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Protein

Tubby protein

Gene

Tub

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight. Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages (By similarity).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

  • phagocytosis, recognition Source: MGI
  • photoreceptor cell maintenance Source: MGI
  • positive regulation of phagocytosis Source: UniProtKB
  • protein localization to ciliary membrane Source: MGI
  • protein localization to photoreceptor outer segment Source: MGI
  • receptor localization to nonmotile primary cilium Source: MGI
  • response to hormone Source: Ensembl
  • retina development in camera-type eye Source: MGI
  • sensory perception of sound Source: MGI
Complete GO annotation...

Keywords - Biological processi

Phagocytosis, Sensory transduction

Names & Taxonomyi

Protein namesi
Recommended name:
Tubby protein
Gene namesi
Name:Tub
Synonyms:Rd5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2651573. Tub.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • Secreted
  • Cell membrane; Peripheral membrane protein; Cytoplasmic side

  • Note: Binds phospholipid and is anchored to the plasma membrane through binding phosphatidylinositol 4,5-bisphosphate. Is released upon activation of phospholipase C. Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha. Does not have a cleavable signal peptide and is secreted by a non-conventional pathway.

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular region Source: MGI
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in Tub are the cause of maturity-onset obesity, insulin resistance and sensory deficits.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi330 – 3301K → A: Abolishes interaction with phosphatidylinositol 4,5-bisphosphate and reduces secretion by 40%; when associated with A-332. 2 Publications
Mutagenesisi332 – 3321R → A: Abolishes interaction with phosphatidylinositol 4,5-bisphosphate and reduces secretion by 40%; when associated with A-330. 2 Publications

Keywords - Diseasei

Obesity

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Tubby proteinPRO_0000186464Add
BLAST

Proteomic databases

PaxDbiP50586.
PRIDEiP50586.

PTM databases

iPTMnetiP50586.
PhosphoSiteiP50586.

Expressioni

Gene expression databases

BgeeiP50586.
CleanExiMM_TUB.
ExpressionAtlasiP50586. baseline and differential.
GenevisibleiP50586. MM.

Interactioni

Subunit structurei

Interacts with GNAQ. Interacts with TULP1.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204371. 1 interaction.
STRINGi10090.ENSMUSP00000033341.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi250 – 2556Combined sources
Beta strandi264 – 2707Combined sources
Beta strandi275 – 2784Combined sources
Beta strandi282 – 2887Combined sources
Beta strandi294 – 31522Combined sources
Helixi317 – 3204Combined sources
Turni321 – 3233Combined sources
Beta strandi328 – 3336Combined sources
Beta strandi337 – 3437Combined sources
Beta strandi345 – 3473Combined sources
Helixi349 – 3513Combined sources
Helixi356 – 3583Combined sources
Beta strandi359 – 3624Combined sources
Beta strandi365 – 3717Combined sources
Beta strandi384 – 3896Combined sources
Helixi405 – 4073Combined sources
Helixi409 – 4146Combined sources
Beta strandi419 – 4268Combined sources
Beta strandi430 – 4323Combined sources
Turni433 – 4364Combined sources
Beta strandi437 – 4426Combined sources
Beta strandi445 – 4484Combined sources
Beta strandi453 – 4575Combined sources
Beta strandi464 – 47310Combined sources
Beta strandi476 – 4816Combined sources
Helixi487 – 49913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8ZX-ray1.90A243-505[»]
1I7EX-ray1.95A243-505[»]
ProteinModelPortaliP50586.
SMRiP50586. Positions 243-505.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50586.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi197 – 2048Asp/Glu-rich
Compositional biasi206 – 2105Poly-Ser

Sequence similaritiesi

Belongs to the TUB family.Curated

Phylogenomic databases

eggNOGiKOG2502. Eukaryota.
ENOG410XQFT. LUCA.
HOGENOMiHOG000016044.
HOVERGENiHBG018010.
InParanoidiP50586.
OMAiATMQRKG.
OrthoDBiEOG77HDDQ.
PhylomeDBiP50586.
TreeFamiTF314076.

Family and domain databases

Gene3Di3.20.90.10. 1 hit.
InterProiIPR000007. Tubby_C.
IPR025659. Tubby_C-like.
IPR018066. Tubby_C_CS.
IPR005398. Tubby_N.
[Graphical view]
PfamiPF01167. Tub. 1 hit.
PF16322. Tub_N. 1 hit.
[Graphical view]
PRINTSiPR01573. SUPERTUBBY.
PR01574. TUBBYPROTEIN.
SUPFAMiSSF54518. SSF54518. 1 hit.
PROSITEiPS01200. TUB_1. 1 hit.
PS01201. TUB_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P50586-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSKPHSDWI PYSVLDDEGS NLRQQKLDRQ RALLEQKQKK KRQEPLMVQA
60 70 80 90 100
NADGRPRSRR ARQSEEQAPL VESYLSSSGS TSYQVQEADS IASVQLGATR
110 120 130 140 150
PPAPASAKKS KGAAASGGQG GAPRKEKKGK HKGTSGPATL AEDKSEAQGP
160 170 180 190 200
VQILTVGQSD HDKDAGETAA GGGAQPSGQD LRATMQRKGI SSSMSFDEDE
210 220 230 240 250
DEDENSSSSS QLNSNTRPSS ATSRKSIREA ASAPSPAAPE PPVDIEVQDL
260 270 280 290 300
EEFALRPAPQ GITIKCRITR DKKGMDRGMY PTYFLHLDRE DGKKVFLLAG
310 320 330 340 350
RKRKKSKTSN YLISVDPTDL SRGGDSYIGK LRSNLMGTKF TVYDNGVNPQ
360 370 380 390 400
KASSSTLESG TLRQELAAVC YETNVLGFKG PRKMSVIVPG MNMVHERVCI
410 420 430 440 450
RPRNEHETLL ARWQNKNTES IIELQNKTPV WNDDTQSYVL NFHGRVTQAS
460 470 480 490 500
VKNFQIIHGN DPDYIVMQFG RVAEDVFTMD YNYPLCALQA FAIALSSFDS

