BSU1_SCHPO
ID BSU1_SCHPO Reviewed; 526 AA.
AC P33532; O13866;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Vitamin B6 transporter bsu1;
DE AltName: Full=Amiloride transporter car1;
DE AltName: Full=Changed amiloride resistance protein 1;
DE AltName: Full=Vitamin B6 uptake protein 1;
GN Name=bsu1; Synonyms=car1, sod1; ORFNames=SPAC17A2.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8246883; DOI=10.1007/bf00284681;
RA Jia Z.-P., McCullough N., Wong L., Young P.G.;
RT "The amiloride resistance gene, car1, of Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 241:298-304(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15701794; DOI=10.1128/ec.4.2.319-326.2005;
RA Stolz J., Woehrmann H.J., Vogl C.;
RT "Amiloride uptake and toxicity in fission yeast are caused by the
RT pyridoxine transporter encoded by bsu1+ (car1+).";
RL Eukaryot. Cell 4:319-326(2005).
CC -!- FUNCTION: Thiamine-regulated, high affinity import carrier of
CC pyridoxine, pyridoxal and pyridoxamine. Also imports, but does not
CC export, amiloride and so confers sensitivity.
CC {ECO:0000269|PubMed:15701794}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15701794}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:15701794}. Note=During
CC mitosis, localizes also to the septum.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000305}.
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DR EMBL; Z14035; CAA78411.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11084.1; -; Genomic_DNA.
DR PIR; S39919; S39919.
DR RefSeq; XP_001713084.1; XM_001713032.2.
DR AlphaFoldDB; P33532; -.
DR BioGRID; 280536; 2.
DR STRING; 4896.SPAC17A2.01.1; -.
DR TCDB; 2.A.1.2.1; the major facilitator superfamily (mfs).
DR iPTMnet; P33532; -.
DR PaxDb; P33532; -.
DR PRIDE; P33532; -.
DR EnsemblFungi; SPAC17A2.01.1; SPAC17A2.01.1:pep; SPAC17A2.01.
DR PomBase; SPAC17A2.01; bsu1.
DR VEuPathDB; FungiDB:SPAC17A2.01; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_11_5_1; -.
DR InParanoid; P33532; -.
DR OMA; KWAVATM; -.
DR PhylomeDB; P33532; -.
DR PRO; PR:P33532; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031925; F:pyridoxal transmembrane transporter activity; IDA:PomBase.
DR GO; GO:0031927; F:pyridoxamine transmembrane transporter activity; IDA:PomBase.
DR GO; GO:0031928; F:pyridoxine transmembrane transporter activity; IDA:PomBase.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IGI:PomBase.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1903090; P:pyridoxal transmembrane transport; IDA:PomBase.
DR GO; GO:1903091; P:pyridoxamine transmembrane transport; IDA:PomBase.
DR GO; GO:1903092; P:pyridoxine transmembrane transport; IDA:PomBase.
DR GO; GO:0071934; P:thiamine transmembrane transport; IGI:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..526
FT /note="Vitamin B6 transporter bsu1"
FT /id="PRO_0000173433"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 33..37
FT /note="SSQSD -> PLNQI (in Ref. 1; CAA78411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 58484 MW; FD5725A338BF454E CRC64;
MASKIASLFS PSETASKDQH ENVAEDLELG TASSQSDGIH ETNSEYDEKK REESPEVIDI
SNLISSDHPA HPQNWHWAKR WSIVFMFCLM QIYVIWTSNG FGSIEYSVMA QFNVSAQVAT
LCLSMNILGS GLGPMFLGPL SDIGGRKPVY FCSIFVYTVF NISCALPRNI VQMIISHFII
GVAGSTALTN VAGGIPDLFP EDTAGVPMSL FVWACAGGAI GAPMATGVDI NAKYGWRWLY
YINIIVGGFF LIVILIIPET LPIKVITRYE NAKGRIVEGI PKNNLKEVLK KCKFVTTMGF
RMMLTEPIIL SMGLYNFYAY GISYFFLTAI WPVFYDTYKM SEMGASCTYL SGFVASTLLF
LYQPIQDWIF RRDKAKNNGV ARPEARFTSA LFITLLFPAG MFLFAFTCHP PFPWMSPIVG
NSMVTVANGH NWMCILNYLT DSYPLLSGSA VAAFTLPSFI GATVFAHVSQ IMFNNMSVKW
AVATMAFISI SIPFIIYTFY FFGQRIRALS SLTGNKALKY LPLENN
