ID   DRC9_BOVIN              Reviewed;         437 AA.
AC   Q2T9V2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 58.
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};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) 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; BC111253; AAI11254.1; -; mRNA.
DR   RefSeq; NP_001033284.1; NM_001038195.1.
DR   AlphaFoldDB; Q2T9V2; -.
DR   SMR; Q2T9V2; -.
DR   STRING; 9913.ENSBTAP00000023995; -.
DR   PaxDb; Q2T9V2; -.
DR   PRIDE; Q2T9V2; -.
DR   GeneID; 613455; -.
DR   KEGG; bta:613455; -.
DR   CTD; 84223; -.
DR   eggNOG; ENOG502QQR7; Eukaryota.
DR   InParanoid; Q2T9V2; -.
DR   Proteomes; UP000009136; 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..437
FT                   /note="Dynein regulatory complex protein 9"
FT                   /id="PRO_0000282560"
FT   DOMAIN          388..417
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  51220 MW;  4492DC82E4022AC9 CRC64;
     MEEGLEASNL PPEAWPSEVT VSVTGEPPNT SVEEKEETAK EAVIETSPEI MKPLSILDVL
     RISAVLEDTT DQLSILNYIM PVQYEKRQSI SMKDNKEMHL EGRSSEKVPL ASNPSKISSP
     LVHKEEPKLP EIRQGGQFNK VQDLIFKKPT RQTIMNTETL KKIQIDRQFL SDVITETLEE
     LQEEGTFTNL LKALGKERES KMHFYDTIAR EENGRKKIKS LQKQLLNVKK ERQAEVQNRN
     EYIAHLKDQL QEMKAKTNME NRYMKRNTEL QISQTQKKCS KTEELLLEEI EKLRLKTEEE
     NRIHAEIELF LRKEQQKLEE KLEFWMEKFD KDTEMKQNEL NALKSAKASD LAHLQELAKT
     IREYEQVIIE DRIEKEKTRK KREQDDLEMR SIIKLQAWWR GTVVRREIGG FKMPKDKDDS
     KDVKGKGKEK DKRRGKK