DRC4_RAT
ID DRC4_RAT Reviewed; 478 AA.
AC Q499U4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Dynein regulatory complex subunit 4 {ECO:0000250|UniProtKB:Q60779};
DE AltName: Full=Growth arrest-specific protein 11;
DE Short=GAS-11;
DE AltName: Full=Growth arrest-specific protein 8;
DE Short=GAS-8;
GN Name=Gas8; Synonyms=Drc4 {ECO:0000250|UniProtKB:Q60779}, Gas11;
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=Prostate;
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. Plays an important role in the assembly of
CC the N-DRC linker. Plays dual roles at both the primary (or non-motile)
CC cilia to regulate hedgehog signaling and in motile cilia to coordinate
CC cilia movement. Required for proper motile cilia functioning.
CC Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh)
CC signaling pathway by facilitating the trafficking of SMO into the
CC cilium and the stimulation of SMO activity in a GRK2-dependent manner.
CC {ECO:0000250|UniProtKB:Q60779, ECO:0000250|UniProtKB:Q7XJ96}.
CC -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC).
CC Interacts with microtubules. Interacts with SMO. Interacts (via coiled-
CC coil domains) with RAB3B (in GTP-bound form) (By similarity). Interacts
CC with DRC7 (By similarity). {ECO:0000250|UniProtKB:Q60779,
CC ECO:0000250|UniProtKB:Q7XJ96}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60779}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O95995}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q60779}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:O95995}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q60779}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O95995}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:O95995}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000250|UniProtKB:Q7XJ96}. Note=Associates with
CC microtubules. Localized to the cytoplasm of round spermatids, the tails
CC of elongating spermatids, and mature spermatid tail bundles protruding
CC into the lumen, and in the flagellum of epididymal spermatozoa.
CC {ECO:0000250|UniProtKB:O95995, ECO:0000250|UniProtKB:Q60779}.
CC -!- SIMILARITY: Belongs to the DRC4 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; BC099759; AAH99759.1; -; mRNA.
DR RefSeq; NP_001034119.1; NM_001039030.1.
DR AlphaFoldDB; Q499U4; -.
DR SMR; Q499U4; -.
DR IntAct; Q499U4; 1.
DR STRING; 10116.ENSRNOP00000031180; -.
DR PaxDb; Q499U4; -.
DR Ensembl; ENSRNOT00000029999; ENSRNOP00000031180; ENSRNOG00000026964.
DR GeneID; 361438; -.
DR KEGG; rno:361438; -.
DR UCSC; RGD:1307817; rat.
DR CTD; 2622; -.
DR RGD; 1307817; Gas8.
DR eggNOG; ENOG502QQDA; Eukaryota.
DR GeneTree; ENSGT00390000009477; -.
DR HOGENOM; CLU_045343_0_0_1; -.
DR InParanoid; Q499U4; -.
DR OMA; SWEHEVL; -.
DR OrthoDB; 1257437at2759; -.
DR PhylomeDB; Q499U4; -.
DR Reactome; R-RNO-5635838; Activation of SMO.
DR PRO; PR:Q499U4; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000026964; Expressed in testis and 19 other tissues.
DR Genevisible; Q499U4; RN.
DR GO; GO:0097729; C:9+2 motile cilium; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0060294; P:cilium movement involved in cell motility; ISO:RGD.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1904526; P:regulation of microtubule binding; ISS:UniProtKB.
DR InterPro; IPR039308; GAS8.
DR InterPro; IPR025593; GAS8_dom.
DR PANTHER; PTHR31543; PTHR31543; 1.
DR Pfam; PF13851; GAS; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW Golgi apparatus; Microtubule; Reference proteome.
FT CHAIN 1..478
FT /note="Dynein regulatory complex subunit 4"
FT /id="PRO_0000306332"
FT REGION 1..114
FT /note="Regulates microtubule-binding"
FT /evidence="ECO:0000250|UniProtKB:Q60779"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..258
FT /note="Microtubule-binding"
FT /evidence="ECO:0000250|UniProtKB:Q60779"
FT REGION 357..478
FT /note="Interaction with SMO"
FT /evidence="ECO:0000250|UniProtKB:O95995"
FT COILED 24..201
FT /evidence="ECO:0000255"
FT COILED 243..427
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 56313 MW; DD3282C9AA68E929 CRC64;
MAPKRRGKKG KAKGNAVVDG VAPEDMSKEQ VEEHVARIRE ELDREREERN YFQLERDKIH
TFWEITRRQL EEKKAELRNK DREMEEAEER HQVEIKVYKQ KVKHLLYEHQ NNLAEVKTEG
TVVMKLAQKE HRAQEGALRK DMRVLKVELK EQELANEVVI KNLRLKQAEE ITKMRNDFER
QVREIEAKYD KKMKMLRDEL DLRRKTEIHE VEERKNGQIS TLMQRHEEAF TDIKNYYNDI
TLNNLALINS LKEQMEDMRK KEEYLEREMA EVSLQNKRLA EPLQRAKEEM SEMQKRLGNH
ERDKQILACT KARLKVTEKE LKDLKWEHEI LEQRFIKVQQ EREELYRKFT AAIQEVQQKT
GFKNLVLERK LQALNAAVEK REVQFNEVLA ASNLDPTALT LVSRKLEDVL ESKNTTIKDL
QYELARVCKA HNDLLRTYEA KLLAFGIPLD NVGFKPLETA VIGQTLGQGP AGLVGAPT