ASNA2_CHLRE
ID ASNA2_CHLRE Reviewed; 362 AA.
AC A8IXB8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATPase ARSA2 {ECO:0000255|HAMAP-Rule:MF_03112};
DE Short=Cr-ArsA2 {ECO:0000303|PubMed:28382961};
DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenical pump-driving ATPase 2 {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenite-stimulated ATPase 2 {ECO:0000255|HAMAP-Rule:MF_03112};
GN Name=ARSA2 {ECO:0000303|PubMed:28382961};
GN ORFNames=CHLREDRAFT_102612 {ECO:0000312|EMBL:EDP03358.1};
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, SUBUNIT, INTERACTION WITH SEC61B, 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 endoplasmic reticulum. Recognizes and
CC selectively binds the transmembrane domain of TA proteins in the
CC cytosol. This complex then targets to the endoplasmic reticulum by
CC membrane-bound receptors, where the tail-anchored protein is released
CC for insertion. This process is regulated by ATP binding and hydrolysis
CC (PubMed:28382961). ATP binding drives the homodimer towards the closed
CC dimer state, facilitating recognition of newly synthesized TA membrane
CC proteins. ATP hydrolysis is required for insertion. Subsequently, the
CC homodimer reverts towards the open dimer state, lowering its affinity
CC for the membrane-bound receptor, and returning it to the cytosol to
CC initiate a new round of targeting (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_03112, ECO:0000269|PubMed:28382961}.
CC -!- SUBUNIT: Homodimer (PubMed:28382961). Interacts with SEC61B
CC (PubMed:28382961). {ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:28382961}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28382961}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}. Endoplasmic reticulum
CC {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP03358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS496126; EDP03358.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A8IXB8; -.
DR SMR; A8IXB8; -.
DR TCDB; 3.A.19.1.5; the guided entry of tail anchored protein (get) family.
DR PaxDb; A8IXB8; -.
DR EnsemblPlants; PNW85801; PNW85801; CHLRE_03g204800v5.
DR Gramene; PNW85801; PNW85801; CHLRE_03g204800v5.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; A8IXB8; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043529; C:GET complex; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IEA:EnsemblPlants.
DR GO; GO:0048767; P:root hair elongation; IEA:EnsemblPlants.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03112; Asna1_Get3; 1.
DR InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR016300; ATPase_ArsA/GET3.
DR InterPro; IPR027542; ATPase_ArsA/GET3_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10803; PTHR10803; 1.
DR Pfam; PF02374; ArsA_ATPase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Transport.
FT CHAIN 1..362
FT /note="ATPase ARSA2"
FT /id="PRO_0000442531"
FT ACT_SITE 58
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
SQ SEQUENCE 362 AA; 39538 MW; 3122EEDE668BFABE CRC64;
MAADMPDPTL QNVVDQKELK WIFVGGKGGV GKTTTSSSLA VALAESGTRN RVLIISTDPA
HNLSDAFRQK FTKTPTLVNG FTNLFAMEVD PQPDIGEMEQ LEWAQDSFLT ELAGSIPGID
EAMSFAEVMK QVQTMDYDTI VFDTAPTGHT LRLLNFPTIL EKGLSKLVAL KGAMGGMMGQ
VTRMLGGMAG GGEGAADLPD QLLGKVEGML DVVRKVSAQF KDPLLTTFVA VCIPEFLSLY
ETERLVQELA KFEIDCRNIV INQIIFPESV GGSRLLDARV RMQQKYLDQF YELYEDFHIL
QLPLLEEEVR GPEALKAFAV NLLKPYVPAP PTDAAARQAA LVSEVAALKK RVAELEAALA
KK
