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VPS73_YEAST
ID   VPS73_YEAST             Reviewed;         486 AA.
AC   P53142; D6VU42;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Vacuolar protein sorting-associated protein 73;
GN   Name=VPS73; OrderedLocusNames=YGL104C; ORFNames=G3090;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-151.
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-486.
RX   PubMed=9046090;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<85::aid-yea53>3.0.co;2-e;
RA   Paoluzi S., Minenkova O., Castagnoli L.;
RT   "The genes encoding the transcription factor yTAFII60, the G4p1 protein and
RT   a putative glucose transporter are contained in a 12.3 kb DNA fragment on
RT   the left arm of Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 13:85-91(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
RA   Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
RT   "Genomic screen for vacuolar protein sorting genes in Saccharomyces
RT   cerevisiae.";
RL   Mol. Biol. Cell 13:2486-2501(2002).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [7]
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   [8]
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).
RN   [9]
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: May be involved in vacuolar protein sorting.
CC       {ECO:0000269|PubMed:12134085}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:14576278}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14576278}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; Z72626; CAA96811.1; -; Genomic_DNA.
DR   EMBL; Z72625; CAA96810.1; -; Genomic_DNA.
DR   EMBL; X97644; CAA66249.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08003.1; -; Genomic_DNA.
DR   PIR; S64111; S64111.
DR   RefSeq; NP_011411.3; NM_001180969.3.
DR   AlphaFoldDB; P53142; -.
DR   SMR; P53142; -.
DR   BioGRID; 33146; 82.
DR   DIP; DIP-1727N; -.
DR   IntAct; P53142; 10.
DR   MINT; P53142; -.
DR   STRING; 4932.YGL104C; -.
DR   TCDB; 2.A.1.1.93; the major facilitator superfamily (mfs).
DR   iPTMnet; P53142; -.
DR   PaxDb; P53142; -.
DR   EnsemblFungi; YGL104C_mRNA; YGL104C; YGL104C.
DR   GeneID; 852774; -.
DR   KEGG; sce:YGL104C; -.
DR   SGD; S000003072; VPS73.
DR   VEuPathDB; FungiDB:YGL104C; -.
DR   eggNOG; KOG0569; Eukaryota.
DR   GeneTree; ENSGT00940000166877; -.
DR   HOGENOM; CLU_001265_30_5_1; -.
DR   InParanoid; P53142; -.
DR   OMA; SYRWRWI; -.
DR   BioCyc; YEAST:G3O-30603-MON; -.
DR   Reactome; R-SCE-189200; Cellular hexose transport.
DR   Reactome; R-SCE-196836; Vitamin C (ascorbate) metabolism.
DR   Reactome; R-SCE-422356; Regulation of insulin secretion.
DR   Reactome; R-SCE-5653890; Lactose synthesis.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-8981373; Intestinal hexose absorption.
DR   PRO; PR:P53142; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53142; protein.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0015149; F:hexose transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISS:SGD.
DR   GO; GO:0015749; P:monosaccharide transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; HMP:SGD.
DR   GO; GO:0055085; P:transmembrane transport; ISS:SGD.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR045263; GLUT.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   PANTHER; PTHR23503; PTHR23503; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Protein transport; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..486
FT                   /note="Vacuolar protein sorting-associated protein 73"
FT                   /id="PRO_0000050462"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..90
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..119
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..146
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..178
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..208
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..305
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..342
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        388..396
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        418..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        454
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        476..486
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   486 AA;  54331 MW;  D924D9112516450D CRC64;
     MNRILSSASL LSNVSMPRQN KHKITKALCY AIIVASIGSI QFGYHLSELN APQQVLSCSE
     FDIPMEGYPY DRTWLGKRGY KQCIPLNDEQ IGIVTSVFCI GGILGSYFAT SLANIYGRKF
     SSLINCTLNI VGSLIIFNSN SYRGLIIGRI LVGISCGSLI VIIPLFIKEV APSGWEGLLG
     SMTQICIRLG VLLTQGIALP LTDSYRWRWI LFGSFLIAVL NFFMWFIVDE SPKWLLAHGR
     VTDAKLSLCK LRGVTFDEAA QEIQDWQLQI ESGDPLIEPT TTNSISGSNS LWKYLRDRTN
     VKSRHVITVL LFGQQFCGIN SIVLYGTKII SQLYPQHAIR INFFISMVNV LVTILVSLLI
     HSLPRKPLLM TSTVLVSVTA FIMGIAMNHN KMNLLIVFSF IYMGVFTMGL NPLPFIIMRE
     VSKPQDMVLA QRYGTICNWV GTFIIAYTFP IIHDVLSGYV FIIFAIIACS ISAFIWKKVP
     ETKRSG
 
 
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