TBC8B_DANRE
ID TBC8B_DANRE Reviewed; 1108 AA.
AC B0R0W9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=TBC1 domain family member 8B;
GN Name=tbc1d8b; ORFNames=si:dkey-110k5.6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30661770; DOI=10.1016/j.ajhg.2018.12.016;
RA Dorval G., Kuzmuk V., Gribouval O., Welsh G.I., Bierzynska A., Schmitt A.,
RA Miserey-Lenkei S., Koziell A., Haq S., Benmerah A., Mollet G., Boyer O.,
RA Saleem M.A., Antignac C.;
RT "TBC1D8B Loss-of-Function Mutations Lead to X-Linked Nephrotic Syndrome via
RT Defective Trafficking Pathways.";
RL Am. J. Hum. Genet. 104:348-355(2019).
CC -!- FUNCTION: Involved in vesicular recycling, probably as a GTPase-
CC activating protein for Rab family protein(s).
CC {ECO:0000250|UniProtKB:Q0IIM8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q0IIM8}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic neural tube, brain,
CC pectoral fins and the pronephric glomerulus (at protein level).
CC {ECO:0000269|PubMed:30661770}.
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}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC pericardial edema, retracted glomerulus in an enlarged Bowman's capsule
CC and glomerular permeability defects. {ECO:0000269|PubMed:30661770}.
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DR EMBL; AL929305; CAQ13286.1; -; Genomic_DNA.
DR RefSeq; NP_001120987.1; NM_001127515.1.
DR AlphaFoldDB; B0R0W9; -.
DR SMR; B0R0W9; -.
DR STRING; 7955.ENSDARP00000084038; -.
DR PaxDb; B0R0W9; -.
DR PeptideAtlas; B0R0W9; -.
DR PRIDE; B0R0W9; -.
DR Ensembl; ENSDART00000135153; ENSDARP00000121850; ENSDARG00000062192.
DR GeneID; 566657; -.
DR KEGG; dre:566657; -.
DR CTD; 54885; -.
DR ZFIN; ZDB-GENE-030131-3135; tbc1d8b.
DR eggNOG; KOG4347; Eukaryota.
DR GeneTree; ENSGT00940000159451; -.
DR HOGENOM; CLU_003535_0_1_1; -.
DR InParanoid; B0R0W9; -.
DR OMA; GTKFAMW; -.
DR OrthoDB; 450360at2759; -.
DR PhylomeDB; B0R0W9; -.
DR Reactome; R-DRE-432722; Golgi Associated Vesicle Biogenesis.
DR PRO; PR:B0R0W9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000062192; Expressed in brain and 24 other tissues.
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; IMP: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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; GTPase activation; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1108
FT /note="TBC1 domain family member 8B"
FT /id="PRO_0000337185"
FT DOMAIN 143..210
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 283..351
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT DOMAIN 469..656
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 822..857
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 961..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 835
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 837
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 839
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 846
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 516
FT /note="Arginine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
FT SITE 555
FT /note="Glutamine finger"
FT /evidence="ECO:0000250|UniProtKB:Q96BZ9"
SQ SEQUENCE 1108 AA; 126737 MW; 688F0BF09B9DEC34 CRC64;
MWLKPEEVLL KNALKLWVTE KSNDYFVLQR RRGYGEDSGG LTGLLVGTLD TVLDSTAKVA
PFRILHQTPD SQVYWTIACG ASLEEISQHW DWLQQNIVRT LSVFDSGEDI TSFVQGKIRG
LIAEEGTSAG DEEDPERFRE AVLRFERLFG LPQREKLVTY FSCSYWRGRV PNQGWIYLST
NFLCFYSYML GNEVKLVYPW DEVSRLERTS SVLLAESIRV RVRGEDHFFS MLLRLQQTYL
IMQQLADYAI VRFFDKETFH AEHPLANPLH ITQRALEIHA RNQSFRSFFR LPQEENLCEV
YESFLWVPFS HVNTLGKICV SENYLCFASQ DGSQCHLIIP LWEVFSVELP DRSSRALTVC
LRGKRALRFS EVRDFERLAA TIRRKCGTLG SPQHCITNPD EEGVMVGQSQ AVSTEALMNV
FHPHDAENLD PKMLKERMKE QSWQIHFAEY GRGTGMFCTK KTRDLIVRGV PETLRGELWM
LFSGAVHDMI SHPGYYGRLL EDCMGSSSLA CDEIERDLHR SLPEHPAFQS DTGISALRRV
LTAYAHRNPK IGYCQAMNIL TSVLLLYAKE EEAFWLLVAV CERMLPDYFN RRIIGALVDQ
AVFEELIREH LTQLTEHMTD LSFFSSVSLS WFLTLFISVL PIESAVNVVD CFFYDGIKAI
LQLGLAVLDY NMDNLLCCND DAEAVTVLNR FFDSVTNKDS PLPATVQQAS ATANDKSIQK
VDISDLIKEA YEKYGDIRTE EVENMRKRNK LYVIQTLEDT TKQNVLRVVA QDVKFSASQL
DELYLLFKNH DPSLPYLDQY QLDQSQFSSL FNLLQPWTTH THSRSLARSA FHLLDENGDG
LVNFKEFICG LDILYNRSFT EKLKLLFKLH LQPDSAEDGV IRKCPERGRA KVDLQEYLKQ
WQEDLQRREE NIKDLPRINQ VQFISLTKTL YSVFHGDEEE ESLYRAVARV TSLLLRMEEV
GRKLQDSSPQ KTPQTTPTST SQPESSPTKP TSPESETPAE SRSTHDQPES PVSQHETAPS
HSDITPNSTS HPSTPTSSPT ETSSPVLDTP TDTPSSPCTV RDGDWSFSFE QILASLLNEP
SVVRFFERVV NTDTLITRAR KNQLKDAH
