IFT74_HUMAN
ID IFT74_HUMAN Reviewed; 600 AA.
AC Q96LB3; Q3B789; Q5VY34; Q6PGQ8; Q9H643; Q9H8G7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Intraflagellar transport protein 74 homolog;
DE AltName: Full=Capillary morphogenesis gene 1 protein {ECO:0000303|PubMed:11683410};
DE Short=CMG-1 {ECO:0000303|PubMed:11683410, ECO:0000303|PubMed:15024030};
DE AltName: Full=Coiled-coil domain-containing protein 2;
GN Name=IFT74; Synonyms=CCDC2, CMG1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Umbilical vein;
RX PubMed=11683410; DOI=10.1242/jcs.114.15.2755;
RA Bell S.E., Mavila A., Salazar R., Bayless K.J., Kanagala S., Maxwell S.A.,
RA Davis G.E.;
RT "Differential gene expression during capillary morphogenesis in 3D collagen
RT matrices: regulated expression of genes involved in basement membrane
RT matrix assembly, cell cycle progression, cellular differentiation and G-
RT protein signaling.";
RL J. Cell Sci. 114:2755-2773(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-224
RP AND ILE-597.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
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 MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-372 (ISOFORM 2).
RC TISSUE=Thymus;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15024030; DOI=10.1083/jcb.200312133;
RA Iomini C., Tejada K., Mo W., Vaananen H., Piperno G.;
RT "Primary cilia of human endothelial cells disassemble under laminar shear
RT stress.";
RL J. Cell Biol. 164:811-817(2004).
RN [8]
RP INTERACTION WITH IFT81.
RX PubMed=15955805; DOI=10.1074/jbc.m505062200;
RA Lucker B.F., Behal R.H., Qin H., Siron L.C., Taggart W.D., Rosenbaum J.L.,
RA Cole D.G.;
RT "Characterization of the intraflagellar transport complex B core: direct
RT interaction of the IFT81 and IFT74/72 subunits.";
RL J. Biol. Chem. 280:27688-27696(2005).
RN [9]
RP INTERACTION WITH ARL13B.
RX PubMed=24339792; DOI=10.1371/journal.pgen.1003977;
RA Cevik S., Sanders A.A., Van Wijk E., Boldt K., Clarke L., van Reeuwijk J.,
RA Hori Y., Horn N., Hetterschijt L., Wdowicz A., Mullins A., Kida K.,
RA Kaplan O.I., van Beersum S.E., Man Wu K., Letteboer S.J., Mans D.A.,
RA Katada T., Kontani K., Ueffing M., Roepman R., Kremer H., Blacque O.E.;
RT "Active transport and diffusion barriers restrict Joubert syndrome-
RT associated ARL13B/ARL-13 to an inv-like ciliary membrane subdomain.";
RL PLoS Genet. 9:E1003977-E1003977(2013).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE IFT COMPLEX B, AND
RP INTERACTION WITH BETA-TUBULIN AND IFT81.
RX PubMed=23990561; DOI=10.1126/science.1240985;
RA Bhogaraju S., Cajanek L., Fort C., Blisnick T., Weber K., Taschner M.,
RA Mizuno N., Lamla S., Bastin P., Nigg E.A., Lorentzen E.;
RT "Molecular basis of tubulin transport within the cilium by IFT74 and
RT IFT81.";
RL Science 341:1009-1012(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP INVOLVEMENT IN BBS22, AND VARIANT MET-579.
RX PubMed=27486776; DOI=10.1016/j.ajhg.2015.04.023;
RA Lindstrand A., Frangakis S., Carvalho C.M., Richardson E.B., McFadden K.A.,
RA Willer J.R., Pehlivan D., Liu P., Pediaditakis I.L., Sabo A., Lewis R.A.,
RA Banin E., Lupski J.R., Davis E.E., Katsanis N.;
RT "Copy-Number variation contributes to the mutational load of Bardet-Biedl
RT syndrome.";
RL Am. J. Hum. Genet. 99:318-336(2016).
RN [13]
RP INTERACTION WITH RABL2B AND IFT81.
RX PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016;
RA Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J., Jackson P.K.;
RT "The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar
RT transport at the ciliary base.";
RL Dev. Cell 42:1-15(2017).
