IC(50)=30 nM, when heterologously expressed in oocytes (PubMed:30944155). Also binds with high affinity to alpha-7/CHRNA7 nAChRs (PubMed:30944155). In addition, shows a weak inhibition of neuronal alpha-3-beta-2/CHRNA3-CHRNB2 nAChR (IC(50)=2.9 uM) (PubMed:30944155). Selectively binds to alpha-1-delta subunit interface of the mouse muscle nicotinic acetylcholine receptor, with a 10-fold higher affinity for the adult than for the fetal receptors (Ref.2, PubMed:30944155). In vivo, when intraperitoneally injected into mice, causes flaccid paralysis and respiratory distress, followed by death within 2-4 hours (PubMed:30944155). Monomer in solution, homodimer in crystal state. Expressed by the venom gland. LD(50) is 170-280 ug/kg by intraperitoneal injection into mice. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
A6MFK4 | MKTLLLTLVVVTIVCLDFGYARTCLKTPEVKSEPCPPGQEVCYTKAWCDRMCSFRGKVIELGCAATCPRQEPGKEITCCSTDDCNTHP | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
P01393 | RTCYKTYSDKSKTCPRGEDICYTKTWCDGFCSQRGKRVELGCAATCPKVKTGVEIKCCSTDYCNPFPVWNPR | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. LD(50) is 0.38 mg/kg by subcutaneous injection. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
P01396 | RTCNKTFSDQSKICPPGENICYTKTWCDAWCSQRGKRVELGCAATCPKVKAGVEIKCCSTDDCDKFQFGKPR | Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission. Expressed by the venom gland. LD(50) is 0.12 mg/kg by subcutaneous injection. Belongs to the snake three-finger toxin family. Long-chain subfamily. Type II alpha-neurotoxin sub-subfamily. |
B0BX67 | MNKLIPLPREFFARDTNVVSTELIGKTLYFQGKTAIITETESYIGQNDPACHAARGRTKRTDIMFGPAGFSYVYLIYGMYYCLNFVTEAKGFPAATLIRGVHVISPENLYLNGPGKLCKYLGINISHNKCDLINNNEFFVGDIGLKLPYSTTARIGITKGTDKLWRYVVTDITNLISQYNVQP | Belongs to the DNA glycosylase MPG family. |
A8GRR0 | MNKLIPLPREFFARDTNVVSTELIGKTLYFQGKTAIITETESYIGQNDPACHAARGRTKRTDIMFGPAGFSYVYLIYGMYYCLNFVTEAKGFPAATLIRGVHVISPENLYLNGPGKLCKYLGINISHNKCDLINNNEFFVGDIGLKLPYSTTARIGITKGTDKLWRYVVTDITNLISQYNVQP | Belongs to the DNA glycosylase MPG family. |
Q68X22 | MNKLIPLPREFFARDTNLVSTELIGKVLYFQGTTAIITETESYIGNDDPACHAARGRTKRTDVMFGPAGFSYVYLIYGMYHCLNFVTEDEGFPAATLIRGVYVISHNDLYTIYTAKVKSQITDEKTQSIIISEDRRSTKFDIPNLEESNLYLNGPGKLCKYLGINTTHNKCDLINNKDFFVSDIGLNLPYSTTKRIGITKGTDKLWRYIVTDNKNALLNINIL | Belongs to the DNA glycosylase MPG family. |
Q1AWF5 | MDLLGCVLVSETPEGTCSGVIVETEAYRPEDPACHAYRGPSMRNRTLFGGPGLAYVYLSYGMHRLLNAVCEGEGVGSAVLIRSLAPLEGVPLMRRRRGRAADLCNGPGRLAESLGVGLSLDGHDLTLGEGLYIAPGPPPRGEIVSTTRIGVSRGAELPWRYLVLGERVSVPPRRISGRGLRRAWNVREPA | Belongs to the DNA glycosylase MPG family. |
Q2S2B5 | MEPLPASFFNRPTVSVARDLLGARLVHEAPTGTRLVGRIVETEAYTEDDPACHASHLSRDPETGEVVGQGRGQDLFAAPGTAYVYLIYGVHWLLNVVTEPEGTAGAVLVRAVEPEEGLQDMRTERGVDRRVDLTNGPGKLAEAFGIDGEFHQTRLTARPLFFADGDSVDDEQVARSSRIGISKGVERSWRWYVAANRFVSPASPSG | Belongs to the DNA glycosylase MPG family. |
Q4LBY8 | MLSNTILSRSFYKRDTLCVAKDLLGKVLKFADYYGVINEVEAYIGQDDPACHAARGYTPRTAAMFGAAGFSYVYLIYGMYHCLNIVTEREGFPAAVLIRGIDLYKPTVLSLNGPGKLCKKLNITKNNNKIDLTQSHGFCVYNTTARPEYMATPRIGIKVGTDKLWRFKSM | Belongs to the DNA glycosylase MPG family. |
A7X5V7 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
A6U471 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
Q2FEF3 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
Q2FVS1 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
A5IVC5 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
Q2YYZ2 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEDGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
Q5HDL2 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
A6QJI5 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
Q99RS9 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
Q6GE90 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEDGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGARLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
Q6G6X6 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
A8Z534 | MDFVNNDTRQIAKNLLGVKVIYQDTTQTYTGYIVETEAYLGLNDRAAHGYGGKITPKVTSLYKRGGTIYAHVMHTHLLINFVTKSEGIPEGVLIRAIEPEEGLSAMFRNRGKKGYEVTNGPGKWTKAFNIPRAIDGATLNDCRLSIDTKNRKYPKDIIASPRIGIPNKGDWTHKSLRYTVKGNPFVSRMRKSDCMFPEDTWK | Belongs to the DNA glycosylase MPG family. |
P0C5H4 | LKCNKLVPLFYKTCPAGKNL | This three-finger cytotoxin has antiproliferative, cytotoxic and apoptotic activities. Both in vivo and in vitro experimental results suggests that this protein possess anticancer potential. Also shows neurotoxicity, cardiotoxicity and myotoxicity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
