YPP1_YEAST
ID YPP1_YEAST Reviewed; 817 AA.
AC P46951; D6VUY0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cargo-transport protein YPP1;
DE AltName: Full=Alpha-synuclein protective protein 1;
GN Name=YPP1; OrderedLocusNames=YGR198W; ORFNames=G7594;
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 204508 / S288c;
RX PubMed=7502584; DOI=10.1002/yea.320111110;
RA Guerreiro P., Maia e Silva A., Barreiros T., Arroyo J., Garcia-Gonzalez M.,
RA Garcia-Saez M.I., Rodrigues-Pousada C., Nombela C.;
RT "The complete sequence of a 9000 bp fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII contains four previously unknown
RT open reading frames.";
RL Yeast 11:1087-1091(1995).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RIBOSOMES.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17576801; DOI=10.1083/jcb.200610071;
RA Flower T.R., Clark-Dixon C., Metoyer C., Yang H., Shi R., Zhang Z.,
RA Witt S.N.;
RT "YGR198w (YPP1) targets A30P alpha-synuclein to the vacuole for
RT degradation.";
RL J. Cell Biol. 177:1091-1104(2007).
CC -!- FUNCTION: Involved in endocytosis. {ECO:0000269|PubMed:17576801}.
CC -!- SUBUNIT: Interacts with ribosomes. {ECO:0000269|PubMed:16702403}.
CC -!- INTERACTION:
CC P46951; P37297: STT4; NbExp=2; IntAct=EBI-23455, EBI-18454;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Cell membrane
CC {ECO:0000269|PubMed:14690591}; Peripheral membrane protein; Cytoplasmic
CC side.
CC -!- MISCELLANEOUS: Present with 1640 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the YPP1 family. {ECO:0000305}.
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DR EMBL; X82775; CAA58017.1; -; Genomic_DNA.
DR EMBL; Z72983; CAA97225.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08291.1; -; Genomic_DNA.
DR PIR; S53921; S53921.
DR RefSeq; NP_011714.3; NM_001181327.3.
DR PDB; 4N5C; X-ray; 3.25 A; A/B/C/D/E/F/G/H=11-817.
DR PDBsum; 4N5C; -.
DR AlphaFoldDB; P46951; -.
DR SMR; P46951; -.
DR BioGRID; 33451; 127.
DR DIP; DIP-6350N; -.
DR IntAct; P46951; 22.
DR MINT; P46951; -.
DR STRING; 4932.YGR198W; -.
DR iPTMnet; P46951; -.
DR MaxQB; P46951; -.
DR PaxDb; P46951; -.
DR PRIDE; P46951; -.
DR EnsemblFungi; YGR198W_mRNA; YGR198W; YGR198W.
DR GeneID; 853112; -.
DR KEGG; sce:YGR198W; -.
DR SGD; S000003430; YPP1.
DR VEuPathDB; FungiDB:YGR198W; -.
DR eggNOG; ENOG502QV6B; Eukaryota.
DR HOGENOM; CLU_019616_0_0_1; -.
DR InParanoid; P46951; -.
DR OMA; VSFKIVC; -.
DR BioCyc; YEAST:G3O-30884-MON; -.
DR PRO; PR:P46951; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P46951; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IDA:SGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:SGD.
DR GO; GO:0019236; P:response to pheromone; IDA:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Endocytosis; Membrane; Reference proteome.
FT CHAIN 1..817
FT /note="Cargo-transport protein YPP1"
FT /id="PRO_0000202843"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 39..57
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 63..82
FT /evidence="ECO:0007829|PDB:4N5C"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 90..111
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 137..157
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 264..282
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 306..322
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 326..353
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:4N5C"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 387..404
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 429..445
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 450..454
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 485..503
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 507..516
FT /evidence="ECO:0007829|PDB:4N5C"
FT TURN 517..521
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:4N5C"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 543..560
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 569..588
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 598..607
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:4N5C"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 626..643
FT /evidence="ECO:0007829|PDB:4N5C"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 649..659
FT /evidence="ECO:0007829|PDB:4N5C"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 668..679
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 686..697
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 702..712
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 747..767
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 769..772
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 775..784
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 791..804
FT /evidence="ECO:0007829|PDB:4N5C"
FT HELIX 812..815
FT /evidence="ECO:0007829|PDB:4N5C"
SQ SEQUENCE 817 AA; 95366 MW; AC42730C8B9C3E4B CRC64;
MPNSNVRIPP TVPSKIIDVV DQALRARLLG GSTFNSGFDS LDSVLNLQFR LHYHVIGSNG
PAKPVCDVLL KESQNLEKNM SMMEELNDYP EITKLVEKIL FNCLGILFFH RGQFQESQRC
LLHSLKIHNN TASQKTALME QYDRYLIVEN LYYRGLVSQD INIMQNVFYK ELLAHVDTIP
PESNGLLFEY ISLIVAKLRF NQIQDLAENF KTTVENPFIL FLYMIKKFQS PLKKHIDNDD
LYLKFGQNVL LKAKFPTASE TNDEALEHFN VFLQYYFKFT HIKKIKVNPS WYNFIISSME
KTFQSIEVSK TAMFLFQNLS DNSNDEIKKK TFKRESILNF VNFVKYNDKY YQLHDNSHRD
IISFIDAYSF ILQNSSKTDS IENVFDYDNT VSTFATSLNS FYKEYNLPLM SQSESLDWLE
NSTRCVYPGN ISKVLTNAWS TLYEIRKYQL DFLVSNNLTS YLCNAMMLST KEKDNADVEE
QEEGEEEKAL RELQFKYSYT LAQQRHIETA IKTLESLILS KNPNYYKAWH LLALCRSVQE
DKEMSYKIVC SVLEAMNESL QNNTLLLNDR WQFIHLKLTQ LALIEEIFGT LEALETLPEV
FELYATLFPD SQPELNSMGP KYSQTKEYLL QMVWIFAANM YMRTKDNDED AKAAIKEASN
VESKFKNLNC NIANGYLSII KDEPGVALKE FETVLYYDEN NLDALVGFAE LIFPEELGVE
ETNLERYYTL SLDKKPGKRA KLTFVNDTDR SAAYARLKFL LECAILESIE AYYSPEVWWY
LSLIYEKYQD DEYKNSLLKC IKYQELNPIR SLRYCNY
