IFT25_MOUSE
ID IFT25_MOUSE Reviewed; 143 AA.
AC Q9D6H2; Q3TZR2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Intraflagellar transport protein 25 homolog;
DE AltName: Full=Heat shock protein beta-11;
DE Short=Hspb11;
DE AltName: Full=Placental protein 25;
DE Short=PP25;
GN Name=Hspb11; Synonyms=Ift25;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, and Spleen;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION IN THE IFT COMPLEX B, INTERACTION WITH IFT88, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19253336; DOI=10.1002/cm.20346;
RA Follit J.A., Xu F., Keady B.T., Pazour G.J.;
RT "Characterization of mouse IFT complex B.";
RL Cell Motil. Cytoskeleton 66:457-468(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22595669; DOI=10.1016/j.devcel.2012.04.009;
RA Keady B.T., Samtani R., Tobita K., Tsuchya M., San Agustin J.T.,
RA Follit J.A., Jonassen J.A., Subramanian R., Lo C.W., Pazour G.J.;
RT "IFT25 links the signal-dependent movement of Hedgehog components to
RT intraflagellar transport.";
RL Dev. Cell 22:940-951(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP IFT27.
RX PubMed=28430876; DOI=10.1093/biolre/iox029;
RA Liu H., Li W., Zhang Y., Zhang Z., Shang X., Zhang L., Zhang S., Li Y.,
RA Somoza A.V., Delpi B., Gerton G.L., Foster J.A., Hess R.A., Pazour G.J.,
RA Zhang Z.;
RT "IFT25, an intraflagellar transporter protein dispensable for ciliogenesis
RT in somatic cells, is essential for sperm flagella formation.";
RL Biol. Reprod. 96:993-1006(2017).
RN [8]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28964737; DOI=10.1016/j.ydbio.2017.09.023;
RA Zhang Y., Liu H., Li W., Zhang Z., Shang X., Zhang D., Li Y., Zhang S.,
RA Liu J., Hess R.A., Pazour G.J., Zhang Z.;
RT "Intraflagellar transporter protein (IFT27), an IFT25 binding partner, is
RT essential for male fertility and spermiogenesis in mice.";
RL Dev. Biol. 432:125-139(2017).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29626631; DOI=10.1016/j.mod.2018.04.001;
RA Desai P.B., San Agustin J.T., Stuck M.W., Jonassen J.A., Bates C.M.,
RA Pazour G.J.;
RT "Ift25 is not a cystic kidney disease gene but is required for early steps
RT of kidney development.";
RL Mech. Dev. 151:10-17(2018).
CC -!- FUNCTION: Component of the IFT complex B required for sonic
CC hedgehog/SHH signaling. May mediate transport of SHH components:
CC required for the export of SMO and PTCH1 receptors out of the cilium
CC and the accumulation of GLI2 at the ciliary tip in response to
CC activation of the SHH pathway, suggesting it is involved in the dynamic
CC transport of SHH signaling molecules within the cilium. Not required
CC for ciliary assembly (PubMed:22595669). Its role in intraflagellar
CC transport is mainly seen in tissues rich in ciliated cells such as
CC kidney and testis. Essential for male fertility, spermiogenesis and
CC sperm flagella formation (PubMed:28430876). Plays a role in the early
CC development of the kidney (PubMed:29626631). May be involved in the
CC regulation of ureteric bud initiation (PubMed:29626631).
CC {ECO:0000269|PubMed:22595669, ECO:0000269|PubMed:28430876,
CC ECO:0000269|PubMed:29626631}.
CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT80, IFT81, and IFT88 (PubMed:19253336). Interacts with IFT27
CC (PubMed:28430876). Interacts with IFT88 (PubMed:19253336).
CC {ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:28430876}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:19253336}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the testis (at protein
CC level). {ECO:0000269|PubMed:28430876, ECO:0000269|PubMed:28964737}.
CC -!- DISRUPTION PHENOTYPE: Null mutants retain the ability to ciliate and
CC survive through gestation. They die shortly after birth due to
CC different phenotypes reminiscent of Shh signaling defects: polydactyly,
CC cleft palate, lung isomerisms, and structural heart defects
CC (PubMed:22595669). Conditional knockout in male germ cells results in
CC infertility, abnormal sperm morphology, significantly reduced sperm
CC count and sperm mobility and disruption of sperm lipid rafts
CC (PubMed:28964737, PubMed:28430876). Mutant mice with germline deletion
CC of HSPB11 die shortly after birth with structural defects in most
CC organs including the kidneys, where duplicated collecting duct system
CC and/or duplex kidney is often observed (PubMed:29626631).