Q9W6W8 | MKTLLLTLVVVTIVCLDLGYTLKCNKLIPIASKTCPAGKNLCYKMFMMSDLTIPVKRGCIDVCPKNSLLVKYVCCNTDRCN | Basic protein that binds to cell membrane and depolarizes cardiomyocytes. It also shows lytic activities on many other cells, including red blood cells. Interaction with sulfatides in the cell membrane induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It targets the mitochondrial membrane and induces mitochondrial swelling and fragmentation (By similarity). It binds to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity and inhibits protein kinases C (PubMed:8448165). It also binds with high affinity to heparin (PubMed:17685633). It also causes skeletal muscle necrosis after intramuscular injection into mice (PubMed:8342169). Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Is classified as a S-type cytotoxin, since a serine residue stands at position 49 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01455 | LKCHKLVPPVWKTCPEGKNLCYKMFMVSTSTVPVKRGCIDVCPKNSALVKYVCCSTDKCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 3 mg/kg by intravenous injection. Is classified as a S-type cytotoxin, since a serine residue stands at position 28 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P0CH80 | LKCNKLVPLFYKTCPAGKNLCYKMFMVSNKTVPVKRGCIDVCPKNSLVLKYVCCNTDRCN | Produces complete blockade of auricular contraction, which is irreversible at high concentrations. Induces apoptosis in leukemic cells. Possesses anti-arthritic and anti-inflammatory potential. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 2.5 mg/kg by intraperitoneal injection into mice. Is classified as a S-type cytotoxin, since a serine residue stands at position 28 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01448 | LECNKLVPIAHKTCPAGKNLCYQMYMVSKSTIPVKRGCIDVCPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 1.37 mg/kg by intravenous injection. Is classified as a S-type cytotoxin, since a serine residue stands at position 28 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01467 | LKCNQLIPPFWKTCPKGKNLCYKMTMRAAPMVPVKRGCIDVCPKSSLLIKYMCCNTNKCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 0.83 mg/kg by intravenous injection. Is classified as a P-type cytotoxin, since a proline residue stands at position 30 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
Q9PSN2 | LKCNKLIPLAYKTCPAGKNLCYKMYMVSNKTVPVKRGCIDVCPKNSLVLKYECCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Is classified as a S-type cytotoxin, since a serine residue stands at position 28 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01456 | LKCHKLVPPVWKTCPEGKNLCYKMFMVSTSTVPVKRGCIDVCPKDSALVKYVCCSTDKCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 2.9 mg/kg by subcutaneous injection into mice. Shows very weak hemolytic activity. Is classified as a S-type cytotoxin, since a serine residue stands at position 28 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01451 | LKCNKLVPIAYKTCPEGKNLCYKMFMMSDLTIPVKRGCIDVCPKNSLLVKYVCCNTDRCN | This three-finger cytotoxin is a basic protein that interacts and penetrates into the cell membrane, with the tips of all the three loops. Cytotoxins which have a 'Pro-30' (P-type) interacts with membrane stronger that those which have a Ser-28 (S-type). CTI interacts with membrane weaker than CTII. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Is classified as a S-type cytotoxin, since a serine residue stands at position 27 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01468 | LKCNQLIPPFWKTCPKGKNLCYKMTMRAAPMVPVKRGCIDVCPKSSLLIKYMCCNTDKCN | Basic protein that binds to cell membrane and depolarizes cardiomyocytes. This cytotoxin also possesses lytic activity on many other cells, including red blood cells. Interaction with sulfatides in the cell membrane induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It targets the mitochondrial membrane and induces mitochondrial swelling and fragmentation. Inhibits protein kinases C. It binds to the integrin alpha-V/beta-3 with a moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 angstroms. Expressed by the venom gland. Positive charges of Lys residues are necessary for cytolytic activity of this toxin, but not for its binding ability. Is classified as a P-type cytotoxin, since a proline residue stands at position 30 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. The venom of this snake was originally thought to be that of N.nigricollis while it is really from N.pallida. |
O93471 | MKTLLLTLVVVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKIFMVATPKVPVKRGCIDVCPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Is classified as a P-type cytotoxin, since a proline residue stands at position 51 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
