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   24-JAN-2024, entry version 141.
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   GlyGen; Q9Z273; 1 site, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; Q9Z273; -.
DR   MaxQB; Q9Z273; -.
DR   PaxDb; 10090-ENSMUSP00000049070; -.
DR   ProteomicsDB; 298028; -.
DR   Antibodypedia; 45745; 107 antibodies from 21 providers.
DR   DNASU; 22157; -.
DR   Ensembl; ENSMUST00000041819.14; ENSMUSP00000049070.7; ENSMUSG00000037446.15.
DR   GeneID; 22157; -.
DR   KEGG; mmu:22157; -.
DR   UCSC; uc008bqv.1; mouse.
DR   AGR; MGI:109571; -.
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; YAKFIRD; -.
DR   OrthoDB; 603296at2759; -.
DR   PhylomeDB; Q9Z273; -.
DR   TreeFam; TF314076; -.
DR   BioGRID-ORCS; 22157; 4 hits in 76 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 66 other cell types or tissues.
DR   ExpressionAtlas; Q9Z273; baseline and differential.
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   InterPro; IPR025659; Tubby-like_C.
DR   InterPro; IPR000007; Tubby_C.
DR   InterPro; IPR018066; Tubby_C_CS.
DR   PANTHER; PTHR16517; TUBBY-RELATED; 1.
DR   PANTHER; PTHR16517:SF12; TUBBY-RELATED PROTEIN 1; 1.
DR   Pfam; PF01167; Tub; 1.
DR   PRINTS; PR01573; SUPERTUBBY.
DR   SUPFAM; SSF54518; Tubby C-terminal domain-like; 1.
DR   PROSITE; PS01200; TUB_1; 1.
DR   PROSITE; PS01201; TUB_2; 1.
DR   Genevisible; Q9Z273; MM.
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
//