ID IQUB_HUMAN Reviewed; 791 AA. AC Q8NA54; A4D0X0; Q49AL6; Q4G189; Q5BJD9; Q6NUH6; Q8N9Y2; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 27-MAR-2024, entry version 153. DE RecName: Full=IQ motif and ubiquitin-like domain-containing protein; GN Name=IQUB; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP MET-126. 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 [4] RP INTERACTION WITH ZMYND10. RX PubMed=29601588; DOI=10.1371/journal.pgen.1007316; RA Cho K.J., Noh S.H., Han S.M., Choi W.I., Kim H.Y., Yu S., Lee J.S., RA Rim J.H., Lee M.G., Hildebrandt F., Gee H.Y.; RT "ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic pre- RT assembly of dynein arms."; RL PLoS Genet. 14:E1007316-E1007316(2018). RN [5] RP STRUCTURE BY NMR OF 121-227. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the novel identified ubiquitin-like domain in the RT human hypothetical protein FLJ35834."; RL Submitted (JUN-2006) to the PDB data bank. RN [6] RP VARIANT [LARGE SCALE ANALYSIS] HIS-735. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [7] RP VARIANT 314-TYR--HIS-791 DEL, FUNCTION, INTERACTION WITH RSPH3 AND RP CALMODULIN, AND INVOLVEMENT IN SPERMATOGENIC FAILURE WITH RADIAL SPOKE RP DEFECTS. RX PubMed=36355624; DOI=10.1093/humrep/deac244; RA Zhang Z., Zhou H., Deng X., Zhang R., Qu R., Mu J., Liu R., Zeng Y., RA Chen B., Wang L., Sang Q., Bao S.; RT "IQUB deficiency causes male infertility by affecting the activity of p- RT ERK1/2/RSPH3."; RL Hum. Reprod. 37:deac244-deac244(2022). CC -!- FUNCTION: Adapter protein that anchors the radial spoke 1 (RS1) complex CC to the A microtubule of outer doublet microtubules in axonemes CC (PubMed:36355624). The triple radial spokes (RS1, RS2 and RS3) are CC required to modulate beating of the sperm flagellum (PubMed:36355624). CC May play a role in inhibiting signaling via MAPK1/ERK2 and MAPK3/ERK1 CC (PubMed:36355624). Additionally, may play a role in the functioning of CC cilia (By similarity). Not required for the functioning of tracheal or CC ependymal cilia (By similarity). {ECO:0000250|UniProtKB:Q8CDK3, CC ECO:0000269|PubMed:36355624}. CC -!- SUBUNIT: Component of the axonemal radial spoke 1 (RS1) complex, at CC least composed of spoke head proteins RSPH1, RSPH3, RSPH9 and the CC cilia-specific component RSPH4A or sperm-specific component RSPH6A, CC spoke stalk proteins RSPH14, DNAJB13, DYDC1, ROPN1L and NME5, and the CC anchor protein IQUB (By similarity). Does not appear to be part of CC radial spoke complexes 2 or 3 (RS2 or RS3) (By similarity). Interacts CC with CALM1 (By similarity). Interacts with DNAJB13 (By similarity). CC Interacts with DYNLL2 (By similarity). Interacts with NME5 (By CC similarity). Interacts with RSPH3 (PubMed:36355624). Interacts with CC RSPH9 (By similarity). Interacts with ZMYND10 (PubMed:29601588). CC Interacts with calmodulin; the interaction occurs in conditions of low CC but not high calcium (PubMed:36355624). {ECO:0000250|UniProtKB:Q8CDK3, CC ECO:0000269|PubMed:29601588, ECO:0000269|PubMed:36355624}. CC -!