A0A7T7DMY7 | MKTLLLTLVVVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMYMVATPKVPVKRGCIDVCPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pores in lipid membranes (By similarity). Exhibits concentration-dependent growth inhibitory effects in the lung cell lines A549 (IC(50)= 0.88) and NL20 (IC(50)= 1.91), in the prostate cell lines PC-3 (IC(50)= 3.13 ug/ml) and RWPE-1 (IC(50)=0.35 ug/ml), and in the breast cell lines MCF-7 (IC(50)= 9.10 ug/ml) and 184B5 (IC(50)=6.21 ug/ml), with high selectivity for the lung cancer cell line A549 (selectivity index=2.17) (PubMed:33263003). Induces primarily necrosis in the A549 lung cancer cell line, and mainly caspase-independent late apoptosis in the breast cancer cells line MCF-7 and in the prostate cancer cell line PC-3 (PubMed:33263003). Monomer in solution; homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Exhibits anticancer properties by inhibiting growth in the A549 lung cancer cell line with high selectivity by inducing necrosis, but not in prostate (PC-3) and breast (MCF-7) cancer cell lines. Is classified as a P-type cytotoxin, since a proline residue stands at position 51 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P86538 | LQCNKLVPIASKTCPPGKNLCYKMFMVSDLTIPVKRGCIDVCPKNSLLVKYECCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity (By similarity). Preferentially binds acidic phospholipids like phosphatidylserine, phosphatidic acid and phosphatidyl glycerol (PubMed:26456928). Has hemolytic activity towards human erythrocytes (EC(50)=1.024 uM) and cytolytic activity towards various cell lines (PubMed:26456928). Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Is classified as a S-type cytotoxin, since a serine residue stands at position 28 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
Q90WJ1 | MKTLLLTLVVVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMYMVATPKVPVKRGCIDVCPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Non-spliced mRNAs of CTX-2A are found in liver, heart, and muscle, but these transcripts give truncated proteins. Is classified as a P-type cytotoxin, since a proline residue stands at position 51 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
Q9PST3 | MKTLLLTLVVVTTVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMYMVATPKVPVKRGCIDVCPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Is classified as a P-type cytotoxin, since a proline residue stands at position 51 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
O93472 | MKTLLLTLVLVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMYMVATPKVPVKRGCIDVYPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. This toxin lacks one of the four disulfide bonds found in similar cardiotoxins. Is classified as a P-type cytotoxin, since a proline residue stands at position 51 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01442 | MKTLLLTLVVVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMFMVSNLTVPVKRGCIDVCPKNSALVKYVCCNTDRCN | Basic protein that binds to cell membrane and depolarizes cardiomyocytes. It also shows lytic activities, but 2-fold less important than that of CTX-A4. It binds to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity. It may interact with sulfatides in the cell membrane which induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It also may target the mitochondrial membrane and induce mitochondrial swelling and fragmentation. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 2.1 mg/kg by intravenous injection into mice. LD(50) is 56 mg/kg by subcutaneous injection into mice. Is classified as a S-type cytotoxin, since a serine residue stands at position 49 (Ser-29 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01462 | LKCHKLVPPFWKTCPEGKNLCYKMYMVATPMLPVKRGCIDVCPKDSALVKYMCCNTDKCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 1.98 mg/kg by intravenous injection. The sequence of the major component is shown, it is called toxin V(II)2 and the minor component is called toxin V(II)2A. Is classified as a P-type cytotoxin, since a proline residue stands at position 30 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
Q9DGH9 | MKTLLLTLVVVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKIFMVATPKVPVKRGCIDVCPKNSALVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. Is classified as a P-type cytotoxin, since a proline residue stands at position 51 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
P01469 | LKCNQLIPPFWKTCPKGKNLCYKMTMRGASKVPVKRGCIDVCPKSSLLIKYMCCNTDKCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity. Monomer in solution; Homodimer and oligomer in the presence of negatively charged lipids forming a pore with a size ranging between 20 and 30 Angstroms. Expressed by the venom gland. LD(50) is 1.11 mg/kg by intravenous injection. Is classified as a S-type cytotoxin, since a serine residue stands at position 30 (Ser-29 in standard classification). S-type are generally found to exhibit higher muscle cell depolarization than P-type. Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IA cytotoxin sub-subfamily. |
