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TUB1_CAEEL
ID   TUB1_CAEEL              Reviewed;         426 AA.
AC   Q09306; Q9UB22;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 3.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Tubby protein homolog 1;
GN   Name=tub-1 {ECO:0000312|WormBase:F10B5.4};
GN   ORFNames=F10B5.4 {ECO:0000312|WormBase:F10B5.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RA   Nelson L., Basson M., Spoerke J., Liu L.X., Yan G., North M.A.,
RA   Johnson C.D.;
RT   "A tubby family member in Caenorhabditis elegans is required for normal
RT   sensory behavior.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=2592410; DOI=10.1083/jcb.109.6.2993;
RA   Driscoll M., Dean E., Reilly E., Bergholz E., Chalfie M.;
RT   "Genetic and molecular analysis of a Caenorhabditis elegans beta-tubulin
RT   that conveys benzimidazole sensitivity.";
RL   J. Cell Biol. 109:2993-3003(1989).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12529643; DOI=10.1038/nature01279;
RA   Ashrafi K., Chang F.Y., Watts J.L., Fraser A.G., Kamath R.S., Ahringer J.,
RA   Ruvkun G.;
RT   "Genome-wide RNAi analysis of Caenorhabditis elegans fat regulatory
RT   genes.";
RL   Nature 421:268-272(2003).
RN   [5]
RP   FUNCTION, INTERACTION WITH RGB-3, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16054097; DOI=10.1016/j.cmet.2005.06.004;
RA   Mukhopadhyay A., Deplancke B., Walhout A.J., Tissenbaum H.A.;
RT   "C. elegans tubby regulates life span and fat storage by two independent
RT   mechanisms.";
RL   Cell Metab. 2:35-42(2005).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15790967; DOI=10.1242/dev.01775;
RA   Efimenko E., Bubb K., Mak H.Y., Holzman T., Leroux M.R., Ruvkun G.,
RA   Thomas J.H., Swoboda P.;
RT   "Analysis of xbx genes in C. elegans.";
RL   Development 132:1923-1934(2005).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16462744; DOI=10.1038/ng1739;
RA   Mak H.Y., Nelson L.S., Basson M., Johnson C.D., Ruvkun G.;
RT   "Polygenic control of Caenorhabditis elegans fat storage.";
RL   Nat. Genet. 38:363-368(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=17762880; DOI=10.1038/sj.embor.7401055;
RA   Mukhopadhyay A., Pan X., Lambright D.G., Tissenbaum H.A.;
RT   "An endocytic pathway as a target of tubby for regulation of fat storage.";
RL   EMBO Rep. 8:931-938(2007).
CC   -!- FUNCTION: Has a role in fat regulation independent of daf-16.
CC       Implicated in ciliar sensory function which is required for normal
CC       sensory behavior such as chemotaxis. Functions in life span control via
CC       the insulin/IGF-1 pathway. Thought to be involved in neuronal
CC       trafficking. {ECO:0000269|PubMed:12529643, ECO:0000269|PubMed:15790967,
CC       ECO:0000269|PubMed:16054097, ECO:0000269|PubMed:16462744,
CC       ECO:0000269|PubMed:17762880}.
CC   -!- SUBUNIT: Interacts with rgb-3. {ECO:0000269|PubMed:16054097}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15790967,
CC       ECO:0000269|PubMed:16054097}. Cell projection, axon
CC       {ECO:0000269|PubMed:16462744}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:16462744}. Cell projection, cilium
CC       {ECO:0000269|PubMed:16462744}.
CC   -!- TISSUE SPECIFICITY: Expressed in ciliated sensory neurons.
CC       {ECO:0000269|PubMed:15790967, ECO:0000269|PubMed:16054097,
CC       ECO:0000269|PubMed:16462744}.
CC   -!- DISRUPTION PHENOTYPE: Twofold increase in fat content. Extension in
CC       life span. Defective in chemotaxis. {ECO:0000269|PubMed:12529643}.
CC   -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
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DR   EMBL; AF143297; AAD33902.1; -; mRNA.
DR   EMBL; Z48334; CAB61010.2; -; Genomic_DNA.
DR   RefSeq; NP_495710.1; NM_063309.4.
DR   AlphaFoldDB; Q09306; -.
DR   SMR; Q09306; -.
DR   BioGRID; 39641; 2.
DR   IntAct; Q09306; 1.
DR   STRING; 6239.F10B5.4; -.
DR   EPD; Q09306; -.
DR   PaxDb; Q09306; -.
DR   PeptideAtlas; Q09306; -.
DR   EnsemblMetazoa; F10B5.4.1; F10B5.4.1; WBGene00006655.
DR   GeneID; 174312; -.
DR   KEGG; cel:CELE_F10B5.4; -.
DR   UCSC; F10B5.4; c. elegans.
DR   CTD; 174312; -.
DR   WormBase; F10B5.4; CE29091; WBGene00006655; tub-1.
DR   eggNOG; KOG2502; Eukaryota.
DR   GeneTree; ENSGT00940000158771; -.
DR   HOGENOM; CLU_028236_1_1_1; -.
DR   InParanoid; Q09306; -.
DR   OMA; KSPQWND; -.
DR   OrthoDB; 1445357at2759; -.
DR   PhylomeDB; Q09306; -.
DR   Reactome; R-CEL-5610787; Hedgehog 'off' state.
DR   PRO; PR:Q09306; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006655; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0061512; P:protein localization to cilium; IBA:GO_Central.
DR   GO; GO:0097500; P:receptor localization to non-motile cilium; IMP:WormBase.
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 projection; Chemotaxis; Coiled coil; Cytoplasm; Lipid metabolism;
KW   Reference proteome; Sensory transduction.
FT   CHAIN           1..426
FT                   /note="Tubby protein homolog 1"
FT                   /id="PRO_0000186474"
FT   REGION          19..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  48454 MW;  F907CA1191E011D3 CRC64;
     MTDTNSQWIE MNLQRQRKML EDKQKQKRHQ SAGSVRTTST AMSMNSMKDY PTFDNSLPFS
     ISDNSSVSVS MNTPLIPTQD PIAQPRMQSM PRQQPQQVQE SLISIGDYPD NDINAKLSKV
     NLTSCVVSDD EDEDKRSYAD SPWNTDVVAD RIPSEVLPDY NFIKNNLAKF VEDPAVEHCL
     YKCSITRQKS GVDKGMFPTY FLHLEEFDTD KRQKIFLLAA RKRKKSTTAN YLLSTDPTNL
     SREGEGYCAK VRSNALGTQF TVYDSGQNPK KTTNHAAIRQ ELAAVIYETN VLGFKGPRKM
     TIVMPGIEPP TENRPAVRCP VRPIQDKHTL LERYRLNDLD SLKILSNKSP QWNDETQSYV
     LNFHGRVTQA SVKNFQIIHQ SSPEYIVMQF GRISDDEFTM DFRYPLSAVQ AFGIAMTSFH
     GKLACE
 
 
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