IFT52_MOUSE
ID IFT52_MOUSE Reviewed; 426 AA.
AC Q62559; Q3TK21; Q8BTX3; Q8CI16;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Intraflagellar transport protein 52 homolog;
DE AltName: Full=Protein NGD5;
GN Name=Ift52; Synonyms=Ngd5;
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 [MRNA].
RC TISSUE=Neuroblastoma;
RX PubMed=7494458; DOI=10.1016/0169-328x(95)00090-f;
RA Wick M.J., Ann D.K., Loh H.H.;
RT "Molecular cloning of a novel protein regulated by opioid treatment of
RT NG108-15 cells.";
RL Brain Res. Mol. Brain Res. 32:171-175(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP FUNCTION, 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=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 INTERACTION WITH TTC30A1; TTC30A2; TTC30B AND KIF17.
RX PubMed=23810713; DOI=10.1016/j.yexcr.2013.06.010;
RA Howard P.W., Jue S.F., Maurer R.A.;
RT "Interaction of mouse TTC30/DYF-1 with multiple intraflagellar transport
RT complex B proteins and KIF17.";
RL Exp. Cell Res. 319:2275-2281(2013).
RN [7]
RP INTERACTION WITH TTC25.
RX PubMed=25860617; DOI=10.1371/journal.pone.0124378;
RA Xu Y., Cao J., Huang S., Feng D., Zhang W., Zhu X., Yan X.;
RT "Characterization of tetratricopeptide repeat-containing proteins critical
RT for cilia formation and function.";
RL PLoS ONE 10:E0124378-E0124378(2015).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=31637240; DOI=10.3389/fcell.2019.00216;
RA Sorusch N., Yildirim A., Knapp B., Janson J., Fleck W., Scharf C.,
RA Wolfrum U.;
RT "SANS (USH1G) Molecularly Links the Human Usher Syndrome Protein Network to
RT the Intraflagellar Transport Module by Direct Binding to IFT-B Proteins.";
RL Front. Cell Dev. Biol. 7:216-216(2019).
CC -!- FUNCTION: Involved in ciliogenesis as part of a complex involved in
CC intraflagellar transport (IFT), the bi-directional movement of
CC particles required for the assembly, maintenance and functioning of
CC primary cilia (PubMed:19253336). Required for the anterograde transport
CC of IFT88 (By similarity). {ECO:0000250|UniProtKB:Q9Y366,
CC ECO:0000269|PubMed:19253336}.
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 IFT88
CC (PubMed:19253336). Interacts with TTC25 (PubMed:25860617). Interacts
CC with TTC21A (By similarity). Interacts with TTC30A1, TTC30A2, TTC30B
CC and KIF17 (PubMed:23810713). Interacts with USH1G (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y366, ECO:0000269|PubMed:19253336,
CC ECO:0000269|PubMed:23810713, ECO:0000269|PubMed:25860617}.
CC -!- INTERACTION:
CC Q62559; Q8N4P2: TTC30B; Xeno; NbExp=2; IntAct=EBI-6959048, EBI-6958994;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:31637240}.
CC -!- INDUCTION: After opioid treatment, expression decreases.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96241.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L38481; AAA96241.1; ALT_FRAME; mRNA.
DR EMBL; AK088467; BAC40371.1; -; mRNA.
DR EMBL; AK144188; BAE25755.1; -; mRNA.
DR EMBL; AK167194; BAE39324.1; -; mRNA.
DR EMBL; BC037708; AAH37708.1; -; mRNA.
DR CCDS; CCDS17005.1; -.
DR RefSeq; NP_742162.2; NM_172150.4.
DR RefSeq; XP_006499604.1; XM_006499541.3.
DR PDB; 5FMS; X-ray; 3.49 A; A/B/C=1-268.
DR PDBsum; 5FMS; -.
DR AlphaFoldDB; Q62559; -.
DR SMR; Q62559; -.
DR BioGRID; 232843; 1.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR IntAct; Q62559; 1.
DR MINT; Q62559; -.
DR STRING; 10090.ENSMUSP00000018002; -.
DR iPTMnet; Q62559; -.
DR PhosphoSitePlus; Q62559; -.
DR EPD; Q62559; -.
DR MaxQB; Q62559; -.
DR PaxDb; Q62559; -.
DR PRIDE; Q62559; -.
DR ProteomicsDB; 269530; -.
DR Antibodypedia; 43646; 39 antibodies from 17 providers.
DR DNASU; 245866; -.
DR Ensembl; ENSMUST00000018002; ENSMUSP00000018002; ENSMUSG00000017858.
DR GeneID; 245866; -.
DR KEGG; mmu:245866; -.
DR UCSC; uc008nsj.1; mouse.
DR CTD; 51098; -.
DR MGI; MGI:2387217; Ift52.
DR VEuPathDB; HostDB:ENSMUSG00000017858; -.
DR eggNOG; KOG3861; Eukaryota.
DR GeneTree; ENSGT00390000011581; -.
DR HOGENOM; CLU_027692_0_0_1; -.
DR InParanoid; Q62559; -.
DR OMA; KNERFQI; -.
DR OrthoDB; 925838at2759; -.
DR PhylomeDB; Q62559; -.
DR TreeFam; TF105916; -.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 245866; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ift52; mouse.
DR PRO; PR:Q62559; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q62559; protein.
DR Bgee; ENSMUSG00000017858; Expressed in dorsal pancreas and 231 other tissues.
DR ExpressionAtlas; Q62559; baseline and differential.
DR Genevisible; Q62559; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0097542; C:ciliary tip; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0044292; C:dendrite terminus; IDA:MGI.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0035720; P:intraciliary anterograde transport; ISO:MGI.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0070613; P:regulation of protein processing; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR InterPro; IPR019196; ABC_transp_unknown.
DR InterPro; IPR039975; IFT52.
DR PANTHER; PTHR12969; PTHR12969; 1.
DR Pfam; PF09822; ABC_transp_aux; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Reference proteome.
FT CHAIN 1..426
FT /note="Intraflagellar transport protein 52 homolog"
FT /id="PRO_0000084168"
FT CONFLICT 385
FT /note="R -> M (in Ref. 3; AAH37708)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:5FMS"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:5FMS"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5FMS"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:5FMS"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:5FMS"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5FMS"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:5FMS"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:5FMS"
SQ SEQUENCE 426 AA; 48248 MW; EC1B2F1E21327105 CRC64;
MEKELRSTIL FNAYKKEVFT TNTGYKSLQK RLRSNWKIQS LKDEITSEKL IGVKLWITAG
PREKFTAAEF EVLKKYLDSG GDILVMLGEG GESRFDTNIN FLLEEYGIMV NNDAVVRNVY
YKYFHPKEAL VSDGVLNREI SRAAGKAVPG VIDEENSGNN AQALTFVYPF GATLSVMKPA
VAVLSTGSVC FPLNRPILAF YHSKNQGFGK LAVLGSCHMF SDQYLDKEEN SKIMDVVFQW
LTTGDIHLNQ IDAEDPEISD YTMVPDTATL SEQLRVCLQE GDENPRDFTT LFDLSIYQLD
TTCLPKVIKA HEELNVKHEP LQLVQPQFEM PLPALQPAVF PPSFRELPPP PLELFDLDET
FSSEKARLAQ ITNKCTDEDL EFYVRKCGDI LGVTSKLPKD QQDAKHILEH IFFQVVEFKK
LNQEAH
