PTHB1_CAEEL
ID PTHB1_CAEEL Reviewed; 744 AA.
AC O01514;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 5.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein pthb1 homolog {ECO:0000305};
DE AltName: Full=Bardet-Biedl syndrome 9 protein homolog {ECO:0000312|WormBase:C48B6.8};
GN Name=bbs-9 {ECO:0000312|WormBase:C48B6.8};
GN ORFNames=C48B6.8 {ECO:0000312|WormBase:C48B6.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22022287; DOI=10.1371/journal.pgen.1002335;
RA Mok C.A., Healey M.P., Shekhar T., Leroux M.R., Heon E., Zhen M.;
RT "Mutations in a guanylate cyclase GCY-35/GCY-36 modify Bardet-Biedl
RT syndrome-associated phenotypes in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002335-E1002335(2011).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BBS-1, AND DISRUPTION PHENOTYPE.
RX PubMed=22922713; DOI=10.1038/ncb2560;
RA Wei Q., Zhang Y., Li Y., Zhang Q., Ling K., Hu J.;
RT "The BBSome controls IFT assembly and turnaround in cilia.";
RL Nat. Cell Biol. 14:950-957(2012).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30014846; DOI=10.7554/elife.36833;
RA Hao Y., Yang W., Ren J., Hall Q., Zhang Y., Kaplan J.M.;
RT "Thioredoxin shapes the C. elegans sensory response to Pseudomonas produced
RT nitric oxide.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Component of the BBSome complex (By similarity). The BBSome
CC complex is thought to function as a coat complex required for sorting
CC of specific membrane proteins to the primary cilia (By similarity). The
CC BBSome complex is required for ciliogenesis but is dispensable for
CC centriolar satellite function (By similarity). Required for proper
CC BBSome complex assembly and its ciliary localization (PubMed:22922713).
CC Required for cilia biogenesis and both the assembly and movement of
CC intraflagellar transport proteins along the ciliary axoneme
CC (PubMed:22022287, PubMed:22922713). In ciliated sensory neurons,
CC required for the sensation of nitric oxide and avoidance of NO-
CC producing organisms like P.aeruginosa (PubMed:30014846).
CC {ECO:0000250|UniProtKB:Q3SYG4, ECO:0000269|PubMed:22022287,
CC ECO:0000269|PubMed:22922713, ECO:0000269|PubMed:30014846}.
CC -!- SUBUNIT: Part of BBSome complex, that contains bbs-1, bbs-2, bbs-4,
CC bbs-5, osm-12, bbs-8/ttc-8 and bbs-9 (By similarity). Interacts with
CC bbs-1 (PubMed:22922713). {ECO:0000250|UniProtKB:Q3SYG4,
CC ECO:0000269|PubMed:22922713}.
CC -!- DISRUPTION PHENOTYPE: Mutants have normal body morphology, but with
CC reduced body length and width, delayed larval development and decreased
CC roaming movements (PubMed:22022287). Defective cilia structure and
CC function characterized by an increased accumulation and mislocalization
CC of intraflagellar transport proteins and impaired movement of
CC intraflagellar transport proteins along the ciliary axoneme
CC (PubMed:22922713). Disrupted assembly of the BBSome complex at the base
CC of the cilia (PubMed:22922713). Defective avoidance of nitric oxide and
CC P.aeruginosa (PubMed:30014846). {ECO:0000269|PubMed:22022287,
CC ECO:0000269|PubMed:22922713, ECO:0000269|PubMed:30014846}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284601; CCD67585.2; -; Genomic_DNA.
DR RefSeq; NP_491973.4; NM_059572.4.
DR AlphaFoldDB; O01514; -.
DR SMR; O01514; -.
DR ComplexPortal; CPX-428; BBSome complex.
DR DIP; DIP-61856N; -.
DR IntAct; O01514; 2.
DR STRING; 6239.C48B6.8; -.
DR EPD; O01514; -.
DR PaxDb; O01514; -.
DR EnsemblMetazoa; C48B6.8.1; C48B6.8.1; WBGene00016744.
DR GeneID; 183572; -.
DR KEGG; cel:CELE_C48B6.8; -.
DR UCSC; C48B6.8; c. elegans.
DR CTD; 183572; -.
DR WormBase; C48B6.8; CE46977; WBGene00016744; bbs-9.
DR eggNOG; KOG3679; Eukaryota.
DR GeneTree; ENSGT00390000000803; -.
DR HOGENOM; CLU_019585_0_0_1; -.
DR InParanoid; O01514; -.
DR OMA; VPVEDWT; -.
DR OrthoDB; 332152at2759; -.
DR PhylomeDB; O01514; -.
DR Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:O01514; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00016744; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0034464; C:BBSome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR028074; PHTB1_C_dom.
DR InterPro; IPR028073; PHTB1_N_dom.
DR InterPro; IPR026511; PTHB1.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR20991; PTHR20991; 1.
DR Pfam; PF14728; PHTB1_C; 1.
DR Pfam; PF14727; PHTB1_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..744
FT /note="Protein pthb1 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435000"
FT REGION 722..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 83047 MW; 7EC492B884500D7D CRC64;
MSLFRLVEWV SQTIPNTSTI LNASFFQDRE QLVIGGENGQ ITISDPGFRD TNAHVLCTTE
TKYAILQMAS DNFLPSMNNI LAVLSPTKLT YYKVHFASPD ETLASLDEIF SHSFSTSAWN
MCVIPIEEST PQILVQSIDC KLSLFQGDQC VFSMVPLRAL QPGPIGYCQT TQTLFVANNG
FLAAIKFSLM SSGSQKKINY DWSFNLGDTA IQMKVTEGSK PTTIVLCRRH VSAFNATGSV
VWQIRLEAVG MAMCLYRSLL INNTQFNRLI VSTSDDTLLI FQDNKLVWNC NAQMSPVALL
VCSYNKSYEN TITMMAPDGK VVVGYLGTEP NLYRLPEDKV IVNYAERMEE YKRMEQKIKE
SDAAGGAIKR KEGIQMKLSI GEIGKRTIEP NAASNAPYCN LIVEFSEVQN VSKLHINILS
ECASPSKQVI LNVGTSKSTA SIEIPFYVGS KKSPTSNKVT IAAHCAFTQL TVTKSIDLPF
KVLFEESQID RNAKYKVTID TAGSVMPLNK LFSEFESENP QAIGFSLHGS DKTVSVFAAN
KSNRYRIQSE HISLLQITSR ELVKRIAESA PGIEIGGVIP FEYMRETLDE IQELQTKKKE
DSKKIDCRTK EVRAIEALSL NSCKTGNMGN LPSLDALFDK SYRELLDAMD SYNSLTAKIE
NQKASLNSLF QLAADLSKLS KVDTILNGSF WANTQQSLRD RLRWAVKTDR GNEMTMIEKL
CEHSPKELPK IREEEEEEEQ QVTA