Q2VBN9 | MKTLLLTFLVVTIVCLDLGYTLICHQVHGLQTCEPAQKFCQKRTTMFFPNHPVLLMGCTYNCPTERYSVCCSTDKCNK | This three-finger toxin binds and inhibits the nicotinic acetylcholine receptor (nAChR). Expressed by the venom gland. Is classified as a P-type cytotoxin, since a proline residue stands at position 49 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. |
Q4VRI0 | MKTLLLTLVVMTIMCLDLGYTLTCYMNPSGTMVCKEHETMCYQLIVWTFQYRVLYLKGCTSSCPEGNNRACCSTGLCNN | Expressed by the venom gland. Belongs to the snake three-finger toxin family. Short-chain subfamily. |
Q53B52 | MKNLLLTFLVVTIVCLDLGYTLICHQRHGLQTCEPAQKFCFAQTVMPFPNHPLTLMGCTYSCPTEKNAVCCSTDKCNR | This three-finger toxin binds and inhibits the nicotinic acetylcholine receptor (nAChR). Expressed by the venom gland. LD(50) is 160 ug/kg by intraperitoneal injection into mice. Is classified as a P-type cytotoxin, since a proline residue stands at position 49 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. |
A0A4P1LYC9 | TICHIQISKTHGILKTCEENSCYKMSVRGWIIGRGCGCPSAVRPRQVQCCTSDKCNY | May have toxic activity. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Short-chain subfamily. |
P0CAR7 | LICYVSRDGKTATCPPQGKCEKYAVSASHTXHXFYVYGCTSXC | Neurotoxin. Blocks muscular nicotinic acetylcholine receptors (nAChR). Expressed by the venom gland. Belongs to the snake three-finger toxin family. Short-chain subfamily. |
P86094 | LKCYGIFRKIMTCPQGQNICEKFAYSPMHNGWMYSWGCTSNCHKGPLDKCCSTDLCNY | Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to and inhibits the endogenous nicotinic acetylcholine receptors (nAChR) in the human rhabdomyosarcoma TE 671 cell line with an IC(50) of 266 mM. Not toxic to mice by intraperitoneal injection or to zebrafish by injection at the back dorsolateral region. Expressed by the venom gland. Belongs to the snake three-finger toxin family. Short-chain subfamily. |
P0DSN0 | MECYRMSNIVTCQPWEKFCYKEVTMFFPNHPVHLSGCASECTETNSKFCCTTDKCNGAGSG | Shows no cytotoxicity and does not inhibit the binding of alpha-bungarotoxin to nicotinic acetylcholine receptors of muscle and alpha-7/CHRNA7 types. However, it potentiates the binding of alpha-bungarotoxin to the acetylcholine-binding protein from Lymnaea stagnalis. Expressed by the venom gland. Is classified as a P-type cytotoxin, since a proline residue stands at position 28 (Pro-31 in standard classification). Belongs to the snake three-finger toxin family. Short-chain subfamily. |
D5MP61 | MKRTYLSLIAAGVMSLSVSAWSLDGVLVPESGILVSVGQDVDSVNDYASALGTIPAGVTNYVGIVNLDGLNSDADAGAGRNNIAELANAYPTSALVVGVSMNGEVDAVASGRYNANIDTLLNTLAGYDRPVYLRWAYEVDGPWNGHSPSGIVTSFQYVHDRIIALGHQAKISLVWQVASYCPTPGGQLDQWWPGSEYVDWVGLSYFAPQDCNWDRVNEAAQFARSKGKPLFLNESTPQRYQVADLTYSADPAKGTNRQSKTSQQLWDEWFAPYFQFMSDNSDIVKGFTYINADWDSQWRWAAPYNEGYWGDSRVQANALIKSNWQQEIAKGQYINHSETLFETLGYGSTGGGDNGGGDNGGTNPPEPCNEEFGYRYVSDSTIEVFHKNNGWSAEWNYVCLNGLCLQGEIKNGEYVKQFDAQLGSTYGIEFKVADGESQFITDKSVTFENKQCGSTGTPGGGDNGSGGDNGGDNGSGGDNGSGGGTDPSQCSADFGYNYRSDTEIEVFHKDLGWSASWNYICLDDYCVPGDKSGDSYNRSFNATLGSDYKITFKVEDSASQFITEKNITFVNTSCAQ | Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylobiose, xylotriose and xylotetraose. Converts beta-1,3-xylotriose into xylose and xylobiose, converts beta-1,3-xylotetraose mainly into xylotriose and xylose, converts beta-1,3-xylopentaose into xylobiose and xylotriose. Does not hydrolyze beta-1,4-xylan, beta-1,4-mannan, beta-1,4-glucan, beta-1,3-xylobiose or p-nitrophenyl-beta-xyloside. Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans. Completely inhibited by Hg(2+), partially inhibited by Mn(2+), Cu(2+) and Pb(2+). Unaffected by Ca(2+), Mg(2+) and EDTA. Optimum pH is 7.0-7.5. Optimum temperature is 37 degrees Celsius. Inactive above 60 degrees Celsius. The carbohydrate binding modules (CBM) bind to insoluble beta-1,3-xylan, but not to insoluble beta-1,4-xylan, beta-1,4-glucan, beta-1,4-mannan, curdlan, chitin, or soluble polysaccharides. Belongs to the glycosyl hydrolase 26 family. |
