HNM1_YEAST
ID HNM1_YEAST Reviewed; 563 AA.
AC P19807; D6VU67;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Choline transport protein;
GN Name=HNM1; Synonyms=CTR, CTR1; OrderedLocusNames=YGL077C;
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].
RC STRAIN=ATCC 26787 / X2180-1B;
RX PubMed=2203793; DOI=10.1016/s0021-9258(18)55496-x;
RA Nikawa J., Hosaka K., Tsukagoshi Y., Yamashita S.;
RT "Primary structure of the yeast choline transport gene and regulation of
RT its expression.";
RL J. Biol. Chem. 265:15996-16003(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Sole choline transporter in yeast.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Inhibition of activity by intracellular choline.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid/choline transporter (ACT) (TC 2.A.3.4) family.
CC {ECO:0000305}.
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DR EMBL; J05603; AAA34537.1; -; Genomic_DNA.
DR EMBL; Z72599; CAA96782.1; -; Genomic_DNA.
DR EMBL; AY723806; AAU09723.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08028.1; -; Genomic_DNA.
DR PIR; S11175; S11175.
DR RefSeq; NP_011438.1; NM_001180942.1.
DR AlphaFoldDB; P19807; -.
DR SMR; P19807; -.
DR BioGRID; 33173; 123.
DR DIP; DIP-7965N; -.
DR IntAct; P19807; 61.
DR MINT; P19807; -.
DR STRING; 4932.YGL077C; -.
DR TCDB; 2.A.3.4.1; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P19807; -.
DR MaxQB; P19807; -.
DR PaxDb; P19807; -.
DR PRIDE; P19807; -.
DR EnsemblFungi; YGL077C_mRNA; YGL077C; YGL077C.
DR GeneID; 852803; -.
DR KEGG; sce:YGL077C; -.
DR SGD; S000003045; HNM1.
DR VEuPathDB; FungiDB:YGL077C; -.
DR eggNOG; KOG1289; Eukaryota.
DR HOGENOM; CLU_004495_2_4_1; -.
DR InParanoid; P19807; -.
DR OMA; THMAFEV; -.
DR BioCyc; YEAST:G3O-30578-MON; -.
DR PRO; PR:P19807; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P19807; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1901235; F:(R)-carnitine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IMP:SGD.
DR GO; GO:0034228; F:ethanolamine transmembrane transporter activity; IMP:SGD.
DR GO; GO:1900749; P:(R)-carnitine transport; IMP:SGD.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0015871; P:choline transport; IMP:SGD.
DR GO; GO:0034229; P:ethanolamine transport; IMP:SGD.
DR GO; GO:0031460; P:glycine betaine transport; IMP:SGD.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004756; AA_permease.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00907; 2A0304; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..563
FT /note="Choline transport protein"
FT /id="PRO_0000054155"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..426
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..491
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 563 AA; 62056 MW; 1A71E1D146DB7807 CRC64;
MSIRNDNASG GYMQPDQSSN ASMHKRDLRV EEEIKPLDDM DSKGAVAADG EVHLRKSFSL
WSILGVGFGL TNSWFGISTS MVAGISSGGP MMIVYGIIIV ALISICIGTS LGELSSAYPH
AGGQFWWSLK LAPPKYKRFA AYMCGSFAYA GSVFTSASTT LSVATEVVGM YALTHPEFIP
KRWHIFVCFE LLHLFLMFFN CYGKSLPIIS SSSLYISLLS FFTITITVLA CSHGKFNDAK
FVFATFNNET GWKNGGIAFI VGLINPAWSF SCLDCATHMA FEVEKPERVI PIAIMGTVAI
GFVTSFCYVI AMFFSIQDLD AVLSSTTGAP ILDIYNQALG NKSGAIFLGC LILFTSFGCV
IACHTWQARL CWSFARDNGL PLSRLWSQVN PHTGVPLNAH LMSCAWITLI GLLYLASSTA
FQSLITGCIA FLLLSYIIPV ICLLAKKRNI AHGPFWLGKF GFFSNIVLLG WTVFSVVFFS
FPPVLPVTKD NMNYVCVVIV GYTAYSILYW KYKGKKEFHA LEESENEQAE YSNNFDTIED
SREFSVAASD VELENEHVPW GKK
