F120A_BOVIN
ID F120A_BOVIN Reviewed; 1114 AA.
AC A6H7H1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Constitutive coactivator of PPAR-gamma-like protein 1;
DE AltName: Full=Oxidative stress-associated Src activator;
DE AltName: Full=Protein FAM120A;
GN Name=FAM120A; Synonyms=OSSA;
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=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Critical component of the oxidative stress-induced survival
CC signaling. Activates src family kinases and acts as a scaffolding
CC protein enabling src family kinases to phosphorylate and activate PI3-
CC kinase. Binds RNA and promotes the secretion of IGF-II. May participate
CC in mRNA transport in the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PURA (By similarity). Interacts with YES1, SRC,
CC FYN. Upon tyrosine phosphorylation, interacts with PIK3R1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Translocates to plasma membrane upon
CC ultraviolet exposure. {ECO:0000250}.
CC -!- PTM: Arg-978 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine by src family kinases upon ultraviolet
CC exposure. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the constitutive coactivator of PPAR-gamma
CC family. {ECO:0000305}.
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DR EMBL; BC146243; AAI46244.1; -; mRNA.
DR RefSeq; NP_001092375.1; NM_001098905.1.
DR AlphaFoldDB; A6H7H1; -.
DR STRING; 9913.ENSBTAP00000030923; -.
DR PaxDb; A6H7H1; -.
DR PeptideAtlas; A6H7H1; -.
DR PRIDE; A6H7H1; -.
DR GeneID; 507997; -.
DR KEGG; bta:507997; -.
DR CTD; 23196; -.
DR eggNOG; ENOG502QQNQ; Eukaryota.
DR InParanoid; A6H7H1; -.
DR OrthoDB; 203269at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR026784; Coact_PPARg.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR PANTHER; PTHR15976; PTHR15976; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasm; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..1114
FT /note="Constitutive coactivator of PPAR-gamma-like protein
FT 1"
FT /id="PRO_0000363779"
FT REGION 339..402
FT /note="Interaction with YES1, SRC and FYN"
FT /evidence="ECO:0000250"
FT REGION 372..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..1114
FT /note="RNA binding"
FT /evidence="ECO:0000250"
FT REGION 918..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 651
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 869
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 880
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 882
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 928
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0A9"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 978
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6A0A9"
FT MOD_RES 982
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
SQ SEQUENCE 1114 AA; 121551 MW; 5C173CD84003D138 CRC64;
MGVQGFQDYI EKHCPSAVVP VELQKLARGS LVGGGRQRPP HTPLRLLVDA DNCLHRLYGG
FYTDWVSGGQ WNHMLGYLAA LAKACFGGNI ELFVFFNGAL EKARLHEWVK RQGNERQTAQ
QIVSHVQNKG TPPPKVWFLP PVCMAHCIRL ALIRFHVKVA QSIEDHHQEV IGFCRENGFH
GLVAYDSDYA LCNIPYYFSA HALKLSRNGK SLTTSQYLMH EVAKQLDLNP NRFPIFAALL
GNHILPDEDL ASFHWSLLGP EHPLASLKVR AHQLVLPPCD VVIKAVADYV RNIQDTSDLD
AIAKDVFQHS QSRTDDKVIR FKRAIGYYSA TSKPMAFHPP HYLARPNPFG MPGIVPPYVP
PQMLNIPQTS LQAKPVAPQV PSPGAPGQGP HPYNLAEPAL TLETSGKNLT EQNYSNIPHE
GKHTPLYERS SPINPAPSGS PNHVDSAYFP GSSTSSSSDN DEGSGGAANH ISGNKIGWEK
TGSHSEPQAR GDPGDQTKAE GSSTASSGSQ LAEGKGNQIG TVQPIPCLLS MPTRNHMDIT
TPPLPPVAPE VLRVAEHRHK KGLMYPYIFH VLTKGEIKIA VSIEDEASKD LPPAALLYRP
VRQYVYGVLF SLAESRKKTE RLAFRKNRLP PEFSPVIIKE WAAYKGKSPQ TPELVEALAF
REWTCPNLKR LWLGKAVEDK NRRMRAFLAC MRSDTPAMLN PASVPTHLTV LCCVLRYMVQ
WPGARILRRQ ELDAFLAQAL SPKLYEPDQL QELKIENLDP RGIQLSALFM SGVDMALFAN
DACGQPVPWE HCCPWMYFDG KLFQSKLLKA SREKTPLIDL CDGQAEQAAK VEKMRQSILE
GLNFSRQSHP LPFPPPAALP FYPTSVYPRH FGPVPPAQGR GRGFAGVCGF GSPYGETVAT
GAYRAFRVAT ATGHCGAFSG SDSSRTSKSQ GGIQPIPSQG GKLEIAGTVV GHWAGSRRGR
GGRGPFPLQV VSVGGPARGR PRGVISTPVI RTFGRGGRYY GRGYKNQGAI QGKPPYAASA
EEVAKELKSR SGESKSSAMS SDGSLAENGV VAEEKPAPQM NGSAGDTRAP SHSESALNND
SKTCNTNPHL NALSTDSGCR RADALEAAVL KKEE