Q9LCB9 | MKKLAKMISVATLGACAFQAHALDGKLVPDQGILVSVGQDVDSVNDYSSAMGTTPAGVTNYVGIVNLDGLSTDADAGAGRNNIVELANQYPTSALIVGVSMNGEVQNVANGQYNANIDTLIRTLGEFDRPVYLRWAYEVDGPWNGHNTEDLKQSFRHVYQRIRELGYADNISMVWQVASYCPTAPGQLGTWWPGDDVVDWVGLSYFAPQDCNWDRVNEAAQWARSHNKPLFINESSPQRYQLADLTYSTDPAKGTNRQAKTDQQIWSEWFEPFFQFMVDNQDILKGFTYINADWDSQWRWAAPYNEGYWGDSRVQVIPYIKQKWQETLSDPKFIRHSDELFAQLGYGNSDGGNGGDNGGDNGGDNGGETPENCTDDFNFNYVSDNEIEVYHVDKGWSAGWNYLCLDDYCLSGTKSNGAFSRSFSAQLGQTYKMTFKVEDITGQGQQIIDKTVTFTNQVCN | Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Weakly active toward beta-1,3-xylotriose, yielding xylose and xylobiose. Converts beta-1,3-xylotetraose into xylotriose, xylobiose and xylose. Converts beta-1,3-xylopentaose into xylotetraose, xylotriose, xylobiose and xylose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, curdlan or carboxymethylcellulose. Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans. Completely inhibited by Cu(2+), Hg(2+) and N-bromosuccinimide. Strongly inhibited by Ag(+), Zn(2+) and Pb(2+). Moderately inhibited by Fe(3+), Al(3+), Mn(2+), dithiothreitol and p-chloromercuribenzoic acid. Slightly activated by Mg(2+) and Ca(2+). Unaffected by Na(+), K(+), Ba(2+), EDTA, iodoacetic acid and N-ethylmalaimide. Optimum pH is 7.0. Stable between pH 5.0 and 8.0. Optimum temperature is 37 degrees Celsius. Stable below 30 degrees Celsius. By beta-1,3-xylan. The carbohydrate binding module (CBM) binds to insoluble beta-1,3-xylan, but not to insoluble beta-1,4-xylan, beta-1,4-glucan, beta-1,4-mannan, curdlan, chitin, or soluble polysaccharides. Belongs to the glycosyl hydrolase 26 family. |
Q8RS40 | MKKLAKMISIATLGACAFSAHALDGKLVPNEGVLVSVGQDVDSVNDYSSAMSTTPAGVTNYVGIVNLDGLASNADAGAGRNNVVELANLYPTSALIVGVSMNGQIQNVAQGQYNANIDTLIQTLGELDRPVYLRWAYEVDGPWNGHNTEDLKQSFRNVYQRIRELGYGDNISMIWQVASYCPTAPGQLSSWWPGDDVVDWVGLSYFAPQDCNWDRVNEAAQWARSHNKPLFINESSPQRYQLADRTYSSDPAKGTNRQSKTEQQIWSEWFAPYFQFMEDNKDILKGFTYINADWDSQWRWAAPYNEGYWGDSRVQVLPYIKQQWQDTLENPKFINHSSDLFAKLGYVADGGDNGGDNGGDNGGDNGGDNGGDNGGTEPPENCQDDFNFNYVSDQEIEVYHVDKGWSAGWNYVCLNDYCLPGNKSNGAFRKTFNAVLGQDYKLTFKVEDRYGQGQQILDRNITFTTQVCN | Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan. Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans. Completely inhibited by CuCl(2), FeCl(3), HgCl(2) and N-bromosuccinimide. Moderately inhibited by AgCl, AlCl(3), Pb(CH(3)COO)(2) and dithiothreitol. BaCl(2), CaCl(2), KCl, MgCl(2), MnCl(2), NaCl, ZnCl(2), ethylenediaminetetraacetic acid, N-ethylmaleimide, iodoacetic acid and p-chloromercuribenzoic acid have little or no effect on activity. Optimum pH is 7.0-7.5. Stable from pH 5.0-11.0. Retains 65% and 70% of activity respectively when incubated at pH 4.0 and 12.0 for 24 hours. Optimum temperature is 40 degrees Celsius. Stable below 40 degrees Celsius. Loses 70% and 99% of activity respectively when incubated for 10 minutes at 50 and 60 degrees Celsius. By beta-1,3-xylan. The carbohydrate binding module (CBM) binds to insoluble beta-1,3-xylan, but not to insoluble beta-1,4-xylan, beta-1,4-glucan, beta-1,4-mannan, curdlan, chitin, or soluble polysaccharides. Belongs to the glycosyl hydrolase 26 family. |
P0DJB0 | LICFICFSPTAH | Probably blocks muscarinic acetylcholine receptors (CHRM), since it inhibits the binding of the selective muscarinic ligand [3H]QNB and inhibits the carbachol-induced [3H]inositol phosphate accumulation in rat hippocampus. Expressed by the venom gland. Contains 4 disulfide bonds. Belongs to the snake three-finger toxin family. |
Q8H7M3 | MFGFGHHGHHGQDQPPQHHGGGGGGAHQPTFKIFCRADEGYCVAVREGNVVLAPTNPRDEHQHWYKDMRFSAKIKDEEGNPAFALVNKATGLAIKHSLGQGHPVKLAPFNPEYPDESVLWTESGDVGKSFRCIRMLNNIRLNFDAFHGDKDHGGVHDGTTIVLWEWAKGDNQCWKILPWGDEAYAGGSANAPRGGNEPTVRIFCKADEGFSVTVRGGSVCLAPTNPRDEYQHWIKDMRHSNSIKDEEGYPAFALVNRVTGEAIKHSQGEGHPVKLVPYNPGYQDESVLWTESRDVGHGFRCIRMVNNIYLNFDALHGDKDHGGVRDGTTVALWKWCEGDNQRWKIVPW | Lectin which binds carbohydrates in vitro. Interacts through its lectin domain with glycan structures containing specific motifs. Expressed in roots and shoots. Induced by abscisic acid (ABA) and salt stress in roots. The ricin B-type lectin domain binds glycan structures. |
Q6Z4N5 | MFGFGHHHNQAPAAPSDPNQIFKIFCRANENYCLTVRDSAVVLAPVNPKDEHQHWFKDMRFSTKVKDGEGMPAFALVNKATGLAVKHSLGQSHPVKLVPFNPEYEDASVLWTESKDVGKGFRCIRMVNNTRLNLDAFHGDKDHGGVRDGTTVVLWEWCKGDNQSWKILPWGPEAHSSSPGAATACTIGGVPVHTVRVFSAAGEDYCLTVRNGTACLAPKNPRDDYQHWIKDMRHSNKIRDEEGYPAFALVNKVTGEAIKHSTGQGHPVKLVPYNPEYQDESVLWTESKDVGKGFRCIRMVNNIYLNFDAFHGDKDHGGIHDGTEIVLWKWCEGDNQRWKILPW | Lectin which binds carbohydrates in vitro. Interacts through its lectin domain with glycan structures containing specific motifs. The ricin B-type lectin domain binds glycan structures. |
O24213 | MDFYGRREQYGGYGGYGGGGALATPGYAPAAPYGMSQVNIEGNGCGRTLPPQPTVKVYCRANPNYAMTARNGAVVLAPANPKDEYQHWIKDMRWSTSIKDEEGYPAFALVNKATGQAIKHSLGQSHPVRLVPYNPEVMDESVLWTESRDVGNGFRCIRMVNNIYLNFDAFHGDKYHGGVRDGTDIVLWKWCEGDNQRWKIQPYY | Lectin which binds carbohydrates in vitro. Interacts through its lectin domain with glycan structures containing specific motifs. Expressed in shoots and lamina. Induced by abscisic acid (ABA) and salt stress in shoots. The ricin B-type lectin domain binds glycan structures. |
