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Whirlin

 WHRN_MOUSE              Reviewed;         918 AA.
Q80VW5; A2AGD2; I6MML6; I6MML7; Q3TZC8; Q5MLF1; Q5MLF2; Q5MLF3;
Q5MLF4; Q5MLF5; Q5MLF6; Q5MLF7; Q5MLF8; Q5MLF9; Q80TC2; Q80VW4;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 3.
16-JAN-2019, entry version 125.
RecName: Full=Whirlin;
Name=Whrn {ECO:0000312|MGI:MGI:2682003}; Synonyms=Dfnb31, Kiaa1526;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9),
INTERACTION WITH MYO15A, AND SUBCELLULAR LOCATION.
STRAIN=C57BL/6J; TISSUE=Inner ear;
PubMed=15654330; DOI=10.1038/ncb1219;
Belyantseva I.A., Boger E.T., Naz S., Frolenkov G.I., Sellers J.R.,
Ahmed Z.M., Griffith A.J., Friedman T.B.;
"Myosin-XVa is required for tip localization of whirlin and
differential elongation of hair-cell stereocilia.";
Nat. Cell Biol. 7:148-156(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 11 AND 12), INTERACTION WITH
RPGR, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=22323458; DOI=10.1167/iovs.11-8845;
Wright R.N., Hong D.H., Perkins B.;
"RpgrORF15 connects to the usher protein network through direct
interactions with multiple whirlin isoforms.";
Invest. Ophthalmol. Vis. Sci. 53:1519-1529(2012).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
STRAIN=C57BL/6J; TISSUE=Inner ear;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-918 (ISOFORM 4).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[6]
DISEASE.
PubMed=12124769; DOI=10.1002/cne.10301;
Holme R.H., Kiernan B.W., Brown S.D.M., Steel K.P.;
"Elongation of hair cell stereocilia is defective in the mouse mutant
whirler.";
J. Comp. Neurol. 450:94-102(2002).
[7]
DISEASE, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=12833159; DOI=10.1038/ng1208;
Mburu P., Mustapha M., Varela A., Weil D., El-Amraoui A., Holme R.H.,
Rump A., Hardisty R.E., Blanchard S., Coimbra R.S., Perfettini I.,
Parkinson N., Mallon A.-M., Glenister P., Rogers M.J., Paige A.J.,
Moir L., Clay J., Rosenthal A., Liu X.Z., Blanco G., Steel K.P.,
Petit C., Brown S.D.;
"Defects in whirlin, a PDZ domain molecule involved in stereocilia
elongation, cause deafness in the whirler mouse and families with
DFNB31.";
Nat. Genet. 34:421-428(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=15590699; DOI=10.1093/hmg/ddi035;
Kikkawa Y., Mburu P., Morse S., Kominami R., Townsend S.,
Brown S.D.M.;
"Mutant analysis reveals whirlin as a dynamic organizer in the growing
hair cell stereocilium.";
Hum. Mol. Genet. 14:391-400(2005).
[9]
SUBUNIT, INTERACTION WITH LRRC4C; MYO7A AND MYO15A, AND SUBCELLULAR
LOCATION.
PubMed=15590698; DOI=10.1093/hmg/ddi036;
Delprat B., Michel V., Goodyear R., Yamasaki Y., Michalski N.,
El-Amraoui A., Perfettini I., Legrain P., Richardson G.,
Hardelin J.-P., Petit C.;
"Myosin XVa and whirlin, two deafness gene products required for hair
bundle growth, are located at the stereocilia tips and interact
directly.";
Hum. Mol. Genet. 14:401-410(2005).
[10]
INTERACTION WITH USH2A.
PubMed=16301217; DOI=10.1093/hmg/ddi416;
Adato A., Lefevre G., Delprat B., Michel V., Michalski N.,
Chardenoux S., Weil D., El-Amraoui A., Petit C.;
"Usherin, the defective protein in Usher syndrome type IIA, is likely
to be a component of interstereocilia ankle links in the inner ear
sensory cells.";
Hum. Mol. Genet. 14:3921-3932(2005).
[11]
DEVELOPMENTAL STAGE.
