WHRN_RAT
ID WHRN_RAT Reviewed; 920 AA.
AC Q810W9;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Whirlin;
DE AltName: Full=CASK-interacting protein CIP98;
GN Name=Whrn {ECO:0000312|RGD:631330};
GN Synonyms=Cip98 {ECO:0000303|PubMed:12641734}, Dfnb31;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CASK, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain, and Cerebellum;
RX PubMed=12641734; DOI=10.1046/j.1471-4159.2003.01647.x;
RA Yap C.C., Liang F., Yamazaki Y., Muto Y., Kishida H., Hayashida T.,
RA Hashikawa T., Yano R.;
RT "CIP98, a novel PDZ domain protein, is expressed in the central nervous
RT system and interacts with calmodulin-dependent serine kinase.";
RL J. Neurochem. 85:123-134(2003).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=17584769; DOI=10.1093/hmg/ddm147;
RA Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
RA Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
RA Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
RT "MPP1 links the Usher protein network and the Crumbs protein complex in the
RT retina.";
RL Hum. Mol. Genet. 16:1993-2003(2007).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16434480; DOI=10.1093/hmg/ddi490;
RA van Wijk E., van der Zwaag B., Peters T., Zimmermann U., Te Brinke H.,
RA Kersten F.F.J., Maerker T., Aller E., Hoefsloot L.H., Cremers C.W.R.J.,
RA Cremers F.P.M., Wolfrum U., Knipper M., Roepman R., Kremer H.;
RT "The DFNB31 gene product whirlin connects to the Usher protein network in
RT the cochlea and retina by direct association with USH2A and VLGR1.";
RL Hum. Mol. Genet. 15:751-765(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23055499; DOI=10.1523/jneurosci.3071-12.2012;
RA Grati M., Shin J.B., Weston M.D., Green J., Bhat M.A., Gillespie P.G.,
RA Kachar B.;
RT "Localization of PDZD7 to the stereocilia ankle-link associates this
RT scaffolding protein with the Usher syndrome protein network.";
RL J. Neurosci. 32:14288-14293(2012).
CC -!- FUNCTION: Involved in hearing and vision as member of the USH2 complex.
CC Necessary for elongation and maintenance of inner and outer hair cell
CC stereocilia in the organ of Corti in the inner ear. Involved in the
CC maintenance of the hair bundle ankle region, which connects stereocilia
CC in cochlear hair cells of the inner ear. In retina photoreceptors,
CC required for the maintenance of periciliary membrane complex that seems
CC to play a role in regulating intracellular protein transport.
CC {ECO:0000250|UniProtKB:Q80VW5}.
CC -!- SUBUNIT: Forms homooligomers (By similarity). Interacts (via C-terminal
CC PDZ domain) with MYO15A; this interaction is necessary for localization
CC of WHRN to stereocilia tips. Interacts (via C-terminal PDZ domain) with
CC MPP1/p55. Interacts with LRRC4C/NGL1. Interacts with MYO7A. Interacts
CC with RPGR. Interacts with EPS8 (By similarity). Interacts with CASK
CC (PubMed:12641734). Interacts with CIB2 (By similarity). Component of
CC USH2 complex, composed of ADGRV1, PDZD7, USH2A and WHRN. Interacts (via
CC PDZ domains) with PDZD7; the interaction is direct. Interacts (via N-
CC terminal PDZ domain) with USH2A (via cytoplasmic region). Interacts
CC with ADGRV1/MASS1 (via cytoplasmic region) (By similarity).
CC {ECO:0000250|UniProtKB:Q80VW5, ECO:0000250|UniProtKB:Q9P202,
CC ECO:0000269|PubMed:12641734}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80VW5}. Cell
CC projection, stereocilium {ECO:0000269|PubMed:16434480,
CC ECO:0000269|PubMed:23055499}. Cell projection, growth cone
CC {ECO:0000269|PubMed:12641734}. Synapse {ECO:0000269|PubMed:12641734,
CC ECO:0000269|PubMed:16434480}. Note=Detected at the level of stereocilia
CC in inner outer hair cells of the cochlea and vestibule
CC (PubMed:16434480). Localizes to both tip and ankle-link stereocilia
CC regions (PubMed:23055499). Colocalizes with the growing ends of actin
CC filaments (By similarity). Colocalizes with MPP1 in the retina, at the
CC outer limiting membrane (OLM), outer plexifirm layer (OPL), basal
CC bodies and at the connecting cilium (CC) (PubMed:16434480,
CC PubMed:17584769). In photoreceptors, localizes at a plasma membrane
CC microdomain in the apical inner segment that surrounds the connecting
CC cilia called periciliary membrane complex (By similarity).
