ARL3_CHLRE
ID ARL3_CHLRE Reviewed; 177 AA.
AC A8ISN6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ADP-ribosylation factor-like protein 3 {ECO:0000250|UniProtKB:Q8QHI3};
GN Name=ARL3 {ECO:0000250|UniProtKB:Q8QHI3};
GN ORFNames=CHLREDRAFT_128761 {ECO:0000312|EMBL:EDP04202.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gotthardt K.;
RL Unpublished observations (SEP-2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
CC -!- FUNCTION: Small GTP-binding protein which cycles between an inactive
CC GDP-bound and an active GTP-bound form, and the rate of cycling is
CC regulated by guanine nucleotide exchange factors (GEF) and GTPase-
CC activating proteins (GAP). Required for normal cytokinesis and cilia
CC signaling. Required for targeting proteins to the ciliary membrane by
CC releasing myristoylated protein from unc119 cargo adapters into the
CC cilium. {ECO:0000250|UniProtKB:P36405}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P36405}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P36405}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P36405}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P36405}. Nucleus {ECO:0000250|UniProtKB:P36405}.
CC Cytoplasm, cytoskeleton, microtubule organizing center
CC {ECO:0000250|UniProtKB:P36405}. Cytoplasm
CC {ECO:0000250|UniProtKB:P36405}. Note=Not detected to interphase
CC microtubules. Present on the mitotic spindle.
CC {ECO:0000250|UniProtKB:P36405}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP04202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS496122; EDP04202.1; ALT_SEQ; Genomic_DNA.
DR PDB; 5DE3; X-ray; 1.42 A; A=17-177.
DR PDB; 5DI3; X-ray; 2.50 A; A=1-177.
DR PDBsum; 5DE3; -.
DR PDBsum; 5DI3; -.
DR AlphaFoldDB; A8ISN6; -.
DR SMR; A8ISN6; -.
DR STRING; 3055.EDP04202; -.
DR PaxDb; A8ISN6; -.
DR PRIDE; A8ISN6; -.
DR ProMEX; A8ISN6; -.
DR EnsemblPlants; PNW84028; PNW84028; CHLRE_04g218250v5.
DR Gramene; PNW84028; PNW84028; CHLRE_04g218250v5.
DR eggNOG; KOG0074; Eukaryota.
DR HOGENOM; CLU_040729_12_0_1; -.
DR InParanoid; A8ISN6; -.
DR OMA; ASEDITQ; -.
DR OrthoDB; 1271528at2759; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044612; ARL2/3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR45697; PTHR45697; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Nucleus; Protein transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..177
FT /note="ADP-ribosylation factor-like protein 3"
FT /id="PRO_0000434553"
FT BINDING 23..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P84080"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P84080"
FT BINDING 159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P84080"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P11076"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:5DE3"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:5DE3"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:5DE3"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5DE3"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5DE3"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5DE3"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5DE3"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:5DE3"
SQ SEQUENCE 177 AA; 19783 MW; 4F34021D06A3492D CRC64;
MGLLSLIRGL KKKEGEARIL VLGLDNAGKT TILKALSEED ITTITPTQGF NIKSLSRDGF
NLKIWDIGGQ KSIRPYWRNY FDQTDALIYV IDSADSKRLS ESEFELTELL QEEKMTGVPL
LVFANKQDLV GALAADEIAS TLDLTSIRDR PWQIQACSAK QGTGLKEGME WMMKQVK