- INTERACTION: CC Q8NA54; Q9H161: ALX4; NbExp=3; IntAct=EBI-10220600, EBI-11317841; CC Q8NA54; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-10220600, EBI-12224467; CC Q8NA54; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-10220600, EBI-5661893; CC Q8NA54; Q9H2G9: BLZF1; NbExp=6; IntAct=EBI-10220600, EBI-2548012; CC Q8NA54; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-10220600, EBI-739580; CC Q8NA54; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10220600, EBI-739624; CC Q8NA54; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-10220600, EBI-742887; CC Q8NA54; P28329-3: CHAT; NbExp=3; IntAct=EBI-10220600, EBI-25837549; CC Q8NA54; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-10220600, EBI-21553822; CC Q8NA54; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10220600, EBI-3867333; CC Q8NA54; Q14689-4: DIP2A; NbExp=3; IntAct=EBI-10220600, EBI-12019962; CC Q8NA54; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-10220600, EBI-12593112; CC Q8NA54; O14645: DNALI1; NbExp=3; IntAct=EBI-10220600, EBI-395638; CC Q8NA54; P50570-2: DNM2; NbExp=3; IntAct=EBI-10220600, EBI-10968534; CC Q8NA54; P63167: DYNLL1; NbExp=3; IntAct=EBI-10220600, EBI-349105; CC Q8NA54; O00167-2: EYA2; NbExp=3; IntAct=EBI-10220600, EBI-12807776; CC Q8NA54; P22607: FGFR3; NbExp=3; IntAct=EBI-10220600, EBI-348399; CC Q8NA54; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-10220600, EBI-11110431; CC Q8NA54; P14136: GFAP; NbExp=3; IntAct=EBI-10220600, EBI-744302; CC Q8NA54; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10220600, EBI-618309; CC Q8NA54; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-10220600, EBI-11519926; CC Q8NA54; P06396: GSN; NbExp=3; IntAct=EBI-10220600, EBI-351506; CC Q8NA54; P01112: HRAS; NbExp=3; IntAct=EBI-10220600, EBI-350145; CC Q8NA54; P04792: HSPB1; NbExp=3; IntAct=EBI-10220600, EBI-352682; CC Q8NA54; Q8IYA8: IHO1; NbExp=4; IntAct=EBI-10220600, EBI-8638439; CC Q8NA54; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-10220600, EBI-1055254; CC Q8NA54; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-10220600, EBI-743591; CC Q8NA54; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10220600, EBI-10975473; CC Q8NA54; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-10220600, EBI-14069005; CC Q8NA54; O14901: KLF11; NbExp=3; IntAct=EBI-10220600, EBI-948266; CC Q8NA54; Q6A162: KRT40; NbExp=3; IntAct=EBI-10220600, EBI-10171697; CC Q8NA54; O95678: KRT75; NbExp=3; IntAct=EBI-10220600, EBI-2949715; CC Q8NA54; Q01546: KRT76; NbExp=3; IntAct=EBI-10220600, EBI-2952745; CC Q8NA54; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10220600, EBI-10172290; CC Q8NA54; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10220600, EBI-10172052; CC Q8NA54; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-10220600, EBI-10176379; CC Q8NA54; P60329: KRTAP12-4; NbExp=6; IntAct=EBI-10220600, EBI-10176396; CC Q8NA54; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-10220600, EBI-12039345; CC Q8NA54; P02545: LMNA; NbExp=3; IntAct=EBI-10220600, EBI-351935; CC Q8NA54; P43360: MAGEA6; NbExp=3; IntAct=EBI-10220600, EBI-1045155; CC Q8NA54; Q99750: MDFI; NbExp=3; IntAct=EBI-10220600, EBI-724076; CC Q8NA54; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-10220600, EBI-11022007; CC Q8NA54; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-10220600, EBI-10232538; CC Q8NA54; Q9Y446: PKP3; NbExp=3; IntAct=EBI-10220600, EBI-2880227; CC Q8NA54; P78424: POU6F2; NbExp=3; IntAct=EBI-10220600, EBI-12029004; CC Q8NA54; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-10220600, EBI-11320284; CC Q8NA54; O60260-5: PRKN; NbExp=3; IntAct=EBI-10220600, EBI-21251460; CC Q8NA54; E9PI22: PRR23D1; NbExp=3; IntAct=EBI-10220600, EBI-23335840; CC Q8NA54; Q15669: RHOH; NbExp=3; IntAct=EBI-10220600, EBI-1244971; CC Q8NA54; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-10220600, EBI-396669; CC Q8NA54; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-10220600, EBI-3957636; CC Q8NA54; Q16637: SMN2; NbExp=6; IntAct=EBI-10220600, EBI-395421; CC Q8NA54; O60504: SORBS3; NbExp=3; IntAct=EBI-10220600, EBI-741237; CC Q8NA54; Q7Z699: SPRED1; NbExp=6; IntAct=EBI-10220600, EBI-5235340; CC Q8NA54; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-10220600, EBI-6872807; CC Q8NA54; O14656-2: TOR1A; NbExp=3; IntAct=EBI-10220600, EBI-25847109; CC Q8NA54; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-10220600, EBI-11952721; CC Q8NA54; Q12933: TRAF2; NbExp=3; IntAct=EBI-10220600, EBI-355744; CC Q8NA54; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-10220600, EBI-359276; CC Q8NA54; P36406: TRIM23; NbExp=7; IntAct=EBI-10220600, EBI-740098; CC Q8NA54; P14373: TRIM27; NbExp=3; IntAct=EBI-10220600, EBI-719493; CC Q8NA54; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-10220600, EBI-5235829; CC Q8NA54; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-10220600, EBI-9867283; CC Q8NA54; Q9BYV2: TRIM54; NbExp=4; IntAct=EBI-10220600, EBI-2130429; CC Q8NA54; O76024: WFS1; NbExp=3; IntAct=EBI-10220600, EBI-720609; CC Q8NA54; P52747: ZNF143; NbExp=3; IntAct=EBI-10220600, EBI-2849334; CC Q8NA54; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-10220600, EBI-11741890; CC Q8NA54; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-10220600, EBI-11035148; CC Q8NA54; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-10220600, EBI-527853; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme CC {ECO:0000250|UniProtKB:Q8CDK3}. Cell projection, cilium CC {ECO:0000250|UniProtKB:Q8CDK3}. Note=Localizes to the axoneme of sperm CC cells and the cilia of tracheal epithelial cells. CC {ECO:0000250|UniProtKB:Q8CDK3}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8NA54-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NA54-2; Sequence=VSP_022830, VSP_022831; CC -!- DISEASE: Note=Defects in IQUB may be the cause of spermatogenic failure CC with radial spoke defects, leading to asthenospermia and male CC infertility (PubMed:36355624). Sperm appear largely normal CC morphologically but with radial spoke defects, and their motility is CC severely reduced (PubMed:36355624). {ECO:0000269|PubMed:36355624}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK093153; BAC04074.1; -; mRNA. DR EMBL; AK093393; BAC04153.1; -; mRNA. DR EMBL; CH236947; EAL24336.1; -; Genomic_DNA. DR EMBL; BC026173; AAH26173.1; -; mRNA. DR EMBL; BC036121; AAH36121.1; -; mRNA. DR EMBL; BC091520; AAH91520.1; -; mRNA. DR EMBL; BC128181; AAI28182.1; -; mRNA. DR CCDS; CCDS5787.1; -. [Q8NA54-1] DR RefSeq; NP_001269784.1; NM_001282855.1. [Q8NA54-1] DR RefSeq; NP_001308222.1; NM_001321293.1. [Q8NA54-1] DR