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
//