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Protein

Transient receptor potential cation channel subfamily V member 4

Gene

Trpv4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11094154). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:14691263, PubMed:16571723). Also activated by heat, low pH, citrate and phorbol esters (PubMed:14691263). Increase of intracellular Ca2+ potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism (By similarity). Acts as a regulator of intracellular Ca2+ in synoviocytes (By similarity). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (By similarity). Together with PKD2, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (PubMed:20413591). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (PubMed:23021218). Regulates expression of chemokines and cytokines related to proinflammatory pathway in adipocytes (PubMed:23021218). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (PubMed:16571723).By similarity7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921ATPBy similarity
Binding sitei201 – 2011ATPBy similarity
Binding sitei239 – 2391ATPBy similarity
Binding sitei248 – 2481ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium channel activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • cation channel activity Source: UniProtKB
  • osmosensor activity Source: MGI
  • protein kinase binding Source: BHF-UCL
  • SH2 domain binding Source: BHF-UCL
  • stretch-activated, cation-selective, calcium channel activity Source: MGI

GO - Biological processi

  • actin cytoskeleton reorganization Source: Ensembl
  • actin filament organization Source: GO_Central
  • blood vessel endothelial cell delamination Source: MGI
  • calcium ion import Source: BHF-UCL
  • calcium ion transmembrane transport Source: MGI
  • calcium ion transport Source: MGI
  • cell-cell junction assembly Source: UniProtKB
  • cellular calcium ion homeostasis Source: UniProtKB
  • cellular hypotonic response Source: BHF-UCL
  • cellular hypotonic salinity response Source: UniProtKB
  • cellular response to heat Source: UniProtKB
  • cellular response to osmotic stress Source: UniProtKB
  • cortical microtubule organization Source: Ensembl
  • diet induced thermogenesis Source: UniProtKB
  • glucose homeostasis Source: UniProtKB
  • hyperosmotic salinity response Source: MGI
  • microtubule polymerization Source: Ensembl
  • multicellular organismal water homeostasis Source: MGI
  • negative regulation of brown fat cell differentiation Source: UniProtKB
  • negative regulation of neuron projection development Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • osmosensory signaling pathway Source: BHF-UCL
  • positive regulation of chemokine (C-C motif) ligand 5 production Source: UniProtKB
  • positive regulation of chemokine (C-X-C motif) ligand 1 production Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: MGI
  • positive regulation of energy homeostasis Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of inflammatory response Source: UniProtKB
  • positive regulation of interleukin-6 secretion Source: UniProtKB
  • positive regulation of JNK cascade Source: UniProtKB
  • positive regulation of macrophage chemotaxis Source: UniProtKB
  • positive regulation of macrophage inflammatory protein 1 alpha production Source: UniProtKB
  • positive regulation of microtubule depolymerization Source: Ensembl
  • positive regulation of monocyte chemotactic protein-1 production Source: UniProtKB
  • positive regulation of vascular permeability Source: UniProtKB
  • regulation of response to osmotic stress Source: MGI
  • response to insulin Source: UniProtKB
  • response to osmotic stress Source: MGI
  • signal transduction involved in regulation of aerobic respiration Source: UniProtKB
  • vasopressin secretion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-3295583. TRP channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 4
Short name:
TrpV4
Alternative name(s):
Osm-9-like TRP channel 4
Short name:
OTRPC4
Transient receptor potential protein 12