RefSeq; NP_849149.3; NM_178827.4. [Q8NA54-1] DR RefSeq; XP_005250218.1; XM_005250161.3. [Q8NA54-1] DR RefSeq; XP_011514135.1; XM_011515833.2. [Q8NA54-1] DR RefSeq; XP_011514136.1; XM_011515834.2. [Q8NA54-1] DR RefSeq; XP_016867260.1; XM_017011771.1. [Q8NA54-1] DR PDB; 2DAF; NMR; -; A=123-227. DR PDB; 8J07; EM; 4.10 A; c2=1-791. DR PDBsum; 2DAF; -. DR PDBsum; 8J07; -. DR AlphaFoldDB; Q8NA54; -. DR EMDB; EMD-35888; -. DR SMR; Q8NA54; -. DR BioGRID; 127562; 79. DR ComplexPortal; CPX-8164; Radial spoke complex, flagellar variant. DR IntAct; Q8NA54; 76. DR MINT; Q8NA54; -. DR STRING; 9606.ENSP00000417769; -. DR iPTMnet; Q8NA54; -. DR PhosphoSitePlus; Q8NA54; -. DR BioMuta; IQUB; -. DR DMDM; 125950212; -. DR EPD; Q8NA54; -. DR MassIVE; Q8NA54; -. DR PaxDb; 9606-ENSP00000417769; -. DR PeptideAtlas; Q8NA54; -. DR ProteomicsDB; 72638; -. [Q8NA54-1] DR ProteomicsDB; 72639; -. [Q8NA54-2] DR Antibodypedia; 17626; 24 antibodies from 10 providers. DR DNASU; 154865; -. DR Ensembl; ENST00000324698.11; ENSP00000324882.6; ENSG00000164675.11. [Q8NA54-1] DR Ensembl; ENST00000466202.5; ENSP00000417769.1; ENSG00000164675.11. [Q8NA54-1] DR Ensembl; ENST00000484508.5; ENSP00000417285.1; ENSG00000164675.11. [Q8NA54-2] DR GeneID; 154865; -. DR KEGG; hsa:154865; -. DR MANE-Select; ENST00000324698.11; ENSP00000324882.6; NM_178827.5; NP_849149.3. DR UCSC; uc003vkn.4; human. [Q8NA54-1] DR AGR; HGNC:21995; -. DR CTD; 154865; -. DR DisGeNET; 154865; -. DR GeneCards; IQUB; -. DR HGNC; HGNC:21995; IQUB. DR HPA; ENSG00000164675; Tissue enriched (testis). DR MIM; 620557; gene. DR neXtProt; NX_Q8NA54; -. DR OpenTargets; ENSG00000164675; -. DR PharmGKB; PA162392258; -. DR VEuPathDB; HostDB:ENSG00000164675; -. DR eggNOG; ENOG502QRQT; Eukaryota. DR GeneTree; ENSGT00390000014326; -. DR HOGENOM; CLU_014415_0_0_1; -. DR InParanoid; Q8NA54; -. DR OMA; WKYIHLR; -. DR OrthoDB; 5478818at2759; -. DR PhylomeDB; Q8NA54; -. DR TreeFam; TF323180; -. DR PathwayCommons; Q8NA54; -. DR SignaLink; Q8NA54; -. DR BioGRID-ORCS; 154865; 12 hits in 1143 CRISPR screens. DR ChiTaRS; IQUB; human. DR EvolutionaryTrace; Q8NA54; -. DR GenomeRNAi; 154865; -. DR Pharos; Q8NA54; Tdark. DR PRO; PR:Q8NA54; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q8NA54; Protein. DR Bgee; ENSG00000164675; Expressed in sperm and 101 other cell types or tissues. DR ExpressionAtlas; Q8NA54; baseline and differential. DR GO; GO:0097729; C:9+2 motile cilium; ISS:UniProtKB. DR GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IBA:GO_Central. DR GO; GO:0001534; C:radial spoke; ISS:UniProtKB. DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central. DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB. DR GO; GO:0007618; P:mating; IMP:UniProtKB. DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl. DR CDD; cd17061; Ubl_IQUB; 1. DR InterPro; IPR037695; IQUB. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR21074:SF0; IQ AND UBIQUITIN-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR21074; UNCHARACTERIZED; 1. DR Pfam; PF00240; ubiquitin; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR Genevisible; Q8NA54; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cilium; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant; KW Flagellum; Reference proteome. FT CHAIN 1..791 FT /note="IQ motif and ubiquitin-like domain-containing FT protein" FT /id="PRO_0000274601" FT DOMAIN 131..207 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT DOMAIN 338..367 FT /note="IQ" FT REGION 1..