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Protein

Transient receptor potential cation channel subfamily A member 1

Gene

Trpa1

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

Functioni

Receptor-activated non-selective cation channel involved in detection of pain and possibly also in cold perception and inner ear function. Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of volatile irritants, such as mustard oil, cinnamaldehyde, garlic and acrolein, an irritant from tears gas and vehicule exhaust fumes. Acts also as a ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana. Is also activated by menthol (in vitro) (By similarity). May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system.By similarity5 Publications

Enzyme regulationi

Inhibited by ruthenium red, a potent blocker of TRPV channels.1 Publication

GO - Molecular functioni

  • calcium channel activity Source: MGI
  • channel activity Source: MGI
  • intracellular ligand-gated calcium channel activity Source: UniProtKB
  • ion channel activity Source: MGI
  • temperature-gated cation channel activity Source: UniProtKB

GO - Biological processi

  • calcium ion transmembrane transport Source: GOC
  • calcium ion transport Source: MGI
  • cation transmembrane transport Source: GOC
  • cell surface receptor signaling pathway Source: BHF-UCL
  • detection of chemical stimulus involved in sensory perception of pain Source: MGI
  • detection of mechanical stimulus involved in sensory perception of pain Source: MGI
  • protein homotetramerization Source: UniProtKB
  • response to cold Source: MGI
  • response to drug Source: MGI
  • response to hydrogen peroxide Source: MGI
  • response to organic cyclic compound Source: BHF-UCL
  • response to organic substance Source: UniProtKB
  • response to pain Source: MGI
  • thermoception Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Sensory transduction, Transport

Enzyme and pathway databases

ReactomeiREACT_319309. TRP channels.

Protein family/group databases

TCDBi1.A.4.6.1. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily A member 1
Alternative name(s):
Ankyrin-like with transmembrane domains protein 1
Gene namesi
Name:Trpa1
Synonyms:Anktm11 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:3522699. Trpa1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 721721CytoplasmicBy similarityAdd
BLAST
Transmembranei722 – 74221Helical; Name=1By similarityAdd
BLAST
Topological domaini743 – 76725ExtracellularBy similarityAdd
BLAST
Transmembranei768 – 78821Helical; Name=2By similarityAdd
BLAST
Topological domaini789 – 80618CytoplasmicBy similarityAdd
BLAST
Transmembranei807 – 82721Helical; Name=3By similarityAdd
BLAST
Topological domaini828 – 8325ExtracellularBy similarity
Transmembranei833 – 85321Helical; Name=4By similarityAdd
BLAST
Topological domaini854 – 87623CytoplasmicBy similarityAdd
BLAST
Transmembranei877 – 89721Helical; Name=5Sequence AnalysisBy similarityAdd
BLAST
Topological domaini898 – 9047ExtracellularBy similarity
Intramembranei905 – 92521Pore-formingBy similarityAdd
BLAST
Topological domaini926 – 93712ExtracellularBy similarityAdd
BLAST
Transmembranei938 – 95922Helical; Name=6By similarityAdd
BLAST
Topological domaini960 – 1125166CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • stereocilium bundle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice display normal cold sensitivity and unimpaired auditory function, suggesting that this channel is not required for the initial detection of noxious cold or sound. However, they exhibit pronounced deficits in bradykinin-evoked nociceptor excitation and pain hypersensitivity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11251125Transient receptor potential cation channel subfamily A member 1PRO_0000215370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi193 ↔ 666Alternate1 Publication
Disulfide bondi463 ↔ 666Alternate1 Publication
Disulfide bondi609 ↔ 622Alternate1 Publication
Disulfide bondi622 ↔ 666Alternate1 Publication
Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi755 – 7551N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

TRPA1 activation by electrophiles occurs though covalent modification of specific cysteine residues in the N-terminal cytoplasmic domain.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8BLA8.

PTM databases

PhosphoSiteiQ8BLA8.

Expressioni

Tissue specificityi

Expressed in inner ear (at protein level). Specifically expressed in a subset of nociceptive neurons. Expressed in the same neurons that TRPV1. In contrast, it is not expressed in neurons expressing TRPM8. Expressed in the superior cervical ganglion.4 Publications

Developmental stagei

During utricle development, it is first expressed at E15 and E16 and peaks at E17. It drops at E18 but increases again at E19, possibly corresponding to a second wave of hair cells that are generated at E15.1 Publication

Gene expression databases

BgeeiQ8BLA8.
GenevisibleiQ8BLA8. MM.

Interactioni

Subunit structurei

Homotetramer (PubMed:21908607). Interacts with TMEM100 (PubMed:25640077).2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043594.

