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Database: UniProt
Entry: Q4R6T7
LinkDB: Q4R6T7
Original site: Q4R6T7 
ID   IQUB_MACFA              Reviewed;         790 AA.
AC   Q4R6T7; Q4R6Q1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=IQ motif and ubiquitin-like domain-containing protein;
GN   Name=IQUB; ORFNames=QtsA-17155, QtsA-17428;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adapter protein that anchors the radial spoke 1 (RS1) complex
CC       to the A microtubule of outer doublet microtubules in axonemes. The
CC       triple radial spokes (RS1, RS2 and RS3) are required to modulate
CC       beating of the sperm flagellum. May play a role in inhibiting signaling
CC       via MAPK1/ERK2 and MAPK3/ERK1. Additionally, may play a role in the
CC       functioning of cilia. Not required for the functioning of tracheal or
CC       ependymal cilia. {ECO:0000250|UniProtKB:Q8CDK3}.
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. Does not appear to be part of radial spoke
CC       complexes 2 or 3 (RS2 or RS3). Interacts with CALM1. Interacts with
CC       DNAJB13. Interacts with DYNLL2. Interacts with NME5 (By similarity).
CC       Interacts with RSPH3 (By similarity). Interacts with RSPH9 (By
CC       similarity). Interacts with ZMYND10. Interacts with calmodulin; the
CC       interaction occurs in conditions of low but not high calcium (By
CC       similarity). {ECO:0000250|UniProtKB:Q8CDK3,
CC       ECO:0000250|UniProtKB:Q8NA54}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE01223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB169129; BAE01223.1; ALT_INIT; mRNA.
DR   EMBL; AB169093; BAE01187.1; -; mRNA.
DR   RefSeq; NP_001270025.1; NM_001283096.1.
DR   AlphaFoldDB; Q4R6T7; -.
DR   SMR; Q4R6T7; -.
DR   STRING; 9541.ENSMFAP00000038347; -.
DR   eggNOG; ENOG502QRQT; Eukaryota.
DR   OrthoDB; 5478818at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0097729; C:9+2 motile cilium; ISS:UniProtKB.
DR   GO; GO:0001534; C:radial spoke; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR   GO; GO:0007618; P:mating; ISS:UniProtKB.
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.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW   Cytoskeleton; Flagellum; Reference proteome.
FT   CHAIN           1..790
FT                   /note="IQ motif and ubiquitin-like domain-containing
FT                   protein"
FT                   /id="PRO_0000274602"
FT   DOMAIN          130..206
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          337..366
FT                   /note="IQ"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        327
FT                   /note="Y -> C (in Ref. 1; BAE01187)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="F -> S (in Ref. 1; BAE01187)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   790 AA;  92399 MW;  6F1493D7C50B935C CRC64;
     MSNQPKKYET QNIANSTEES DAFDIVTIPV PSEEPQESDQ TEEHESGIEQ FSESHAIHVE
     EQSDRSFSSL EPDSEQLMKE VISPRQVSYT PQHHEKQYAM QSPNDDSLAF LDKIKAIKES
     LQESMEDSLA TVKVVLIPVG QEIVISFKVD TVLKYLKDYF SHLLGIPLSV LQIRYSGKIL
     RNNETLVQHG VKPQEIIQVE IFSTNPDLYP VKRIDGLTDV SQIITVTVQT GLDRYQQVAV
     EIVKSDFHKP FLGGFRHKVT GVEYHHAGTQ TVPKKIPERL SVFCRDTQTV FQKKNLQQTT
     NTTSTQMTNI GVYVSNMTDK LVTPGKYFSA AEYHAQRLKA VIVIQTYYRQ WHAKIFVEDL
     RRQKSLRLEW ETQQELRKIR EKEEWVKLDY HRRHNPKTSE DFEFLYNALE FWRQEELKRI
     NQSFTGAERK AALCELLEKE TQIIASIGRH RYIAYTANQE AAIQAFLDKC SAPKIWRTPN
     GKTIEMDTQF TIRARELQNI YKCIMLKNIS QDERLDVLLT LKHTVKEHEC KLTQEILELI
     DREVDLMMRG VKHHNLEGLR KRIATLFFHY IKTPLFNPEV AKYLKVPQDP LKFYKKIYFC
     HSCQLYLPST EFSISSTSRR IYRCRNCISL ENEAQKRESF LKYRCLLQQL YFTEADYEDD
     SKIAFLMQLQ DIQYLTENIW ASQSVLSAWD DLSDLVMVRW NKSLEWSPWN CILLTKDEAA
     AHLNLTSIEE GYERSFIHKI KHKHILAKNY FSQIPVLASF ILDDPEIDEI RWKHHSDTTP
     KIIESQRPPP
//
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