Q8KD41 | MGTRWFAKNTTMSKNSIVIGVDLDGVCADFYGRMRQIASEWFERPIDELPEEVSWGLSEWGITNPSQYDSLHRFAVTQRELFSSMEAIPGARKYLRQLSDEGFRIRIITHRLFIHYFHATAVQQTVNWLDSHGIPYWDLCFVKEKTQVGADIYIEDSPENVAQLRGRGLFTICFGNSTNRHIEELRAASWQDVYDMIKAFVT | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q97JQ5 | MNKPTLGIDLDTTLNTLDREWVKRYNEIYKDKLLPSDIKGWDIENYVKPECGKKIYDILKEPHFFRNLGVQPFAETALEELTSIFNIYIVSATHYKVCEDKGNWIKEKFPFISYQNIIFCHNKGLVHLDILIDDNPLNLENFKGNKILFDAHHNKSENRFVRARDWYEAKALCESLKDFL | Dephosphorylates nucleoside monophosphates such as the 5' and 2'(3')-phosphates of deoxyribonucleotides in vitro. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q5UQH3 | MDNCELVGSRIRLGLDMDGVLFDFDSKIMDKFAEMGIQFTDVKEMSSAVEFDKSIKQRHREIYHVPGFFANLPPIKGAVNAYKYLKSLTDINNNKIFEIFIVSTPSFRNQTCCIDKINDLNKYFGPELLEKVFFCRDKTLVNLDILIDDKPEIRGFNGSSECLSDSNSVTNKMSFQHIRFHSDMYKYSDDVPIINNWIDGTYIDVVKNVCVDKNLLREVVV | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q5HHU8 | MTRKSIAIDMDEVLADTLGEIIDAVNFRADLGIKMEALNGQKLKHVIPEHDGLITEVLREPGFFRHLKVMPYAQEVVKKLTEHYDVYIATAAMDVPTSFSDKYEWLLEFFPFLDPQHFVFCGRKNIVKADYLIDDNPRQLEIFTGTPIMFTAVHNINDDRFERVNSWKDVEQYFLDNIEK | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q99VP8 | MTRKSIAIDMDEVLADTLGEIIDAVNFRADLGIKMEALNGQKLKHVIPEHDGLITEVLREPGFFRHLKVMPHAQEVVKKLTEHYDVYIATAAMDVPTSFSDKYEWLLEFFPFLDPQHFVFCGRKNIVKADYLIDDNPRQLEIFTGTPIMFTAVHNINDDRFERVNSWKDVEQYFLDNIEK | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q6GIR7 | MTRKSIAIDMDEVLADTLGEIIDAVNFRADLGIKMEALNGQKLKHVIPEHDGLITEVLREPGFFRHLKVMPHAQEVVKKLTEHYDVYIATAAMDVPTSFSDKYEWLLEFFPFLDPQHFVFCGRKNIVKADYLIDDNPRQLEIFTGTPIMFTAVHNINDDRFERVNSWKDVEQYFLDNIEK | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q6GBA5 | MTRKSIAIDMDEVLADTLGEIIDAVNFRADLGIKMEALNGQKLKHVIPEHDGLITEVLREPGFFRHLKVMPYAQEVVKKLTEHYDVYIATAAMDVPTSFSDKYEWLLEFFPFLDPQHFVFCGRKNIVKADYLIDDNPRQLEIFTGTPIMFTAVHNINDDRFERVNSWKDVEQYFLDNIEK | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q8NXN2 | MTRKSIAIDMDEVLADTLGEIIDAVNFRADLGIKMEALNGQKLKHVIPEHDGLITEVLREPGFFRHLKVMPYAQEVVKKLTEHYDVYIATAAMDVPTSFSDKYEWLLEFFPFLDPQHFVFCGRKNIVKADYLIDDNPRQLEIFTGTPIMFTAVHNINDDRFERVNSWKDVEQYFLDNIEK | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q5HR07 | MTRQRIAIDMDEVLADTLGAVVKAVNERADLNIKMESLNGKKLKHMIPEHEGLVMDILKEPGFFRNLDVMPHAQEVVKQLNEHYDIYIATAAMDVPTSFHDKYEWLLEYFPFLDPQHFVFCGRKNIILADYLIDDNPKQLEIFEGKSIMFTASHNVNEHRFERVSGWRDVKNYFNSIEK | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q8CTG7 | MTRQRIAIDMDEVLADTLGAVVKAVNERADLNIKMESLNGKKLKHMIPEHEGLVMDILKEPGFFRNLDVMPHAQEVVKQLNEHYDIYIATAAMDVPTSFHDKYEWLLEYFPFLDPQHFVFCGRKNIILADYLIDDNPKQLEIFEGKSIMFTASHNVYEHRFERVSGWRDVKNYFNSIEK | Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Belongs to the 5'(3')-deoxyribonucleotidase family. |
Q6PQJ9 | MSWWWAGAIGAAKKRLEEDDAQPKHSSVALIVGVTGIIGNSLAEILPLADTPGGPWKVYGVARRTRPAWHEDNPINYVQCDISDPDDSQAKLSPLTDVTHVFYVTWANRSTEQENCEANSKMFRNVLDAVIPNCPNLKHISLQTGRKHYMGPFESYGKIESHDPPYTEDLPRLKYMNFYYDLEDIMLEEVEKKEGLTWSVHRPGNIFGFSPYSMMNLVGTLCVYAAICKHEGKVLRFTGCKAAWDGYSDCSDADLIAEHHIWAAVDPYAKNEAFNVSNGDVFKWKHFWKVLAEQFGVGCGEYEEGVDLKLQDLMKGKEPVWEEIVRENGLTPTKLKDVGIWWFGDVILGNECFLDSMNKSKEHGFLGFRNSKNAFISWIDKAKAYKIVP | Involved in cardenolide biosynthesis. Catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione. Can use progesterone, testosterone, 4-androstene-3,17-dione, cortisol and cortisone as substrates, but not pregnenolone, 21-OH-pregnenolone or isoprogesterone. NADPH could not be replaced by NADH. 5beta-cholestan-3-one + NADP(+) = cholest-4-en-3-one + H(+) + NADPH 4,5beta-dihydrocortisone + NADP(+) = cortisone + H(+) + NADPH Optimum pH is 7.8. Optimum temperature is 40 degrees Celsius. Homodimer. Belongs to the short-chain dehydrogenases/reductases (SDR) family. Highly divergent. |
A8ADU7 | MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGQVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPDELRDIFAPLIDEHAYSEEEKSVVKQADALCAYLKCLEELSAGNNEFLLAKTRLEKTLASRRSEEMDYFMAVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
A7MH33 | MSQSHFFAYLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAVIKNRKFQGNVNPERIALLAMYHDASEVLTGDLPTPVKYFNSQIAHEYKAIEKIAQQKLIAMVPEELQDIFAPLLDEHHYTEDEKSLVKQADALCAYLKCLEELSAGNNEFLLAKSRLEKTLAQRHSAEMDYFMQVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
A7ZPA5 | MKQSHFFAHLSRLKLINRWPLMRNVLTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
B7UFU9 | MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAKEYKAIEKIAQQKLVDMVPEELQDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
B7MG55 | MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELQDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
B7LBE5 | MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
Q8XCV3 | MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
B5YXT1 | MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAPLIDEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFMEVFVPSFHLSLDEISQDSPL | Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Homodimer. Belongs to the 5DNU family. |