Short name:
TRP12
Vanilloid receptor-like channel 2
Vanilloid receptor-like protein 2
Vanilloid receptor-related osmotically-activated channel
Short name:
VR-OAC
Gene namesi
Name:Trpv4
Synonyms:Trp12, Vrl2, Vroac
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1926945. Trpv4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 465465CytoplasmicSequence analysisAdd
BLAST
Transmembranei466 – 48621HelicalSequence analysisAdd
BLAST
Topological domaini487 – 50822ExtracellularSequence analysisAdd
BLAST
Transmembranei509 – 52921HelicalSequence analysisAdd
BLAST
Topological domaini530 – 55021CytoplasmicSequence analysisAdd
BLAST
Transmembranei551 – 57121HelicalSequence analysisAdd
BLAST
Topological domaini572 – 5721ExtracellularSequence analysis
Transmembranei573 – 59321HelicalSequence analysisAdd
BLAST
Topological domaini594 – 61623CytoplasmicSequence analysisAdd
BLAST
Transmembranei617 – 63721HelicalSequence analysisAdd
BLAST
Intramembranei648 – 67831Pore-formingCuratedAdd
BLAST
Transmembranei691 – 71121HelicalSequence analysisAdd
BLAST
Topological domaini712 – 871160CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: UniProtKB-SubCell
  • cell surface Source: Ensembl
  • cilium Source: MGI
  • cortical actin cytoskeleton Source: Ensembl
  • cytoplasmic microtubule Source: Ensembl
  • cytoplasmic vesicle Source: Ensembl
  • cytosol Source: Ensembl
  • filopodium Source: Ensembl
  • focal adhesion Source: Ensembl
  • growth cone Source: Ensembl
  • integral component of plasma membrane Source: GO_Central
  • lamellipodium Source: Ensembl
  • plasma membrane Source: UniProtKB
  • ruffle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cilium, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display impairment of the intercellular junction-dependent barrier function in the skin (PubMed:20413591). Increased energy expenditure and improved insulin sensitivity in white adipose tissues (PubMed:23021218). Reduced Ca2+ entry and loss of regulatory volume decrease in response to hypotonicity in acinar cells (PubMed:16571723).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101Y → F: Increases protein abundance at plasma membrane. Greatly reduces channel activity. 1 Publication
Mutagenesisi142 – 1432PP → AL: Strongly reduced interaction with PACSIN3. 1 Publication
Mutagenesisi253 – 2531Y → F: Results are conflicting as to whether hypotonicity-dependent channel activity is abolished. 2 Publications
Mutagenesisi556 – 5561Y → A: Reduces channel activation by 4-alpha-PDD and heat but not hypo-osmotic cell swelling. 1 Publication
Mutagenesisi556 – 5561Y → F: No changes in channel activation by 4-alpha-PDD or heat. 1 Publication
Mutagenesisi557 – 5571S → A: No changes in channel activity. 1 Publication
Mutagenesisi672 – 6721D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-682. 1 Publication
Mutagenesisi675 – 6751K → A: No effect on channel pore properties. 1 Publication
Mutagenesisi680 – 6801M → A: Impairs Ca(2+) permeation. 1 Publication
Mutagenesisi682 – 6821D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-672. 1 Publication
Mutagenesisi805 – 8051Y → F: No changes in channel activity. 1 Publication
Mutagenesisi824 – 8241S → A: Loss of phosphorylation but no significant effect on channel activity. 1 Publication
Mutagenesisi824 – 8241S → D: Phosphomimetic mutant which enhances channel function. 1 Publication

Chemistry

ChEMBLiCHEMBL6126.
GuidetoPHARMACOLOGYi510.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 871871Transient receptor potential cation channel subfamily V member 4PRO_0000215348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101Phosphotyrosine; by SRC-type Tyr-kinases1 Publication
Modified residuei253 – 2531Phosphotyrosine; by LYN1 Publication
Modified residuei805 – 8051Phosphotyrosine; by SRC-type Tyr-kinases1 Publication
Modified residuei824 – 8241Phosphoserine; by PKC and PKA1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9EPK8.
PaxDbiQ9EPK8.
PRIDEiQ9EPK8.

PTM databases

iPTMnetiQ9EPK8.
PhosphoSiteiQ9EPK8.

