TBCD1_BOVIN
ID TBCD1_BOVIN Reviewed; 1165 AA.
AC O97790; F1MKC9;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=TBC1 domain family member 1;
DE AltName: Full=Lyncein;
GN Name=TBC1D1; Synonyms=LYN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 610-1165.
RC TISSUE=Retina;
RX PubMed=9813038; DOI=10.1074/jbc.273.47.31297;
RA Xu X.-Z.S., Wes P.D., Chen H., Li H.-S., Yu M., Morgan S., Liu Y.,
RA Montell C.;
RT "Retinal targets for calmodulin include proteins implicated in synaptic
RT transmission.";
RL J. Biol. Chem. 273:31297-31307(1998).
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s). May play a role in the cell cycle and differentiation of
CC various tissues. Involved in the trafficking and translocation of
CC GLUT4-containing vesicles and insulin-stimulated glucose uptake into
CC cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with APPL2 (via BAR domain); interaction is
CC dependent of TBC1D1 phosphorylation at Ser-232; interaction diminishes
CC the phosphorylation of TBC1D1 at Thr-593, resulting in inhibition of
CC SLC2A4/GLUT4 translocation and glucose uptake.
CC {ECO:0000250|UniProtKB:Q86TI0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Insulin-stimulated phosphorylation by AKT family kinases
CC stimulates SLC2A4/GLUT4 translocation. {ECO:0000250}.
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DR EMBL; DAAA02017438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02017439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02017440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02017441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02017442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02017443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y17923; CAA76943.1; -; mRNA.
DR RefSeq; NP_001159996.1; NM_001166524.1.
DR RefSeq; XP_005207895.1; XM_005207838.3.
DR AlphaFoldDB; O97790; -.
DR SMR; O97790; -.
DR STRING; 9913.ENSBTAP00000018206; -.
DR PaxDb; O97790; -.
DR PRIDE; O97790; -.
DR Ensembl; ENSBTAT00000018206; ENSBTAP00000018206; ENSBTAG00000013699.
DR GeneID; 282704; -.
DR KEGG; bta:282704; -.
DR CTD; 23216; -.
DR VEuPathDB; HostDB:ENSBTAG00000013699; -.
DR VGNC; VGNC:35623; TBC1D1.
DR eggNOG; KOG4436; Eukaryota.
DR GeneTree; ENSGT00940000157949; -.
DR HOGENOM; CLU_005350_13_0_1; -.
DR InParanoid; O97790; -.
DR OrthoDB; 323342at2759; -.
DR TreeFam; TF317184; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000013699; Expressed in myometrium and 107 other tissues.
DR ExpressionAtlas; O97790; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR021785; DUF3350.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF11830; DUF3350; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 2: Evidence at transcript level;
KW GTPase activation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1165
FT /note="TBC1 domain family member 1"
FT /id="PRO_0000208021"
FT DOMAIN 243..401
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 797..991
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 207..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 232
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 234
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 502
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TI0"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TI0"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TI0"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86TI0"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 624
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT MOD_RES 949
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60949"
FT CONFLICT 610..612
FT /note="GSP -> ARA (in Ref. 2; CAA76943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1165 AA; 132097 MW; 96FE5920B177A309 CRC64;
MEPITFTARK HPFPNEVSVD FGLQLVGSLP VHSLTTMPML PWVVAEVRRL SGQSSKKEPG
TKPVRLCVSP SGLRCEPEPG KSQQWDPLIC SSIFECKPQR VHKLIHNSHD PSYFACLIKN
DAANQQSICY VFKADDQTKV PEIISSIRQA GKIARQEELR CPSEFDDTFA KKFEVLFCGR
VAVAHRKAPP ALIDECIEGF SHVSGGFSSD QSRSALQPPG DGERGPRPMR KSFSQPGLRS
LAFRKEFQDA GLRSSSFFSS FEESDIENHL ISGHNIVQPT DIEENRTMLF TIGQSEVYLI
SPDTKKIALQ KNFKEISFCS QGIRHVDHFG FICRESSGGG GFHFVCYVFQ CTNEALVDEI
MMTLKQAFTV AAVQQTAKAP AQLCEGCPLQ GLHKLCERIE GMNSSKTKLE LQKHLTTLTN
QEQATIFEEV QKLRPRNEQR ENELIISFLR CLYEEKQKVH IHIGEIKQTS QIAAENIGSE
LPSSATRFRL DMLKNKAKRS LTESLESILS RGNKARGLQE HSASLDLDSS VSSMFSNTSK
EPSGYEKEAL PISESCFRLL GSSDDLSSDS ESQLTEEPAL LSPKQGFRRR ANTLSHVPVE
CQEPPQLVRG SPGVSQRKLV RYHSVSTETP HERKDFESKA DHISDASRTP VKTRRHSWRQ
QIFLRVATPQ KACESPKRYE DYSELGELPP RSPLEPVCED GPFGPVPEEK KRTSHELREL
WQKAILQQIL LLRMEKENQK LQASENDLLN KRLKLDYEEI TPCLKEVTTV WEKILSTPGR
SKIKFDMEKM HSAVGQGVPR HHRGEIWKFL AEQYHLKHPF PCKQQPKDTP YKELLKQLTS
QQHAILIDLG RTFPTHPYYS AQLGAGQLSL YNILKAYSLL DQEVGYCQGL SFVAGILLLH
MGEEEAFNML KFLMFDMGLR KQYRPDMIIL QIQMYQLSRL LHDYHRDLYN HLEEHEIGPS
LYAAPWFLTV FASQFPLGFV ARVFDMIFLQ GSEVIFKVAL SLLGSHKPLI LQHENLETIV
DFIKSTLPNL GLVQMEKTIS QVFETDISKQ LQAYEVEYHV LQEELIDSSP LSDNQRMDKL
EKTNSSLRKQ NLDLLEQLQV ANGRIQSLEA TVEKLLTSES KLKQATLALE LERSALLQTV
EQLRRQTAEL GSQESDPTLP KPSGD
