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TPN1_YEAST
ID   TPN1_YEAST              Reviewed;         579 AA.
AC   P53099; D6VTW8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Vitamin B6 transporter TPN1;
DE   AltName: Full=Transport of pyridoxine protein 1;
GN   Name=TPN1; OrderedLocusNames=YGL186C; ORFNames=G1370;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=12649274; DOI=10.1074/jbc.m300949200;
RA   Stolz J., Vielreicher M.;
RT   "Tpn1p, the plasma membrane vitamin B6 transporter of Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 278:18990-18996(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9046087;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA   Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT   "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT   from Saccharomyces cerevisiae.";
RL   Yeast 13:55-64(1997).
RN   [3]
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   [4]
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   [5]
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).
CC   -!- FUNCTION: Thiamine-regulated, high affinity import carrier of
CC       pyridoxine, pyridoxal and pyridoxamine. {ECO:0000269|PubMed:12649274}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12649274}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:12649274}.
CC   -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC       {ECO:0000305}.
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DR   EMBL; X91489; CAA62788.1; -; Genomic_DNA.
DR   EMBL; Z72708; CAA96898.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07929.1; -; Genomic_DNA.
DR   PIR; S61131; S61131.
DR   RefSeq; NP_011329.1; NM_001181051.1.
DR   AlphaFoldDB; P53099; -.
DR   BioGRID; 33069; 60.
DR   IntAct; P53099; 1.
DR   STRING; 4932.YGL186C; -.
DR   TCDB; 2.A.39.2.2; the nucleobase:cation symporter-1 (ncs1) family.
DR   iPTMnet; P53099; -.
DR   MaxQB; P53099; -.
DR   PaxDb; P53099; -.
DR   PRIDE; P53099; -.
DR   EnsemblFungi; YGL186C_mRNA; YGL186C; YGL186C.
DR   GeneID; 852689; -.
DR   KEGG; sce:YGL186C; -.
DR   SGD; S000003154; TPN1.
DR   VEuPathDB; FungiDB:YGL186C; -.
DR   eggNOG; ENOG502QR29; Eukaryota.
DR   GeneTree; ENSGT00940000176331; -.
DR   HOGENOM; CLU_026016_2_1_1; -.
DR   InParanoid; P53099; -.
DR   OMA; SLCYSIT; -.
DR   BioCyc; MetaCyc:G3O-30671-MON; -.
DR   BioCyc; YEAST:G3O-30671-MON; -.
DR   PRO; PR:P53099; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53099; protein.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0031924; F:vitamin B6 transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0090482; F:vitamin transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0051180; P:vitamin transport; IDA:SGD.
DR   InterPro; IPR012681; NCS1.
DR   InterPro; IPR001248; Pur-cyt_permease.
DR   InterPro; IPR026030; Pur-cyt_permease_Fcy2/21/22.
DR   InterPro; IPR030175; Tpn1.
DR   PANTHER; PTHR31806; PTHR31806; 1.
DR   PANTHER; PTHR31806:SF8; PTHR31806:SF8; 1.
DR   Pfam; PF02133; Transp_cyt_pur; 1.
DR   PIRSF; PIRSF002744; Pur-cyt_permease; 1.
DR   TIGRFAMs; TIGR00800; ncs1; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..579
FT                   /note="Vitamin B6 transporter TPN1"
FT                   /id="PRO_0000197929"
FT   TOPO_DOM        1..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..122
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..274
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..302
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..362
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384..394
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        416..421
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        443..519
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        541..545
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        546..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        567..579
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   579 AA;  64546 MW;  26686199D1FD8522 CRC64;
     MNRDNMDTTK RKEDHTKHTT DVIEFYEEGT AASSLNIATE KANSSPSILR RIINRAAWLS
     KKVDAMGVES TGIQRISPYE RGTSKKQFLH VAGLWLSATG GLSSMSSFLL GPLLFGLSFR
     ESVASSLISV TIGCLIAAYC SIMGPQSGCR QMVTARYLFG WWFVKLVALA SIIGVMGWSV
     VNSVVGGEML AAISNDKVPL WVGIVIVTVC SFLVAIFGIK QVIKVETYLS VPVLTAFLLL
     YISSSDKYSF VNAYVSKGNL DSSTRKGNWM SFFSLCYSIT ATWGSITADY YILFPEDTPY
     IQIFCLTFFG TFLPTCFVGI LGLLLASVAM SYKPWSVEYD SHGMGGLLWA GFQRWNGFGK
     FCVVVLVFSL VSNNIINTYS AAFSIQLSSV FCAKIPRWFW SIVCTIICLV CALIGRNHFS
     TILGNFLPMI GYWISMYFIL LFEENLVFRR FFLHLYTKEF PTVTGEINGP ELVGSSKEVE
     KDAVTNIHLL KRKHKVTKHR YNWDKWEDYE VLTHGYAATF AFIVGVAGVV VGMAQAYWIG
     PIAAKFGEYG GDVAMWLSMA FSGVVYPPCR YLELRKFGR
 
 
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