Structurei

3D structure databases

ProteinModelPortaliQ8BLA8.
SMRiQ8BLA8. Positions 61-636, 793-973.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati63 – 9432ANK 1Add
BLAST
Repeati98 – 12730ANK 2Add
BLAST
Repeati131 – 16131ANK 3Add
BLAST
Repeati165 – 19430ANK 4Add
BLAST
Repeati198 – 22730ANK 5Add
BLAST
Repeati239 – 26830ANK 6Add
BLAST
Repeati272 – 30130ANK 7Add
BLAST
Repeati309 – 33830ANK 8Add
BLAST
Repeati342 – 37130ANK 9Add
BLAST
Repeati413 – 44230ANK 10Add
BLAST
Repeati446 – 47530ANK 11Add
BLAST
Repeati482 – 51130ANK 12Add
BLAST
Repeati514 – 54330ANK 13Add
BLAST
Repeati548 – 57730ANK 14Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1048 – 10547Inositolphosphate bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1044 – 107330By similarityAdd
BLAST

Domaini

C-terminal helices from the four subunits associate to form atypical coiled coil structure; this region is probably involved in binding the inositol polyphosphates that are required for optimal channel activity (in vitro).By similarity
The ANK repeat domain consists of a convex stem structure followed by a crescent-shaped structure that surrounds the protein core.By similarity

Sequence similaritiesi

Contains 14 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00780000121959.
HOGENOMiHOG000044486.
HOVERGENiHBG059027.
InParanoidiQ8BLA8.
KOiK04984.
OMAiWLAYGFR.
OrthoDBiEOG7P02H2.
PhylomeDBiQ8BLA8.
TreeFamiTF317264.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR030288. TRPA1/painless.
[Graphical view]
PANTHERiPTHR24190:SF5. PTHR24190:SF5. 1 hit.
PfamiPF12796. Ank_2. 6 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 14 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BLA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRGLRRILL PEERKEVQGV VYRGVGEDMD CSKESFKVDI EGDMCRLEDF
60 70 80 90 100
IKNRRKLSKY EDENLCPLHH AAAEGQVELM ELIINGSSCE VLNIMDGYGN
110 120 130 140 150
TPLHCAAEKN QVESVKFLLS QGANPNLRNR NMMSPLHIAV HGMYNEVIKV
160 170 180 190 200
LTEHKATNIN LEGENGNTAL MSTCAKDNSE ALQILLEKGA KLCKSNKWGD
210 220 230 240 250
YPVHQAAFSG AKKCMELILA YGEKNGYSRE THINFVNHKK ASPLHLAVQS
260 270 280 290 300
GDLDMIKMCL DNGAHIDMME NAKCMALHFA ATQGATDIVK LMISSYTGSS
310 320 330 340 350
DIVNAVDGNQ ETLLHRASLF DHHDLAEYLI SVGADINSTD SEGRSPLILA
360 370 380 390 400
TASASWNIVN LLLCKGAKVD IKDHLGRNFL HLTVQQPYGL RNLRPEFMQM
410 420 430 440 450
QHIKELVMDE DNDGCTPLHY ACRQGVPVSV NNLLGFNVSI HSKSKDKKSP
460 470 480 490 500
LHFAASYGRI NTCQRLLQDI SDTRLLNEGD LHGMTPLHLA AKNGHDKVVQ
510 520 530 540 550
LLLKKGALFL SDHNGWTALH HASMGGYTQT MKVILDTNLK CTDRLDEEGN
560 570 580 590 600
TALHFAAREG HAKAVAMLLS YNADILLNKK QASFLHIALH NKRKEVVLTT
610 620 630 640 650
IRNKRWDECL QVFTHNSPSN RCPIMEMVEY LPECMKVLLD FCMIPSTEDK
660 670 680 690 700
SCQDYHIEYN FKYLQCPLSM TKKVAPTQDV VYEPLTILNV MVQHNRIELL
710 720 730 740 750
NHPVCREYLL MKWCAYGFRA HMMNLGSYCL GLIPMTLLVV KIQPGMAFNS
760 770 780 790 800
TGIINGTSST HEERIDTLNS FPIKICMILV FLSSIFGYCK EVIQIFQQKR
810 820 830 840 850
NYFLDYNNAL EWVIYTTSII FVLPLFLNIP AYMQWQCGAI AIFFYWMNFL
860 870 880 890 900
LYLQRFENCG IFIVMLEVIF KTLLRSTGVF IFLLLAFGLS FYVLLNFQDA
910 920 930 940 950
FSTPLLSLIQ TFSMMLGDIN YRDAFLEPLF RNELAYPVLT FGQLIAFTMF
960 970 980 990 1000
VPIVLMNLLI GLAVGDIAEV QKHASLKRIA MQVELHTNLE KKLPLWYLRK
1010 1020 1030 1040 1050
VDQRSTIVYP NRPRHGRMLR FFHYFLNMQE TRQEVPNIDT CLEMEILKQK
1060 1070 1080 1090 1100
YRLKDLTSLL EKQHELIKLI IQKMEIISET EDEDNHCSFQ DRFKKERLEQ
1110 1120
MHSKWNFVLN AVKTKTHCSI SHPDF
Length:1,125
Mass (Da):128,467
Last modified:March 1, 2003 - v1
Checksum:iCD718BF3ED4AC291
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY231177 mRNA. Translation: AAO43183.1.
AK045771 mRNA. Translation: BAC32487.1.
BC120563 mRNA. Translation: AAI20564.1.
BC131963 mRNA. Translation: AAI31964.1.
CCDSiCCDS35516.1.
RefSeqiNP_808449.1. NM_177781.4.
UniGeneiMm.186329.