PubMed=16434480; DOI=10.1093/hmg/ddi490;
van Wijk E., van der Zwaag B., Peters T., Zimmermann U., Te Brinke H.,
Kersten F.F.J., Maerker T., Aller E., Hoefsloot L.H.,
Cremers C.W.R.J., Cremers F.P.M., Wolfrum U., Knipper M., Roepman R.,
Kremer H.;
"The DFNB31 gene product whirlin connects to the Usher protein network
in the cochlea and retina by direct association with USH2A and
VLGR1.";
Hum. Mol. Genet. 15:751-765(2006).
[12]
INTERACTION WITH MPP1.
PubMed=16829577; DOI=10.1073/pnas.0600923103;
Mburu P., Kikkawa Y., Townsend S., Romero R., Yonekawa H., Brown S.D.;
"Whirlin complexes with p55 at the stereocilia tip during hair cell
development.";
Proc. Natl. Acad. Sci. U.S.A. 103:10973-10978(2006).
[13]
DISEASE.
PubMed=17326148; DOI=10.1002/cm.20199;
Mogensen M.M., Rzadzinska A., Steel K.P.;
"The deaf mouse mutant whirler suggests a role for whirlin in actin
filament dynamics and stereocilia development.";
Cell Motil. Cytoskeleton 64:496-508(2007).
[14]
INTERACTION WITH MPP1, AND SUBCELLULAR LOCATION.
PubMed=17584769; DOI=10.1093/hmg/ddm147;
Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
"MPP1 links the Usher protein network and the Crumbs protein complex
in the retina.";
Hum. Mol. Genet. 16:1993-2003(2007).
[15]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
PubMed=17567809; DOI=10.1523/JNEUROSCI.0342-07.2007;
Michalski N., Michel V., Bahloul A., Lefevre G., Barral J., Yagi H.,
Chardenoux S., Weil D., Martin P., Hardelin J.P., Sato M., Petit C.;
"Molecular characterization of the ankle-link complex in cochlear hair
cells and its role in the hair bundle functioning.";
J. Neurosci. 27:6478-6488(2007).
[16]
FUNCTION, DISRUPTION PHENOTYPE (ISOFORM 1), SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND IDENTIFICATION IN THE USH2 COMPLEX.
PubMed=20502675; DOI=10.1371/journal.pgen.1000955;
Yang J., Liu X., Zhao Y., Adamian M., Pawlyk B., Sun X.,
McMillan D.R., Liberman M.C., Li T.;
"Ablation of whirlin long isoform disrupts the USH2 protein complex
and causes vision and hearing loss.";
PLoS Genet. 6:E1000955-E1000955(2010).
[17]
INTERACTION WITH EPS8.
PubMed=21236676; DOI=10.1016/j.cub.2010.12.046;
Manor U., Disanza A., Grati M., Andrade L., Lin H., Di Fiore P.P.,
Scita G., Kachar B.;
"Regulation of stereocilia length by myosin XVa and whirlin depends on
the actin-regulatory protein Eps8.";
Curr. Biol. 21:167-172(2011).
[18]
INTERACTION WITH USH2 AND ADGRV1.
PubMed=23055499; DOI=10.1523/JNEUROSCI.3071-12.2012;
Grati M., Shin J.B., Weston M.D., Green J., Bhat M.A., Gillespie P.G.,
Kachar B.;
"Localization of PDZD7 to the stereocilia ankle-link associates this
scaffolding protein with the Usher syndrome protein network.";
J. Neurosci. 32:14288-14293(2012).
[19]
SUBCELLULAR LOCATION.
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=24334608; DOI=10.1093/hmg/ddt629;
Zou J., Zheng T., Ren C., Askew C., Liu X.P., Pan B., Holt J.R.,
Wang Y., Yang J.;
"Deletion of PDZD7 disrupts the Usher syndrome type 2 protein complex
in cochlear hair cells and causes hearing loss in mice.";
Hum. Mol. Genet. 23:2374-2390(2014).
[20]
IDENTIFICATION IN THE USH2 COMPLEX, AND SUBUNIT.