KLACE
Length:505
Mass (Da):55,362
Last modified:October 1, 1996 - v1
Checksum:i32E160BBF5265211
GO
Isoform Short (identifier: P50586-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     153-208: Missing.

Show »
Length:449
Mass (Da):49,563
Checksum:i498167BD335C0776
GO

Sequence cautioni

The sequence AAC52512.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 20856Missing in isoform Short. CuratedVSP_006675Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54643 mRNA. Translation: AAB53495.1.
U52433 mRNA. Translation: AAC52510.1.
U52824 mRNA. Translation: AAC52512.1. Different initiation.
AJ296303 Genomic DNA. Translation: CAC39309.1.
CCDSiCCDS21732.1. [P50586-1]
PIRiS68518.
RefSeqiNP_068685.1. NM_021885.4. [P50586-1]
UniGeneiMm.439722.

Genome annotation databases

EnsembliENSMUST00000033341; ENSMUSP00000033341; ENSMUSG00000031028. [P50586-1]
GeneIDi22141.
KEGGimmu:22141.
UCSCiuc009jdf.1. mouse. [P50586-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54643 mRNA. Translation: AAB53495.1.
U52433 mRNA. Translation: AAC52510.1.
U52824 mRNA. Translation: AAC52512.1. Different initiation.
AJ296303 Genomic DNA. Translation: CAC39309.1.
CCDSiCCDS21732.1. [P50586-1]
PIRiS68518.
RefSeqiNP_068685.1. NM_021885.4. [P50586-1]
UniGeneiMm.439722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8ZX-ray1.90A243-505[»]
1I7EX-ray1.95A243-505[»]
ProteinModelPortaliP50586.
SMRiP50586. Positions 243-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204371. 1 interaction.
STRINGi10090.ENSMUSP00000033341.

PTM databases

iPTMnetiP50586.
PhosphoSiteiP50586.

Proteomic databases

PaxDbiP50586.
PRIDEiP50586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033341; ENSMUSP00000033341; ENSMUSG00000031028. [P50586-1]
GeneIDi22141.
KEGGimmu:22141.
UCSCiuc009jdf.1. mouse. [P50586-1]

Organism-specific databases

CTDi7275.
MGIiMGI:2651573. Tub.

Phylogenomic databases

eggNOGiKOG2502. Eukaryota.
ENOG410XQFT. LUCA.
HOGENOMiHOG000016044.
HOVERGENiHBG018010.
InParanoidiP50586.
OMAiATMQRKG.
OrthoDBiEOG77HDDQ.
PhylomeDBiP50586.
TreeFamiTF314076.

Miscellaneous databases

EvolutionaryTraceiP50586.
PROiP50586.
SOURCEiSearch...

Gene expression databases

BgeeiP50586.
CleanExiMM_TUB.
ExpressionAtlasiP50586. baseline and differential.
GenevisibleiP50586. MM.

Family and domain databases

Gene3Di3.20.90.10. 1 hit.
InterProiIPR000007. Tubby_C.
IPR025659. Tubby_C-like.
IPR018066. Tubby_C_CS.
IPR005398. Tubby_N.
[Graphical view]
PfamiPF01167. Tub. 1 hit.
PF16322. Tub_N. 1 hit.
[Graphical view]
PRINTSiPR01573. SUPERTUBBY.
PR01574. TUBBYPROTEIN.
SUPFAMiSSF54518. SSF54518. 1 hit.
PROSITEiPS01200. TUB_1. 1 hit.
PS01201. TUB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J and CD-1.
    Tissue: Brain and Testis.
  3. "Mouse chromosome 7 BAC clone 287P4, sequenced in DHGP-project: comparative sequencing of 1 Mb region in man (Chromosome 11p15) and mouse (Chromosome 7)."
    Brueckmann T., Winterpacht A., Hankeln T., Schmidt E.R., Zabel B.U.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Unconventional secretion of tubby and tubby-like protein 1."
    Caberoy N.B., Li W.
    FEBS Lett. 583:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-330 AND ARG-332.
  5. "Identification of tubby and tubby-like protein 1 as eat-me signals by phage display."
    Caberoy N.B., Maiguel D., Kim Y., Li W.
    Exp. Cell Res. 316:245-257(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TULP1.
  6. "Implication of tubby proteins as transcription factors by structure-based functional analysis."
    Boggon T.J., Shan W.-S., Santagata S., Myers S.C., Shapiro L.
    Science 286:2119-2125(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 241-505, SUBCELLULAR LOCATION, DNA-BINDING, FUNCTION.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 243-505, SUBCELLULAR LOCATION, INTERACTION WITH GNAQ, PHOSPHOLIPID BINDING, MUTAGENESIS OF LYS-330 AND ARG-332, FUNCTION.

Entry informationi

Entry nameiTUB_MOUSE
AccessioniPrimary (citable) accession number: P50586
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.