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Protein

Potassium voltage-gated channel subfamily B member 1

Gene

KCNB1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain. Plays also a role in the regulation of exocytosis independently of its electrical function. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes (By similarity). Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells. Channel properties are also modulated by cytoplasmic ancillary beta subunits, such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the delayed-rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus. Contributes to the regulation of the glucose-induced amplitude and duration of action potentials in pancreatic beta-cells, hence limiting calcium influx and insulin secretion. Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions. Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits. Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner.By similarity

Enzyme regulationi

Inhibited by 12.7 nM stromatoxin 1 (ScTx1), a spider venom toxin of the tarantula S.calceata. Inhibited by 42 nM hanatoxin 1 (HaTx1), a spider venom toxin of the tarantula G.spatulata. Modestly sensitive to millimolar levels of tetraethylammonium (TEA). Modestly sensitive to millimolar levels of 4-aminopyridine (4-AP). Completely insensitive to toxins such as dendrotoxin (DTX) and charybdotoxin (CTX).2 Publications

Kineticsi

Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents which are activated during membrane depolarization, i.e within a risetime of more than 20 msec. After that, inactivate very slowly, i.e within more than 5 sec. Their activation requires low threshold potentials at about -20 to -30 mV with a midpoint activation at about 10 mV. For inactivation, the voltage at half-maximal amplitude is about -20 mV. The time constant for recovery after inactivation is about 1.6 sec. Channels have an unitary conductance of about 8 pS. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system, the presence or absence of ancillary subunits and post-translational modifications.2 Publications

      GO - Molecular functioni

      GO - Biological processi

      Complete GO annotation...

      Keywords - Molecular functioni

      Ion channel, Potassium channel, Voltage-gated channel

      Keywords - Biological processi

      Exocytosis, Ion transport, Potassium transport, Transport

      Keywords - Ligandi

      Potassium

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Potassium voltage-gated channel subfamily B member 1By similarity
      Alternative name(s):
      Delayed rectifier potassium channel 1By similarity
      Short name:
      DRK1By similarity
      Voltage-gated potassium channel subunit Kv2.1
      Gene namesi
      Name:KCNB1By similarity
      OrganismiSus scrofa (Pig)
      Taxonomic identifieri9823 [NCBI]
      Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
      Proteomesi
      • UP000008227 Componenti: Unplaced

      Subcellular locationi

      • Cell membrane By similarity
      • Perikaryon By similarity
      • Cell projectionaxon By similarity
      • Cell projectiondendrite By similarity
      • Membrane; Multi-pass membrane protein
      • Cell junctionsynapsepostsynaptic cell membrane By similarity
      • Cell junctionsynapse By similarity
      • Cell junctionsynapsesynaptosome By similarity
      • Lateral cell membrane By similarity
      • Cell membranesarcolemma By similarity

      • Note: Localizes to high-density somatodendritic clusters and non-clustered sites on the surface of neocortical and hippocampal pyramidal neurons in a cortical actin cytoskeleton-dependent manner. Localizes also to high-density clusters in the axon initial segment (AIS), at ankyrin-G-deficient sites, on the surface of neocortical and hippocampal pyramidal neurons. KCNB1-containing AIS clusters localize either in close apposition to smooth endoplasmic reticulum cisternal organelles or with GABA-A receptor-containing synapses of hippocampal and cortical pyramidal neurons, respectively. Localizes to high-density clusters on the cell surface of atrial and ventricular myocytes and at the lateral plasma membrane in epithelial cells. Localizes both to the axial and transverse tubules (T tubule) and sarcolemma in ventricular myocytes. Associated with lipid raft domains. In cortical neurons, apoptotic injuries induce de novo plasma membrane insertion in a SNARE-dependent manner causing an apoptotic potassium current surge.By similarity