PubMed=25406310; DOI=10.1074/jbc.M114.610535;
Chen Q., Zou J., Shen Z., Zhang W., Yang J.;
"Whirlin and PDZ domain-containing 7 (PDZD7) proteins are both
required to form the quaternary protein complex associated with Usher
syndrome type 2.";
J. Biol. Chem. 289:36070-36088(2014).
-!- FUNCTION: Involved in hearing and vision as member of the USH2
complex (PubMed:20502675). Necessary for elongation and
maintenance of inner and outer hair cell stereocilia in the organ
of Corti in the inner ear (PubMed:15590699). Involved in the
maintenance of the hair bundle ankle region, which connects
stereocilia in cochlear hair cells of the inner ear
(PubMed:20502675, PubMed:24334608). In retina photoreceptors,
required for the maintenance of periciliary membrane complex that
seems to play a role in regulating intracellular protein transport
(PubMed:20502675). {ECO:0000269|PubMed:15590699,
ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}.
-!- SUBUNIT: Forms homooligomers (PubMed:15590698, PubMed:25406310).
Interacts (via C-terminal PDZ domain) with MYO15A; this
interaction is necessary for localization of WHRN to stereocilia
tips (PubMed:15654330, PubMed:15590698). Interacts (via C-terminal
PDZ domain) with MPP1/p55 (PubMed:16829577, PubMed:17584769).
Interacts with LRRC4C/NGL1 (PubMed:15590698). Interacts with MYO7A
(PubMed:15590698). Interacts with RPGR (PubMed:22323458).
Interacts with EPS8 (PubMed:21236676). Interacts with CASK.
Interacts with CIB2 (By similarity). Component of USH2 complex,
composed of ADGRV1, PDZD7, USH2A and WHRN (PubMed:20502675,
PubMed:25406310). Interacts (via PDZ domains) with PDZD7; the
interaction is direct (PubMed:25406310). Interacts (via N-terminal
PDZ domain) with USH2A (via cytoplasmic region) (PubMed:16301217,
PubMed:20502675, PubMed:23055499). Interacts with ADGRV1/MASS1
(via cytoplasmic region) (PubMed:20502675, PubMed:23055499).
{ECO:0000250|UniProtKB:Q810W9, ECO:0000250|UniProtKB:Q9P202,
ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15654330,
ECO:0000269|PubMed:16301217, ECO:0000269|PubMed:16829577,
ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:20502675,
ECO:0000269|PubMed:21236676, ECO:0000269|PubMed:22323458,
ECO:0000269|PubMed:23055499, ECO:0000269|PubMed:25406310}.
-!- INTERACTION:
Q8C031:Lrrc4c; NbExp=4; IntAct=EBI-7417603, EBI-7417983;
P70290:Mpp1; NbExp=4; IntAct=EBI-7417603, EBI-8315951;
Q9QZZ4:Myo15a; NbExp=5; IntAct=EBI-7417603, EBI-4281382;
Q9R0X5-5:Rpgr; NbExp=2; IntAct=EBI-6915655, EBI-6915646;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, stereocilium
{ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15590699,
ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:17567809,
ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}. Cell
projection, growth cone {ECO:0000269|PubMed:17584769}.
Photoreceptor inner segment {ECO:0000269|PubMed:20502675,
ECO:0000269|PubMed:24334608}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q810W9}. Note=Detected at the level of
stereocilia in inner and outer hair cells of the cochlea and
vestibule. Localizes to both tip and ankle-link stereocilia
regions. Colocalizes with the growing ends of actin filaments
(PubMed:15590699, PubMed:15590698, PubMed:15654330,
PubMed:24334608). Colocalizes with MPP1 in the retina, at the
outer limiting membrane (OLM), outer plexifirm layer (OPL), basal
bodies and at the connecting cilium (CC) (PubMed:17584769). In
photoreceptors, localizes at a plasma membrane microdomain in the
apical inner segment that surrounds the connecting cilia called
periciliary membrane complex (PubMed:20502675, PubMed:24334608).
{ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15590699,
ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:17584769,
ECO:0000269|PubMed:20502675, ECO:0000269|PubMed:24334608}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=1;
IsoId=Q80VW5-1; Sequence=Displayed;
Name=2;
IsoId=Q80VW5-2; Sequence=VSP_029939, VSP_029941;
Name=3;
IsoId=Q80VW5-3; Sequence=VSP_029941;
Note=Major isoform.;
Name=4;
IsoId=Q80VW5-4; Sequence=VSP_029941, VSP_029943;
Name=5;
IsoId=Q80VW5-5; Sequence=VSP_029937, VSP_029938, VSP_029941;
Name=6;
IsoId=Q80VW5-6; Sequence=VSP_029936;
Name=7;
IsoId=Q80VW5-7; Sequence=VSP_029936, VSP_029941;
Name=8;
IsoId=Q80VW5-8; Sequence=VSP_029935, VSP_029941;
Name=9;
IsoId=Q80VW5-9; Sequence=VSP_029934;
Name=10;
IsoId=Q80VW5-10; Sequence=VSP_029940, VSP_029942;
Note=No experimental confirmation available.;
Name=11; Synonyms=WhirlinNT2;
IsoId=Q80VW5-11; Sequence=VSP_045294, VSP_045295;
Note=May be due to intron retention.;
Name=12; Synonyms=WhirlinNT1;
IsoId=Q80VW5-12; Sequence=VSP_045293;
Note=May be due to intron retention.;
-!- TISSUE SPECIFICITY: Expressed in the retina. Colocalizes with RPGR
in the photoreceptor connecting cilium, a thin bridge linking the
cell body and the light-sensing outer segment (at protein level).
Detected in the inner ear throughout development from embryonic
day 12 to 20 days after birth. Displays a dynamic pattern of
expression after birth, demonstrating an ordered appearance and
fade-out across stereocilia rows. Isoforms 5, 6, 7 and 8 are not
detected in the retina (PubMed:20502675).
{ECO:0000269|PubMed:12833159, ECO:0000269|PubMed:15590699,
ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:20502675,
ECO:0000269|PubMed:22323458}.
-!- DEVELOPMENTAL STAGE: At E10.5, expressed in the basal plate of the
spinal cord, in the ventralneural epithelium of the developing
brain and in the region of the lung bud. At E12.5, expressed in
the complete neuroepithelium except for the neocortex. In the
developing eye, expressed in the inner neuroblastic layer. At
E14.5, detected in the intervertebral cartilage, the cortex of the
developing kidney, the tongue, the region of the urethra and
strongly in specific regions of the brain, e.g. striatum, optic
recess, ventral tegmental area, roof of the midbrain, choroid
plexus of the lateral ventricles and the fourth ventricle. The
developing neocortex is devoid of expression. At this timepoint,
expression is first notable in the inner ear in the developing
maculae of the saccule and the utricle, in the cristae of the
semicircular canals and in the vestibulocochlear ganglion. In the
developing neural retina, a strong signal is present in the inner
neuroblastic layer. At E16.5, expression is very similar to that
at E14.5. At E18.5, expression is mainly as in E16.5. Expression
in the ganglion layers of the retina decreases and is no longer
detected in the innermost region of these layers. From postnatal
day 7 (P7) onwards, also the developing photoreceptor cells
express whirlin (PubMed:16434480). Expression decreases by 11 days
after birth in inner ear hair cells and by 14 days after birth in
outer ear hair cells. Expressed in vestibular hair cells at high
levels through to adulthood. {ECO:0000269|PubMed:15590699,
ECO:0000269|PubMed:16434480}.
-!- DISEASE: Note=Defects in Whrn are the cause of the phenotype
whirler (wi). Mutants are characterized by deafness due to
malformation of the cochlear inner and outer hair cells and by
circling behavior. Stereocilia are shorter and wider than in wild-
type animals and there is a decrease in the number of actin
filaments in inner and outer hair cells. The number of outer hair
cell stereocilia is reduced with increased spacing between them.
{ECO:0000269|PubMed:12124769, ECO:0000269|PubMed:12833159,
ECO:0000269|PubMed:17326148}.
