TULP1_MOUSE
ID TULP1_MOUSE Reviewed; 543 AA.
AC Q9Z273;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tubby-related protein 1;
DE AltName: Full=Tubby-like protein 1;
GN Name=Tulp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Naggert J.K., Nishina P.M., Fitch D., McGinnis N., Basson M., Yan G.,
RA Cardon L., Shiva N., Duyao M., Ikeda A., McGinnis A., North M.A.;
RT "Molecular evolution of the tubby gene family.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Ikeda S., Sorokina I., Naggert J.K., North M.A., Nishina P.M.;
RT "Apoptotic photoreceptor cell death in tubby mice and the localization of
RT tubby gene family members in the retina.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11481257;
RA Hagstrom S.A., Adamian M., Scimeca M., Pawlyk B.S., Yue G., Li T.;
RT "A role for the Tubby-like protein 1 in rhodopsin transport.";
RL Invest. Ophthalmol. Vis. Sci. 42:1955-1962(2001).
RN [4]
RP INTERACTION WITH DNM1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, SUBUNIT, AND FUNCTION.
RX PubMed=17525220; DOI=10.1167/iovs.06-0059;
RA Xi Q., Pauer G.J.T., Ball S.L., Rayborn M., Hollyfield J.G., Peachey N.S.,
RA Crabb J.W., Hagstrom S.A.;
RT "Interaction between the photoreceptor-specific tubby-like protein 1 and
RT the neuronal-specific GTPase dynamin-1.";
RL Invest. Ophthalmol. Vis. Sci. 48:2837-2844(2007).
RN [5]
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).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19218615; DOI=10.1167/iovs.08-3190;
RA Grossman G.H., Pauer G.J.T., Narendra U., Peachey N.S., Hagstrom S.A.;
RT "Early synaptic defects in tulp1-/- mice.";
RL Invest. Ophthalmol. Vis. Sci. 50:3074-3083(2009).
RN [7]
RP INTERACTION WITH TYRO3.
RX PubMed=20978472; DOI=10.1038/emboj.2010.265;
RA Caberoy N.B., Zhou Y., Li W.;
RT "Tubby and tubby-like protein 1 are new MerTK ligands for phagocytosis.";
RL EMBO J. 29:3898-3910(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH TUB.
RX PubMed=19837063; DOI=10.1016/j.yexcr.2009.10.008;
RA Caberoy N.B., Maiguel D., Kim Y., Li W.;
RT "Identification of tubby and tubby-like protein 1 as eat-me signals by
RT phage display.";
RL Exp. Cell Res. 316:245-257(2010).
RN [9]
RP INTERACTION WITH HMGB2; ABCF1; PSIP1 AND ZEB1.
RX PubMed=19718693; DOI=10.1002/jmr.983;
RA Caberoy N.B., Zhou Y., Jiang X., Alvarado G., Li W.;
RT "Efficient identification of tubby-binding proteins by an improved system
RT of T7 phage display.";
RL J. Mol. Recognit. 23:74-83(2010).
CC -!- FUNCTION: Required for normal development of photoreceptor synapses.
CC Required for normal photoreceptor function and for long-term survival
CC of photoreceptor cells. Interacts with cytoskeleton proteins and may
CC play a role in protein transport in photoreceptor cells. Binds lipids,
CC especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4-
CC phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-
CC bisphosphate, phosphatidylinositol 4,5-bisphosphate,
CC phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and
CC phosphatidic acid (in vitro) (By similarity). Contribute to stimulation
CC of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and
CC macrophages. {ECO:0000250, ECO:0000269|PubMed:11481257,
CC ECO:0000269|PubMed:17525220, ECO:0000269|PubMed:19218615,
CC ECO:0000269|PubMed:19837063}.
CC -!- SUBUNIT: Homodimer (Probable). May interact with ABCF1, PSIP1, ZEB1 and
CC HMGB2 (Potential). Interacts with F-actin (By similarity). Interacts
CC with DNM1. Interacts with TUB. Interacts with TYRO3. {ECO:0000250,
CC ECO:0000269|PubMed:17525220, ECO:0000269|PubMed:19718693,
CC ECO:0000269|PubMed:19837063, ECO:0000269|PubMed:20978472, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Secreted. Synapse. Note=Detected at synapses between
CC photoreceptor cells and second-order neurons. Does not have a cleavable
CC signal peptide and is secreted by an alternative pathway.
