DRC9_RAT
ID DRC9_RAT Reviewed; 419 AA.
AC Q5PQQ6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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}.
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; BC087078; AAH87078.1; -; mRNA.
DR RefSeq; NP_001014252.1; NM_001014230.1.
DR AlphaFoldDB; Q5PQQ6; -.
DR SMR; Q5PQQ6; -.
DR STRING; 10116.ENSRNOP00000037862; -.
DR PhosphoSitePlus; Q5PQQ6; -.
DR PaxDb; Q5PQQ6; -.
DR PRIDE; Q5PQQ6; -.
DR GeneID; 363796; -.
DR KEGG; rno:363796; -.
DR UCSC; RGD:1311606; rat.
DR CTD; 84223; -.
DR RGD; 1311606; Iqcg.
DR eggNOG; ENOG502QQR7; Eukaryota.
DR InParanoid; Q5PQQ6; -.
DR PhylomeDB; Q5PQQ6; -.
DR PRO; PR:Q5PQQ6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
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:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0044782; P:cilium organization; IBA:GO_Central.
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..419
FT /note="Dynein regulatory complex protein 9"
FT /id="PRO_0000282564"
FT DOMAIN 371..400
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 48757 MW; 74EC3E75356D8C2A CRC64;
MEGEELETTG SLSEVFQPEV TMAVTGEPPK PAEEELEEEE EETSPEVIDT LSLLDVLRVS
AIMEDIIDQL SILGYIIPVQ YERRQSLSQK TSHEGAPMVP STPKISASLI AKDKPVVSDS
KQRGQDFFFK KATKQTTMTL ETMRKIQNDR QYFSDVIANA MMEMQACGSF SSLLEALGKE
RDAKMNFHDV ITREGKGRKQ IKSLQKQLVD VKRERQMQVQ NGNEYIAHLR DQLQEVKAKT
NLENLYMKRN TELQVSQTQK KCNRAEELLL EEIEKLRLKT EEENRVHMEI EMFLRNQQQK
LEEKLEFWME KFDKDTEAKQ NELNALKAAK ASDLAHLQDL AKMIREYEQV IIEDRLEKEK
TRKKLEQDDL ELRSIVKLQA WWRGTVVRRE IGSFKMPKKE KDDSKDAKGK EKDKRRGKK