-!- DISRUPTION PHENOTYPE: Mutant mice for isoform 1 appear viable and
comparable to their wild-type littermates in growth
characteristics, reproductive performance and general health
(PubMed:20502675). At 2 and 9 month of age, knockouts show a
profound hearing loss across all cochlear frequencies
(PubMed:20502675). At 28 to 33 months, they show signs for retinal
degenration such as a thinner phtoreceptor nuclear layer and outer
segments sortened (PubMed:20502675).
{ECO:0000269|PubMed:20502675}.
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EMBL; AY739114; AAV87519.1; -; mRNA.
EMBL; AY739115; AAV87520.1; -; mRNA.
EMBL; AY739116; AAV87521.1; -; mRNA.
EMBL; AY739117; AAV87522.1; -; mRNA.
EMBL; AY739118; AAV87523.1; -; mRNA.
EMBL; AY739119; AAV87524.1; -; mRNA.
EMBL; AY739120; AAV87525.1; -; mRNA.
EMBL; AY739121; AAV87526.1; -; mRNA.
EMBL; AY739122; AAV87527.1; -; mRNA.
EMBL; HQ148552; AEL23234.1; -; mRNA.
EMBL; HQ148553; AEL23235.1; -; mRNA.
EMBL; AK157955; BAE34281.1; -; mRNA.
EMBL; AL683828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK122523; BAC65805.1; -; mRNA.
CCDS; CCDS18255.1; -. [Q80VW5-1]
CCDS; CCDS18256.1; -. [Q80VW5-4]
CCDS; CCDS18257.1; -. [Q80VW5-3]
CCDS; CCDS38778.1; -. [Q80VW5-2]
RefSeq; NP_001008791.1; NM_001008791.2. [Q80VW5-1]
RefSeq; NP_001008792.1; NM_001008792.2. [Q80VW5-2]
RefSeq; NP_001008793.1; NM_001008793.2. [Q80VW5-4]
RefSeq; NP_001263300.1; NM_001276371.1. [Q80VW5-12]
RefSeq; NP_082916.1; NM_028640.2. [Q80VW5-3]
RefSeq; XP_017175899.1; XM_017320410.1. [Q80VW5-5]
UniGene; Mm.300397; -.
PDB; 6FDD; X-ray; 1.75 A; A/B/C/D/E/F=420-499.
PDB; 6FDE; X-ray; 1.85 A; A=420-499.
PDBsum; 6FDD; -.
PDBsum; 6FDE; -.
ProteinModelPortal; Q80VW5; -.
SMR; Q80VW5; -.
CORUM; Q80VW5; -.
DIP; DIP-42047N; -.
IntAct; Q80VW5; 5.
MINT; Q80VW5; -.
STRING; 10090.ENSMUSP00000081557; -.
iPTMnet; Q80VW5; -.
PhosphoSitePlus; Q80VW5; -.
PaxDb; Q80VW5; -.
PRIDE; Q80VW5; -.
Ensembl; ENSMUST00000063650; ENSMUSP00000069664; ENSMUSG00000039137. [Q80VW5-3]
Ensembl; ENSMUST00000063672; ENSMUSP00000065838; ENSMUSG00000039137. [Q80VW5-10]
Ensembl; ENSMUST00000084510; ENSMUSP00000081557; ENSMUSG00000039137. [Q80VW5-1]
Ensembl; ENSMUST00000095037; ENSMUSP00000092647; ENSMUSG00000039137. [Q80VW5-8]
Ensembl; ENSMUST00000095038; ENSMUSP00000092648; ENSMUSG00000039137. [Q80VW5-6]
Ensembl; ENSMUST00000102867; ENSMUSP00000099931; ENSMUSG00000039137. [Q80VW5-4]
Ensembl; ENSMUST00000107393; ENSMUSP00000103016; ENSMUSG00000039137. [Q80VW5-2]
Ensembl; ENSMUST00000119294; ENSMUSP00000114030; ENSMUSG00000039137. [Q80VW5-7]
GeneID; 73750; -.
KEGG; mmu:73750; -.
