USH1C_BOVIN
ID USH1C_BOVIN Reviewed; 551 AA.
AC Q3MHQ0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Harmonin;
DE AltName: Full=Usher syndrome type-1C protein homolog;
GN Name=USH1C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Anchoring/scaffolding protein that is a part of the
CC functional network formed by USH1C, USH1G, CDH23 and MYO7A that
CC mediates mechanotransduction in cochlear hair cells. Required for
CC normal development and maintenance of cochlear hair cell bundles (By
CC similarity). As part of the intermicrovillar adhesion complex/IMAC
CC plays a role in brush border differentiation, controlling microvilli
CC organization and length. Probably plays a central regulatory role in
CC the assembly of the complex, recruiting CDHR2, CDHR5 and MYO7B to the
CC microvilli tips (By similarity). {ECO:0000250|UniProtKB:Q9ES64,
CC ECO:0000250|UniProtKB:Q9Y6N9}.
CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B,
CC USH1C, CDHR2 and CDHR5 (By similarity). Part of a complex composed of
CC USH1C, USH1G and MYO7A (By similarity). Interacts with F-actin (By
CC similarity). Interacts with USH2A (By similarity). Interacts with
CC SLC4A7. Interacts (via PDZ1 domain) with the C-terminus of USHBP1 (By
CC similarity). Interacts (via N-terminus and PDZ 2 domain) with CDH23 (By
CC similarity). Interacts with USH1G (By similarity). Interacts with MYO7B
CC (By similarity). Interacts with CDHR2 and CDHR5; may mediate their
CC interaction with MYO7B at the microvilli tip (By similarity). Interacts
CC (via PDZ 1 domain) with ANKS4B (By similarity). Interacts (via PDZ 1
CC domain) with DOCK4 (By similarity). {ECO:0000250|UniProtKB:Q9ES64,
CC ECO:0000250|UniProtKB:Q9Y6N9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Y6N9}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9Y6N9}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:Q9Y6N9}. Note=Colocalizes with F-actin. Detected
CC at the tip of cochlear hair cell stereocilia (By similarity). Enriched
CC in microvilli of the intestinal brush border (By similarity).
CC {ECO:0000250|UniProtKB:Q9ES64, ECO:0000250|UniProtKB:Q9Y6N9}.
CC -!- DOMAIN: The PDZ 1 domain mediates interaction with ANKS4B, USHBP1,
CC USH1G, SLC4A7. {ECO:0000250|UniProtKB:Q9Y6N9}.
CC -!- DOMAIN: The N-terminal region constitutes an independently folded
CC domain that has structural similarity with the CCM2 C-terminus, despite
CC very low sequence similarity. {ECO:0000250|UniProtKB:Q9Y6N9}.
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DR EMBL; BC105153; AAI05154.1; -; mRNA.
DR RefSeq; NP_001030459.1; NM_001035382.2.
DR AlphaFoldDB; Q3MHQ0; -.
DR BMRB; Q3MHQ0; -.
DR SMR; Q3MHQ0; -.
DR PaxDb; Q3MHQ0; -.
DR PRIDE; Q3MHQ0; -.
DR GeneID; 530709; -.
DR KEGG; bta:530709; -.
DR CTD; 10083; -.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; Q3MHQ0; -.
DR OrthoDB; 1252899at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:1904970; P:brush border assembly; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1904106; P:protein localization to microvillus; ISS:UniProtKB.
DR GO; GO:0032532; P:regulation of microvillus length; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR030237; Harmonin.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR23116:SF36; PTHR23116:SF36; 2.
DR Pfam; PF00595; PDZ; 3.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; SSF50156; 3.
DR PROSITE; PS50106; PDZ; 3.
PE 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW Hearing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..551
FT /note="Harmonin"
FT /id="PRO_0000287208"
FT DOMAIN 87..169
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 211..293
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 452..536
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..86
FT /note="N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N9"
FT REGION 194..532
FT /note="Mediates interaction with MYO7B"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N9"
FT REGION 401..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 318..377
FT /evidence="ECO:0000255"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES64"
SQ SEQUENCE 551 AA; 62065 MW; 2AE7FE5CD28C6564 CRC64;
MDRKVAREFR HKVDFLIEND AEKDYLYDVL RMYHQTMDVA VLVGDLKLVI NEPSRLPLFD
AIRPLIPLKH QVEYDQLTPR RSRKLKEVRL DRLHPEGLGL SVRGGLEFGC GLFISHLIKD
GQADSVGLQV GDEIVRINGY SISSCTHEEV INLIRTKKTV SIKVRHIGLI PVKSSPDEPL
KWQYVDQFVS ESGGGRSSLG SPGSQENKEK KVFISLVGSR GLGCSISSGP IQKPGIFISH
VKPGSLSAEV GLETGDQIVE VNGIDFSNLD HKEAVNVLKS SRSLTISIVA GAGRELFMTD
QERLAEVRQR ELQRQELLMQ KRLAMESNKI LQEQQEMERQ RKKEIAQKAA EENERYRKEM
EQIVEEEEKF RKQWEEDWGS KEQLRSPKTI TAEVHPIPLR KPKYDLGVDP EFDPADDLDG
GTNKRGEQDF RKYEEGFDPY SMFTPEQIMG KDVRLLRVKK EGALDLALEG GVDSPIGKVV
VSAVYEGGAA ERHGGIVKGD EIMAINGKIV TDYTLAEAEA ALQKAWNQGD WIDLVVAVCP
PKEYDDELTF F