RN [14]
RP INTERACTION WITH RABL2B AND IFT81.
RX PubMed=28428259; DOI=10.1091/mbc.e17-01-0017;
RA Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.;
RT "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and
RT participates in ciliary assembly.";
RL Mol. Biol. Cell 28:1652-1666(2017).
RN [15]
RP INVOLVEMENT IN JBTS40, AND VARIANTS JBTS40 GLU-179 AND 285-GLU--ASN-600
RP DEL.
RX PubMed=34539760; DOI=10.3389/fgene.2021.738157;
RA Zhongling K., Guoming L., Yanhui C., Xiaoru C.;
RT "Case Report: Second Report of Joubert Syndrome Caused by Biallelic
RT Variants in IFT74.";
RL Front. Genet. 12:738157-738157(2021).
RN [16]
RP INVOLVEMENT IN JBTS40, VARIANTS JBTS40 29-ARG--ASN-600 DEL AND GLU-179,
RP CHARACTERIZATION OF VARIANT JBTS40 GLU-179, AND INTERACTION WITH IFT27 AND
RP IFT81.
RX PubMed=33531668; DOI=10.1038/s41436-021-01106-z;
RA Luo M., Lin Z., Zhu T., Jin M., Meng D., He R., Cao Z., Shen Y., Lu C.,
RA Cai R., Zhao Y., Wang X., Li H., Wu S., Zou X., Luo G., Cao L., Huang M.,
RA Jiao H., Gao H., Sui R., Zhao C., Ma X., Cao M.;
RT "Disrupted intraflagellar transport due to IFT74 variants causes Joubert
RT syndrome.";
RL Genet. Med. 23:1041-1049(2021).
RN [17]
RP INVOLVEMENT IN SPGF58, VARIANT SPGF58 SER-86, CHARACTERIZATION OF VARIANT
RP SPGF58 SER-86, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=33689014; DOI=10.1007/s00439-021-02270-7;
RA Lores P., Kherraf Z.E., Amiri-Yekta A., Whitfield M., Daneshipour A.,
RA Stouvenel L., Cazin C., Cavarocchi E., Coutton C., Llabador M.A.,
RA Arnoult C., Thierry-Mieg N., Ferreux L., Patrat C., Hosseini S.H.,
RA Mustapha S.F.B., Zouari R., Dulioust E., Ray P.F., Toure A.;
RT "A missense mutation in IFT74, encoding for an essential component for
RT intraflagellar transport of Tubulin, causes asthenozoospermia and male
RT infertility without clinical signs of Bardet-Biedl syndrome.";
RL Hum. Genet. 140:1031-1043(2021).
CC -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B:
CC together with IFT81, forms a tubulin-binding module that specifically
CC mediates transport of tubulin within the cilium (PubMed:23990561).
CC Binds beta-tubulin via its basic region (PubMed:23990561). Required for
CC ciliogenesis (PubMed:23990561). Essential for flagellogenesis during
CC spermatogenesis (PubMed:33689014). {ECO:0000269|PubMed:23990561,
CC ECO:0000269|PubMed:33689014}.
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:23990561, PubMed:33531668). Interacts
CC with IFT81; the interaction is direct (PubMed:15955805,
CC PubMed:23990561, PubMed:33531668). Within the IFT complex B, IFT74 and
CC IFT81 mediate the transport of tubulin within the cilium
CC (PubMed:15955805, PubMed:23990561). Interacts (via basic region) with
CC beta-tubulin (via acidic region); interaction is direct
CC (PubMed:23990561). Interacts with ARL13B and IFT88 (PubMed:24339792).
CC Interacts (via the IFT74/IFT81 heterodimer) with RABL2B
CC (PubMed:28428259, PubMed:28625565). Interacts with IFT57 and TTC30B (By
CC similarity). {ECO:0000250|UniProtKB:Q8BKE9,
CC ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:23990561,
CC ECO:0000269|PubMed:24339792, ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:33531668}.
