LOCUS       NP_001297540            1255 aa            linear   ROD 30-APR-2024
DEFINITION  TBC1 domain family member 1 isoform 3 [Mus musculus].
ACCESSION   NP_001297540 XP_006504098
VERSION     NP_001297540.1
DBSOURCE    REFSEQ: accession NM_001310611.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1255)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1255)
  AUTHORS   Larsen,J.K., Larsen,M.R., Birk,J.B., Steenberg,D.E., Hingst,J.R.,
            Hojlund,K., Chadt,A., Al-Hasani,H., Deshmukh,A.S.,
            Wojtaszewski,J.F.P. and Kjobsted,R.
  TITLE     Illumination of the Endogenous Insulin-Regulated TBC1D4 Interactome
            in Human Skeletal Muscle
  JOURNAL   Diabetes 71 (5), 906-920 (2022)
   PUBMED   35192682
REFERENCE   3  (residues 1 to 1255)
  AUTHORS   Zhang,Z., Ma,T., Fu,Z., Feng,Y., Wang,Z., Tian,S., Liu,Z., Wei,W.,
            Li,X., Chen,J. and Zhao,W.
  TITLE     TBC1Domain Family Member 25 deficiency aggravates cerebral
            ischemia-reperfusion injury via TAK1-JNK/p38 pathway
  JOURNAL   J Neurochem 160 (3), 392-411 (2022)
   PUBMED   34837397
  REMARK    GeneRIF: TBC1Domain Family Member 25 deficiency aggravates cerebral
            ischemia-reperfusion injury via TAK1-JNK/p38 pathway.
REFERENCE   4  (residues 1 to 1255)
  AUTHORS   Chen,Z.Y., Sun,Y.T., Wang,Z.M., Hong,J., Xu,M., Zhang,F.T.,
            Zhou,X.Q., Rong,P., Wang,Q., Wang,H.Y., Wang,H., Chen,S. and
            Chen,L.
  TITLE     Rab2A regulates the progression of nonalcoholic fatty liver disease
            downstream of AMPK-TBC1D1 axis by stabilizing PPARgamma
  JOURNAL   PLoS Biol 20 (1), e3001522 (2022)
   PUBMED   35061665
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1255)
  AUTHORS   de Wendt,C., Espelage,L., Eickelschulte,S., Springer,C., Toska,L.,
            Scheel,A., Bedou,A.D., Benninghoff,T., Cames,S., Stermann,T.,
            Chadt,A. and Al-Hasani,H.
  TITLE     Contraction-Mediated Glucose Transport in Skeletal Muscle Is
            Regulated by a Framework of AMPK, TBC1D1/4, and Rac1
  JOURNAL   Diabetes 70 (12), 2796-2809 (2021)
   PUBMED   34561225
REFERENCE   6  (residues 1 to 1255)
  AUTHORS   Giesen,K., Plum,L., Kluge,R., Ortlepp,J. and Joost,H.G.
  TITLE     Diet-dependent obesity and hypercholesterolemia in the New Zealand
            obese mouse: identification of a quantitative trait locus for
            elevated serum cholesterol on the distal mouse chromosome 5
  JOURNAL   Biochem Biophys Res Commun 304 (4), 812-817 (2003)
   PUBMED   12727230
REFERENCE   7  (residues 1 to 1255)
  AUTHORS   Plum,L., Giesen,K., Kluge,R., Junger,E., Linnartz,K., Schurmann,A.,
            Becker,W. and Joost,H.G.
  TITLE     Characterisation of the mouse diabetes susceptibilty locus
            Nidd/SJL: islet cell destruction, interaction with the obesity QTL
            Nob1, and effect of dietary fat
  JOURNAL   Diabetologia 45 (6), 823-830 (2002)
   PUBMED   12107726
REFERENCE   8  (residues 1 to 1255)
  AUTHORS   Kluge,R., Giesen,K., Bahrenberg,G., Plum,L., Ortlepp,J.R. and
            Joost,H.G.
  TITLE     Quantitative trait loci for obesity and insulin resistance (Nob1,
            Nob2) and their interaction with the leptin receptor allele
            (LeprA720T/T1044I) in New Zealand obese mice
  JOURNAL   Diabetologia 43 (12), 1565-1572 (2000)
   PUBMED   11151768
REFERENCE   9  (residues 1 to 1255)
  AUTHORS   White,R.A., Pasztor,L.M., Richardson,P.M. and Zon,L.I.
  TITLE     The gene encoding TBC1D1 with homology to the tre-2/USP6 oncogene,
            BUB2, and cdc16 maps to mouse chromosome 5 and human chromosome 4
  JOURNAL   Cytogenet Cell Genet 89 (3-4), 272-275 (2000)
   PUBMED   10965142
REFERENCE   10 (residues 1 to 1255)
  AUTHORS   Richardson,P.M. and Zon,L.I.
