DRC4_BOVIN
ID DRC4_BOVIN Reviewed; 478 AA.
AC A5D7M3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Dynein regulatory complex subunit 4 {ECO:0000250|UniProtKB:O95995};
DE AltName: Full=Growth arrest-specific protein 8;
DE Short=GAS-8;
GN Name=GAS8; Synonyms=DRC4 {ECO:0000250|UniProtKB:O95995};
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=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) 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. 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}.
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DR EMBL; BC140613; AAI40614.1; -; mRNA.
DR RefSeq; NP_001091038.1; NM_001097569.2.
DR AlphaFoldDB; A5D7M3; -.
DR SMR; A5D7M3; -.
DR STRING; 9913.ENSBTAP00000009333; -.
DR PaxDb; A5D7M3; -.
DR PRIDE; A5D7M3; -.
DR GeneID; 504318; -.
DR KEGG; bta:504318; -.
DR CTD; 2622; -.
DR eggNOG; ENOG502QQDA; Eukaryota.
DR InParanoid; A5D7M3; -.
DR OrthoDB; 1257437at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IBA:GO_Central.
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 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_0000306331"
FT REGION 1..114
FT /note="Regulates microtubule-binding"
FT /evidence="ECO:0000250|UniProtKB:Q60779"
FT REGION 1..31
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 27..201
FT /evidence="ECO:0000255"
FT COILED 246..427
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 56049 MW; 95BFDA2C4FCF0A40 CRC64;
MAPKKKGKKG KGKGTPIVDG LAPEDMSKEQ VEEHIGRIRE ELDREREERN YFQLERDKIH
TFWEITRRQL EEKKAELRNK DREMEEAEER HQVEIKVYKQ KVKHLLYEHQ SSLTEMKAEG
TVVMKLAQKE HRAQEGTLRR DMRALKVELK EQELANEVMV KNLRLKHTEE ITKMRNDFER
QVREIEAKYD KKMKMLRDEL DLRRKTEIHE VEERKNGQIT TLMQRHEEAF TDIKNYYNDI
TLNNLALINS LKEQMEDMGK KEEHLEKEMT EVAMQNRRLA DPLQKAREEM SDMQKKLGSY
ERDKQILVCT KARLKVTEKE LKSLRWEHEV LEQRFIKVQQ ERDDLYHKFT SAILEVQQKA
GFRNLVLERK VQALVAAVEK KEVQFNEVLA ASNLDPAALT LVSRKLEDVL ESKNSAIKDL
QYELARVCKA HNDLLRTYEA KLLAFGVPLD NVGFKPLDTA VIGQTLGQGP AGLVGTPT