CC -!- INTERACTION:
CC Q96LB3-2; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-12066130, EBI-10181422;
CC Q96LB3-2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-12066130, EBI-11988027;
CC Q96LB3-2; O14964: HGS; NbExp=3; IntAct=EBI-12066130, EBI-740220;
CC Q96LB3-2; Q8WYA0-3: IFT81; NbExp=3; IntAct=EBI-12066130, EBI-11944793;
CC Q96LB3-2; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-12066130, EBI-3437878;
CC Q96LB3-2; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-12066130, EBI-455078;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:15024030}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:11683410}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:33689014}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q8BKE9}. Note=Localizes along primary
CC cilia at interphase and around the basal body/centriole at interphase
CC and mitosis (PubMed:15024030). In male germ cells, strongly expressed
CC in the vesicles of spermatocytes and round spermatids and also in the
CC acrosome and centrosome regions of elongating spermatids and in
CC developing sperm tails (By similarity). {ECO:0000250|UniProtKB:Q8BKE9,
CC ECO:0000269|PubMed:15024030}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96LB3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96LB3-2; Sequence=VSP_041328;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult and fetal kidney and
CC expressed at lower level in adult heart, placenta, lung, liver and
CC pancreas, and in fetal heart, lung and liver. Little to no expression
CC was detected in adult brain and skeletal muscle or in fetal brain,
CC thymus and spleen (PubMed:11683410). Detected in sperm (at protein
CC level) (PubMed:33689014). {ECO:0000269|PubMed:11683410,
CC ECO:0000269|PubMed:33689014}.
CC -!- DISEASE: Bardet-Biedl syndrome 22 (BBS22) [MIM:617119]: A form of
CC Bardet-Biedl syndrome, a syndrome characterized by usually severe
CC pigmentary retinopathy, early-onset obesity, polydactyly,
CC hypogenitalism, renal malformation and intellectual disability.
CC Secondary features include diabetes mellitus, hypertension and
CC congenital heart disease. Bardet-Biedl syndrome inheritance is
CC autosomal recessive, but three mutated alleles (two at one locus, and a
CC third at a second locus) may be required for clinical manifestation of
CC some forms of the disease. {ECO:0000269|PubMed:27486776}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Joubert syndrome 40 (JBTS40) [MIM:619582]: A form of Joubert
CC syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC delay. Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. JBTS40 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:33531668, ECO:0000269|PubMed:34539760}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Spermatogenic failure 58 (SPGF58) [MIM:619585]: An autosomal
CC recessive male infertility disorder characterized by absent or severely
CC reduced sperm motility, due to multiple morphological abnormalities of
CC the sperm flagellum. {ECO:0000269|PubMed:33689014}. Note=The disease is
CC caused by variants affecting the gene represented in this entry. A
CC homozygous variant at codon 86 has been identified in 2 unrelated
CC affected individuals. In addition to encoding a missense, this variant
CC also affects splicing, predominantly through the induction of an in-
CC frame deletion of 10 amino acids within exon 3. Other minor transcripts
CC can be detected in patient's sperm that use cryptic donor sites present
CC in intron 3, leading either to the retention of 18 bp of intron 3 and
CC an in-frame insertion of 6 amino acids, or to the retention of 108 bp
CC of intron 3, which induces a frameshift and a truncated protein.
CC {ECO:0000269|PubMed:33689014}.
CC -!- SIMILARITY: Belongs to the IFT74 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14650.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15423.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY040325; AAK77221.1; -; mRNA.
DR EMBL; AK023707; BAB14650.1; ALT_SEQ; mRNA.
DR EMBL; AK026274; BAB15423.1; ALT_INIT; mRNA.
DR EMBL; AL355432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58573.1; -; Genomic_DNA.
DR EMBL; BC107742; AAI07743.1; -; mRNA.
DR EMBL; BX436367; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS43793.1; -. [Q96LB3-1]
DR CCDS; CCDS47955.1; -. [Q96LB3-2]
DR RefSeq; NP_001092692.1; NM_001099222.1. [Q96LB3-1]
DR RefSeq; NP_001092693.1; NM_001099223.1. [Q96LB3-1]
DR RefSeq; NP_001092694.1; NM_001099224.1. [Q96LB3-2]
DR RefSeq; NP_079379.2; NM_025103.2. [Q96LB3-1]
DR AlphaFoldDB; Q96LB3; -.
