TUB_RAT
ID TUB_RAT Reviewed; 505 AA.
AC O88808; Q9Z1A2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Tubby protein homolog;
GN Name=Tub;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H.,
RA Suto T., Nakagawa K., Nakahara Y., Higashi K.;
RT "Molecular cloning of rat TUBBY gene.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 291-404.
RC STRAIN=Wistar;
RA Koritschoner N.P., Alvarez-Dolado M., Zenke M.;
RT "Cloning and expression of the rat gene tubby.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=19695251; DOI=10.1016/j.febslet.2009.08.015;
RA Caberoy N.B., Li W.;
RT "Unconventional secretion of tubby and tubby-like protein 1.";
RL FEBS Lett. 583:3057-3062(2009).
CC -!- FUNCTION: Functions in signal transduction from heterotrimeric G
CC protein-coupled receptors. Binds to membranes containing
CC phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May
CC contribute to the regulation of transcription in the nucleus. Could be
CC involved in the hypothalamic regulation of body weight (By similarity).
CC Contribute to stimulation of phagocytosis of apoptotic retinal pigment
CC epithelium (RPE) cells and macrophages (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GNAQ. Interacts with TULP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19695251}. Nucleus
CC {ECO:0000250}. Secreted {ECO:0000269|PubMed:19695251}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Binds phospholipid and is anchored to the
CC plasma membrane through binding phosphatidylinositol 4,5-bisphosphate.
CC Is released upon activation of phospholipase C. Translocates from the
CC plasma membrane to the nucleus upon activation of guanine nucleotide-
CC binding protein G(q) subunit alpha. Does not have a cleavable signal
CC peptide and is secreted by a non-conventional pathway (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
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DR EMBL; AB011544; BAA32734.1; -; mRNA.
DR EMBL; U92546; AAD09251.1; -; mRNA.
DR RefSeq; NP_037209.1; NM_013077.1.
DR AlphaFoldDB; O88808; -.
DR SMR; O88808; -.
DR BioGRID; 247638; 1.
DR STRING; 10116.ENSRNOP00000064486; -.
DR jPOST; O88808; -.
DR PaxDb; O88808; -.
DR Ensembl; ENSRNOT00000074636; ENSRNOP00000064486; ENSRNOG00000046566.
DR GeneID; 25609; -.
DR KEGG; rno:25609; -.
DR CTD; 7275; -.
DR RGD; 3918; Tub.
DR eggNOG; KOG2502; Eukaryota.
DR GeneTree; ENSGT00940000158372; -.
DR HOGENOM; CLU_028236_1_1_1; -.
DR InParanoid; O88808; -.
DR OMA; MTSKHHS; -.
DR OrthoDB; 1445357at2759; -.
DR PhylomeDB; O88808; -.
DR PRO; PR:O88808; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000046566; Expressed in frontal cortex and 11 other tissues.
DR Genevisible; O88808; RN.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0120160; F:intraciliary transport particle A binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0042073; P:intraciliary transport; ISO:RGD.
DR GO; GO:0006910; P:phagocytosis, recognition; ISO:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; ISO:RGD.
DR GO; GO:0097500; P:receptor localization to non-motile cilium; ISO:RGD.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR Gene3D; 3.20.90.10; -; 1.
DR InterPro; IPR025659; Tubby-like_C.
DR InterPro; IPR000007; Tubby_C.
DR InterPro; IPR018066; Tubby_C_CS.
DR InterPro; IPR005398; Tubby_N.
DR Pfam; PF01167; Tub; 1.
DR Pfam; PF16322; Tub_N; 1.
DR PRINTS; PR01573; SUPERTUBBY.
DR PRINTS; PR01574; TUBBYPROTEIN.
DR SUPFAM; SSF54518; SSF54518; 1.
DR PROSITE; PS01200; TUB_1; 1.
DR PROSITE; PS01201; TUB_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Membrane; Nucleus; Obesity; Phagocytosis;
KW Reference proteome; Secreted; Sensory transduction.
FT CHAIN 1..505
FT /note="Tubby protein homolog"
FT /id="PRO_0000186465"
FT REGION 35..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 362..379
FT /note="LRQELAAVCYETNVLGFK -> CARSWQPCAMRQMSRLQ (in Ref. 2;
FT AAD09251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 55318 MW; 8ECAAB751B06469F CRC64;
MTSKPHSDWI PYSVLDDEGS NLRQQKLDRQ RALLEQKQKK KRQEPLMVQA NADGRPRSRR
ARQSEEQAPL VESYLSSSGS TSYQVQEADS LASVQPGATR PPAPASAKKT KGAAASGGQG
GAPRKEKKGK HKGTSGPATL AEDKSEAQGP VQILTVGQSD HAKDAGETAA GGGAQPSGQD
LRATMQRKGI SSSMSFDEEE DEDENSSSSS QLNSNTRPSS ATSRKSTREA ASAPSPAAPE
PPVDIEVQDL EEFALRPAPQ GITIKCRITR DKKGMDRGMY PTYFLHLDRE DGKKVFLLAG
RKRKKSKTSN YLISVDPTDL SRGGDSYIGK LRSNLMGTKF TVYDNGVNPQ KASSSTLESG
TLRQELAAVC YETNVLGFKG PRKMSVIVPG MNMVHERVCI RPRNEHETLL ARWQNKNTES
IIELQNKTPV WNDDTQSYVL NFHGRVTQAS VKNFQIIHGN DPDYIVMQFG RVAEDVFTMD
YNYPLCALQA FAIALSSFDS KLACE