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..23 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 42..61 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 587..680 FT /note="VPQDPLKFYKKIYFCHSCQLYLPSTEFSVSSTSRRIYRCRNCINLQNEAQKR FT ESFLKYKCLLQQLYYTEADYEDDSKIAFLMQLQDIQYLTENI -> MGGEYLSMAL FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_022830" FT VAR_SEQ 681..791 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_022831" FT VARIANT 126 FT /note="V -> M (in dbSNP:rs10255061)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_030332" FT VARIANT 314..791 FT /note="Missing (found in a patient with spermatogenic FT failure with radial spoke defects; binding to RSPH3 and FT calmodulin is abrogated; dbSNP:rs1418690066)" FT /evidence="ECO:0000269|PubMed:36355624" FT /id="VAR_087798" FT VARIANT 691 FT /note="D -> N (in dbSNP:rs17146009)" FT /id="VAR_030333" FT VARIANT 735 FT /note="R -> H (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs1525626)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036291" FT VARIANT 735 FT /note="R -> P (in dbSNP:rs1525626)" FT /id="VAR_030334" FT CONFLICT 4 FT /note="Q -> R (in Ref. 1; BAC04074)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="F -> S (in Ref. 1; BAC04074)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="I -> T (in Ref. 1; BAC04074)" FT /evidence="ECO:0000305" FT STRAND 131..137 FT /evidence="ECO:0007829|PDB:2DAF" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:2DAF" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:2DAF" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:2DAF" FT HELIX 154..165 FT /evidence="ECO:0007829|PDB:2DAF" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:2DAF" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:2DAF" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:2DAF" FT HELIX 187..190 FT /evidence="ECO:0007829|PDB:2DAF" FT STRAND 197..205 FT /evidence="ECO:0007829|PDB:2DAF" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:2DAF" SQ SEQUENCE 791 AA; 92581 MW; 3D16F8BF4BAED522 CRC64; MSNQQEKYEA QNIVNSTEES DDAFDTVTIP VPSEEPQESD QTEEHESGIE QFSESHAIHV EEQSDQSFSS LEPDNEQLME EVISPRQVSY TPQHHEKQYA MQRPNDDSLA FLDKIKSVKE SLQESVEDSL ATVKVVLIPV GQEIVIPFKV DTILKYLKDH FSHLLGIPHS VLQIRYSGKI LKNNETLVQH GVKPQEIVQV EIFSTNPDLY PVRRIDGLTD VSQIITVTVQ TGLDQYQQVP VEIVKSDFHK PFLGGFRHKV TGVEYHNAGT QTVPKRIPER LSIFCRDTQT VFQKKNLQQT TNTTSTQMTN IGVYVSNMTD KLVTPGKYFS AAEYHAQRLK AVIVIQTYYR QWHAKIFVEN LRRQKSLRLE WETQQELRKI REKEEWIKLD YHRRHNPKTN EDFEFLYNAL EFWRQEELTR INQSFTGAER KAALCELLEK ETQIIASIGR HRYIAYMANQ EAAIQAFLDK CSAPKIWRTP NGKTIEMDTQ FTIRARELQN IYKCIMLKNI SQDERLDVLL TLKHTVKEHE CKLTQEILEL IDREVDLMMR GVKHHNLEGL RKRIATLFFH YIKTPLFNPE VAKYLKVPQD PLKFYKKIYF CHSCQLYLPS TEFSVSSTSR RIYRCRNCIN LQNEAQKRES FLKYKCLLQQ LYYTEADYED DSKIAFLMQL QDIQYLTENI WASQSVLSAC DNLSDLVMVR WNKSLEWSPW NCILLTKDEA AAHLKLTSIE EGYERSFIHK IKHKHILAKN YFSQVPVLAS FILDDGEIDE IRWKYHSDTT PKIIESQRPP H //