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   03-AUG-2022, entry version 110.
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   PRIDE; Q2KIK0; -.
DR   Ensembl; ENSBTAT00000002771; ENSBTAP00000002771; ENSBTAG00000002137.
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; WDKLVGD; -.
DR   OrthoDB; 1426397at2759; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000002137; Expressed in oocyte and 105 other 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:chaperone binding; IEA:InterPro.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.60.40.790; -; 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; PTHR45862; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF05002; SGS; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF49764; SSF49764; 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