DR SMR; Q96LB3; -.
DR BioGRID; 123156; 115.
DR ComplexPortal; CPX-5022; IFT-B complex.
DR CORUM; Q96LB3; -.
DR IntAct; Q96LB3; 53.
DR MINT; Q96LB3; -.
DR STRING; 9606.ENSP00000404122; -.
DR iPTMnet; Q96LB3; -.
DR PhosphoSitePlus; Q96LB3; -.
DR BioMuta; IFT74; -.
DR DMDM; 50400610; -.
DR EPD; Q96LB3; -.
DR jPOST; Q96LB3; -.
DR MassIVE; Q96LB3; -.
DR MaxQB; Q96LB3; -.
DR PaxDb; Q96LB3; -.
DR PeptideAtlas; Q96LB3; -.
DR PRIDE; Q96LB3; -.
DR ProteomicsDB; 77187; -. [Q96LB3-1]
DR ProteomicsDB; 77188; -. [Q96LB3-2]
DR Antibodypedia; 5487; 199 antibodies from 32 providers.
DR DNASU; 80173; -.
DR Ensembl; ENST00000380062.10; ENSP00000369402.5; ENSG00000096872.17. [Q96LB3-1]
DR Ensembl; ENST00000429045.6; ENSP00000393907.2; ENSG00000096872.17. [Q96LB3-2]
DR Ensembl; ENST00000433700.5; ENSP00000389224.1; ENSG00000096872.17. [Q96LB3-1]
DR Ensembl; ENST00000443698.5; ENSP00000404122.1; ENSG00000096872.17. [Q96LB3-1]
DR GeneID; 80173; -.
DR KEGG; hsa:80173; -.
DR MANE-Select; ENST00000380062.10; ENSP00000369402.5; NM_025103.4; NP_079379.2.
DR UCSC; uc003zqf.5; human. [Q96LB3-1]
DR CTD; 80173; -.
DR DisGeNET; 80173; -.
DR GeneCards; IFT74; -.
DR HGNC; HGNC:21424; IFT74.
DR HPA; ENSG00000096872; Tissue enhanced (testis).
DR MalaCards; IFT74; -.
DR MIM; 608040; gene.
DR MIM; 617119; phenotype.
DR MIM; 619582; phenotype.
DR MIM; 619585; phenotype.
DR neXtProt; NX_Q96LB3; -.
DR OpenTargets; ENSG00000096872; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR PharmGKB; PA134976961; -.
DR VEuPathDB; HostDB:ENSG00000096872; -.
DR eggNOG; ENOG502QS4E; Eukaryota.
DR GeneTree; ENSGT00390000007109; -.
DR HOGENOM; CLU_027673_2_0_1; -.
DR InParanoid; Q96LB3; -.
DR OMA; MQDDLSF; -.
DR OrthoDB; 622935at2759; -.
DR PhylomeDB; Q96LB3; -.
DR TreeFam; TF318352; -.
DR PathwayCommons; Q96LB3; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q96LB3; -.
DR BioGRID-ORCS; 80173; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; IFT74; human.
DR GeneWiki; IFT74; -.
DR GenomeRNAi; 80173; -.
DR Pharos; Q96LB3; Tbio.
DR PRO; PR:Q96LB3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96LB3; protein.
DR Bgee; ENSG00000096872; Expressed in bronchial epithelial cell and 185 other tissues.
DR ExpressionAtlas; Q96LB3; baseline and differential.
DR Genevisible; Q96LB3; 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:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
DR GO; GO:0031514; C:motile cilium; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB.
DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR InterPro; IPR029602; IFT74.
DR PANTHER; PTHR31432; PTHR31432; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bardet-Biedl syndrome; Cell projection; Ciliopathy;
KW Cilium; Cilium biogenesis/degradation; Coiled coil; Cytoplasmic vesicle;
KW Developmental protein; Disease variant; Flagellum; Joubert syndrome;
KW Methylation; Obesity; Phosphoprotein; Reference proteome.
