AMT1_SCHPO
ID AMT1_SCHPO Reviewed; 497 AA.
AC Q9C0V1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ammonium transporter 1;
GN Name=amt1; ORFNames=SPCPB1C11.01;
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 [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 [2]
RP FUNCTION.
RC STRAIN=FY7406;
RX PubMed=16999738; DOI=10.1111/j.1365-2443.2006.01014.x;
RA Mitsuzawa H.;
RT "Ammonium transporter genes in the fission yeast Schizosaccharomyces pombe:
RT role in ammonium uptake and a morphological transition.";
RL Genes Cells 11:1183-1195(2006).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Transporter for ammonium to use as a nitrogen source. Under
CC ammonium limitation acts as an ammonium sensor, generating a signal
CC that leads to pseudohyphal growth. {ECO:0000269|PubMed:16999738}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16823372}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
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DR EMBL; CU329672; CAC36934.1; -; Genomic_DNA.
DR RefSeq; NP_588424.1; NM_001023415.2.
DR AlphaFoldDB; Q9C0V1; -.
DR SMR; Q9C0V1; -.
DR BioGRID; 275898; 37.
DR STRING; 4896.SPCPB1C11.01.1; -.
DR iPTMnet; Q9C0V1; -.
DR MaxQB; Q9C0V1; -.
DR PaxDb; Q9C0V1; -.
DR EnsemblFungi; SPCPB1C11.01.1; SPCPB1C11.01.1:pep; SPCPB1C11.01.
DR GeneID; 2539332; -.
DR KEGG; spo:SPCPB1C11.01; -.
DR PomBase; SPCPB1C11.01; amt1.
DR VEuPathDB; FungiDB:SPCPB1C11.01; -.
DR eggNOG; KOG0682; Eukaryota.
DR HOGENOM; CLU_000445_33_0_1; -.
DR InParanoid; Q9C0V1; -.
DR OMA; ITPACGE; -.
DR PhylomeDB; Q9C0V1; -.
DR PRO; PR:Q9C0V1; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015398; F:high-affinity secondary active ammonium transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0072488; P:ammonium transmembrane transport; IMP:PomBase.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR001905; Ammonium_transpt.
DR InterPro; IPR018047; Ammonium_transpt_CS.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR PANTHER; PTHR43029; PTHR43029; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR TIGRFAMs; TIGR00836; amt; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE 3: Inferred from homology;
KW Ammonia transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..497
FT /note="Ammonium transporter 1"
FT /id="PRO_0000278387"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 440..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 53387 MW; F3A5212635AFB9C7 CRC64;
MSSTTDATPT PSGVNGGDSM TVNLNQFYNN GDVAWILTST ALVFIMIPGV GFFYSGLARR
RSAISMLFLS MMSVAIVAFQ WFFWGYSLTF SHEGGPYIGS LANFGLRQTL GRPSSGASSV
PDILFCVFQG MFAAITPALA IGAAADRGRM FPCMVFMFLW TSIVYDPIAF WTWNPNGWLN
KLGSYDFAGG SPVHISSGMA ALAYSIVIGK RCDHGTTKYR PHNVPHVVLG TVFLWFGWFG
FNGGSSAAAN MRGVMAVVVT HLAASVGGIV WCVIDFAKNR HWSVVGFCEG AVAGLVAITP
GSGFVPPWAA VVIGALGAVF CYAATYLKKI IRVDDALDIF AEHGVGGMVG NILTALFAAD
YIEALDGSGT AYTGGWITHH YIQLGYQLAD TVSCAAYSFA VSCALLFVMN YIPGLSLRVS
REDEVLGLDK IELGESAYYY KDSTDEPPPI TTSGVQYTSP TVSDSASNEK EQEHRAQNEA
QKEEEYRAES EAQAPAI
