ID   PTHB1_MOUSE             Reviewed;         885 AA.
AC   Q811G0; P97498; Q3UMR2; Q7TQH9; Q8BKD7; Q8K0T5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Protein PTHB1;
DE   AltName: Full=Bardet-Biedl syndrome 9 protein homolog;
DE   AltName: Full=Parathyroid hormone-responsive B1 gene protein homolog;
GN   Name=Bbs9; Synonyms=Pthb1;
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 MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 105-885 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 667-885.
RC   TISSUE=Fetus;
RA   Keen T.J.;
RT   "Positional candidates for the RP9 retinitis pigmentosa gene.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
RN   [5]
RP   INTERACTION WITH LZTL1, AND IDENTIFICATION IN THE BBSOME COMPLEX.
RX   PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
RA   Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
RA   Sheffield V.C.;
RT   "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and
RT   Smoothened.";
RL   PLoS Genet. 7:E1002358-E1002358(2011).
CC   -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC       required for sorting of specific membrane proteins to the primary
CC       cilia. The BBSome complex is required for ciliogenesis but is
CC       dispensable for centriolar satellite function. This ciliogenic function
CC       is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC       localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC       the primary cilium and promotes extension of the ciliary membrane.
CC       Firstly the BBSome associates with the ciliary membrane and binds to
CC       RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC       Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC       carrier vesicles to the base of the ciliary membrane. Required for
CC       proper BBSome complex assembly and its ciliary localization (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC       BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with LZTL1; the interaction
CC       mediates the association of LZTL1 with the BBsome complex and regulates
CC       BBSome ciliary trafficking. {ECO:0000269|PubMed:22072986}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}.
CC       Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriolar satellite {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q811G0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q811G0-2; Sequence=VSP_018430;
CC       Name=3;
CC         IsoId=Q811G0-3; Sequence=VSP_018429, VSP_018431, VSP_018432;
CC       Name=4;
CC         IsoId=Q811G0-4; Sequence=VSP_018429;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30419.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK053503; BAC35408.1; -; mRNA.
DR   EMBL; AK144730; BAE26036.1; -; mRNA.
DR   EMBL; BC030419; AAH30419.1; ALT_INIT; mRNA.
DR   EMBL; BC046426; AAH46426.1; -; mRNA.
DR   EMBL; BC054441; AAH54441.1; -; mRNA.
DR   EMBL; U85993; AAB61920.1; -; mRNA.
DR   CCDS; CCDS22928.1; -. [Q811G0-2]
DR   CCDS; CCDS90520.1; -. [Q811G0-1]
DR   RefSeq; NP_848502.1; NM_178415.1. [Q811G0-2]
DR   RefSeq; NP_851833.2; NM_181316.4. [Q811G0-2]
DR   RefSeq; XP_006510478.1; XM_006510415.3.
DR   RefSeq; XP_006510479.1; XM_006510416.3. [Q811G0-1]
DR   RefSeq; XP_006510480.1; XM_006510417.3. [Q811G0-1]
DR   RefSeq; XP_006510481.1; XM_006510418.3. [Q811G0-1]
DR   RefSeq; XP_006510482.1; XM_006510419.3.
DR   AlphaFoldDB; Q811G0; -.
DR   SMR; Q811G0; -.
DR   BioGRID; 235567; 1.
DR   ComplexPortal; CPX-1909; BBSome complex.
DR   IntAct; Q811G0; 5.
DR   STRING; 10090.ENSMUSP00000122058; -.
DR   GlyGen; Q811G0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q811G0; -.
DR   PhosphoSitePlus; Q811G0; -.
DR   SwissPalm; Q811G0; -.
DR   EPD; Q811G0; -.
DR   MaxQB; Q811G0; -.
DR   PaxDb; 10090-ENSMUSP00000116629; -.
DR   ProteomicsDB; 291621; -. [Q811G0-1]
DR   ProteomicsDB; 291622; -. [Q811G0-2]
DR   ProteomicsDB; 291623; -. [Q811G0-3]
DR   ProteomicsDB; 291624; -. [Q811G0-4]
DR   Antibodypedia; 12805; 192 antibodies from 23 providers.
DR   DNASU; 319845; -.
DR   Ensembl; ENSMUST00000039798.16; ENSMUSP00000043042.10; ENSMUSG00000035919.17. [Q811G0-2]
DR   Ensembl; ENSMUST00000147405.8; ENSMUSP00000120927.2; ENSMUSG00000035919.17. [Q811G0-1]
DR   Ensembl; ENSMUST00000147712.8; ENSMUSP00000122058.2; ENSMUSG00000035919.17. [Q811G0-2]
DR   Ensembl; ENSMUST00000150395.8; ENSMUSP00000116629.2; ENSMUSG00000035919.17. [Q811G0-2]
DR   GeneID; 319845; -.
DR   KEGG; mmu:319845; -.
DR   UCSC; uc009oor.1; mouse. [Q811G0-2]
DR   UCSC; uc009oou.1; mouse. [Q811G0-1]
DR   UCSC; uc009oov.1; mouse. [Q811G0-3]
DR   UCSC; uc012gpo.1; mouse. [Q811G0-4]
DR   AGR; MGI:2442833; -.
DR   CTD; 27241; -.
