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PAM71_ARATH
ID   PAM71_ARATH             Reviewed;         370 AA.
AC   Q94AX5; Q9SH65;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protein PAM71, chloroplastic {ECO:0000303|PubMed:27020959};
DE   AltName: Full=CA(2+)/H(+) ANTIPORTER 1 {ECO:0000303|PubMed:27302341};
DE   AltName: Full=GDT1-like protein 1 {ECO:0000305};
DE   AltName: Full=PHOTOSYNTHESIS AFFECTED MUTANT71 {ECO:0000303|PubMed:27020959};
DE   Flags: Precursor;
GN   Name=PAM71 {ECO:0000303|PubMed:27020959};
GN   Synonyms=CCHA1 {ECO:0000303|PubMed:27302341};
GN   OrderedLocusNames=At1g64150 {ECO:0000312|Araport:AT1G64150};
GN   ORFNames=F22C12.9 {ECO:0000312|EMBL:AAF24562.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=27302341; DOI=10.1016/j.molp.2016.05.015;
RA   Wang C., Xu W., Jin H., Zhang T., Lai J., Zhou X., Zhang S., Liu S.,
RA   Duan X., Wang H., Peng C., Yang C.;
RT   "A putative chloroplast-localized Ca(2+)/H(+) antiporter CCHA1 is involved
RT   in calcium and pH homeostasis and required for PSII function in
RT   Arabidopsis.";
RL   Mol. Plant 9:1183-1196(2016).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, AND
RP   TOPOLOGY.
RX   PubMed=27020959; DOI=10.1105/tpc.15.00812;
RA   Schneider A., Steinberger I., Herdean A., Gandini C., Eisenhut M., Kurz S.,
RA   Morper A., Hoecker N., Ruehle T., Labs M., Fluegge U.I., Geimer S.,
RA   Schmidt S.B., Husted S., Weber A.P., Spetea C., Leister D.;
RT   "The evolutionarily conserved protein PHOTOSYNTHESIS AFFECTED MUTANT71 is
RT   required for efficient manganese uptake at the thylakoid membrane in
RT   Arabidopsis.";
RL   Plant Cell 28:892-910(2016).
CC   -!- FUNCTION: Mn(2+)/H(+) exchanger, which transport Mn(2+)from the
CC       chloroplast stroma into the acidic thylakoid lumen (PubMed:27020959).
CC       Might be a chloroplast-localized Ca(2+)/H(+) antiporter
CC       (PubMed:27302341). Regulates Ca(2+), Mn(2+) and pH homeostasis
CC       (PubMed:27302341). Required for chloroplast development
CC       (PubMed:27302341). {ECO:0000269|PubMed:27020959,
CC       ECO:0000269|PubMed:27302341}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27020959}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:27302341}; Multi-pass membrane protein
CC       {ECO:0000255}. Thylakoid {ECO:0000269|PubMed:27020959}.
CC   -!- DISRUPTION PHENOTYPE: Defects in photosynthesis and reduced growth rate
CC       (PubMed:27302341, PubMed:27020959). Pale yellow leaves with reduced
CC       PSII activity (PubMed:27302341). Altered Ca(2+) and Mn(2+) partitioning
CC       in chloroplasts and reduced Mn(2+) binding to PSII (PubMed:27020959).
CC       {ECO:0000269|PubMed:27020959, ECO:0000269|PubMed:27302341}.
CC   -!- SIMILARITY: Belongs to the GDT1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF24562.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007764; AAF24562.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34202.1; -; Genomic_DNA.
DR   EMBL; AY045639; AAK73997.1; -; mRNA.
DR   EMBL; AY143875; AAN28814.1; -; mRNA.
DR   RefSeq; NP_564825.1; NM_105088.4.
DR   AlphaFoldDB; Q94AX5; -.
DR   BioGRID; 27940; 25.
DR   IntAct; Q94AX5; 25.
DR   STRING; 3702.AT1G64150.1; -.
DR   TCDB; 2.A.106.1.5; the ca(2+):h(+) antiporter-2 (caca2) family.
DR   PaxDb; Q94AX5; -.
DR   PRIDE; Q94AX5; -.
DR   ProteomicsDB; 248747; -.
DR   EnsemblPlants; AT1G64150.1; AT1G64150.1; AT1G64150.
DR   GeneID; 842719; -.
DR   Gramene; AT1G64150.1; AT1G64150.1; AT1G64150.
DR   KEGG; ath:AT1G64150; -.
DR   Araport; AT1G64150; -.
DR   TAIR; locus:2024628; AT1G64150.
DR   eggNOG; KOG2881; Eukaryota.
DR   HOGENOM; CLU_050130_1_0_1; -.
DR   InParanoid; Q94AX5; -.
DR   OMA; VRCISSK; -.
DR   OrthoDB; 919566at2759; -.
DR   PhylomeDB; Q94AX5; -.
DR   PRO; PR:Q94AX5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q94AX5; baseline and differential.
DR   Genevisible; Q94AX5; AT.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015085; F:calcium ion transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IMP:TAIR.
DR   GO; GO:0005384; F:manganese ion transmembrane transporter activity; IMP:TAIR.
DR   GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IDA:TAIR.
DR   GO; GO:0006816; P:calcium ion transport; IMP:TAIR.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEP:TAIR.
DR   GO; GO:0032468; P:Golgi calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0032472; P:Golgi calcium ion transport; IBA:GO_Central.
DR   GO; GO:0071421; P:manganese ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0010270; P:photosystem II oxygen evolving complex assembly; IMP:TAIR.
DR   InterPro; IPR001727; Gdt1.
DR   PANTHER; PTHR12608; PTHR12608; 1.
DR   Pfam; PF01169; UPF0016; 2.
DR   PROSITE; PS01214; UPF0016; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; Plastid; Reference proteome; Thylakoid;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..73
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           74..370
FT                   /note="Protein PAM71, chloroplastic"
FT                   /id="PRO_0000398764"
FT   TOPO_DOM        74..113
FT                   /note="Stromal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..161
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..188
FT                   /note="Stromal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..228
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..275
FT                   /note="Stromal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..315
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..348
FT                   /note="Stromal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000269|PubMed:27020959"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        54
FT                   /note="Y -> S (in Ref. 3; AAN28814/AAK73997)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  39074 MW;  5D3FF0E824889BE7 CRC64;
     MLSLNLSESL RIPFQNPRPP KSDFSSTSSS PSSSSRRCVS AYPIPIGFSV RNQYFSRCLT
     QLRRNESQQL GFRCFQRNDA ACYLEKAESE EHDRNLDVLV ESSIAHSRRE IQRVLMFLAV
     SGSVALLGTD PAFAASSIPN VTQSLVTSFG DLGDISSGFA SAFLLIFFSE LGDKTFFIAA
     LLAARNSAAT VFVGTFGALG IMTIISVVLG RTFHYVDEVL PFRFGGTDLP IDDIAAVCLL
     VYFGVSTLLD AVSDEGKADE EQKEAELAVS ELSGNGAGIV AAANTIISTF ALVFVAEWGD
     KSFFSTIALA AASSPLGVIA GALAGHGAAT LLAVLGGSLL GNFLSEKAIA YVGGVLFLVF
     AAVTVAEIVT
 
 
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