UCSC; uc008tgf.1; mouse. [Q80VW5-9]
UCSC; uc008tgg.1; mouse. [Q80VW5-5]
UCSC; uc008tgh.2; mouse. [Q80VW5-1]
UCSC; uc008tgi.2; mouse. [Q80VW5-4]
UCSC; uc008tgj.2; mouse. [Q80VW5-2]
UCSC; uc008tgk.2; mouse. [Q80VW5-3]
UCSC; uc008tgm.1; mouse. [Q80VW5-8]
UCSC; uc008tgn.1; mouse. [Q80VW5-7]
UCSC; uc008tgp.2; mouse. [Q80VW5-10]
UCSC; uc033icr.1; mouse. [Q80VW5-12]
CTD; 25861; -.
MGI; MGI:2682003; Whrn.
eggNOG; ENOG410ITAG; Eukaryota.
eggNOG; ENOG410XTF7; LUCA.
GeneTree; ENSGT00940000153656; -.
HOVERGEN; HBG056634; -.
InParanoid; Q80VW5; -.
KO; K21879; -.
OMA; GINKPGF; -.
OrthoDB; 168224at2759; -.
PhylomeDB; Q80VW5; -.
TreeFam; TF325033; -.
ChiTaRS; Whrn; mouse.
PRO; PR:Q80VW5; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000039137; Expressed in 125 organ(s), highest expression level in brain.
CleanEx; MM_WHRN; -.
ExpressionAtlas; Q80VW5; baseline and differential.
Genevisible; Q80VW5; MM.
GO; GO:0005884; C:actin filament; IDA:MGI.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0036064; C:ciliary basal body; IDA:MGI.
GO; GO:0005929; C:cilium; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0043198; C:dendritic shaft; ISO:MGI.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:1990075; C:periciliary membrane compartment; IDA:UniProtKB.
GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0002141; C:stereocilia ankle link; IDA:UniProtKB.
GO; GO:0002142; C:stereocilia ankle link complex; IDA:MGI.
GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
GO; GO:0032421; C:stereocilium bundle; IDA:MGI.
GO; GO:0032426; C:stereocilium tip; IDA:MGI.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:1990696; C:USH2 complex; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
GO; GO:0021694; P:cerebellar Purkinje cell layer formation; IMP:CACAO.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IDA:UniProtKB.
GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:UniProtKB.
GO; GO:1990227; P:paranodal junction maintenance; IMP:CACAO.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0001895; P:retina homeostasis; IDA:UniProtKB.
GO; GO:0050953; P:sensory perception of light stimulus; ISO:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR033028; Whirlin.
PANTHER; PTHR23116:SF37; PTHR23116:SF37; 1.
Pfam; PF00595; PDZ; 3.
SMART; SM00228; PDZ; 3.
SUPFAM; SSF50156; SSF50156; 3.
PROSITE; PS50106; PDZ; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Deafness; Hearing; Phosphoprotein;
Reference proteome; Repeat; Synapse.
CHAIN 1 918 Whirlin.
/FTId=PRO_0000065969.
DOMAIN 141 224 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 280 362 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 827 910 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
COMPBIAS 9 32 Ala/Gly/Ser-rich.
COMPBIAS 584 723 Pro-rich.
MOD_RES 696 696 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P202}.
VAR_SEQ 1 552 Missing (in isoform 9).
{ECO:0000303|PubMed:15654330}.
/FTId=VSP_029934.
VAR_SEQ 1 503 Missing (in isoform 8).
{ECO:0000303|PubMed:15654330}.
/FTId=VSP_029935.
VAR_SEQ 1 442 Missing (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:15654330}.
/FTId=VSP_029936.
VAR_SEQ 1 357 Missing (in isoform 5).
{ECO:0000303|PubMed:15654330}.
/FTId=VSP_029937.
VAR_SEQ 323 918 Missing (in isoform 12).
{ECO:0000303|PubMed:22323458}.
/FTId=VSP_045293.
VAR_SEQ 358 402 KDVGRLPHARTTVDQTKWIASSRIGESVANSAGFPGDHTEE
GTSK -> MTTWCHRPRVRWSGSCVCGDHQHNARSHSLPRS
LDSSGLCPSVFQ (in isoform 5).
{ECO:0000303|PubMed:15654330}.