CC {ECO:0000269|PubMed:22595669, ECO:0000269|PubMed:28430876,
CC ECO:0000269|PubMed:28964737, ECO:0000269|PubMed:29626631}.
CC -!- SIMILARITY: Belongs to the IFT25 family. {ECO:0000305}.
CC -!- CAUTION: Was initially classified as a member of the small heat shock
CC family protein. However, it was later shown that it is not the case
CC (PubMed:22595669). {ECO:0000305|PubMed:22595669}.
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DR EMBL; AK013636; BAB28934.1; -; mRNA.
DR EMBL; AK157651; BAE34145.1; -; mRNA.
DR EMBL; AL645723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466527; EDL30781.1; -; Genomic_DNA.
DR EMBL; CH466527; EDL30782.1; -; Genomic_DNA.
DR EMBL; CH466527; EDL30783.1; -; Genomic_DNA.
DR CCDS; CCDS18435.1; -.
DR RefSeq; NP_082670.1; NM_028394.2.
DR RefSeq; XP_006503487.1; XM_006503424.3.
DR RefSeq; XP_006503488.1; XM_006503425.1.
DR RefSeq; XP_006503489.1; XM_006503426.2.
DR AlphaFoldDB; Q9D6H2; -.
DR SMR; Q9D6H2; -.
DR BioGRID; 215658; 2.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR STRING; 10090.ENSMUSP00000048810; -.
DR PhosphoSitePlus; Q9D6H2; -.
DR EPD; Q9D6H2; -.
DR MaxQB; Q9D6H2; -.
DR PaxDb; Q9D6H2; -.
DR PeptideAtlas; Q9D6H2; -.
DR PRIDE; Q9D6H2; -.
DR ProteomicsDB; 267112; -.
DR Antibodypedia; 33127; 85 antibodies from 21 providers.
DR Ensembl; ENSMUST00000046558; ENSMUSP00000048810; ENSMUSG00000063172.
DR Ensembl; ENSMUST00000106749; ENSMUSP00000102360; ENSMUSG00000063172.
DR Ensembl; ENSMUST00000152717; ENSMUSP00000118617; ENSMUSG00000063172.
DR GeneID; 72938; -.
DR KEGG; mmu:72938; -.
DR UCSC; uc008tzn.1; mouse.
DR CTD; 51668; -.
DR MGI; MGI:1920188; Hspb11.
DR VEuPathDB; HostDB:ENSMUSG00000063172; -.
DR eggNOG; KOG3437; Eukaryota.
DR GeneTree; ENSGT00390000012620; -.
DR HOGENOM; CLU_132151_0_0_1; -.
DR InParanoid; Q9D6H2; -.
DR OMA; EHTEGHL; -.
DR OrthoDB; 1454920at2759; -.
DR PhylomeDB; Q9D6H2; -.
DR TreeFam; TF336031; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 72938; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Hspb11; mouse.
DR PRO; PR:Q9D6H2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D6H2; protein.
DR Bgee; ENSMUSG00000063172; Expressed in saccule of membranous labyrinth and 259 other tissues.
DR Genevisible; Q9D6H2; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IC:ComplexPortal.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IC:MGI.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR033558; IFT25.
DR PANTHER; PTHR33906; PTHR33906; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Cilium; Differentiation; Metal-binding;
KW Protein transport; Reference proteome; Spermatogenesis; Stress response;
KW Transport.
FT CHAIN 1..143
FT /note="Intraflagellar transport protein 25 homolog"
FT /id="PRO_0000058532"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CONFLICT 74
FT /note="I -> T (in Ref. 1; BAB28934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 143 AA; 16281 MW; C05B1E8A496DB5EC CRC64;
MRKVDLCSVT EGTEVILATS SDEKHPPENI IDGNPETFWT TTGMFPQEFI ICFHKHVKIE
KLVIQSYLVR TLRIEKTTSK EPLDFEQWVE KDLVHTEGQL QNEEIVARDG YATFLRFIIV
SAFDHFASVH SISAEGLTVS SLP
