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PHO19_ARATH
ID   PHO19_ARATH             Reviewed;         800 AA.
AC   Q9LJW0; Q6R8G1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phosphate transporter PHO1 homolog 9;
DE   AltName: Full=Protein PHO1 homolog 9;
DE            Short=AtPHO1;H9;
GN   Name=PHO1-H9; OrderedLocusNames=At3g29060; ORFNames=MRI12.4;
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 [MRNA], TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=15122012; DOI=10.1104/pp.103.037945;
RA   Wang Y., Ribot C., Rezzonico E., Poirier Y.;
RT   "Structure and expression profile of the Arabidopsis PHO1 gene family
RT   indicates a broad role in inorganic phosphate homeostasis.";
RL   Plant Physiol. 135:400-411(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [3]
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).
CC   -!- FUNCTION: May transport inorganic phosphate (Pi). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in pollen grains.
CC       {ECO:0000269|PubMed:15122012}.
CC   -!- INDUCTION: Not induced by Pi deficiency. {ECO:0000269|PubMed:15122012}.
CC   -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR   EMBL; AY507961; AAR99491.1; -; mRNA.
DR   EMBL; AP000388; BAB02948.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77530.1; -; Genomic_DNA.
DR   RefSeq; NP_189549.2; NM_113828.3.
DR   AlphaFoldDB; Q9LJW0; -.
DR   STRING; 3702.AT3G29060.1; -.
DR   PaxDb; Q9LJW0; -.
DR   PRIDE; Q9LJW0; -.
DR   ProteomicsDB; 235059; -.
DR   EnsemblPlants; AT3G29060.1; AT3G29060.1; AT3G29060.
DR   GeneID; 822550; -.
DR   Gramene; AT3G29060.1; AT3G29060.1; AT3G29060.
DR   KEGG; ath:AT3G29060; -.
DR   Araport; AT3G29060; -.
DR   TAIR; locus:2092783; AT3G29060.
DR   eggNOG; KOG1162; Eukaryota.
DR   HOGENOM; CLU_006116_2_0_1; -.
DR   InParanoid; Q9LJW0; -.
DR   OMA; KHRITYF; -.
DR   OrthoDB; 536327at2759; -.
DR   PhylomeDB; Q9LJW0; -.
DR   PRO; PR:Q9LJW0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LJW0; baseline and differential.
DR   Genevisible; Q9LJW0; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0000822; F:inositol hexakisphosphate binding; IBA:GO_Central.
DR   GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central.
DR   GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
DR   CDD; cd14476; SPX_PHO1_like; 1.
DR   InterPro; IPR004342; EXS_C.
DR   InterPro; IPR034092; PHO1_SPX.
DR   InterPro; IPR004331; SPX_dom.
DR   Pfam; PF03124; EXS; 1.
DR   Pfam; PF03105; SPX; 1.
DR   PROSITE; PS51380; EXS; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Phosphate transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..800
FT                   /note="Phosphate transporter PHO1 homolog 9"
FT                   /id="PRO_0000398163"
FT   TOPO_DOM        1..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..439
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        461..483
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..520
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        542..670
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        671..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        692..718
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        719..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        740..800
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..346
FT                   /note="SPX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT   DOMAIN          606..800
FT                   /note="EXS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT   REGION          38..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..119
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        200
FT                   /note="R -> K (in Ref. 1; AAR99491)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        490
FT                   /note="S -> P (in Ref. 1; AAR99491)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   800 AA;  92441 MW;  57080C8237D02ADF CRC64;
     MKFGREFETQ MIQEWKEAYM DYRSLKSIVK QILRYRLQKQ QRPPPPPPPP STGDTVPLKT
     DGGEGGGGGG GGGPGLSRRI SLYRAFSGLT NRASRSPKKS HKHHNPLSSK RHHHHHNHHH
     YHLFDDDEEQ IILINEDETA SYTTTFLNSA EEGGEMEVQF FRRLDGEFNK VLRFYKQKVE
     NVMEEADELS RQLNVLIALR VKVENPHVHL PPDLNSVASA PSSPHSTMRT PAPSPMDVIR
     EMEKTEDKKV FKPAPVEMLD HVKLKIDPET PLLTLKMMIL GLPSEQTFSK PELRRAEELM
     NRAFVEFYQK LRFLKSYCFL NQLAFAKILK KYDKTTSRNA SKPYLNTVDH SYLGSCDEVS
     RLMSRVEATF IKHFANGNHR EGMKCLRPKT KREKHRITYF LGFFSGCAVA LAIAITVLVH
     IRGLTKSEGR HQYMENIFPL YSLFGFVAVH LFMYAADIYF WSRYRVNYPF IFGFEQGNDL
     GYREVLLVGS GLAVLTFGGV ISNLDMEMDP RTKSFSVITE LVPLALLVCL MMVLFCPFNI
     IYRSSRYFFV GSVFRCLLSP LYKVILPDFF LADQLTSQVQ TFRSLLFYVC YYGWGGDFKR
     RTHTCYDSEI YKELYLVVAI IPYWFRFAQS IRRLVEEKDK MHGLNALKYL STILAVAART
     IFEMKRGTYW LTVAVTTSSI ATLFNTYWDI FRDWGLMNRN SKNPWLRDKL LVPYKSIYFI
     VMVANVVLRL AWMQTVLGIK EAPFLHKRAL VAVVASLEIV RRGIWNFFRL ENEHLNNVGK
     YRAFKSVPLP FQELGGSKSV
 
 
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