ASNA1_CHLRE
ID ASNA1_CHLRE Reviewed; 777 AA.
AC A8JGB0;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=ATPase ARSA1 {ECO:0000305};
DE Short=Cr-ArsA1 {ECO:0000303|PubMed:28382961};
DE EC=3.6.-.- {ECO:0000305};
DE AltName: Full=Arsenical pump-driving ATPase homolog 1 {ECO:0000305};
DE AltName: Full=Arsenite-stimulated ATPase homolog 1 {ECO:0000305};
DE AltName: Full=Protein ANTENNA SIZE MUTANT 1 {ECO:0000303|PubMed:23167510};
GN Name=ARSA1 {ECO:0000303|PubMed:28382961};
GN Synonyms=AS1 {ECO:0000303|PubMed:23167510};
GN ORFNames=CHLREDRAFT_132949 {ECO:0000312|EMBL:EDO97076.1};
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 [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).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23167510; DOI=10.1111/tpj.12077;
RA Formighieri C., Cazzaniga S., Kuras R., Bassi R.;
RT "Biogenesis of photosynthetic complexes in the chloroplast of Chlamydomonas
RT reinhardtii requires ARSA1, a homolog of prokaryotic arsenite transporter
RT and eukaryotic TRC40 for guided entry of tail-anchored proteins.";
RL Plant J. 73:850-861(2013).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH TOC34, AND SUBCELLULAR LOCATION.
RX PubMed=28382961; DOI=10.1038/srep46022;
RA Maestre-Reyna M., Wu S.M., Chang Y.C., Chen C.C., Maestre-Reyna A.,
RA Wang A.H., Chang H.Y.;
RT "In search of tail-anchored protein machinery in plants: reevaluating the
RT role of arsenite transporters.";
RL Sci. Rep. 7:46022-46022(2017).
CC -!- FUNCTION: ATPase required for the post-translational delivery of tail-
CC anchored (TA) proteins to the chloroplast. Required for the
CC accumulation of TOC34, an essential component of the outer chloroplast
CC membrane translocon (TOC) complex (PubMed:23167510, PubMed:28382961).
CC Recognizes and selectively binds the transmembrane domain of TA
CC proteins in the cytosol. This complex then targets to chloroplast,
CC where the tail-anchored protein is released for insertion. This process
CC is regulated by ATP binding and hydrolysis (PubMed:28382961).
CC {ECO:0000269|PubMed:23167510, ECO:0000269|PubMed:28382961}.
CC -!- SUBUNIT: Monomer (PubMed:28382961). Interacts with TOC34
CC (PubMed:28382961). {ECO:0000269|PubMed:28382961}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23167510,
CC ECO:0000269|PubMed:28382961}.
CC -!- DISRUPTION PHENOTYPE: Small chloroplast and strong decrease in
CC chlorophyll content. Defect in the accumulation of photosystem protein
CC complexes. Defect in the accumulation of TOC34, an essential component
CC of the outer chloroplast membrane translocon (TOC) complex, which, in
CC turn, catalyzes the import of nucleus-encoded precursor polypeptides
CC into the chloroplast. {ECO:0000269|PubMed:23167510}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDO97076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS496183; EDO97076.1; ALT_SEQ; Genomic_DNA.
DR PDB; 5ZME; X-ray; 3.60 A; A=91-777.
DR PDB; 5ZMF; X-ray; 3.56 A; A=91-777.
DR PDBsum; 5ZME; -.
DR PDBsum; 5ZMF; -.
DR AlphaFoldDB; A8JGB0; -.
DR SMR; A8JGB0; -.
DR STRING; 3055.EDO97076; -.
DR TCDB; 3.A.19.1.4; the guided entry of tail anchored protein (get) family.
DR PaxDb; A8JGB0; -.
DR EnsemblPlants; PNW69686; PNW69686; CHLRE_24g755097v5.
DR Gramene; PNW69686; PNW69686; CHLRE_24g755097v5.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_2_1_1; -.
DR InParanoid; A8JGB0; -.
DR OrthoDB; 992208at2759; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR016300; ATPase_ArsA/GET3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10803; PTHR10803; 2.
DR Pfam; PF02374; ArsA_ATPase; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Transport.
FT CHAIN 1..777
FT /note="ATPase ARSA1"
FT /id="PRO_0000442530"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:Q12154"
FT ACT_SITE 483
FT /evidence="ECO:0000250|UniProtKB:Q12154"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q12154"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q12154"
FT BINDING 454..461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q12154"
FT BINDING 712
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q12154"
SQ SEQUENCE 777 AA; 82383 MW; 5233CC2D29FF1E5B CRC64;
MALASGNRLG SARGQTCADA SGRVAPRLLS RACSGSPLAL GVLACLGAAS SVKPHPRLPA
TTSAASAPLP ARGPAPCAAV PTVVTPDNAT GVFEELAAGQ QRKYIMISGK GGVGKTSLSA
SLAVKLAAAG HTTLVVSTDP AHSLSDSLAQ DVSGGRPVLL QGTDLPLWGL EIDPEEAKRE
FFEGSGAGQD GEAGGPSAAS QVSDFMNRMG MGFVIDQLKE LKLGELLNTP PPGLDEAVAI
AKVVQFVQAA EYARFSRIVF DTAPTGHTLR LLALPDFVDA SLAKVIRLRK KLNGATSVVR
GLFGAGESQD EAVEKLELLQ QRVRMVKALF RDKTQTEFII ATIPTYLGVN ESSRLLQALR
AEQIPCKRII VNQIVGPQQG DAYLRMKMKD QIAALEMVAN DPGLRPLRKV IAPMVDVEVR
GVPALSYFGN VVWKDVYDQM NQGADRKFFL LGGKGGVGKT SCSSSLAVHF ANDGLPTLVV
STDPAHSLSD AFDQDLSGGS PVKITSPLGD ELPLWGLQLD PEQAKAELRA VLADDGGKKL
NETLDGLGLG VISDQLKDLQ LGELLDTPPP GVDEAIAIAK VVQFLKAPEY SHFKRIVFDT
APTGHTLRLL SLPDFLDASI GKLVRLRQKL SAATSAVKNL FSGGQPGEED VAVKRLEALQ
ASMEDAKAMF RNQQTTEFII VTIPTVMATA ESCRLASALQ HEGIPLKTII VNQVVQANAT
DKFLTARRAD QARALHHLEE DTGPDGLASL QLIKAPLCDL EVRGVPALSY FGNVVWK
