ID   PTM1_YEAS7              Reviewed;         523 AA.
AC   A6ZZS6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Membrane protein PTM1;
DE   Flags: Precursor;
GN   Name=PTM1; ORFNames=SCY_3336;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Early endosome membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC       Note=Copurifies with the late Golgi SNARE TLG2. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LU7TM family. {ECO:0000305}.
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DR   EMBL; AAFW02000152; EDN59869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZZS6; -.
DR   EnsemblFungi; EDN59869; EDN59869; SCY_3336.
DR   HOGENOM; CLU_024065_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009637; GPR107/GPR108-like.
DR   PANTHER; PTHR21229; PTHR21229; 1.
DR   Pfam; PF06814; Lung_7-TM_R; 1.
PE   3: Inferred from homology;
KW   Endosome; Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..523
FT                   /note="Membrane protein PTM1"
FT                   /id="PRO_0000343449"
FT   TOPO_DOM        27..197
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..265
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..333
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        355..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        403..417
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        439..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          483..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32857"
FT   MOD_RES         483
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P32857"
FT   MOD_RES         498
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P32857"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   523 AA;  60078 MW;  86E7A339FA82F7EC CRC64;
     MRVYQFCRPF QLFTYFLCYL LVFVKANKEK ISQKNYQVCA GMYSKEDWKG KIDPFISFNL
     KKISGLSDES DPGLVVAIYD FQDFEHLGVQ LPDEEMYYIC DDYAIDIGIC EEENRDEFIV
     QDVVYDPYTS TNRSLANPIM TFSQNEVGLH DTRYPIKETG FYCVTAFRSS TSTKFNAVVN
     FRNAYGQLAG TEINKLPLYG LLAVAYVVAM ALYSFAFWKH KHELLPLQKY LLAFFVFLTA
     ETIFVWAYYD LKNEKGDTAG IKVYMVFLSI LTAGKVTFSF FLLLIIALGY GIVYPKLNKT
     LMRRCQMYGA LTYAICIGFL IQSYLTDMEA PSPLILITLI PMALALIIFY YMIIRSMTKT
     VIYLKEQRQI VKLNMYKKLL YIIYASFLSV LAGSIVSSFI YVGMNTIDMI EKNWRSRFFV
     TDFWPTLVYF IVFVTIAFLW RPTDTSYMLA ASQQLPTDPE NVADFDLGDL QSFDDQDDAS
     IITGERGIDE DDLNLNFTDD EEGHDNVNNH SQGHGPVSPS PTK