/FTId=VSP_029938.
VAR_SEQ 390 390 G -> GSGLR (in isoform 2).
{ECO:0000303|PubMed:15654330}.
/FTId=VSP_029939.
VAR_SEQ 544 571 ERLLWLIDLMENTLDLEGTGETTQGSTN -> VSHPCPILG
EKVRARIRCFPPKPRVPHL (in isoform 10).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_029940.
VAR_SEQ 544 554 Missing (in isoform 2, isoform 3, isoform
4, isoform 5, isoform 7 and isoform 8).
{ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:15654330}.
/FTId=VSP_029941.
VAR_SEQ 555 566 NTLDLEGTGETT -> VPSFCRGRLGVP (in isoform
11). {ECO:0000303|PubMed:22323458}.
/FTId=VSP_045294.
VAR_SEQ 567 918 Missing (in isoform 11).
{ECO:0000303|PubMed:22323458}.
/FTId=VSP_045295.
VAR_SEQ 572 918 Missing (in isoform 10).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_029942.
VAR_SEQ 758 758 Missing (in isoform 4).
{ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:15654330}.
/FTId=VSP_029943.
CONFLICT 504 504 M -> V (in Ref. 3; BAE34281).
{ECO:0000305}.
HELIX 425 434 {ECO:0000244|PDB:6FDD}.
HELIX 437 451 {ECO:0000244|PDB:6FDD}.
HELIX 457 467 {ECO:0000244|PDB:6FDD}.
HELIX 471 474 {ECO:0000244|PDB:6FDD}.
HELIX 476 481 {ECO:0000244|PDB:6FDD}.
HELIX 486 488 {ECO:0000244|PDB:6FDD}.
HELIX 489 495 {ECO:0000244|PDB:6FDD}.
SEQUENCE 918 AA; 98012 MW; 7D5EA44DE0645AA4 CRC64;
MNAQLDGLSV SSSSTGSLGS AAAAAGGGGG AGLRLLSANV RQLHQALTAL LSEPEREQFT
HCLNAYHARR NVFDLVRTLR VLLDSPVKRR LLPMLRLVIP RSDQLLFDQY TAEGLYLPAT
TPYRQPAWAA PDGAGPGEVR LVSLRRAKAH EGLGFSIRGG SEHGVGIYVS LVEPGSLAEK
EGLRVGDQIL RVNDKSLARV THAEAVKALK GSKKLVLSVY SAGRIPGGYV TNHIYTWVDP
QGRSTSPPSS LPQPHGSTLR QREDDRRSTL HLLQSGDEKK VNLVLGDGRS LGLTIRGGAE
YGLGIYITGV DPGSEAESSG LKVGDQILEV NGRSFLNILH DEAVKLLKSS RHLILTVKDV
GRLPHARTTV DQTKWIASSR IGESVANSAG FPGDHTEEGT SKPGFYKGPA GSQVTLSSLG
NQTRALLDDQ ARHLLTEQER ATMMYYLAQY RGGTISVEAM VMALFELLNT HAKFSLLSEV
RSIISPQDLD RFDHLVLRRE IESMKARQPP GPGVGDTYSM VSYSDTGSST GSHGTSTTVS
SARERLLWLI DLMENTLDLE GTGETTQGST NALPDVSVDD VKSPSEDLPG IKPPPPPPPL
AQGHDRLLGQ PRKPGREDPA PLSSAAHSGI VFSAPRNRSP PPGTAPTPGP SSAQDSPSSP
IYASISHANP SSRKPLDTHL ALVNQHPIGP FPRVQSPPHL KSPPAETPGA GACLPPPSPS
EHPDAVGANQ HFVLVEVHRP DSEPDVNEVR ALPQTRTAST LSQLSDSGQT LSEDSGVDAG
ETEASTSGRG RQTASAKNKN GKEQPRTERT AEGANKPPGL LEPTSTLVRV RKSAATLGIA
IEGGANTRQP LPRIVTIQRG GSAHNCGQLK VGHVILEVNG QTLRGKEHKE AARIIAEAFK
TKERDYIDFL VTEFNVML


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