PTM1_YEAST
ID PTM1_YEAST Reviewed; 523 AA.
AC P32857; D6VXP7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Membrane protein PTM1;
DE Flags: Precursor;
GN Name=PTM1; OrderedLocusNames=YKL039W; ORFNames=YKL252;
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].
RA Haarer B.K., Petzold A.S., Brown S.S.;
RT "PTM1, a putative transmembrane protein, enhances recovery from
RT transformation of a profilin deletion strain.";
RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1481573; DOI=10.1002/yea.320081108;
RA Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT "The sequence of a 12 kb fragment on the left arm of yeast chromosome XI
RT reveals five new open reading frames, including a zinc finger protein and a
RT homolog of the UDP-glucose pyrophosphorylase from potato.";
RL Yeast 8:977-986(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA Inadome H., Noda Y., Adachi H., Yoda K.;
RT "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT a novel membrane protein, Svp26, discovered in the Sed5-containing
RT compartments.";
RL Mol. Cell. Biol. 25:7696-7710(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; THR-483 AND THR-498, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16107716}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16107716}. Early endosome membrane
CC {ECO:0000269|PubMed:16107716}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16107716}. Note=Copurifies with the late Golgi
CC SNARE TLG2.
CC -!- SIMILARITY: Belongs to the LU7TM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49300.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA81874.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L11895; AAA34921.1; -; Genomic_DNA.
DR EMBL; X69584; CAA49300.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z28039; CAA81874.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006944; DAA09117.1; -; Genomic_DNA.
DR PIR; S30011; S30011.
DR RefSeq; NP_012885.2; NM_001179605.1.
DR AlphaFoldDB; P32857; -.
DR BioGRID; 34093; 84.
DR DIP; DIP-1244N; -.
DR IntAct; P32857; 14.
DR MINT; P32857; -.
DR STRING; 4932.YKL039W; -.
DR iPTMnet; P32857; -.
DR MaxQB; P32857; -.
DR PaxDb; P32857; -.
DR PRIDE; P32857; -.
DR EnsemblFungi; YKL039W_mRNA; YKL039W; YKL039W.
DR GeneID; 853827; -.
DR KEGG; sce:YKL039W; -.
DR SGD; S000001522; PTM1.
DR VEuPathDB; FungiDB:YKL039W; -.
DR eggNOG; KOG2568; Eukaryota.
DR GeneTree; ENSGT00940000169607; -.
DR HOGENOM; CLU_024065_1_0_1; -.
DR InParanoid; P32857; -.
DR OMA; HWQTRWF; -.
DR BioCyc; YEAST:G3O-31840-MON; -.
DR PRO; PR:P32857; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32857; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR InterPro; IPR009637; GPR107/GPR108-like.
DR PANTHER; PTHR21229; PTHR21229; 1.
DR Pfam; PF06814; Lung_7-TM_R; 1.
PE 1: Evidence at protein level;
KW Endosome; Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..523
FT /note="Membrane protein PTM1"
FT /id="PRO_0000022180"
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:0007744|PubMed:18407956"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 523 AA; 60018 MW; 86E7A339FE192DEC CRC64;
MRVYQFCRPF QLFTCFLCYL 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