P79399 | VEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRAPDLPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLAMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMFNEDFKQAFHK | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). Homodimer. Heterodimer with HTR1D (By similarity). Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. Phosphorylated. Palmitoylated. A residue in the 7th transmembrane region ('Thr-355' in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists. Belongs to the G-protein coupled receptor 1 family. |
P49144 | MEEPGAQCAPPLAAGSQIAVPQANLSAAHSHNCSAEGYIYQDSIALPWKVLLVLLLALFTLATTLSNAFVVATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDLWLSSDITCCTASIMHLCVIALDRYWAITDAVEYSAKRTPKRAAIMIRLVWVFSICISLPPFFWRQAKAEEEVSECLVNTDHVLYTVYSTVGAFYLPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTTSVTSINSRAPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGVFIVCWLPFFIISLVMPICKDACWFHQAIFDFFTWLGYVNSLINPIIYTMSNEDFKQAFHKLIRFKCTS | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries. Homodimer. Heterodimer with HTR1D (By similarity). Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. Phosphorylated. Palmitoylated. A residue in the 7th transmembrane region ('Thr-355' in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists. Belongs to the G-protein coupled receptor 1 family. |
P28564 | MEEQGIQCAPPPPATSQTGVPLANLSHNCSADDYIYQDSIALPWKVLLVALLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDFWLSSDITCCTASIMHLCVIALDRYWAITDAVDYSAKRTPKRAAIMIVLVWVFSISISLPPFFWRQAKAEEEVLDCFVNTDHVLYTVYSTVGAFYLPTLLLIALYGRIYVEARSRILKQTPNKTGKRLTRAQLITDSPGSTSSVTSINSRVPEVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHMAIFDFFNWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCTG | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries. Homodimer. Heterodimer with HTR1D (By similarity). Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. Phosphorylated. Palmitoylated. A residue in the 7th transmembrane region ('Thr-355' in human, Asn-351 in mouse and rat) is important for species-specific sensitivity to various agonists. Belongs to the G-protein coupled receptor 1 family. |
P56496 | MEEPGARCAPPPPAGSQTQTPSSNLSHNCSADSYIYQDSIALPWKVLLVALLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDFWLSSDITCCTASIMHLCVIALDRYWAITDAVEYSAKRTPRRAAVMIALVWVFSISISLPRFFWRQAKAEEEVLDCLVNTDHVLYTVYSTVGAFYLPTLLLIALYGRIYVEARSRILKQTPNKTGKRLSRAQLISDSPGSTSSVTSINSRVPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHMAIFDFFNWLGYLNSLINPIIYTMPNEDFKQAFHKLIRFKCTG | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). Homodimer. Heterodimer with HTR1D (By similarity). Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. Phosphorylated. Palmitoylated. A residue in the 7th transmembrane region ('Thr-355' in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists. Belongs to the G-protein coupled receptor 1 family. |
Q6XXX8 | MEDAGTPCAPPPPAGSQTGAPPANLSSAPHNCSAEGYIYQDSIALPWKVLLAILLALLTLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYAVTGRWTLGQVVCDLWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISISLPPFFWRQAKAEEEVSDCVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSVNSRAPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCAS | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). Homodimer. Heterodimer with HTR1D (By similarity). Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. Phosphorylated. Palmitoylated. A residue in the 7th transmembrane region ('Thr-355' in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists. Belongs to the G-protein coupled receptor 1 family. |
P11614 | MSPPNQSLEGLLQEASNRSLNATETPEAWGPETLQALKISLALLLSIITMATALSNAFVLTTIFLTRKLHTPANYLIGSLAMTDLLVSILVMPISIAYTTTRTWSFGQILCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGRAAVMIATVWVISICISIPPLFWRQAKAQEDMSDCQVNTSQISYTIYSTCGAFYIPSVLLIILYGRIYVAARNRILNPPSLYGKRFTTAQLITGSAGSSLCSLSPSLQEERSHAAGPPLFFNHVQVKLAEGVLERKRISAARERKATKTLGIILGAFIVCWLPFFVASLVLPICRASCWLHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQRVVHVRKAS | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. Homodimer. Heterodimer with HTR1B (By similarity). Belongs to the G-protein coupled receptor 1 family. |
O08891 | MSPPNQSEEGLPQEASNRSLNATETPGDWDPGLLQALKVSLVVVLSIITLATVLSNAFVLTTILLTRKLHTPANYLIGSLATTDLLVSILVMPISIAYTTTRTWNFGQILCDIWVSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAGAMIAAVWVISICISIPPLFWRQAQAQEEMSDCLVNTSQISYTIYSTCGAFYIPSVLLIILYSRIYRAARSRILNPPSLSGKRFTTAHLITGSAGSSLCSLNPSLHEGHMHPGSPLFFNHVRIKLADSVLERKRISAARERKATKTLGIILGAFIVCWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEDFRQAFQKVVHFRKAS | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. Homodimer. Heterodimer with HTR1B (By similarity). Belongs to the G-protein coupled receptor 1 family. |
