TBC23_PONAB
ID TBC23_PONAB Reviewed; 684 AA.
AC Q5R8I6; Q5R8W3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=TBC1 domain family member 23;
GN Name=TBC1D23;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative Rab GTPase-activating protein which plays a role in
CC vesicular trafficking. Involved in endosome-to-Golgi trafficking. Acts
CC as a bridging protein by binding simultaneously to golgins, including
CC GOLGA1 and GOLGA4, located at the trans-Golgi, and to the WASH complex,
CC located on endosome-derived vesicles. Together with WDR11 complex
CC facilitates the golgin-mediated capture of vesicles generated using AP-
CC 1 (By similarity). Plays a role in brain development, including in
CC cortical neuron positioning (By similarity). May also be important for
CC neurite outgrowth, possibly through its involvement in membrane
CC trafficking and cargo delivery, 2 processes that are essential for
CC axonal and dendritic growth (By similarity). May act as a general
CC inhibitor of innate immunity signaling, strongly inhibiting multiple
CC TLR and dectin/CLEC7A-signaling pathways. Does not alter initial
CC activation events, but instead affects maintenance of inflammatory gene
CC expression several hours after bacterial lipopolysaccharide (LPS)
CC challenge (By similarity). {ECO:0000250|UniProtKB:Q8K0F1,
CC ECO:0000250|UniProtKB:Q9NUY8}.
CC -!- SUBUNIT: Directly interacts with GOLGA1 and GOLGA4. Interacts with
CC FAM91A1, C17ORF75 and WDR11; the interaction recruits TBC1D23 to AP-1-
CC derived vesicles. Directly interacts with WASHC1 and WASHC2A/FAM21A.
CC Interacts with FKBP15. {ECO:0000250|UniProtKB:Q9NUY8}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9NUY8}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9NUY8}. Note=Localization to the trans-Golgi is
CC regulated by ARL1 and ARL5B/ARL8. ARL1 increases Golgi localization,
CC while ARL5B decreases it. Recruitment to the trans-Golgi network
CC requires the presence of GOLGA1 and GOLGA4, but not that of FAM91A1.
CC Recruited on AP-1-derived vesicles by WDR11 complex.
CC {ECO:0000250|UniProtKB:Q9NUY8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R8I6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R8I6-2; Sequence=VSP_025522;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91797.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR859635; CAH91797.1; ALT_FRAME; mRNA.
DR EMBL; CR859766; CAH91924.1; -; mRNA.
DR RefSeq; NP_001128947.1; NM_001135475.1. [Q5R8I6-1]
DR AlphaFoldDB; Q5R8I6; -.
DR SMR; Q5R8I6; -.
DR STRING; 9601.ENSPPYP00000015209; -.
DR GeneID; 100189910; -.
DR KEGG; pon:100189910; -.
DR CTD; 55773; -.
DR eggNOG; KOG3636; Eukaryota.
DR InParanoid; Q5R8I6; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR GO; GO:0099041; P:vesicle tethering to Golgi; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR039755; TBC1D23.
DR InterPro; IPR045799; TBC1D23_C.
DR PANTHER; PTHR13297; PTHR13297; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF19430; TBC1D23_C; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Developmental protein;
KW Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..684
FT /note="TBC1 domain family member 23"
FT /id="PRO_0000287499"
FT DOMAIN 44..225
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 334..446
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 459..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..684
FT /note="May mediate the interaction with WASHC1"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT REGION 514..558
FT /note="May mediate the interaction with C17orf75, FAM91A1
FT and WDR11"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT REGION 559..684
FT /note="May mediate the interaction with FKBP15 and WASHC2;
FT required for endosome to Golgi trafficking"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUY8"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0F1"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUY8"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUY8"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUY8"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUY8"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025522"
FT CONFLICT 502
FT /note="W -> R (in Ref. 1; CAH91797)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="D -> H (in Ref. 1; CAH91797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 76559 MW; 9BBFE54D1E1C5279 CRC64;
MAEGEDVLPL PTSSGDGWEK DLEEALEAGG CDLETLRNII QGRPLPADLR AKVWKIALNV
AGKGDSLASW DGILDLPEQN TIHKDCLQFI DQLSVPEEKA AELLLDIESV ITFYCKSRNI
KYSTSLSWIH LLKPLVHLQL PRSDLYNCFY AIMNKYIPRD CSQKGRPFHL FRLLIQYHEP
ELCSYLDTKK ITPDSYALNW LGSLFACYCS IEVTQAIWDG YLQQADPFFI YFLMLIILVN
AKEVILTQES DSKEEVIQFL ENTPSSLNIE DIEDLFSLAQ YYCSKTPASF RKDNHHLFGS
TLLGIKDDDA DLSQALCLAI SVSEILQANQ LQGEGVRFFV VDCRPAEQYN AGHLSTAFHL
DSDLMLQNPS EFAQSVKSLL EAQKQSIESG SIAGGEHLCF MGSGREEEDM YMNMVLAHFL
QKNKEYVSIA SGGFMALQQH LADINVDGPE NGYGHWIAST SGSRSSINSV DGESPNGSSD
RGMKSLVNKM TVALKTKSVN VWEKVISFIE NTSTPVDRHV SSSDRVGKPY RGVKPVFSIG
DEEEYDTDEI DSSSMSDDDR KEVVNIQTWI NKPDVKHHFP CKEVKESGHM FPSHLLVTAT
HMYCLREIVS RKGLAYIQSR QALNSVVKIT SKKKHPELIT FKYGNSSASG IEILAIERYL
IPNAGDATKA IKQQIMKVLD ALES
