ID F1RVV1_PIG Unreviewed; 461 AA.
AC F1RVV1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=USH1 protein network component sans {ECO:0000313|Ensembl:ENSSSCP00000018247.2};
GN Name=USH1G {ECO:0000313|Ensembl:ENSSSCP00000018247.2,
GN ECO:0000313|VGNC:VGNC:94739};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000018247.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000018247.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000018247.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000018247.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a central role during spermatogenesis by repressing
CC transposable elements and preventing their mobilization, which is
CC essential for the germline integrity. Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC governs the methylation and subsequent repression of transposons. Its
CC association with pi-bodies suggests a participation in the primary
CC piRNAs metabolic process. Required prior to the pachytene stage to
CC facilitate the production of multiple types of piRNAs, including those
CC associated with repeats involved in the regulation of retrotransposons.
CC May act by mediating protein-protein interactions during germ cell
CC maturation. {ECO:0000256|ARBA:ARBA00025297}.
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DR RefSeq; XP_003131267.1; XM_003131219.4.
DR RefSeq; XP_013836222.1; XM_013980768.1.
DR AlphaFoldDB; F1RVV1; -.
DR SMR; F1RVV1; -.
DR STRING; 9823.ENSSSCP00000018247; -.
DR PaxDb; 9823-ENSSSCP00000018247; -.
DR Ensembl; ENSSSCT00000018749.5; ENSSSCP00000018247.2; ENSSSCG00000017223.5.
DR GeneID; 100512251; -.
DR KEGG; ssc:100512251; -.
DR CTD; 124590; -.
DR VGNC; VGNC:94739; USH1G.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00390000017548; -.
DR HOGENOM; CLU_028071_0_0_1; -.
DR InParanoid; F1RVV1; -.
DR OMA; VMYVGTF; -.
DR OrthoDB; 5395431at2759; -.
DR TreeFam; TF324946; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Bgee; ENSSSCG00000017223; Expressed in hindlimb bud and 4 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0015030; C:Cajal body; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0097546; C:ciliary base; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
DR GO; GO:0050957; P:equilibrioception; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0050953; P:sensory perception of light stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR CDD; cd21803; CEN_USH1G; 1.
DR CDD; cd09586; SAM_USH1G; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037602; USH1G_SAM.
DR PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24161:SF24; USHER SYNDROME TYPE-1G PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 31..63
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 64..96
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 385..449
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT REGION 206..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 51591 MW; C4851D7C4FAFA600 CRC64;
MNDQYHRAAR DGYLELLKEA TRKELNAPDE DGMTPTLWAA YHGNLESLRL IVSRGGDPDK
CDIWGNTPLH LAASNGHLHC LSFLVSFGAN IWCLDNDYHT PLDMGAMKGH MECVRYLDSI
AAKQSSLNPK LVGKLKDKAF REAERRIREC AKMQRKHHER MERRYRRELA ERSDTLSFSS
LTSSTLSRRL QHLALGSHVP YSQATLHGTA KGKTKIQRKL ERRKQGGEGT FKISEDGRKS
VRSLSGLQLG SDVMFVRQGT YANPKEWGRA PLRDMFLSDE DSVSRATLAA EPAHSEVSTD
SGHDSLFTRP GLGTMVFRRN YLSSGLHGLG REDAALDGGG TPRARLQSSP SLDDDSLGSA
NSLQDRSCGE ELPWDELDLG LDEDLEPETS PLETFLASLH MEDFTPLLRQ EKIDLEALML
CSDLDLRSIS VPLGPRKKIM GAVRRRRQTL ERPPALEDTE L
//
