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ANXC1_CRYNH
ID   ANXC1_CRYNH             Reviewed;         470 AA.
AC   J9VS56;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Annexin C1 {ECO:0000303|PubMed:31140968};
GN   Name=ANXC1 {ECO:0000303|PubMed:31140968};
GN   Synonyms=ANX1 {ECO:0000303|PubMed:31140968},
GN   ANXC3.1 {ECO:0000303|PubMed:31140968};
GN   ORFNames=CNAG_02415 {ECO:0000312|EMBL:AFR95419.1};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN   [1] {ECO:0000312|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=31140968; DOI=10.1099/mic.0.000815;
RA   Maryam M., Fu M.S., Alanio A., Camacho E., Goncalves D.S., Faneuff E.E.,
RA   Grossman N.T., Casadevall A., Coelho C.;
RT   "The enigmatic role of fungal annexins: the case of Cryptococcus
RT   neoformans.";
RL   Microbiology 165:852-862(2019).
CC   -!- FUNCTION: Does not appear to play a major role in virulence
CC       (PubMed:31140968). May play a role in titan cell formation
CC       (PubMed:31140968). {ECO:0000269|PubMed:31140968}.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid. {ECO:0000255|RuleBase:RU003540}.
CC   -!- DISRUPTION PHENOTYPE: Increases titan cell formation (low penetrance)
CC       (PubMed:31140968). Low or no sensitivity to high temperature or
CC       tacrolimus (calcineurin inhibitor); sensitivity may be background
CC       dependent (PubMed:31140968). No cell population growth phenotype in a
CC       variety of conditions including high pH, low calcium, in presence of
CC       the antifungals amphotericin B or fluconazole, heavy metals (nickel or
CC       zinc), osmotic stress (NaCl), cell wall integrity stressors (Calcofluor
CC       White, caffeine, or Congo Red), oxidative stress (H2O2), or nitro-
CC       oxidative stress (NaNO2 or H2O2), or following ultraviolet light
CC       radiation (PubMed:31140968). Normal mating (PubMed:31140968). Normal
CC       virulence factor secretion; assayed using melanin and urease
CC       (PubMed:31140968). Normal virulence in mouse intranasal, intravenous,
CC       and intratracheal infection models or in an invertebrate infection
CC       model (PubMed:31140968). Normal survival rate following amoebal
CC       ingestion (PubMed:31140968). {ECO:0000269|PubMed:31140968}.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245}.
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DR   EMBL; CP003825; AFR95419.1; -; Genomic_DNA.
DR   RefSeq; XP_012050133.1; XM_012194743.1.
DR   AlphaFoldDB; J9VS56; -.
DR   SMR; J9VS56; -.
DR   EnsemblFungi; AFR95419; AFR95419; CNAG_02415.
DR   GeneID; 23886037; -.
DR   VEuPathDB; FungiDB:CNAG_02415; -.
DR   HOGENOM; CLU_025300_4_2_1; -.
DR   Proteomes; UP000010091; Chromosome 6.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.220.10; -; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 1.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   3: Inferred from homology;
KW   Annexin; Calcium; Calcium/phospholipid-binding; Repeat.
FT   CHAIN           1..470
FT                   /note="Annexin C1"
FT                   /id="PRO_0000451157"
FT   REPEAT          161..232
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          233..304
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          316..388
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          395..468
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REGION          1..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  51754 MW;  51C276C4912F6BDD CRC64;
     MYGQQNNYGA PPPQQWGQAP PQGYQPGYQN GPPAVNYGAH PSQQQQWGAP PGPPQHQPYG
     APPVNQYGAP PQHQQGYGGH SPQPPFGAPS PAPAGYGAPP TAPQGQYGAP SPYPQQPPQQ
     GFGGPQQGYG SQPQGQSPMM YLGVPIPAPP PAVPVSTLAG YDARFDAERI RKATKGFGTD
     ERTIIDTLSP LDAFQMDVLS RTYEQTVGRS LKSTLEKELS SWLEYTLVLL SLGPLGGDVY
     LLHRACNGMG THEDLLNEVL LGRTNQEIFL LKEAYRRTYN QDLVQIVQGE LSMKTERMFN
     MALSGQRDES PYLNHQLVQQ DVETLYRAGP GKIGTDEIAI CGILISRSKE HLKAIAQAFP
     ARHRVSLSQM IHSEFSGHMR DALFFIARGV EADGDGVVRD CELLHAAMAG MGTKDERMIY
     RLVRNHWNRP RFNAIKNQYQ VLYRNSLRRA VEGETTGKYE KALVGIIEQN
 
 
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