FT CHAIN 1..600
FT /note="Intraflagellar transport protein 74 homolog"
FT /id="PRO_0000084169"
FT REGION 1..90
FT /note="Basic region"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..600
FT /note="Important for interaction with IFT27"
FT /evidence="ECO:0000269|PubMed:33531668"
FT COILED 98..482
FT /evidence="ECO:0000255"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKE9"
FT VAR_SEQ 352..600
FT /note="GEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVALLEHCSRN
FT INRIEQISSITNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESK
FT MTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQERMILSTHRNAFKKIMEK
FT QNIEYEALKTQLQENETHSQLTNLERKWQHLEQNNFAMKEFIATKSQESDYQPIKKNVT
FT KQIAEYNKTIVDALHSTSGN -> DPTNYGWKILEKNTGSFKKQV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_041328"
FT VARIANT 29..600
FT /note="Missing (in JBTS40; dbSNP:rs751583919)"
FT /evidence="ECO:0000269|PubMed:33531668"
FT /id="VAR_086331"
FT VARIANT 55
FT /note="I -> M (in dbSNP:rs10812505)"
FT /id="VAR_051062"
FT VARIANT 85
FT /note="K -> R (in dbSNP:rs11555693)"
FT /id="VAR_061667"
FT VARIANT 86
FT /note="G -> S (in SPGF58; affects subcellular location,
FT instead of being homogenously distributed along the sperm
FT flagellum, concentrates in the proximal part of the
FT flagellum; also affects splicing)"
FT /evidence="ECO:0000269|PubMed:33689014"
FT /id="VAR_086332"
FT VARIANT 110
FT /note="T -> A (in dbSNP:rs12004404)"
FT /id="VAR_051063"
FT VARIANT 179
FT /note="Q -> E (in JBTS40; partial loss of function;
FT contrary to wild-type, only partially rescues the phenotype
FT of IFT74 knockdown zebrafish; does not affect interaction
FT with IFT81 and IFT27; does not affect protein level;
FT dbSNP:rs150219690)"
FT /evidence="ECO:0000269|PubMed:33531668"
FT /id="VAR_086333"
FT VARIANT 224
FT /note="F -> L (in dbSNP:rs17694549)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_051064"
FT VARIANT 285..600
FT /note="Missing (in JBTS40; dbSNP:rs1056125920)"
FT /evidence="ECO:0000269|PubMed:34539760"
FT /id="VAR_086334"
FT VARIANT 355
FT /note="N -> T (in dbSNP:rs34628525)"
FT /id="VAR_051065"
FT VARIANT 579
FT /note="V -> M (in dbSNP:rs138591335)"
FT /evidence="ECO:0000269|PubMed:27486776"
FT /id="VAR_076977"
FT VARIANT 597
FT /note="T -> I (in dbSNP:rs3429)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_051066"
FT CONFLICT 172
FT /note="D -> G (in Ref. 2; BAB14650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 69239 MW; 01366A697500D52D CRC64;
MASNHKSSAA RPVSRGGVGL TGRPPSGIRP LSGNIRVATA MPPGTARPGS RGCPIGTGGV
LSSQIKVAHR PVTQQGLTGM KTGTKGPQRQ ILDKSYYLGL LRSKISELTT EVNKLQKGIE
MYNQENSVYL SYEKRAETLA VEIKELQGQL ADYNMLVDKL NTNTEMEEVM NDYNMLKAQN
DRETQSLDVI FTERQAKEKQ IRSVEEEIEQ EKQATDDIIK NMSFENQVKY LEMKTTNEKL
LQELDTLQQQ LDSQNMKKES LEAEIAHSQV KQEAVLLHEK LYELESHRDQ MIAEDKSIGS
PMEEREKLLK QIKDDNQEIA SMERQLTDTK EKINQFIEEI RQLDMDLEEH QGEMNQKYKE
LKKREEHMDT FIETFEETKN QELKRKAQIE ANIVALLEHC SRNINRIEQI SSITNQELKM
MQDDLNFKST EVQKSQSTAQ NLTSDIQRLQ LDLQKMELLE SKMTEEQHSL KSKIKQMTTD
LEIYNDLPAL KSSGEEKIKK LHQERMILST HRNAFKKIME KQNIEYEALK TQLQENETHS
QLTNLERKWQ HLEQNNFAMK EFIATKSQES DYQPIKKNVT KQIAEYNKTI VDALHSTSGN
