TBC8B_MOUSE
ID TBC8B_MOUSE Reviewed; 1114 AA.
AC A3KGB4; B9EJW4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=TBC1 domain family member 8B;
GN Name=Tbc1d8b;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in vesicular recycling, probably as a RAB11B GTPase-
CC activating protein. {ECO:0000250|UniProtKB:Q0IIM8}.
CC -!- SUBUNIT: Interacts (via domain Rab-GAP TBC) with RAB11B (in GTP-bound
CC form). {ECO:0000250|UniProtKB:Q0IIM8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q0IIM8}.
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250|UniProtKB:Q96BZ9}.
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DR EMBL; AL672243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147581; AAI47582.1; -; mRNA.
DR CCDS; CCDS41146.1; -.
DR RefSeq; NP_001074968.1; NM_001081499.2.
DR AlphaFoldDB; A3KGB4; -.
DR SMR; A3KGB4; -.
DR BioGRID; 232816; 4.
DR STRING; 10090.ENSMUSP00000094036; -.
DR iPTMnet; A3KGB4; -.
DR PhosphoSitePlus; A3KGB4; -.
DR EPD; A3KGB4; -.
DR jPOST; A3KGB4; -.
DR MaxQB; A3KGB4; -.
DR PaxDb; A3KGB4; -.
DR PeptideAtlas; A3KGB4; -.
DR PRIDE; A3KGB4; -.
DR ProteomicsDB; 263075; -.
DR Antibodypedia; 15056; 29 antibodies from 11 providers.
DR Ensembl; ENSMUST00000096313; ENSMUSP00000094036; ENSMUSG00000042473.
DR GeneID; 245638; -.
DR KEGG; mmu:245638; -.
DR UCSC; uc009ukj.2; mouse.
DR CTD; 54885; -.
DR MGI; MGI:1918101; Tbc1d8b.
DR VEuPathDB; HostDB:ENSMUSG00000042473; -.
DR eggNOG; KOG4347; Eukaryota.
DR GeneTree; ENSGT00940000159451; -.
DR HOGENOM; CLU_003535_0_2_1; -.
DR InParanoid; A3KGB4; -.
DR OMA; GTKFAMW; -.
DR OrthoDB; 450360at2759; -.
DR PhylomeDB; A3KGB4; -.
DR TreeFam; TF313145; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 245638; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Tbc1d8b; mouse.
DR PRO; PR:A3KGB4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A3KGB4; protein.
DR Bgee; ENSMUSG00000042473; Expressed in vault of skull and 205 other tissues.
DR Genevisible; A3KGB4; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0003094; P:glomerular filtration; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd13350; PH-GRAM1_TBC1D8B; 1.
DR CDD; cd13352; PH-GRAM2_TBC1D8B; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR036012; TBC1D8B_PH-GRAM1.
DR InterPro; IPR036015; TBC1D8B_PH-GRAM2.
DR Pfam; PF02893; GRAM; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Reference proteome; Repeat.
FT CHAIN 1..1114
FT /note="TBC1 domain family member 8B"
FT /id="PRO_0000337184"
FT DOMAIN 145..212
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 285..353
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT DOMAIN 486..673
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 857..892
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 399..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 533
FT /note="Arginine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
FT SITE 572
FT /note="Glutamine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
SQ SEQUENCE 1114 AA; 127893 MW; 38EFAD9B55420628 CRC64;
MWLKPEEVLL KNALKLWLME RSNEYFVLQR RRGYGEEGGG GLTGLLVGTL DSVLDSTAKV
APFRILHQTP DSQVYLSIAC GANREEITKH WDWLEQNIMK TLSVFDSNED ITNFVQGKIR
GLIAEEGKQS FAKEDDPEKF REALLKFEKS FGLPEQEKLV TYYSCSYWRG RVPCQGWLYL
STNFLSFYSF LLGSEIKLII SWDAISKLEK TSTVILTESI HVCSQGENHY FSMFLHINET
YLLMEQLANY AIKRLFDKET FDNDPVLDDP LQITKRGLEY RAHSEQFKAF FRLPKEETLK
EVHECFLWVP FSHFSSHGKM CISENYICFA SQDGNLCSVI IPLREVLAID KTDDSNRSVI
ISIKGKTAFR FSELKDFEQL VAKLRLKCRA ASTQDDVSTE VAVSSDSTGP SENFEEQPLT
CPKECSKTVN TEALMTVFHP QNLENLDSKM LKEKMKEQSW NILFSECGRG VSMFRTKKTR
DLVVRGIPET LRGELWMLFS GAVNDMATNP GYYAEVVEQS LGTSNLATEE IERDLRRSLP
EHPAFQSDTG ISALRRVLTA YAYRNPKIGY CQAMNILTSV LLLYAKEEEA FWLLVAVCER
MLPDYFNRRI IGALVDQAVF EELIRDHLPQ LTDHMTDMTF FSSVSLSWFL TLFISVLPIE
SAVNVVDCFF YDGIKAILQL GLAILDYNLD KLLTCKDDAE AVTALNRFFD NVINKDSPLP
SNVQQGSNIS NEKSDHTKVD ITDLIKESNE KYGSIRYEDI HSMRCRNRLY VIQTLEETTK
QNVLRVVSQD VKMSLQELDE LYVIFKKELF ISCYWYLSCP GLKHHDPSLP YLEQYQIDCQ
QFRVLYHLLS PWAHSANRDS LALWTFRLLD ENSDCLINFK EFSSAIDIMY NGSFTDKLKL
LFKLHIPPAY TEVMSKTSSK GDELSTEELL YFSQLQVSKP ADEKETESGR NSPEKGKGKI
DIQAYLSQWQ DELLKKEETI KDLPRMNQSQ FIQFSKTLYN LFHEDPEEES LYQAIAIVTN
LLLRMEEVGR KLHSPASSAS TARDSGPSEG NAESSVKKDL PSPREEHQWS FAFEQILASL
LNEPALVRFF ERPLDLKAKL ENAKSSQLRS RTKM
