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VHT1_YEAST
ID   VHT1_YEAST              Reviewed;         593 AA.
AC   P53241; D6VUJ9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Vitamin H transporter;
DE   AltName: Full=H(+)/biotin symporter;
GN   Name=VHT1; OrderedLocusNames=YGR065C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=10373489; DOI=10.1074/jbc.274.26.18741;
RA   Stolz J., Hoja U., Meier S., Sauer N., Schweizer E.;
RT   "Identification of the plasma membrane H+-biotin symporter of Saccharomyces
RT   cerevisiae by rescue of a fatty acid-auxotrophic mutant.";
RL   J. Biol. Chem. 274:18741-18746(1999).
RN   [4]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33 AND SER-43, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in uptake of biotin with the concomitant entry of
CC       protons.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC       permease family. {ECO:0000305}.
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DR   EMBL; Z72850; CAA97067.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08160.1; -; Genomic_DNA.
DR   PIR; S64360; S64360.
DR   RefSeq; NP_011579.1; NM_001181194.1.
DR   AlphaFoldDB; P53241; -.
DR   BioGRID; 33309; 230.
DR   DIP; DIP-5519N; -.
DR   IntAct; P53241; 10.
DR   MINT; P53241; -.
DR   STRING; 4932.YGR065C; -.
DR   TCDB; 2.A.1.14.12; the major facilitator superfamily (mfs).
DR   iPTMnet; P53241; -.
DR   MaxQB; P53241; -.
DR   PaxDb; P53241; -.
DR   PRIDE; P53241; -.
DR   EnsemblFungi; YGR065C_mRNA; YGR065C; YGR065C.
DR   GeneID; 852956; -.
DR   KEGG; sce:YGR065C; -.
DR   SGD; S000003297; VHT1.
DR   VEuPathDB; FungiDB:YGR065C; -.
DR   eggNOG; KOG2533; Eukaryota.
DR   HOGENOM; CLU_001265_4_2_1; -.
DR   InParanoid; P53241; -.
DR   OMA; WYAPDEI; -.
DR   BioCyc; YEAST:G3O-30779-MON; -.
DR   PRO; PR:P53241; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53241; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015225; F:biotin transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015878; P:biotin transport; IDA:SGD.
DR   Gene3D; 1.20.1250.20; -; 1.
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   Biotin; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..593
FT                   /note="Vitamin H transporter"
FT                   /id="PRO_0000121372"
FT   TOPO_DOM        1..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..190
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        454..460
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..492
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        514..526
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        527..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        548..593
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   593 AA;  69083 MW;  8B91D6247867386D CRC64;
     MTISNKSWRS YFPHLRKLPE DDQYLYSDDT NSSIIAEEEL HHSVDKSSKT DVTAETTAVE
     PHPHNLRHDL PYEVRDEAGR KWWKYFDEFE YRVNKEYKKS RKWYEFLYPN HTTQTKAERR
     LLYKLDIIIA LYFFMLCWSK SVDLNNYTNA YVSNMKEDLN MKGNDYVYTS TIANVGAIVF
     QLPFMYLLPR FPSHIILPVM DLGWTWFTFA CYRANSLAEL RAYRFILSAF GAAYYPVSQY
     ILGCWYAPDE INSRVCLFFC GQQLGSVTSG LLQSRIFKSL NGVHGLAGWR WMFLIDAIAI
     SLPTAIIGFF VIPGVPSKCY SLFLTDEEIR IARARNKRNQ IKDGVDKSKL APLWSRKLWK
     KVFCTPAFWV LVVFDTCSWN NMTAYSGSYT LWLKSNTKYS IAQVNNLSVI PACLGFAYVI
     FCAFGADLFR CKWIFMVFAA IMNTVSCALL IKWDIPSKAK WYAFFTTYFS VAASPCLWSF
     INDFLRFDPQ VKAITWIAIY SFSQSTYAWI PTLAWPTVES PRFKTGYTVS LIFGAIYGLW
     TFVVLFFYKR NEKKHALGNG IILYDSNKGE ELPEFVKKNM EERDGYYYLK RSS
 
 
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