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VPY_PETHY
ID   VPY_PETHY               Reviewed;         535 AA.
AC   C7B178;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Protein VAPYRIN {ECO:0000303|PubMed:20804456};
DE            Short=PhVpy {ECO:0000303|PubMed:20804456};
DE   AltName: Full=Protein PENETRATION AND ARBUSCULE MORPHOGENESIS 1 {ECO:0000303|PubMed:17573800};
GN   Name=VPY {ECO:0000303|PubMed:20804456};
GN   Synonyms=PAM1 {ECO:0000303|PubMed:17573800};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   INDUCTION BY RAM1 AND RHIZOPHAGUS IRREGULARIS, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. W115;
RX   PubMed=20804456; DOI=10.1111/j.1365-313x.2010.04341.x;
RA   Feddermann N., Muni R.R., Zeier T., Stuurman J., Ercolin F., Schorderet M.,
RA   Reinhardt D.;
RT   "The PAM1 gene of petunia, required for intracellular accommodation and
RT   morphogenesis of arbuscular mycorrhizal fungi, encodes a homologue of
RT   VAPYRIN.";
RL   Plant J. 64:470-481(2010).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. W138;
RX   PubMed=17573800; DOI=10.1111/j.1365-313x.2007.03175.x;
RA   Reddy D.M.R.S., Schorderet M., Feller U., Reinhardt D.;
RT   "A petunia mutant affected in intracellular accommodation and morphogenesis
RT   of arbuscular mycorrhizal fungi.";
RL   Plant J. 51:739-750(2007).
RN   [3]
RP   REPRESSION BY INORGANIC PHOSPHATE.
RX   PubMed=21143680; DOI=10.1111/j.1365-313x.2010.04385.x;
RA   Breuillin F., Schramm J., Hajirezaei M., Ahkami A., Favre P., Druege U.,
RA   Hause B., Bucher M., Kretzschmar T., Bossolini E., Kuhlemeier C.,
RA   Martinoia E., Franken P., Scholz U., Reinhardt D.;
RT   "Phosphate systemically inhibits development of arbuscular mycorrhiza in
RT   Petunia hybrida and represses genes involved in mycorrhizal functioning.";
RL   Plant J. 64:1002-1017(2010).
CC   -!- FUNCTION: Required for arbuscular mycorrhizal (AM) symbiosis with AM
CC       fungi (e.g. Glomus intraradices, G. mosseae and Gigaspora margarita)
CC       both during fungal passage across root epidermis and for arbuscule
CC       formation in cortical cells; this symbiosis promotes phosphorus (P) and
CC       copper (Cu) uptake (PubMed:20804456, PubMed:17573800). Essential for
CC       infection by symbiotic nitrogen-fixing rhizobial bacteria leading to
CC       the formation of root nodules (By similarity).
CC       {ECO:0000250|UniProtKB:D3J162, ECO:0000269|PubMed:17573800,
CC       ECO:0000269|PubMed:20804456}.
CC   -!- SUBUNIT: Interacts with EX70I at the periarbuscular membrane (PAM)
CC       around the arbuscule hyphal tips. {ECO:0000250|UniProtKB:D3J162}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20804456}.
CC       Nucleus {ECO:0000269|PubMed:20804456}. Cell membrane
CC       {ECO:0000250|UniProtKB:D3J162}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Associated with
CC       mobile spherical structures that are associated with the tonoplast
CC       referred to as 'tonospheres'. In mycorrhizal roots, tonospheres are
CC       observed in the vicinity of intracellular hyphae (arbuscules)
CC       (PubMed:20804456). Observed associated with EX70I in zones adjacent to
CC       the periarbuscular membrane (PAM) around the arbuscule hyphal tips (By
CC       similarity). {ECO:0000250|UniProtKB:D3J162,
CC       ECO:0000269|PubMed:20804456}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots and, to a lower extent,
CC       in shoot tips, stems, leaves and flowers.
CC       {ECO:0000269|PubMed:20804456}.
CC   -!- DEVELOPMENTAL STAGE: During arbuscular mycorrhizal (AM) symbiosis with
CC       (AM) fungi (e.g. Glomus intraradices), accumulates mostly in root
CC       cortex cells containing arbuscules. {ECO:0000269|PubMed:20804456}.
CC   -!- INDUCTION: Regulated by RAM1 during arbuscular mycorrhiza (AM)
CC       formation after inoculation with Rhizophagus irregularis
CC       (PubMed:20804456). Repressed by inorganic phosphate (Pi), leading to
CC       defects in cortical AM colonization of roots in high Pi conditions
CC       (PubMed:21143680). {ECO:0000269|PubMed:20804456,
CC       ECO:0000269|PubMed:21143680}.
CC   -!- DISRUPTION PHENOTYPE: Impaired arbuscular mycorrhiza (AM) fungi (e.g.
CC       Glomus intraradices, G. mosseae and Gigaspora margarita) passage across
CC       root epidermis and abolished arbuscule formation in root cortex during
CC       AM symbiosis, thus leading to aborted hyphopodia and no arbuscules.
CC       {ECO:0000269|PubMed:17573800, ECO:0000269|PubMed:20804456}.
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DR   EMBL; FJ717417; ACU00619.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7B178; -.
DR   SMR; C7B178; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR   GO; GO:0010035; P:response to inorganic substance; IEP:UniProtKB.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000535; MSP_dom.
DR   InterPro; IPR008962; PapD-like_sf.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF13857; Ank_5; 1.
DR   Pfam; PF00635; Motile_Sperm; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
DR   PROSITE; PS50202; MSP; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Cell membrane; Cytoplasm; Membrane; Nucleus; Repeat.
FT   CHAIN           1..535
FT                   /note="Protein VAPYRIN"
FT                   /id="PRO_0000450031"
FT   DOMAIN          4..135
FT                   /note="MSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT   REPEAT          135..164
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          172..201
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          205..234
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          238..267
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          271..300
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          305..334
FT                   /note="ANK 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          338..359
FT                   /note="ANK 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          360..388
FT                   /note="ANK 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          392..421
FT                   /note="ANK 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          425..454
FT                   /note="ANK 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          458..487
FT                   /note="ANK 11"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   535 AA;  58333 MW;  C0F48E57DC6E1A02 CRC64;
     MDRLLSLEPS NVVTIRLEPG QKCSGVLTLR NVMYTMPVAF RLQPLNKIRY SIRPQSGIIS
     PLTTITLEII YHLPPNTTLP DSFPHCDDSF LLHSVVAPGA TAKDTSSTLD MVPSDWFTTK
     RKQVFIDSAI KIMFVGSPVL CYLVRKGYMD EIREVLEKSD TTWKSVDSVN FEGQTLLHLA
     ISQGRPDLVQ LLLEFGPNIE AHSRSCSSPL EAASATGEAL IVELLLAKKA STERTEFSAS
     GPIHLAAGNG HLEVLKLLLL KGANVNSLTK DGNTALHLAV EERRRDCARL LLANGARADI
     CSTGNGDTPL HIAAGLGDEH MVRVLLQKGA EKYIRNKYGK TAYDVAAEHG HNKLFDALRL
     GDSLCVAARK GEVRTVQRLL ENGASINGRD QHGWTALHRA CFKGRIEVVK ALIDNGIDVN
     ARDEDGYTAL HCAVESGHVD VAELLVKKGA DIELRTSKGI TALQIAQSLH YSGLTRVLMQ
     GGATKEVGTM ETNIVKSSGK IAVRDLDIGT IKKRSVNKSR TRRSSFDRNA PLAVL
 
 
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