CC -!- TISSUE SPECIFICITY: Retina specific. Detected in the outer plexiform
CC layer in photoreceptor cells (at protein level).
CC {ECO:0000269|PubMed:19218615}.
CC -!- DISRUPTION PHENOTYPE: Malformation of photoreceptor synapses, followed
CC by photoreceptor degeneration. {ECO:0000269|PubMed:19218615}.
CC -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
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DR EMBL; AF085681; AAD13757.1; -; mRNA.
DR EMBL; AF105711; AAD38451.1; -; mRNA.
DR CCDS; CCDS28578.1; -.
DR RefSeq; NP_067453.1; NM_021478.2.
DR AlphaFoldDB; Q9Z273; -.
DR SMR; Q9Z273; -.
DR BioGRID; 204383; 3.
DR STRING; 10090.ENSMUSP00000049070; -.
DR PhosphoSitePlus; Q9Z273; -.
DR MaxQB; Q9Z273; -.
DR PaxDb; Q9Z273; -.
DR PRIDE; Q9Z273; -.
DR ProteomicsDB; 298028; -.
DR Antibodypedia; 45745; 99 antibodies from 21 providers.
DR DNASU; 22157; -.
DR Ensembl; ENSMUST00000041819; ENSMUSP00000049070; ENSMUSG00000037446.
DR GeneID; 22157; -.
DR KEGG; mmu:22157; -.
DR UCSC; uc008bqv.1; mouse.
DR CTD; 7287; -.
DR MGI; MGI:109571; Tulp1.
DR VEuPathDB; HostDB:ENSMUSG00000037446; -.
DR eggNOG; KOG2502; Eukaryota.
DR GeneTree; ENSGT00940000158771; -.
DR HOGENOM; CLU_028236_5_1_1; -.
DR InParanoid; Q9Z273; -.
DR OMA; MRWQNKN; -.
DR OrthoDB; 1445357at2759; -.
DR PhylomeDB; Q9Z273; -.
DR TreeFam; TF314076; -.
DR BioGRID-ORCS; 22157; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Tulp1; mouse.
DR PRO; PR:Q9Z273; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z273; protein.
DR Bgee; ENSMUSG00000037446; Expressed in retinal neural layer and 62 other tissues.
DR ExpressionAtlas; Q9Z273; baseline and differential.
DR Genevisible; Q9Z273; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IMP:UniProtKB.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:MGI.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:UniProtKB.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0001895; P:retina homeostasis; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:MGI.
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 Pfam; PF01167; Tub; 1.
DR PRINTS; PR01573; SUPERTUBBY.
DR SUPFAM; SSF54518; SSF54518; 1.
DR PROSITE; PS01200; TUB_1; 1.
DR PROSITE; PS01201; TUB_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Phagocytosis; Reference proteome;
KW Secreted; Sensory transduction; Synapse; Vision.
FT CHAIN 1..543
FT /note="Tubby-related protein 1"
FT /id="PRO_0000186467"
FT REGION 1..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 60336 MW; 0F0D9E4D2A2731E7 CRC64;
MPLQEETLRE VWASDSGHEE DCLSPEPPLR PKQRPAQGQK LRKKKPETPD SLESKPRKAG
AGRRKHEEPP ADSAEPRAAQ TVYAKFLRDP EAKKRDPREN FLVARAPDLG GEENSEEDSD
DDDNDDDEEE EEKKEGKKEK SSLPPKKAPK EREKKAKALG PRGDVGSPDA PRKPLRTKKK
EVGEGTKLRK AKKKGPGETD KDPAGSPAAL RKEFPAAMFL VGEGGAAEKG VKKKGPPKGS
EEEKKEEEEE VEEEVASAVM KNSNQKGRAK GKGKKKVKEE RASSPPVEVG EPREFVLQPA
PQGRAVRCRL TRDKKGMDRG MYPSYFLHLD TEKKVFLLAG RKRKRSKTAN YLISSDPTNL
SRGGENFIGK LRSNLLGNRF TVFDNGQNPQ RGGGGDVGSL RQELAAVVYE TNVLGFRGPR
RMTVIIPGMN SDNERVPIRP RNASDGLLVR WQNKTLESLI ELHNKPPIWN EDSGSYTLNF
QGRVTQASVK NFQIVHADDP DYIVLQFGRV AEDAFTLDYR YPLCALQAFA IALSSFDGKL
ACE