      Topology

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Topological domaini1 – 186186CytoplasmicBy similarityAdd
      BLAST
      Transmembranei187 – 20822Helical; Name=Segment S1By similarityAdd
      BLAST
      Topological domaini209 – 22820ExtracellularBy similarityAdd
      BLAST
      Transmembranei229 – 25022Helical; Name=Segment S2By similarityAdd
      BLAST
      Topological domaini251 – 2599CytoplasmicBy similarity
      Transmembranei260 – 28021Helical; Name=Segment S3By similarityAdd
      BLAST
      Topological domaini281 – 29414ExtracellularBy similarityAdd
      BLAST
      Transmembranei295 – 31622Helical; Voltage-sensor; Name=Segment S4By similarityAdd
      BLAST
      Topological domaini317 – 33014CytoplasmicBy similarityAdd
      BLAST
      Transmembranei331 – 35121Helical; Name=Segment S5By similarityAdd
      BLAST
      Topological domaini352 – 36413ExtracellularBy similarityAdd
      BLAST
      Intramembranei365 – 37612Helical; Name=Pore helixBy similarityAdd
      BLAST
      Intramembranei377 – 3848By similarity
      Topological domaini385 – 3917ExtracellularBy similarity
      Transmembranei392 – 42029Helical; Name=Segment S6By similarityAdd
      BLAST
      Topological domaini421 – 858438CytoplasmicBy similarityAdd
      BLAST

      GO - Cellular componenti

      Complete GO annotation...

      Keywords - Cellular componenti

      Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 858858Potassium voltage-gated channel subfamily B member 1PRO_0000054044Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Modified residuei15 – 151PhosphoserineBy similarity
      Modified residuei128 – 1281Phosphotyrosine; by SrcBy similarity
      Modified residuei444 – 4441PhosphoserineBy similarity
      Modified residuei457 – 4571PhosphoserineBy similarity
      Cross-linki475 – 475Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
      Modified residuei484 – 4841PhosphoserineBy similarity
      Modified residuei496 – 4961PhosphoserineBy similarity
      Modified residuei503 – 5031PhosphoserineBy similarity
      Modified residuei519 – 5191PhosphoserineBy similarity
      Modified residuei520 – 5201Phosphoserine; by CDK5; in vitroBy similarity
      Modified residuei541 – 5411PhosphoserineBy similarity
      Modified residuei567 – 5671PhosphoserineBy similarity
      Modified residuei590 – 5901PhosphoserineBy similarity
      Modified residuei607 – 6071Phosphoserine; by CDK5By similarity
      Modified residuei656 – 6561Phosphoserine; by CDK5; in vitroBy similarity
      Modified residuei720 – 7201PhosphoserineBy similarity
      Modified residuei772 – 7721PhosphoserineBy similarity
      Modified residuei800 – 8001PhosphoserineBy similarity
      Modified residuei805 – 8051Phosphoserine; by CDK5, MAPK14; in vitroBy similarity

      Post-translational modificationi

      Phosphorylated. Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons. Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities. Tyr-128 can be phosphorylated by Src and dephosphorylated by cytoplasmic form of the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity. Phosphorylated on Tyr-128 by Src and on Ser-805 by MAPK14/P38MAPK; phosphorylations are necessary and sufficient for an increase in plasma membrane insertion, apoptotic potassium current surge and completion of the neuronal cell death program. Phosphorylated on Ser-520, Ser-607, Ser-656 and Ser-805 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation. The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS). Highly phosphorylated on serine residues in the C-terminal cytoplasmic tail in resting neurons. Phosphorylated in pancreatic beta cells in response to incretin hormones stimulation in a PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5; levels then increase to reach adult levels by P14. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties. Dephosphorylation by phosphatase PTPRE confers neuroprotection by its inhibitory influence on the neuronal apoptotic potassium current surge in a Zn2+-dependent manner. Dephosphorylated at Ser-607 by protein phosphatase PPP1CA. Hypoxia-, seizure- or glutamate-induced neuronal activity promote calcium/calcineurin-dependent dephosphorylation resulting in a loss of KCNB1-containing clustering and enhanced channel activity. In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-720 are less dephosphorylated. In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced. Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic nerve tissue.By similarity
      Acetylated. Acetylation occurs in pancreatic beta cells in response to stimulation by incretin hormones in a histone acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent signaling pathway, promoting beta cell survival.By similarity
      Sumoylated on Lys-475, preferentially with SUMO1; sumoylation induces a positive shift in the voltage-dependence of activation and inhibits channel activity. Sumoylation increases the frequency of repetitive action potential firing at the cell surface of hippocampal neurons and decreases its frequency in pancreatic beta cells. Desumoylated by SENP1.By similarity

      Keywords - PTMi

      Isopeptide bond, Phosphoprotein, Ubl conjugation

      Proteomic databases

      PaxDbiO18868.
      PeptideAtlasiO18868.

