ID   DRC9_MACFA              Reviewed;         443 AA.
AC   Q9GKR7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Dynein regulatory complex protein 9 {ECO:0000250|UniProtKB:A8HQ54};
DE   AltName: Full=IQ domain-containing protein G;
GN   Name=IQCG; Synonyms=DRC9 {ECO:0000250|UniProtKB:A8HQ54};
GN   ORFNames=QnpA-20160;
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=Parietal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a
CC       key regulator of ciliary/flagellar motility which maintains the
CC       alignment and integrity of the distal axoneme and regulates microtubule
CC       sliding in motile axonemes. Binds calmodulin when cellular Ca(2+)
CC       levels are low and thereby contributes to the regulation of calcium and
CC       calmodulin-dependent protein kinase IV (CAMK4) activity; contributes to
CC       the regulation of CAMK4 signaling cascades. Required for normal axoneme
CC       assembly in sperm flagella, normal sperm tail formation and for male
CC       fertility. {ECO:0000250|UniProtKB:A3KQH2, ECO:0000250|UniProtKB:A8HQ54,
CC       ECO:0000250|UniProtKB:Q80W32}.
CC   -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC).
CC       Interacts (via IQ domain) with CALM when calcium levels are low. Does
CC       not interact with CALM in the presence of Ca(2+). Interacts with the
CC       HSP70 proteins HSPA1L and HSPA8. May form a complex with CAMK4 and
CC       HSP70. {ECO:0000250|UniProtKB:A8HQ54, ECO:0000250|UniProtKB:Q80W32,
CC       ECO:0000250|UniProtKB:Q9H095}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80W32}. Cell
CC       projection, cilium, flagellum {ECO:0000250|UniProtKB:Q80W32}. Cell
CC       projection, cilium {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm,
CC       cytoskeleton {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm, cytoskeleton,
CC       flagellum axoneme {ECO:0000250|UniProtKB:A8HQ54}. Note=First detected
CC       in the cytoplasm of pachytene spermatocytes. Colocalizes with alpha-
CC       tubulin at the manchette in developing spermatids. Detected in the
CC       flagellum of mature testicular spermatozoa, and in the flagellum and
CC       post-acrosomal region of the head of epididymal spermatozoa. Detected
CC       in cilia in trachea and oviduct. {ECO:0000250|UniProtKB:Q80W32}.
CC   -!- DOMAIN: The IQ domain mediates interaction with calmodulin when
CC       cellular Ca(2+) levels are low. {ECO:0000250|UniProtKB:Q9H095}.
CC   -!- SIMILARITY: Belongs to the DRC9 family. {ECO:0000305}.
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DR   EMBL; AB052178; BAB18984.1; -; mRNA.
DR   RefSeq; NP_001271774.1; NM_001284845.1.
DR   AlphaFoldDB; Q9GKR7; -.
DR   SMR; Q9GKR7; -.
DR   STRING; 9541.XP_005595492.1; -.
DR   GeneID; 102121144; -.
DR   CTD; 84223; -.
DR   eggNOG; ENOG502QQR7; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0002177; C:manchette; ISS:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0007288; P:sperm axoneme assembly; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR042618; IQCG.
DR   PANTHER; PTHR14871; PTHR14871; 1.
DR   Pfam; PF00612; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW   Differentiation; Flagellum; Reference proteome; Spermatogenesis.
FT   CHAIN           1..443
FT                   /note="Dynein regulatory complex protein 9"
FT                   /id="PRO_0000282562"
FT   DOMAIN          393..422
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   443 AA;  51708 MW;  BC6AA6AF38661395 CRC64;
     MEEDSQEDSN LPPKVWHSEM TVSVTGKPPS TVEEDGLPKE TDVETIPEIL ETREPLSLPD
     VLRISAVLED TTDQLSILNY IMPIQYEGRQ SVCVKSREMN LEGKNLDKLP VASTVTKTPS
     PLITKERPSL PEIRQGGQFA VEFCKTQDLL FKKPARQTIM TTETLKKIQI DRQFFSDVIA
     DTIEELQDSG TYNSLLQALS KERENKMHFY DVIAREEKGR KQIISLQKQL INVKKEWQFE
     VQSQNEYIAN LKDQLQEMKA KSNLENRYMK TNTELQIAQT QRKCNRTEEV LLEEIEKLRM
     KTEEEARIHM DIEMFLRKQQ QKLEERLEFW MEKYDKDTEM KQNELNALKA TKASDLAHLQ
     DLAKTIRECE QVIIEDRIEK EKSKNKIEQD LLELKSVIKL QAWWRGTMIR REIGGFKMPK
     DKVDSKDSKG KGKGKDKRRG KKK