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DRC9_MOUSE
ID   DRC9_MOUSE              Reviewed;         419 AA.
AC   Q80W32;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
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).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, MISCELLANEOUS, AND TISSUE SPECIFICITY.
RX   PubMed=24362311; DOI=10.1534/g3.113.009563;
RA   Harris T.P., Schimenti K.J., Munroe R.J., Schimenti J.C.;
RT   "IQ motif-containing G (Iqcg) is required for mouse spermiogenesis.";
RL   G3 (Bethesda) 4:367-372(2014).
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH CAMK4 AND HSP70.
RX   PubMed=24787902; DOI=10.1038/ncomms4811;
RA   Chen L.T., Liang W.X., Chen S., Li R.K., Tan J.L., Xu P.F., Luo L.F.,
RA   Wang L., Yu S.H., Meng G., Li K.K., Liu T.X., Chen Z., Chen S.J.;
RT   "Functional and molecular features of the calmodulin-interacting protein
RT   IQCG required for haematopoiesis in zebrafish.";
RL   Nat. Commun. 5:3811-3811(2014).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH CALMODULIN.
RX   PubMed=24849454; DOI=10.1371/journal.pone.0098053;
RA   Li R.K., Tan J.L., Chen L.T., Feng J.S., Liang W.X., Guo X.J., Liu P.,
RA   Chen Z., Sha J.H., Wang Y.F., Chen S.J.;
RT   "Iqcg is essential for sperm flagellum formation in mice.";
RL   PLoS ONE 9:E98053-E98053(2014).
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 (By similarity). Required
CC       for normal axoneme assembly in sperm flagella, normal sperm tail
CC       formation and for male fertility (PubMed:24362311, PubMed:24849454).
CC       {ECO:0000250|UniProtKB:A3KQH2, ECO:0000250|UniProtKB:A8HQ54,
CC       ECO:0000269|PubMed:24362311, ECO:0000269|PubMed:24849454}.
CC   -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC) (By
CC       similarity). Interacts (via IQ domain) with CALM when calcium levels
CC       are low. Does not interact with CALM in the presence of Ca(2+)
CC       (PubMed:24849454). Interacts with the HSP70 proteins HSPA1L and HSPA8
CC       (By similarity). May form a complex with CAMK4 and HSP70 (Probable).
CC       {ECO:0000250|UniProtKB:A8HQ54, ECO:0000250|UniProtKB:Q9H095,
CC       ECO:0000269|PubMed:24849454, ECO:0000305|PubMed:24787902}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24849454}. Cell
CC       projection, cilium, flagellum {ECO:0000269|PubMed:24849454}. Cell
CC       projection, cilium {ECO:0000269|PubMed:24849454}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:24849454}. 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:0000269|PubMed:24849454}.
CC   -!- TISSUE SPECIFICITY: Detected in testis (PubMed:24362311,
CC       PubMed:24849454). Also detected in oviduct (at protein level)
CC       (PubMed:24849454). Detected in testis (PubMed:24362311,
CC       PubMed:24849454). Also detected in oviduct and trachea
CC       (PubMed:24849454). {ECO:0000269|PubMed:24362311,
CC       ECO:0000269|PubMed:24849454}.
CC   -!- DEVELOPMENTAL STAGE: First detected in testis 17 days after birth when
CC       pachytene spermatocytes are seen in testes. Expression remains high
CC       during the first three weeks after birth and in adults (at protein
CC       level). {ECO:0000269|PubMed:24362311}.
CC   -!- DOMAIN: The IQ domain mediates interaction with calmodulin when
CC       cellular Ca(2+) levels are low. {ECO:0000250|UniProtKB:Q9H095}.
CC   -!- DISRUPTION PHENOTYPE: No obvious phenotype, except complete male
CC       sterility (PubMed:24362311, PubMed:24849454). Female fertility is not
CC       altered (PubMed:24849454). {ECO:0000269|PubMed:24362311,
CC       ECO:0000269|PubMed:24849454}.
