ID A0A3P8ZX01_ESOLU Unreviewed; 762 AA.
AC A0A3P8ZX01;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Dynein axonemal assembly factor 1 {ECO:0000256|ARBA:ARBA00024429, ECO:0000256|RuleBase:RU364076};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000033415.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000033415.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000033415.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Cilium-specific protein required for the stability of the
CC ciliary architecture. Plays a role in cytoplasmic preassembly of dynein
CC arms. Involved in regulation of microtubule-based cilia and actin-based
CC brush border microvilli. {ECO:0000256|RuleBase:RU364076}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000256|ARBA:ARBA00004138, ECO:0000256|RuleBase:RU364076}.
CC -!- SIMILARITY: Belongs to the DNAAF1 family.
CC {ECO:0000256|ARBA:ARBA00006453, ECO:0000256|RuleBase:RU364076}.
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 AlphaFoldDB; A0A3P8ZX01; -.
DR Ensembl; ENSELUT00000000751.2; ENSELUP00000033415.2; ENSELUG00000011663.2.
DR GeneTree; ENSGT00940000158494; -.
DR InParanoid; A0A3P8ZX01; -.
DR OMA; RDHQEGD; -.
DR Proteomes; UP000265140; LG02.
DR Bgee; ENSELUG00000011663; Expressed in mesonephros and 4 other cell types or tissues.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0060271; P:cilium assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR45973:SF19; DYNEIN AXONEMAL ASSEMBLY FACTOR 1; 1.
DR PANTHER; PTHR45973; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT SDS22-RELATED; 1.
DR Pfam; PF14580; LRR_9; 1.
DR SMART; SM00365; LRR_SD22; 4.
DR SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
DR PROSITE; PS51450; LRR; 3.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|RuleBase:RU364076};
KW Cilium {ECO:0000256|ARBA:ARBA00023069, ECO:0000256|RuleBase:RU364076};
KW Leucine-rich repeat {ECO:0000256|RuleBase:RU364076};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Repeat {ECO:0000256|RuleBase:RU364076}.
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 87533 MW; 2137A1E444D44C40 CRC64;
MHDPKPLDPA EVKVEDESNK ESNRVTFQTG EAISATSTRE NAPTANRNSQ PPEVDKLIQV
KQQEKVKDSG PRMTKQVLKE HCKQNKLYAT PRLNDTLYLH YKGFSTIENL EEYTGLKCLW
LECNGLQRIQ NLQAQTDLRC LFLHQNLIHK LENLEPLSKL CTLNVCNNYI RTIENIGCLP
DLGTLQIAHN KLQTVGDIEH LSQCFSISVL DMSHNLLDDP EILTVLEKMP DLRVLNLMGN
EVVKKIPSYR KTLIIRLKQL TYLDDRPVFP KDRACAEAWG AGGPKAELRE RELWKTRERK
KIQDCLDAIA TIRDQPRERR RLREQQERGE CETPTTPEVE SPSEENQSSS QKEKIQTFGE
DSLEACEEFL QTSKEEAEKE ELGNKQPQKE QLYRDQPERG QQQGDQPERG QQQGDQPERG
QQQGDQPERG QQQGDQPERG QQQGDQPEQG QQQGDQPERG QKQGDQPERG QHQGDHPYRE
QLQGDQLDRE QLQGDQLDRE QLQGDQLDRE QLQGDQLDRQ QLQGDQPARE QLQGDQPARE
QLQRDQPARE QLQQDQPARE QLQGDQPARE QLQGDQPARE QLQRDQPARE KQQGDQTDRK
KSNMEWSVNR RSQGQKAEAI MEHGPGPLVT ELEETEEIDT IHLGSHPQLY IDDLPDLEDI
DLEDPERICL FSSERVLRPK IEVISGDDNN EELISHQNGI VLASETMHTS NQCSDSLFSV
YNTISNKLPT YAPELISISQ EQPRHRQSPE AIKPHGLIEE LD
//
