ID SGT1_BOVIN Reviewed; 338 AA.
AC Q2KIK0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 117.
DE RecName: Full=Protein SGT1 homolog {ECO:0000250|UniProtKB:Q08446};
DE AltName: Full=Suppressor of G2 allele of SKP1 homolog {ECO:0000250|UniProtKB:Q08446};
GN Name=SUGT1 {ECO:0000250|UniProtKB:Q9Y2Z0};
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=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in ubiquitination and subsequent proteasomal
CC degradation of target proteins.
CC -!- SUBUNIT: Probably associates with SCF (SKP1-CUL1-F-box protein) complex
CC through interaction with SKP1. Interacts with S100A6. Interacts with
CC HSP90 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocates to the nucleus upon heat shock, requiring S100A6.
CC {ECO:0000250}.
CC -!- DOMAIN: The CS domain mediates interaction with HSP90. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-254 and Ser-304, dephosphorylation promotes
CC nuclear translocation, most likely due to disruption of the SUGT1-HSP90
CC complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SGT1 family. {ECO:0000305}.
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DR EMBL; BC112610; AAI12611.1; -; mRNA.
DR RefSeq; NP_001039668.1; NM_001046203.2.
DR AlphaFoldDB; Q2KIK0; -.
DR SMR; Q2KIK0; -.
DR STRING; 9913.ENSBTAP00000002770; -.
DR Ensembl; ENSBTAT00000002771.6; ENSBTAP00000002771.6; ENSBTAG00000002137.6.
DR GeneID; 515509; -.
DR KEGG; bta:515509; -.
DR CTD; 10910; -.
DR VEuPathDB; HostDB:ENSBTAG00000002137; -.
DR VGNC; VGNC:35465; SUGT1.
DR GeneTree; ENSGT00390000013700; -.
DR HOGENOM; CLU_039532_1_1_1; -.
DR InParanoid; Q2KIK0; -.
DR OMA; QRAYCYI; -.
DR OrthoDB; 5479399at2759; -.
DR Reactome; R-BTA-844456; The NLRP3 inflammasome.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000002137; Expressed in oocyte and 105 other cell types or tissues.
DR ExpressionAtlas; Q2KIK0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB.
DR CDD; cd06489; p23_CS_hSgt1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR044563; Sgt1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45862; PROTEIN SGT1 HOMOLOG; 1.
DR PANTHER; PTHR45862:SF1; PROTEIN SGT1 HOMOLOG; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT CHAIN 2..338
FT /note="Protein SGT1 homolog"
FT /evidence="ECO:0000250"
FT /id="PRO_0000330901"
FT REPEAT 11..45
FT /note="TPR 1"
FT REPEAT 46..79
FT /note="TPR 2"
FT REPEAT 80..113
FT /note="TPR 3"
FT DOMAIN 142..231
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 249..338
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z0"
SQ SEQUENCE 338 AA; 38074 MW; 4B9AE6540DC1852C CRC64;
MAAAAAGPVA AASRLFRSFS DALIEQDPQA ALEELTKALE QKPDDAPYYC QRAYCHILLG
NYSDAVADAK KSLELNPNSS TALLRKGICE YHEKNYAAAL ETFTEGQKLN SADADLTAWI
KRCQEAQNGS QPEVSASQRT HQSKIKYDWY QTESQVIITL MIKNVQKNDV NVEFSEKELS
ALVKLPSGDD YSLKLRLLHP IIPEQSTFKV LSTKIEIKMK KPEAVRWEKL EGQGDVPNPK
PFIADVKNLY PSSSHYTRNW DKLVGEIKEE EKNEKLEGDA ALNKLFQQIY SDGSDEVKRA
MNKSFMESGG TVLSTNWSDV GKRKVEINPP DDMEWKKY
//
