ID A0A401RJL7_CHIPU Unreviewed; 905 AA.
AC A0A401RJL7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Dynein axonemal assembly factor 1 {ECO:0000256|ARBA:ARBA00024429, ECO:0000256|RuleBase:RU364076};
GN ORFNames=chiPu_0017889 {ECO:0000313|EMBL:GCC18319.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC18319.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC18319.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC18319.1}.
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DR EMBL; BEZZ01001403; GCC18319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RJL7; -.
DR STRING; 137246.A0A401RJL7; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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; 5.
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:UP000287033};
KW Repeat {ECO:0000256|RuleBase:RU364076}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 102136 MW; 9E85C929E86E0160 CRC64;
MGDSTEQTEF EGHQVNEQLT CSEETETLRS EGECKLQKGD QLHDQKGADC LGVHELNSTK
PQEKAKDSGS SSIIPALTLS AMGDGAVQTE NHQGTDQLSC NEETKPVRSV GESKLQKGEQ
LYDQEGMESL EIHEPNFRKA QEKRKDSEYS SVIPAVLVSA MGDGTVQTNT EDHHENKQLS
SGEEAEPVRS ESENKLQKGD QLHHQEGMDS GEVHELNSRK PEEKAKKDSE SSSVIPAVAL
SAIRDGTVQT ESENPHVTEQ SYFSEGTVPV RSEEQNKLQK DDKLHDQEGT KSPELHELNS
RRPQEKVKKD SGPRMTKQFL RRHCKEQKLY QTPYLNDTLY LHFKGFSCIE NLEEYTGLRC
LWLESNGLLR IENLDAQTEL RCLFLHQNLI HKIENLEPLQ KLDSLNLSNN YIKSIENLSC
LPALKTLQLA HNRLSTVKDI EHLKECPSLS VLDLSHNKLT DPDIITVFEA MPDLHVLNLM
GNEVIKKISN YRKVVTVRLH HLTYLDDRPV FPKDRACAEA WARGGWKAEK EERMQWETSE
RKKIQDSLDA LSVIKRKAEE KRRLQEMEER GEDSNSKSND PEIIPCYSSF ESQQKIETFV
NDVVKIQEEI LEDQQQLAER KTETATENQP KGSSTRIVDQ AALTCSLDRG NSTEFAQSEE
QVFSPSLDPS DQLQSTVFNS NIADSSSNKM PAERVLVTEL AKTNTIETIC LEEDRKLYID
DLPDLEELSD SSEPDQASSY KTVYRPKIEI IAAEYDNSEL DTGEGMEGLI WNITDEINEE
SSADLKENEC GDKTSQKELS EISEEKSATQ LTTSKIGNML TSERNVEITT LELSTPPGIP
EEDQPTRILI GEISSQSVTE STDQIKLLTE GNFTHRGPEG EKIKEELAIL ELDHIHTEDI
EFGLD
//