      Interactioni

      Subunit structurei

      Homotetramer or heterotetramer with KCNB2. Heterotetramer with non-conducting channel-forming alpha subunits such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1. Channel activity is regulated by association with ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3. Self-associates (via N-terminus and C-terminus); self-association is required to regulate trafficking, gating and C-terminal phosphorylation-dependent modulation of the channel. Interacts (via C-terminus) with STX1A (via C-terminus); this decreases the rate of channel activation and increases the rate of channel inactivation in pancreatic beta cells, induces also neuronal apoptosis in response to oxidative injury as well as pore-independent enhancement of exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta cells and from the soma of dorsal root ganglia (DRG) neurons. Interacts (via N-terminus) with SNAP25; this decreases the rate of channel inactivation in pancreatic beta cells and also increases interaction during neuronal apoptosis in a N-methyl-D-aspartate receptor (NMDAR)-dependent manner. Interacts (via N-terminus and C-terminus) with VAMP2 (via N-terminus); stimulates channel inactivation rate. Interacts with CREB1; this promotes channel acetylation in response to stimulation by incretin hormones. Interacts (via N-terminus and C-terminus) with MYL12B. Interacts (via N-terminus) with PIAS3; this increases the number of functional channels at the cell surface. Interacts with SUMO1. Interacts (via phosphorylated form) with PTPRE; this reduces phosphorylation and channel activity in heterologous cells.By similarity

      GO - Molecular functioni

      Protein-protein interaction databases

      STRINGi9823.ENSSSCP00000007950.

      Structurei

      3D structure databases

      ProteinModelPortaliO18868.
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Region

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Regioni59 – 7517Self-associationBy similarityAdd
      BLAST
      Regioni448 – 48134Self-associationBy similarityAdd
      BLAST

      Motif

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Motifi377 – 3826Selectivity filterBy similarity

      Compositional bias

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Compositional biasi517 – 5204Poly-Ser
      Compositional biasi701 – 7066Poly-Ala

      Domaini

      The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity
      The N-terminal and C-terminal cytoplasmic regions mediate homooligomerization; self-association is required to regulate trafficking, gating and C-terminal phosphorylation-dependent modulation of the channel. The N-terminal cytoplasmic region is important for interaction with other channel-forming alpha subunits and with ancillary beta subunits. The C-terminus is necessary and sufficient for the restricted localization to, and clustering within, both in soma and proximal portions of dendrite of neurons and in lateral membrane of non-neuronal polarized cells. The C-terminus is both necessary and sufficient as a mediator of cholinergic and calcium-stimulated modulation of channel cell membrane clustering localization and activity in hippocampal neurons.By similarity

      Sequence similaritiesi

      Keywords - Domaini

      Transmembrane, Transmembrane helix

      Phylogenomic databases

      eggNOGiKOG3713. Eukaryota.
      COG1226. LUCA.
      HOGENOMiHOG000113206.
      HOVERGENiHBG052225.
      InParanoidiO18868.
      KOiK04885.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. BTB/POZ_dom.
      IPR027359. Channel_four-helix_dom.
      IPR005821. Ion_trans_dom.
      IPR003968. K_chnl_volt-dep_Kv.
      IPR003973. K_chnl_volt-dep_Kv2.
      IPR004350. K_chnl_volt-dep_Kv2.1.
      IPR011333. SKP1/BTB/POZ.
      IPR003131. T1-type_BTB.
      IPR028325. VG_K_chnl.
      [Graphical view]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      PF03521. Kv2channel. 2 hits.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01514. KV21CHANNEL.
      PR01491. KVCHANNEL.
      PR01495. SHABCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 1 hit.

      Sequencei

      Sequence statusi: Complete.