CC   -!- MISCELLANEOUS: Early spermiogenesis defective 12d (esgd12d) is caused
CC       by mutations disrupting this gene. Affected male mice display complete
CC       loss of fertility; their sperm cells lack tails and are nonmotile.
CC       {ECO:0000269|PubMed:24362311}.
CC   -!- SIMILARITY: Belongs to the DRC9 family. {ECO:0000305}.
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DR   EMBL; BC049990; AAH49990.1; -; mRNA.
DR   CCDS; CCDS37316.1; -.
DR   RefSeq; NP_848465.1; NM_178378.3.
DR   RefSeq; XP_011244306.1; XM_011246004.2.
DR   AlphaFoldDB; Q80W32; -.
DR   SMR; Q80W32; -.
DR   STRING; 10090.ENSMUSP00000110752; -.
DR   iPTMnet; Q80W32; -.
DR   PhosphoSitePlus; Q80W32; -.
DR   jPOST; Q80W32; -.
DR   PaxDb; Q80W32; -.
DR   PRIDE; Q80W32; -.
DR   ProteomicsDB; 301666; -.
DR   Antibodypedia; 51727; 75 antibodies from 11 providers.
DR   DNASU; 69707; -.
DR   Ensembl; ENSMUST00000115100; ENSMUSP00000110752; ENSMUSG00000035578.
DR   GeneID; 69707; -.
DR   KEGG; mmu:69707; -.
DR   UCSC; uc007yzt.2; mouse.
DR   CTD; 84223; -.
DR   MGI; MGI:1916957; Iqcg.
DR   VEuPathDB; HostDB:ENSMUSG00000035578; -.
DR   eggNOG; ENOG502QQR7; Eukaryota.
DR   GeneTree; ENSGT00730000111263; -.
DR   HOGENOM; CLU_052522_0_0_1; -.
DR   InParanoid; Q80W32; -.
DR   OMA; IMNTETL; -.
DR   OrthoDB; 1353340at2759; -.
DR   PhylomeDB; Q80W32; -.
DR   TreeFam; TF326203; -.
DR   BioGRID-ORCS; 69707; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Iqcg; mouse.
DR   PRO; PR:Q80W32; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q80W32; protein.
DR   Bgee; ENSMUSG00000035578; Expressed in spermatocyte and 88 other tissues.
DR   Genevisible; Q80W32; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0002177; C:manchette; IDA:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR   GO; GO:0044782; P:cilium organization; IBA:GO_Central.
DR   GO; GO:0007288; P:sperm axoneme assembly; IMP:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; IMP: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   1: Evidence at protein 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_0000282563"
FT   DOMAIN          372..401
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..45
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  49168 MW;  C38867360202E88E CRC64;
     MDEEEVEVVE SPSEVLQPEV TVVVTGEPPE AAEEDLDYEE EEETSPEVIE TLSLLDVLRV
     SAVMEDVIDQ LSILGYIIPV QYERRQSLTQ KASHEGASMI TTTPKKSTSL LTKEKSMMAE
     NKQRGQDFTF KKPTKQTMMT LETLKKIQND RQYFSDVIAN AMMEMQDSGS FTSLLKALGK
     ERDSKMNFHD VITREEKGRK QIKTLQKQLL DVKRERQMQV QNGNEYIAHL RDQLQEMKAK
     TNLENLYMKR NAELQISQTQ KKCNRAEELL LEEIEKLRMK TEEENRVHTE IEMFLKKQQQ
     KLEEKLEFWM EKFDKDTEAK QNELNALKAA KASDLVHLQD LAKMIREYEQ VIIEDRIEKE
     KTRKKLEQDD LELRSIVKLQ AWWRGSVVRK EIGNFKMPKK DKDDSKDSKG KEKEKRRKK
 
 
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