ID W5NH33_LEPOC Unreviewed; 755 AA.
AC W5NH33;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Dynein regulatory complex protein 1 {ECO:0000256|ARBA:ARBA00013815};
DE AltName: Full=Coiled-coil domain-containing protein 164 {ECO:0000256|ARBA:ARBA00031554};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019942.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019942.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000256|ARBA:ARBA00004430}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000256|ARBA:ARBA00004611}.
CC -!- SIMILARITY: Belongs to the DRC1 family.
CC {ECO:0000256|ARBA:ARBA00009688}.
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DR EMBL; AHAT01015811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01015812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NH33; -.
DR STRING; 7918.ENSLOCP00000019942; -.
DR Ensembl; ENSLOCT00000019975.1; ENSLOCP00000019942.1; ENSLOCG00000016179.1.
DR eggNOG; ENOG502QQ2B; Eukaryota.
DR GeneTree; ENSGT00940000153804; -.
DR InParanoid; W5NH33; -.
DR OMA; MPQELHN; -.
DR Proteomes; UP000018468; Linkage group LG1.
DR Bgee; ENSLOCG00000016179; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IBA:GO_Central.
DR GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central.
DR GO; GO:0003352; P:regulation of cilium movement; IBA:GO_Central.
DR InterPro; IPR039505; DRC1/2_N.
DR InterPro; IPR039750; DRC1/DRC2.
DR InterPro; IPR029440; DRC1_C.
DR PANTHER; PTHR21625:SF1; DYNEIN REGULATORY COMPLEX PROTEIN 1; 1.
DR PANTHER; PTHR21625; NYD-SP28 PROTEIN; 1.
DR Pfam; PF14772; NYD-SP28; 1.
DR Pfam; PF14775; NYD-SP28_assoc; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Flagellum {ECO:0000256|ARBA:ARBA00022846};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 92..193
FT /note="Dynein regulatory complex protein 1/2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14772"
FT DOMAIN 673..732
FT /note="Dynein regulatory complex protein 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14775"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..228
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 274..308
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 337..382
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 46..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 89149 MW; 5BC4331CA61D2854 CRC64;
MNQAENGGEE REESGPSVQS ENPEERIAAR RLRIAARIEA KKRILREALG DSSHEKKDKE
EMRKSQKQVE QSCKRMIKLQ ADGTELVTNI QVAGDWKESQ RRTEEEEARR QRTEKLESEA
KTSLEKFEEI TKKWTSARMK EIPQDLREAL NMQQQQCALL IEEKNKLITD LQQELKASDD
RYVKDLKKQA EDIDLMIERM EEQIKNLIKS YREELDQIEK AFELERRELL DNNRKKWEQM
MQSRRDKELE YLILRMKRVE EHEKQLQQLR VEDAEEYNMI KIKLETDVQI LEQQLQQMKA
TYQLNQEKLE YNFQVLKKRD EENTITKSQQ KRKITSLLRL QDVLNNLRIK CAKQEKQSRE
ENHSLTDDYK RIMQQYKEMQ KKIRHFAAID AKTFEDIWLM NEAEVKELVE KALQTDRLIH
EQQLGVAWVR PPLPFMEHLG PIIPQRKLKK SAGQLAGELL SQDQDVTDTE HPVSTAEDHM
KISAKTVKRL LEILCDETGF LIESKLLKLL SPLEKDEQSL MKLDAIFLAL GIENEEDVYK
LADFFMTYKQ QQKEDEDEDV GCIMSTVLSE IFYCTFLQFL NCLSKRNSLN TFLKFSEKPW
EMSQEQRRSR VLEREDSSSV PHSSSLDPIH PNDVLKALQA FTTEYCRPRS KTQPQCQSNV
LNLEERDDSE DRAYWESMAN VIPESKLKIW DALETALEKY YNVLTERAKL IDETDGLKQQ
NAELRMLLHQ YVNSRVNAEL EIPPTQVMQL EPAWN
//
