SSH4_YEAST
ID SSH4_YEAST Reviewed; 579 AA.
AC P32343; D6VX71;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein SSH4;
DE AltName: Full=Multicopy suppressor of leflunomide protein 4;
DE AltName: Full=Suppressor of SHR3 null mutation protein 4;
GN Name=SSH4; Synonyms=MLF4; OrderedLocusNames=YKL124W; ORFNames=YKL529;
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=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 [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 41-579.
RX PubMed=1514329; DOI=10.1002/yea.320080410;
RA Colleaux L., Richard G.-F., Thierry A., Dujon B.;
RT "Sequence of a segment of yeast chromosome XI identifies a new
RT mitochondrial carrier, a new member of the G protein family, and a protein
RT with the PAAKK motif of the H1 histones.";
RL Yeast 8:325-336(1992).
RN [4]
RP FUNCTION.
RX PubMed=9610367; DOI=10.1006/bbrc.1998.8630;
RA Fujimura H.;
RT "Molecular cloning of Saccharomyces cerevisiae MLF4/SSH4 gene which confers
RT the immunosuppressant leflunomide resistance.";
RL Biochem. Biophys. Res. Commun. 246:378-381(1998).
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=17287526; DOI=10.1534/genetics.106.069716;
RA Kota J., Melin-Larsson M., Ljungdahl P.O., Forsberg H.;
RT "Ssh4, Rcr2 and Rcr1 affect plasma membrane transporter activity in
RT Saccharomyces cerevisiae.";
RL Genetics 175:1681-1694(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP 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).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-367, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Components of the endosome-vacuole trafficking pathway that
CC regulates nutrient transport. May be involved in processes which
CC determine whether plasma membrane proteins are degraded or routed to
CC the plasma membrane. Confers leflunomide resistance when overexpressed.
CC {ECO:0000269|PubMed:17287526, ECO:0000269|PubMed:9610367}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17287526};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:17287526}.
CC Endosome membrane {ECO:0000269|PubMed:17287526}; Single-pass type II
CC membrane protein {ECO:0000269|PubMed:17287526}.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SSH4 family. {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; Z28123; CAA81964.1; -; Genomic_DNA.
DR EMBL; S44213; AAB23074.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09037.1; -; Genomic_DNA.
DR PIR; S37953; S37953.
DR RefSeq; NP_012798.1; NM_001179690.1.
DR AlphaFoldDB; P32343; -.
DR SMR; P32343; -.
DR BioGRID; 34012; 75.
DR DIP; DIP-5420N; -.
DR IntAct; P32343; 1.
DR MINT; P32343; -.
DR STRING; 4932.YKL124W; -.
DR iPTMnet; P32343; -.
DR MaxQB; P32343; -.
DR PaxDb; P32343; -.
DR PRIDE; P32343; -.
DR EnsemblFungi; YKL124W_mRNA; YKL124W; YKL124W.
DR GeneID; 853735; -.
DR KEGG; sce:YKL124W; -.
DR SGD; S000001607; SSH4.
DR VEuPathDB; FungiDB:YKL124W; -.
DR eggNOG; KOG1477; Eukaryota.
DR HOGENOM; CLU_026177_0_0_1; -.
DR InParanoid; P32343; -.
DR OMA; FIKDRGI; -.
DR BioCyc; YEAST:G3O-31906-MON; -.
DR PRO; PR:P32343; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32343; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IGI:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IGI:SGD.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027713; Ssh4_Saccharomycetales.
DR PANTHER; PTHR12864:SF20; PTHR12864:SF20; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 1: Evidence at protein level;
KW Endosome; Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Vacuole.
FT CHAIN 1..579
FT /note="Protein SSH4"
FT /id="PRO_0000203153"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..579
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 166..364
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 499..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..579
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 579 AA; 65061 MW; 700F1CBA07A49754 CRC64;
MYVTFNEALD SSFGNLESPN HDFKVGDPNM VPTPPMDSDS AAISLAFLIS LSITFAILML
ILVVIAAYVT FCGDDESEYD EENALGTRTS GTLHSLFGKK HSGILLDSSF ASPGGFDDEI
VLQERELEEL PKMSAYEVEL YIRAKEFQMM SPPMVKDFGT YLDSDDQQFI KDRGIQSYFL
LPSINDNIDE YGNFLPSFIV QDKLDIQFSK FNKSSSTVMN YPLPHNRKDA VYFEVKIFRH
IQKSNSIFSI GLTTVPYPYF RVPGMAKYSI AYESTGKLRI NNPFTASTLL PKLEEGDTVG
FGYRYKTGTI FITHNGKKLM DVTQNIGIDL FIGIGAFNAA YTRTYTRDGL LEDPDNVSFR
EALSEGKDIE VAKDLQRVHD PHDESDEMTS DEVELHVNLG QVGFVFIEAN VKKYAFGSVY
GQIGIPPAYN GTEIKKDTIL QKGEELPPRY ADTDNFFGSM KVKEGSSSRI TAQTSKPLWS
VGTYERISSN FDRENNVYHD SLETDDNNTD NNVNNNDENA GCNENSPLLE DDGNKRPENS
NTPREVSDGA INKNPRNKST KKRQRNRGKS SKKKNRSRK
