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SIT1_ASPFU
ID   SIT1_ASPFU              Reviewed;         577 AA.
AC   Q4WGS5;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Siderophore iron transporter 1 {ECO:0000303|PubMed:26929401};
GN   Name=sit1 {ECO:0000303|PubMed:26929401}; ORFNames=AFUA_7G06060;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION, INDUCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=26929401; DOI=10.1042/bcj20160066;
RA   Park Y.S., Kim J.Y., Yun C.W.;
RT   "Identification of ferrichrome- and ferrioxamine B-mediated iron uptake by
RT   Aspergillus fumigatus.";
RL   Biochem. J. 473:1203-1213(2016).
CC   -!- FUNCTION: Major facilitator transporter involved in ferrichrome (FC)
CC       and ferrioxamine B (FOB) uptake (PubMed:26929401).
CC       {ECO:0000269|PubMed:26929401}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.96 uM for ferrichrome (FC) uptake {ECO:0000269|PubMed:26929401};
CC         KM=9.40 uM for ferrioxamine B (FOB) uptake
CC         {ECO:0000269|PubMed:26929401};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26929401};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Highly expressed under low-iron conditions and down-
CC       regulated under high-iron conditions (PubMed:26929401). Expression is
CC       regulated by hapX under low-iron conditions (PubMed:26929401).
CC       {ECO:0000269|PubMed:26929401}.
CC   -!- DISRUPTION PHENOTYPE: Leads to lower ferrichrome (FC) and ferrioxamine
CC       B (FOB) uptake activities, which are reduced to approximately 60% and
CC       50% of the wild-type activities, respectively (PubMed:26929401).
CC       {ECO:0000269|PubMed:26929401}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000009; EAL86866.1; -; Genomic_DNA.
DR   RefSeq; XP_748904.1; XM_743811.1.
DR   AlphaFoldDB; Q4WGS5; -.
DR   SMR; Q4WGS5; -.
DR   STRING; 746128.CADAFUBP00008912; -.
DR   EnsemblFungi; EAL86866; EAL86866; AFUA_7G06060.
DR   GeneID; 3506444; -.
DR   KEGG; afm:AFUA_7G06060; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_012970_2_1_1; -.
DR   InParanoid; Q4WGS5; -.
DR   OMA; VMLNTAW; -.
DR   OrthoDB; 641071at2759; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0015343; F:siderophore transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Ion transport; Iron; Iron transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..577
FT                   /note="Siderophore iron transporter 1"
FT                   /id="PRO_0000444405"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        537..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   577 AA;  62903 MW;  8911D16DC6833D13 CRC64;
     MAMHDPHEKN GPDAVESRVQ TDFPVERFGG NGSPGVRRIE VISSQFNLVH RIIFFFGVFL
     IAYVYGLDGT IRYTYQPLAT AEYQSHSLLA TVNVLRSVIA AAAQPTAAKI ADVFGRVELI
     LLSIVFYTVG TIVEASANHL YEFCAGAVLY QIGYTSVILL VEVLIADVTS TRSRLLFSYI
     PALPFLINTW ISGNVTSAVL KVTSWQWGIG MFAIIYPVCT IPLLAVLFVG HLKARRANPQ
     AYKFSLLDQG VGQFFIDLFW YLDVVGILLL IAILALILVP FTIAGGAVTQ WKTAKVIAPL
     VIGVLCVPAF IVWERWCPHP MVPFKLLKDR AIWGALGIAV MLNTAWTLQG DYLYTVLIVS
     FDESVMSATR ITSLYSFVSV ITGTILGAIV IYVRRLKPFI VAGTLVFMAA FGILIRFRGG
     ADGTNHAGII GGQILLGFAG GLFPYPAQAS VQVASKHKYL AVITGIYLAT YNVGSALGNT
     ISGAIWTQVL PGELENRLGN ATLAAEVYAN PFAFTQVNPV GTPDRDAVIL AYKHAQRLLC
     ITGICLTVPL IAFSLCIRNP RLTKEQTLKE AEEIDDK
 
 
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