IFT25_HUMAN
ID IFT25_HUMAN Reviewed; 144 AA.
AC Q9Y547; A6NG57; D3DQ45; Q9Y684;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 174.
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=C1orf41, IFT25; ORFNames=HSPC034;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bellyei S., Than N.G., Szigeti A., Sumegi B., Bohn H., Than G.N.;
RT "Isolation and sequence analysis of a cDNA encoding placental protein 25
RT (PP25).";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=2018407; DOI=10.1007/bf02390087;
RA Bohn H., Winckler W.;
RT "Isolation and characterization of five new soluble placental tissue
RT proteins (PP22, PP23, PP24, PP25, PP26).";
RL Arch. Gynecol. Obstet. 248:111-115(1991).
RN [8]
RP PHYLOGENETIC ANALYSIS.
RX PubMed=19921466; DOI=10.1007/s12192-009-0155-4;
RA Kappe G., Boelens W.C., de Jong W.W.;
RT "Why proteins without an alpha-crystallin domain should not be included in
RT the human small heat shock protein family HSPB.";
RL Cell Stress Chaperones 15:457-461(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP STRUCTURE BY NMR OF 1-144, AND X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF
RP 1-144.
RX PubMed=18816799; DOI=10.1002/prot.22229;
RA Ramelot T.A., Raman S., Kuzin A.P., Xiao R., Ma L.-C., Acton T.B.,
RA Hunt J.F., Montelione G.T., Baker D., Kennedy M.A.;
RT "Improving NMR protein structure quality by Rosetta refinement: a molecular
RT replacement study.";
RL Proteins 75:147-167(2009).
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. Its role in intraflagellar transport is mainly
CC seen in tissues rich in ciliated cells such as kidney and testis.
CC Essential for male fertility, spermiogenesis and sperm flagella
CC formation. Plays a role in the early development of the kidney. May be
CC involved in the regulation of ureteric bud initiation (By similarity).
CC {ECO:0000250|UniProtKB:Q9D6H2}.
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. Interacts with IFT27. Interacts with IFT88 (By
CC similarity). {ECO:0000250|UniProtKB:Q9D6H2}.
CC -!- INTERACTION:
CC Q9Y547; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-747101, EBI-739467;
CC Q9Y547; Q9BW83: IFT27; NbExp=20; IntAct=EBI-747101, EBI-747093;
CC Q9Y547; Q9Y6Y8: SEC23IP; NbExp=3; IntAct=EBI-747101, EBI-1767971;
CC Q9Y547; Q13114: TRAF3; NbExp=3; IntAct=EBI-747101, EBI-357631;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9D6H2}.
CC -!- TISSUE SPECIFICITY: Detected in placenta. {ECO:0000269|PubMed:2018407}.
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:19921466). {ECO:0000305|PubMed:19921466}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43011.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF416725; AAQ03618.1; -; mRNA.
DR EMBL; AF417114; AAQ03994.1; -; mRNA.
DR EMBL; AF100747; AAD43011.1; ALT_FRAME; mRNA.
DR EMBL; AL031427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06717.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06719.1; -; Genomic_DNA.
DR EMBL; BC005245; AAH05245.1; -; mRNA.
DR CCDS; CCDS41341.1; -.
DR RefSeq; NP_001303864.1; NM_001316935.1.
DR RefSeq; NP_057210.2; NM_016126.3.
DR PDB; 1TVG; X-ray; 1.60 A; A=1-143.
DR PDB; 1XPW; NMR; -; A=1-144.
DR PDBsum; 1TVG; -.
DR PDBsum; 1XPW; -.
DR AlphaFoldDB; Q9Y547; -.
DR BMRB; Q9Y547; -.
DR SMR; Q9Y547; -.
DR BioGRID; 119671; 23.
DR ComplexPortal; CPX-5022; IFT-B complex.
DR CORUM; Q9Y547; -.
DR IntAct; Q9Y547; 20.
DR MINT; Q9Y547; -.
DR STRING; 9606.ENSP00000194214; -.
DR iPTMnet; Q9Y547; -.
DR PhosphoSitePlus; Q9Y547; -.
DR BioMuta; HSPB11; -.
DR DMDM; 67460979; -.
DR EPD; Q9Y547; -.
DR jPOST; Q9Y547; -.
DR MassIVE; Q9Y547; -.
DR MaxQB; Q9Y547; -.
DR PaxDb; Q9Y547; -.
DR PeptideAtlas; Q9Y547; -.
DR PRIDE; Q9Y547; -.
DR ProteomicsDB; 86288; -.
DR Antibodypedia; 33127; 85 antibodies from 21 providers.
DR DNASU; 51668; -.
DR Ensembl; ENST00000194214.10; ENSP00000194214.5; ENSG00000081870.12.
DR GeneID; 51668; -.
DR KEGG; hsa:51668; -.
DR MANE-Select; ENST00000194214.10; ENSP00000194214.5; NM_016126.4; NP_057210.2.
DR UCSC; uc001cwh.4; human.
DR CTD; 51668; -.
DR DisGeNET; 51668; -.
DR GeneCards; HSPB11; -.
DR HGNC; HGNC:25019; HSPB11.
DR HPA; ENSG00000081870; Low tissue specificity.
DR neXtProt; NX_Q9Y547; -.
DR OpenTargets; ENSG00000081870; -.
DR PharmGKB; PA162391751; -.
DR VEuPathDB; HostDB:ENSG00000081870; -.
DR eggNOG; KOG3437; Eukaryota.
DR GeneTree; ENSGT00390000012620; -.
DR HOGENOM; CLU_132151_0_0_1; -.
DR InParanoid; Q9Y547; -.
DR OMA; EHTEGHL; -.
DR OrthoDB; 1454920at2759; -.
DR PhylomeDB; Q9Y547; -.
DR TreeFam; TF336031; -.
DR PathwayCommons; Q9Y547; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q9Y547; -.
DR BioGRID-ORCS; 51668; 9 hits in 1030 CRISPR screens.
DR ChiTaRS; HSPB11; human.
DR EvolutionaryTrace; Q9Y547; -.
DR GenomeRNAi; 51668; -.
DR Pharos; Q9Y547; Tbio.
DR PRO; PR:Q9Y547; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y547; protein.
DR Bgee; ENSG00000081870; Expressed in oocyte and 209 other tissues.
DR ExpressionAtlas; Q9Y547; baseline and differential.
DR Genevisible; Q9Y547; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
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; IEA:Ensembl.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR033558; IFT25.
DR PANTHER; PTHR33906; PTHR33906; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell projection; Cilium; Differentiation;
KW Metal-binding; Protein transport; Reference proteome; Spermatogenesis;
KW Stress response; Transport.
FT CHAIN 1..144
FT /note="Intraflagellar transport protein 25 homolog"
FT /id="PRO_0000058531"
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 HELIX 9..11
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1XPW"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 45..77
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 110..125
FT /evidence="ECO:0007829|PDB:1TVG"
FT STRAND 128..139
FT /evidence="ECO:0007829|PDB:1TVG"
SQ SEQUENCE 144 AA; 16297 MW; 43B7DBDD47A528C9 CRC64;
MRKIDLCLSS EGSEVILATS SDEKHPPENI IDGNPETFWT TTGMFPQEFI ICFHKHVRIE
RLVIQSYFVQ TLKIEKSTSK EPVDFEQWIE KDLVHTEGQL QNEEIVAHDG SATYLRFIIV
SAFDHFASVH SVSAEGTVVS NLSS