P28221 | MSPLNQSAEGLPQEASNRSLNATETSEAWDPRTLQALKISLAVVLSVITLATVLSNAFVLTTILLTRKLHTPANYLIGSLATTDLLVSILVMPISIAYTITHTWNFGQILCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAATMIAIVWAISICISIPPLFWRQAKAQEEMSDCLVNTSQISYTIYSTCGAFYIPSVLLIILYGRIYRAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLNSSLHEGHSHSAGSPLFFNHVKIKLADSALERKRISAARERKATKILGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQKIVPFRKAS | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. Homodimer. Heterodimer with HTR1B. Detected in brain neocortex and caudate nucleus (at protein level). Belongs to the G-protein coupled receptor 1 family. |
Q8BUW7 | MSPPNQSLEGLPQEASNRSLNVTGAWDPEVLQALRISLVVVLSVITLATVLSNAFVLTTILLTKKLHTPANYLIGSLATTDLLVSILVMPISIAYTTTRTWNFGQILCDIWVSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAAVWIISICISIPPLFWRQATAHEEMSDCLVNTSQISYTIYSTCGAFYIPSILLIILYGRIYVAARSRILNPPSLYGKRFTTAQLITGSAGSSLCSLNPSLHESHTHTVGSPLFFNQVKIKLADSILERKRISAARERKATKTLGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPVIYTVFNEDFRQAFQKVVHFRKIS | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. Homodimer. Heterodimer with HTR1B (By similarity). Detected in the motor column in spinal cord, and in several cranial motor nuclei, including nucleus ambiguous, oculomotoris, trochelaris and abducens. Detected in gamma motor neurons in the lumbar spinal cord. Detected in proprioceptive sensory neurons in dorsal root ganglia. No visible phenotype. Depending on the task, mutant mice show improved motor coordination, especially in avoiding hind limb slips when crossing a narrow beam and in climbing onto a horizontal hanging wire. Belongs to the G-protein coupled receptor 1 family. |
P79400 | AMTDLLVSILVMPISIPYTITQTWSFGQLLCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAIVWAISICISIPPLFWRQARAHEEISDCLVNTSQISYTIYSTCGAFYIPSLLLIILYGRIYRAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLNPSLHEGHSHSAGSPLFFNHVKIKLADSVLERKRISAARERKATKTLGIILGAFIICWLPFFVASLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQKVV | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction (By similarity). Homodimer. Heterodimer with HTR1B (By similarity). Belongs to the G-protein coupled receptor 1 family. |
O02823 | MSPSNQSAEGLPQEAANRSLNATGTPEAWDPGTLQALKISLAVVLSIITVATVLSNTFVLTTILLTRKLHTPANYLIGSLATTDLLVSILVMPISIAYTITHTWNFGQVLCDIWVSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAVVWAISICISIPPLFWRQAKAHEEVSDCLVNTSQISYTIYSTCGAFYIPSVLLIVLYGRIYMAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLSPSLGEGHSHSAGSPLFFNPVRIKLADSVLERKRISAARERKATKTLGIILGAFIGCWLPFFVASLVLPICRDSCWMPPGLFDFFTWLGYLNSLINPIIYTVFNEDFRQAFQRVIHFRKAF | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction (By similarity). Homodimer. Heterodimer with HTR1B (By similarity). Belongs to the G-protein coupled receptor 1 family. |
P28565 | MSLPNQSLEGLPQEASNRSLNATGAWDPEVLQALRISLVVVLSIITLATVLSNAFVLTTILLTKKLHTPANYLIGSLATTDLLVSILVMPISIAYTTTRTWNFGQILCDIWVSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAAAMIAAVWAISICISIPPLFWRQATAHEEMSDCLVNTSQISYTIYSTCGAFYIPSILLIILYGRIYVAARSRILNPPSLYGKRFTTAQLITGSAGSSLCSLNPSLHESHTHTVGSPLFFNQVKIKLADSILERKRISAARERKATKTLGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPVIYTVFNEDFRQAFQRVVHFRKAS | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction. Homodimer. Heterodimer with HTR1B (By similarity). Detected in dorsal raphe. Belongs to the G-protein coupled receptor 1 family. |
P79748 | MELDNNSLDYFSSNFTDIPSNTTVAHWTEATLLGLQISVSVVLAIVTLATMLSNAFVIATIFLTRKLHTPANFLIGSLAVTDMLVSILVMPISIVYTVSKTWSLGQIVCDIWLSSDITFCTASILHLCVIALDRYWAITDALEYSKRRTMRRAAVMVAVVWVISISISMPPLFWRQAKAHEELKECMVNTDQISYTLYSTFGAFYVPTVLLIILYGRIYVAARSRIFKTPSYSGKRFTTAQLIQTSAGSSLCSLNSASNQEAHLHSGAGGEGGGSPLFVNSVKVKLADNVLERKRLCAARERKATKTLGIILGAFIICWLPFFVVTLVWAICKECSFDPLLFDVFTWLGYLNSLINPVIYTVFNDEFKQAFQKLIKFRR | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction (By similarity). Belongs to the G-protein coupled receptor 1 family. |
Q6VB83 | MNITNCTTDASMVVRPKTVTEKMLICMTLVIITTLTMLLNSAVIMAICTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIMYIVMDSWRLGYFICEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAGLMILTVWTISIFISMPPLFWRSHRQLSPPPSQCTIQHDHVIYTIYSTFGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKIHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYTVSSEVGDFLTWLGYVNSLINPLLYTSFNEDFKLAFKKLIRCREHT | G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Detected in the brain with the greatest abundance in the hippocampus, followed by the olfactory bulb. Lower levels are detected in the cortex, thalamus, pons, hypothalamus, midbrain, striatum, and cerebellum. Belongs to the G-protein coupled receptor 1 family. |