  TITLE     Molecular cloning of a cDNA with a novel domain present in the
            tre-2 oncogene and the yeast cell cycle regulators BUB2 and cdc16
  JOURNAL   Oncogene 11 (6), 1139-1148 (1995)
   PUBMED   7566974
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132271.5 and AC131679.2.
            
            On Jul 16, 2015 this sequence version replaced XP_006504098.1.
            
            Transcript Variant: This variant (3) contains two alternate
            in-frame exons compared to variant 1. The encoded isoform (3) is
            longer than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10223971.5805.1,
                                           SRR10223969.5507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1255
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 32.8 cM"
     Protein         1..1255
                     /product="TBC1 domain family member 1 isoform 3"
                     /note="tre-2/USP6, BUB2, cdc16) domain family, member 1"
                     /calculated_mol_wt=141895
     Region          21..150
                     /region_name="PTB"
                     /note="Phosphotyrosine-binding (PTB) PH-like fold;
                     cd00934"
                     /db_xref="CDD:269911"
     Site            order(24,112,133)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269911"
     Site            order(101..106,120,144,148)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269911"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          164..365
                     /region_name="PTB_TBC1D1_like"
                     /note="TBC1 domain family member 1 and related proteins
                     Phosphotyrosine-binding (PTB) domain; cd01269"
                     /db_xref="CDD:269967"
     Site            order(176,322,347)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269967"
     Region          208..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60949.3)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            order(311..316,329,358,362)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269967"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          509..544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60949.3)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          559..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60949.3)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86TI0; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86TI0; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19740738,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          595..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60949.3)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          621..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60949.3)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:19740738,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:19740738,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          764..786
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60949.3)"
     Region          777..832
                     /region_name="DUF3350"
                     /note="Domain of unknown function (DUF3350); pfam11830"
                     /db_xref="CDD:463365"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          884..1101
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            1028
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Site            1039
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          1139..>1239
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Site            1218
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19740738; propagated from
                     UniProtKB/Swiss-Prot (Q60949.3)"
     Region          1233..1255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60949.3)"
     CDS             1..1255
                     /gene="Tbc1d1"
                     /gene_synonym="1110062G02Rik; mKIAA1108; Nob1; Nobq1;
                     Tbc1"
                     /coded_by="NM_001310611.1:339..4106"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS80287.1"
                     /db_xref="GeneID:57915"
                     /db_xref="MGI:MGI:1889508"
ORIGIN      
        1 meaitftark hpfpnevsvd fglqlvgslp vhslttmpml pwvvaevrrl sgqcskkepr
       61 tkqvrlwvsp sglrcepdle ksqpwdplic ssifeckpqr vhklihnshd psyfaclike
      121 daahrqslcy vfkaddqtkv peiissirqa gkiarqeelr cpsefddtfa kkfevlfcgr
      181 vtvahkkapp alideciekf nhvscgrrtd weaptgqpsa pgprpmrksf sqpglrslaf
      241 rkefqdaslr sstfssfdnd ienhligghn vvqptdmeen rtmlftigqs evylispdtk
      301 kialeknfke isfcsqgirh vdhfgficre csgggsggfh fvcyvfqctn ealvdeimmt
      361 lkqaftvaav qqtakapaql cegcplqglh klceriegmn ssktklelqk hlttltnqeq
      421 atifeevqkl rprneqrene liisflrcly eekqkehsht gepkqtlqva aenigsdlpp
      481 sasrfrldsl knrakrslte slesilsrgn karglqdhsa svdldsstss tlsntskels
      541 mgdkeafpvs etsfkllgss ddlssdsegh iaeesallsp qqafrrrant lshfpvecpa
      601 ppepaqsspg vsqrklmryh svstetpher nvdhlpgges qgcpgqpsap ppprlnpsas
      661 spnffkylkh nssgeqsgna vpksvsyrna lrkklhssss vpnflkflap vdenntcdfk
      721 ntnrdfeska nhlgdtdgtp vktrrhswrq qiflrvatpq kacdspsrye dyselgelpp
      781 rsplepvced gpfgpvqeek rktsrelrel wkkailqqil llrmekenqk lqasendlln
      841 krlkldyeei tpclkevttv wekmlstpgr skikfdmekv hsavgqgvpr hhrgeiwkfl
      901 aeqfhlkhpf pskqqpkdvp ykellkklts qqhailidlg rtfpthpyfs aqlgagqlsl
      961 ynilkaysll dqevgycqgl sfvagilllh mseeeafkml kflmfdmglr kqyrpdmiil
     1021 qiqmyqlsrl lhdyhrdlyn hleeheigps lyaapwfltv fasqfplgfv arvfdmiflq
     1081 gsevifkval sllgshkpli lqhenletiv dfikntlpnl glvqmektis qvfemdiakq
     1141 lqayeveyhv lqeeliessp lsdnqrmekl ektnsslrkq nldlleqlqv anariqslea
     1201 tveklltses klkqaaltle versallqmv eelrrqsarp stpepdctql eptgd
//