Expressioni

Tissue specificityi

Detected in liver, kidney, heart, brain cortex, cerebellum and brainstem (at protein level). Expressed in salivary glands (at protein level) (PubMed:16571723). Expressed in heart, lung, spleen, liver, kidney, brain, skeletal muscle and testis. In the central nervous system, expressed in the lamina terminalis (arched vascular organ and neurons of the subfornical organ), median preoptic area, ventral hippocampal commissure, and ependymal cells of the choroid plexus. In the cochlea, expressed in both inner and outer hair cells, and in marginal cells of the cochlear stria vascularis. Expressed in large neurons of the trigeminal ganglion. In the kidney cortex, strongly expressed by epithelial cells of tubules and much weaker in glomeruli.6 Publications

Gene expression databases

BgeeiENSMUSG00000014158.
ExpressionAtlasiQ9EPK8. baseline and differential.
GenevisibleiQ9EPK8. MM.

Interactioni

Subunit structurei

Interacts with calmodulin (By similarity). Interacts with CTNNB1 (PubMed:20413591). The TRPV4 and CTNNB1 complex can interact with CDH1 (PubMed:20413591). Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1 (By similarity). Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES (PubMed:14517216, PubMed:12538589). Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain) (PubMed:16627472, PubMed:18174177). Interacts with ITPR3 (By similarity). Interacts with AQP5; the interaction is probably indirect and regulates TRPV4 activation by hypotonicity (PubMed:16571723). Interacts with ANO1 (PubMed:24509911). Interacts (via C-terminus) with PKD2 (via C-terminus) (PubMed:18695040).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBCP0CG483EBI-7091763,EBI-3390054From a different organism.

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • SH2 domain binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-44011N.
IntActiQ9EPK8. 2 interactions.
MINTiMINT-4050076.
STRINGi10090.ENSMUSP00000071859.

Chemistry

BindingDBiQ9EPK8.

Structurei

3D structure databases

ProteinModelPortaliQ9EPK8.
SMRiQ9EPK8. Positions 148-755.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati237 – 26630ANK 1Add
BLAST
Repeati284 – 31330ANK 2Add
BLAST
Repeati369 – 39830ANK 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni812 – 83120Interaction with calmodulin and ITPR3By similarityAdd
BLAST

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9EPK8.
KOiK04973.
OMAiVPTYPAC.
OrthoDBiEOG091G016O.
PhylomeDBiQ9EPK8.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR008348. TRPV4_channel.
[Graphical view]
PANTHERiPTHR10582:SF4. PTHR10582:SF4. 2 hits.
PfamiPF00023. Ank. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
PR01769. VRL2RECEPTOR.
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPGDGPRA APGEVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS
60 70 80 90 100
PVDASRPAGP GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK
110 120 130 140 150
KAPMDSLFDY GTYRHHPSDN KRWRRKVVEK QPQSPKAPAP QPPPILKVFN
160 170 180 190 200
RPILFDIVSR GSTADLDGLL SFLLTHKKRL TDEEFREPST GKTCLPKALL
210 220 230 240 250
NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT SLHIAIERRC
260 270 280 290 300
KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI
310 320 330 340 350
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL
360 370 380 390 400
LKCSRLFPDS NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR
410 420 430 440 450
HLSRKFKDWA YGPVYSSLYD LSSLDTCGEE VSVLEILVYN SKIENRHEML
460 470 480 490 500
AVEPINELLR DKWRKFGAVS FYINVVSYLC AMVIFTLTAY YQPLEGTPPY
510 520 530 540 550
PYRTTVDYLR LAGEVITLFT GVLFFFTSIK DLFTKKCPGV NSLFVDGSFQ
560 570 580 590 600
LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG
610 620 630 640 650
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCDEDQS
660 670 680 690 700
NCTVPTYPAC RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV
710 720 730 740 750
TYIILTFVLL LNMLIALMGE TVGQVSKESK HIWKLQWATT ILDIERSFPV
760 770 780 790 800
FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV DEVNWSHWNQ NLGIINEDPG
810 820 830 840 850
KSEIYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSSADE VVVPLDNLGN
860 870
PNCDGHQQGY APKWRTDDAP L
Length:871
Mass (Da):98,027
Last modified:March 1, 2001 - v1
Checksum:i5BAC6E33F89CEA05
GO