CC {ECO:0000250|UniProtKB:Q80VW5, ECO:0000269|PubMed:16434480,
CC ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:23055499}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, spleen, lung
CC and liver. Highly expressed in brain, in the olfactory bulb, thalamus,
CC layers III-V of the cerebral cortex and the molecular layer of
CC cerebellum. Detected in soma and dendrites of thalamic neurons, and in
CC cerebrum in cell bodies and apical dendrites of pyramidal neurons.
CC Expressed in retina and inner ear (PubMed:16434480, PubMed:23055499).
CC {ECO:0000269|PubMed:12641734, ECO:0000269|PubMed:16434480,
CC ECO:0000269|PubMed:23055499}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY227205; AAO72534.1; -; mRNA.
DR RefSeq; NP_851602.1; NM_181088.1.
DR AlphaFoldDB; Q810W9; -.
DR SMR; Q810W9; -.
DR IntAct; Q810W9; 1.
DR MINT; Q810W9; -.
DR STRING; 10116.ENSRNOP00000002309; -.
DR CarbonylDB; Q810W9; -.
DR iPTMnet; Q810W9; -.
DR PhosphoSitePlus; Q810W9; -.
DR PaxDb; Q810W9; -.
DR PRIDE; Q810W9; -.
DR GeneID; 313255; -.
DR KEGG; rno:313255; -.
DR UCSC; RGD:631330; rat.
DR CTD; 25861; -.
DR RGD; 631330; Whrn.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; Q810W9; -.
DR OrthoDB; 168224at2759; -.
DR PhylomeDB; Q810W9; -.
DR PRO; PR:Q810W9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR GO; GO:0044303; C:axon collateral; IDA:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:1990075; C:periciliary membrane compartment; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:RGD.
DR GO; GO:0002141; C:stereocilia ankle link; IDA:UniProtKB.
DR GO; GO:0002142; C:stereocilia ankle link complex; ISS:UniProtKB.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0032421; C:stereocilium bundle; ISO:RGD.
DR GO; GO:0032426; C:stereocilium tip; IDA:UniProtKB.
DR GO; GO:1990696; C:USH2 complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISO:RGD.
DR GO; GO:0021694; P:cerebellar Purkinje cell layer formation; ISO:RGD.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; ISS:UniProtKB.
DR GO; GO:1990227; P:paranodal junction maintenance; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR033028; Whirlin.
DR PANTHER; PTHR23116:SF37; PTHR23116:SF37; 1.
DR Pfam; PF00595; PDZ; 3.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; SSF50156; 3.
DR PROSITE; PS50106; PDZ; 3.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Hearing; Phosphoprotein; Reference proteome;
KW Repeat; Synapse.
FT CHAIN 1..920
FT /note="Whirlin"
FT /id="PRO_0000065970"
FT DOMAIN 141..224
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 278..360
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 829..912
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 241..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P202"
SQ SEQUENCE 920 AA; 98345 MW; 2F4978F7183689FD 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 LPHGSTLRQH EDDRRSALHL LQSGDEKKVN LVLGDGRSLG LTIRGGAEYG
LGIYITGVDP GSEAESSGLK VGDQILEVNG RSFLSILHDE AVKLLKSSRH LILTVKDVGR
LPHARTTVDQ TKWIASSRIG ESITNSAGFP GDLTEEGTNK PGFYKGPAGS QVTLSSLGNQ
TRALLDDQAR HLLTEQERAT MMYYLDQYRG GTISVEALVM ALFELLNTHA KFSLLSEVRG
IISPQDLDRF DHLVLRREIE SMKARQPPGP GVGDTYSMVS YSDTGSSTGS HGTSTTVSSA
RERLLWLIDL MENTLDLEGT CETTQGSTNA LPDVSVDDVR SPSEDLPGIK PPPPPPPLAQ
GHDRLLGQTR KPVREDSAPL SSAAHSGIVF SAPRNRSPPP PPGIAPTPTP GPSSARDSPS
SPIYASISHA NPSSRKPLDT HLALVNQHPI GPFPRVQSPP HLKSPPAEAP GAGACLPPPS
PSEHADAMGA NQHFVLVEVH RPDSEPDVNE VRALPQTRTA STLSQLSDSG QTLSEDSGVD
AGETEASTSG RGRQTANTKN KNGKELPQTE RTTEGANKPP GLLEPTSTLI RVRKSAATLG
IAIEGGANTR QPLPRIVTIQ RGGSAHNCGQ LKVGHVILEV NGQTLRGKEH REAARVIAEA
FKTKERDYID FLVTEFNVML