DR   MGI; MGI:2442833; Bbs9.
DR   VEuPathDB; HostDB:ENSMUSG00000035919; -.
DR   eggNOG; KOG3679; Eukaryota.
DR   GeneTree; ENSGT00390000000803; -.
DR   HOGENOM; CLU_015674_1_0_1; -.
DR   InParanoid; Q811G0; -.
DR   OMA; VPVEDWT; -.
DR   OrthoDB; 5475689at2759; -.
DR   PhylomeDB; Q811G0; -.
DR   TreeFam; TF314513; -.
DR   Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR   BioGRID-ORCS; 319845; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Bbs9; mouse.
DR   PRO; PR:Q811G0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q811G0; Protein.
DR   Bgee; ENSMUSG00000035919; Expressed in spermatocyte and 248 other cell types or tissues.
DR   ExpressionAtlas; Q811G0; baseline and differential.
DR   GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR   GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR   GO; GO:0035869; C:ciliary transition zone; ISO:MGI.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0000242; C:pericentriolar material; ISO:MGI.
DR   GO; GO:0060271; P:cilium assembly; IMP:FlyBase.
DR   GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR   GO; GO:0061512; P:protein localization to cilium; ISO:MGI.
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   PANTHER; PTHR20991; PARATHYROID HORMONE-RESPONSIVE B1 GENE; 1.
DR   PANTHER; PTHR20991:SF0; PROTEIN PTHB1; 1.
DR   Pfam; PF14728; PHTB1_C; 1.
DR   Pfam; PF14727; PHTB1_N; 1.
DR   Genevisible; Q811G0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..885
FT                   /note="Protein PTHB1"
FT                   /id="PRO_0000235270"
FT   REGION          1..406
FT                   /note="Seven-bladed beta-propeller"
FT                   /evidence="ECO:0000250|UniProtKB:Q3SYG4"
FT   REGION          684..764
FT                   /note="Interaction with LZTL1"
FT                   /evidence="ECO:0000250"
FT   SITE            141
FT                   /note="Critical for protein stability"
FT                   /evidence="ECO:0000250|UniProtKB:Q3SYG4"
FT   VAR_SEQ         1..576
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018429"
FT   VAR_SEQ         512..516
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018430"
FT   VAR_SEQ         706..800
FT                   /note="IALADAIEENQDRLLQSFSGLKSATHLLILLIRLWQRLSADQTAILEAAFLP
FT                   LQEDTQELGWEETVDAAIAYLLKTCLSKSSKEQALNLSSQLNI -> SAMSGQMCVSTP
FT                   VSSFPRVRRQGTDICWTVGSGCVCDAFGVAYKYSFSSLFSQETTTCSQYLYDYNEDLGL
FT                   LVSSWVSTWDHYFVLKIILAVFTL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018431"
FT   VAR_SEQ         801..885
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018432"
FT   CONFLICT        325
FT                   /note="Q -> R (in Ref. 1; BAE26036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        885
FT                   /note="E -> V (in Ref. 1; BAE26036)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   885 AA;  99057 MW;  46C4580518630E36 CRC64;
     MSLFKARDWW STVLGEKEEF DQGCLCLADV DNSGNGHDKI IVGSFMGYLR IFSPHSVKAG
     GGPQAEDLLL EVHLRDPVLQ VEVGKFVSGT EMLHLAVLHS RKLCVYSVSG TLGNVEHGNQ
     YQIKLMYEHH LQRTACNMTY GPFGGVKGRD LICIQSLDGM LMVFEQESYA FGRFLPGFLL
     PGPLAYSPRT DSFITVSSCR QVESYKYQVL AFATDADKKQ EMEQQKLGSG KRLVVDWTLN
     IGEQALDICI FPLNQSASSV FVLGERNFFC LKDNGQIRFM KKLGYNPSCF LPYCSVSEGT
     INTLIGNHNH MLHIYQDVTL KWATQLPHVP VAVRVGCFHD LKGVIVTLSD DGHLQCSYLG
     TDPSLFQAPK VESRELNYDE LDVELKELQK IIKDVKLQGV WPLTEQEDDL KVSASVSSTL
     DSVSQATNVE PGADSVPSIT VKITLQNRVV LQKVKLSIYV QPPLQLTCDQ FTFDFTVPDM
     TSSVAFSVYL KRNYTPSELE GNAVVSYSRP TDRNPDGIPR VVQCKFRLPL KLICLPGQPS
     KTASHKLTID TNKSPVSLLG LFPDFANPSD DDQVNVMGFR LLGGARVTLL ASRTSQRYRI
     QSEQFEDLWL ITNELILRLQ EHFEKQGTKD FSCSFSGCVP LQEYFELIDH HFELRINGKK
     LEELLSERAV QFRAIQRRLL TRFRDKTPAP LQHLDTLLDG TYKQVIALAD AIEENQDRLL
     QSFSGLKSAT HLLILLIRLW QRLSADQTAI LEAAFLPLQE DTQELGWEET VDAAIAYLLK
     TCLSKSSKEQ ALNLSSQLNI PKDTSRLKKH ITLLCDRLAK GGRLCVSTDA AAPQAMVVPG
     GCTPIPESDL EERSLDDSTE LFTNHKHLMT EPPMPEVSAR QGVLE
//