Sequence cautioni

The sequence AAG28028 differs from that shown. Reason: Frameshift at positions 47, 50, 53, 72 and 73. Curated
The sequence AAK69486 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451G → S in AAG28028 (PubMed:11081638).Curated
Sequence conflicti90 – 901L → R in AAG17543 (PubMed:11025659).Curated
Sequence conflicti90 – 901L → R in AAK69486 (Ref. 5) Curated
Sequence conflicti137 – 1371A → T in BAA83731 (PubMed:12692122).Curated
Sequence conflicti210 – 2112IP → LQ in BAA83731 (PubMed:12692122).Curated
Sequence conflicti477 – 4771S → P in AAG28028 (PubMed:11081638).Curated
Sequence conflicti784 – 7841N → S in BAA83731 (PubMed:12692122).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263522 mRNA. Translation: AAG28028.1. Frameshift.
AJ296078 mRNA. Translation: CAC20703.1.
AF208026 mRNA. Translation: AAG17543.1.
AB021875 mRNA. Translation: BAA83731.2.
AF279672 mRNA. Translation: AAK69486.1. Different initiation.
BC127052 mRNA. Translation: AAI27053.1.
CCDSiCCDS19568.1.
RefSeqiNP_071300.2. NM_022017.3.
XP_006530495.2. XM_006530432.2.
UniGeneiMm.266450.

Genome annotation databases

EnsembliENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158.
ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158.
GeneIDi63873.
KEGGimmu:63873.
UCSCiuc008yzu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263522 mRNA. Translation: AAG28028.1. Frameshift.
AJ296078 mRNA. Translation: CAC20703.1.
AF208026 mRNA. Translation: AAG17543.1.
AB021875 mRNA. Translation: BAA83731.2.
AF279672 mRNA. Translation: AAK69486.1. Different initiation.
BC127052 mRNA. Translation: AAI27053.1.
CCDSiCCDS19568.1.
RefSeqiNP_071300.2. NM_022017.3.
XP_006530495.2. XM_006530432.2.
UniGeneiMm.266450.

3D structure databases

ProteinModelPortaliQ9EPK8.
SMRiQ9EPK8. Positions 148-755.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-44011N.
IntActiQ9EPK8. 2 interactions.
MINTiMINT-4050076.
STRINGi10090.ENSMUSP00000071859.

Chemistry

BindingDBiQ9EPK8.
ChEMBLiCHEMBL6126.
GuidetoPHARMACOLOGYi510.

PTM databases

iPTMnetiQ9EPK8.
PhosphoSiteiQ9EPK8.

Proteomic databases

MaxQBiQ9EPK8.
PaxDbiQ9EPK8.
PRIDEiQ9EPK8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158.
ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158.
GeneIDi63873.
KEGGimmu:63873.
UCSCiuc008yzu.1. mouse.

Organism-specific databases

CTDi59341.
MGIiMGI:1926945. Trpv4.

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9EPK8.
KOiK04973.
OMAiVPTYPAC.
OrthoDBiEOG091G016O.
PhylomeDBiQ9EPK8.
TreeFamiTF314711.

Enzyme and pathway databases

ReactomeiR-MMU-3295583. TRP channels.

Miscellaneous databases

PROiQ9EPK8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000014158.
ExpressionAtlasiQ9EPK8. baseline and differential.
GenevisibleiQ9EPK8. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR008348. TRPV4_channel.
[Graphical view]
PANTHERiPTHR10582:SF4. PTHR10582:SF4. 2 hits.
PfamiPF00023. Ank. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
PR01769. VRL2RECEPTOR.
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRPV4_MOUSE
AccessioniPrimary (citable) accession number: Q9EPK8
Secondary accession number(s): A0JNY0
, Q91XR5, Q9EQZ4, Q9ERZ7, Q9ES76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 129 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.