Genome annotation databases

EnsembliENSMUST00000041447; ENSMUSP00000043594; ENSMUSG00000032769.
GeneIDi277328.
KEGGimmu:277328.
UCSCiuc007ajc.1. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

The power behind pain - Issue 82 of May 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY231177 mRNA. Translation: AAO43183.1.
AK045771 mRNA. Translation: BAC32487.1.
BC120563 mRNA. Translation: AAI20564.1.
BC131963 mRNA. Translation: AAI31964.1.
CCDSiCCDS35516.1.
RefSeqiNP_808449.1. NM_177781.4.
UniGeneiMm.186329.

3D structure databases

ProteinModelPortaliQ8BLA8.
SMRiQ8BLA8. Positions 61-636, 793-973.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043594.

Chemistry

BindingDBiQ8BLA8.
ChEMBLiCHEMBL1075310.
GuidetoPHARMACOLOGYi485.

Protein family/group databases

TCDBi1.A.4.6.1. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteiQ8BLA8.

Proteomic databases

PRIDEiQ8BLA8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041447; ENSMUSP00000043594; ENSMUSG00000032769.
GeneIDi277328.
KEGGimmu:277328.
UCSCiuc007ajc.1. mouse.

Organism-specific databases

CTDi8989.
MGIiMGI:3522699. Trpa1.

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00780000121959.
HOGENOMiHOG000044486.
HOVERGENiHBG059027.
InParanoidiQ8BLA8.
KOiK04984.
OMAiWLAYGFR.
OrthoDBiEOG7P02H2.
PhylomeDBiQ8BLA8.
TreeFamiTF317264.

Enzyme and pathway databases

ReactomeiREACT_319309. TRP channels.

Miscellaneous databases

NextBioi393737.
PROiQ8BLA8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BLA8.
GenevisibleiQ8BLA8. MM.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR030288. TRPA1/painless.
[Graphical view]
PANTHERiPTHR24190:SF5. PTHR24190:SF5. 1 hit.
PfamiPF12796. Ank_2. 6 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 14 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ANKTM1, a TRP-like channel expressed in nociceptive neurons, is activated by cold temperatures."
    Story G.M., Peier A.M., Reeve A.J., Eid S.R., Mosbacher J., Hricik T.R., Earley T.J., Hergarden A.C., Anderson D.A., Hwang S.W., McIntyre P., Jegla T., Bevan S., Patapoutian A.
    Cell 112:819-829(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: C57BL/6.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "Cold-sensitive, menthol-insensitive neurons in the murine sympathetic nervous system."
    Smith M.P., Beacham D., Ensor E., Koltzenburg M.
    NeuroReport 15:1399-1403(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Noxious cold ion channel TRPA1 is activated by pungent compounds and bradykinin."
    Bandell M., Story G.M., Hwang S.W., Viswanath V., Eid S.R., Petrus M.J., Earley T.J., Patapoutian A.
    Neuron 41:849-857(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Nociceptor and hair cell transducer properties of TRPA1, a channel for pain and hearing."
    Nagata K., Duggan A., Kumar G., Garcia-Anoveros J.
    J. Neurosci. 25:4052-4061(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
  8. "TRPA1 mediates the inflammatory actions of environmental irritants and proalgesic agents."
    Bautista D.M., Jordt S.E., Nikai T., Tsuruda P.R., Read A.J., Poblete J., Yamoah E.N., Basbaum A.I., Julius D.
    Cell 124:1269-1282(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Identification of in vivo disulfide conformation of TRPA1 ion channel."
    Wang L., Cvetkov T.L., Chance M.R., Moiseenkova-Bell V.Y.
    J. Biol. Chem. 287:6169-6176(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  10. "Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy."
    Cvetkov T.L., Huynh K.W., Cohen M.R., Moiseenkova-Bell V.Y.
    J. Biol. Chem. 286:38168-38176(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (16 ANGSTROMS), SUBUNIT.
  11. "Tmem100 Is a regulator of TRPA1-TRPV1 complex and contributes to persistent pain."
    Weng H.J., Patel K.N., Jeske N.A., Bierbower S.M., Zou W., Tiwari V., Zheng Q., Tang Z., Mo G.C., Wang Y., Geng Y., Zhang J., Guan Y., Akopian A.N., Dong X.
    Neuron 85:833-846(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM100.

Entry informationi

Entry nameiTRPA1_MOUSE
AccessioniPrimary (citable) accession number: Q8BLA8
Secondary accession number(s): Q0VBN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 111 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.