      O18868-1 [UniParc]FASTAAdd to basket

      « Hide

              10         20         30         40         50
      MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD
      60 70 80 90 100
      RLPRTRLGKL RDCNTHDSLL EVCDDYSLDD NEYFFDRHPG AFTSILNFYR
      110 120 130 140 150
      TGRLHMMEEM CALSFSQELD YWGIDEIYLE SCCQARYHQK KEQMNEELKR
      160 170 180 190 200
      EAETLREREG EEFDNTCCAE KRKKLWDLLE KPNSSVAAKI LAIISIMFIV
      210 220 230 240 250
      LSTIALSLNT LPELQSLDEF GQTTDNPQLA HVEAVCIAWF TMEYLLRFLS
      260 270 280 290 300
      SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR
      310 320 330 340 350
      IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF
      360 370 380 390 400
      FAEKDEDDTK FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA
      410 420 430 440 450
      GVLVIALPIP IIVNNFSEFY KEQKRQEKAI KRREALERAK RNGSIVSMNM
      460 470 480 490 500
      KDAFPRSIEM MDIVVEKNVE NMGQKDKVQD NHLSPNKWKW TKRTLSETSS
      510 520 530 540 550
      SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYNKMAKTQ SQPILNTKES
      560 570 580 590 600
      ATQSKPKEEL EMESIPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
      610 620 630 640 650
      ATRFSHSPLA SLPSKSGGSM APEVGWRGAL GATGGRFVEA NPTPDASHHS
      660 670 680 690 700
      TFFIESPKSS MKTTNPLKLR ALKVNFMEGD PSPLVPVLGM YHDPLRNRGG
      710 720 730 740 750
      AAAAVAGLEC ATLLDRPVLS PESSIYTTAS ARTPPRSPEK HTAIAFNFEA
      760 770 780 790 800
      GIHQYIDADT DDEGQVLYSV DSSPPKSLHG STSPKFSIGT RSEKNHFESS
      810 820 830 840 850
      PLPTSPKFLR QNCIYSTEAL TGKAPSGQEK CKLENHISPD VRVLPGGGAH

      GSTRDQSI
      Length:858
      Mass (Da):96,118
      Last modified:January 1, 1998 - v1
      Checksum:iA9E24C3A8E13B491
      GO

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AF026006 mRNA. Translation: AAB88809.1.
      RefSeqiNP_999383.1. NM_214218.1.
      UniGeneiSsc.16142.

      Genome annotation databases

      GeneIDi397433.
      KEGGissc:397433.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AF026006 mRNA. Translation: AAB88809.1.
      RefSeqiNP_999383.1. NM_214218.1.
      UniGeneiSsc.16142.

      3D structure databases

      ProteinModelPortaliO18868.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      STRINGi9823.ENSSSCP00000007950.

      Proteomic databases

      PaxDbiO18868.
      PeptideAtlasiO18868.

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      GeneIDi397433.
      KEGGissc:397433.

      Organism-specific databases

      CTDi3745.

      Phylogenomic databases

      eggNOGiKOG3713. Eukaryota.
      COG1226. LUCA.
      HOGENOMiHOG000113206.
      HOVERGENiHBG052225.
      InParanoidiO18868.
      KOiK04885.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. BTB/POZ_dom.
      IPR027359. Channel_four-helix_dom.
      IPR005821. Ion_trans_dom.
      IPR003968. K_chnl_volt-dep_Kv.
      IPR003973. K_chnl_volt-dep_Kv2.
      IPR004350. K_chnl_volt-dep_Kv2.1.
      IPR011333. SKP1/BTB/POZ.
      IPR003131. T1-type_BTB.
      IPR028325. VG_K_chnl.
      [Graphical view]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      PF03521. Kv2channel. 2 hits.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01514. KV21CHANNEL.
      PR01491. KVCHANNEL.
      PR01495. SHABCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 1 hit.
      ProtoNetiSearch...

      Entry informationi

      Entry nameiKCNB1_PIG
      AccessioniPrimary (citable) accession number: O18868
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: October 25, 2002
      Last sequence update: January 1, 1998
      Last modified: July 6, 2016
      This is version 104 of the entry and version 1 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program

      Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. SIMILARITY comments
        Index of protein domains and families

      Similar proteinsi

      Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
      100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
      90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
      50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.