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   27-MAR-2024, entry version 160.
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}.
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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; 76.
DR   DIP; DIP-5420N; -.
DR   IntAct; P32343; 1.
DR   MINT; P32343; -.
DR   STRING; 4932.YKL124W; -.
DR   GlyCosmos; P32343; 6 sites, No reported glycans.
DR   GlyGen; P32343; 6 sites.
DR   iPTMnet; P32343; -.
DR   MaxQB; P32343; -.
DR   PaxDb; 4932-YKL124W; -.
DR   PeptideAtlas; P32343; -.
DR   EnsemblFungi; YKL124W_mRNA; YKL124W; YKL124W.
DR   GeneID; 853735; -.
DR   KEGG; sce:YKL124W; -.
DR   AGR; SGD:S000001607; -.
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   OrthoDB; 5479594at2759; -.
DR   BioCyc; YEAST:G3O-31906-MONOMER; -.
DR   BioGRID-ORCS; 853735; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P32343; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P32343; Protein.
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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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   PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR   PANTHER; PTHR12864:SF54; SPRY DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//