SSH4_YEAS7
ID SSH4_YEAS7 Reviewed; 579 AA.
AC A6ZZJ6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
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; ORFNames=SCY_3256;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type
CC II membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SSH4 family. {ECO:0000305}.
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DR EMBL; AAFW02000151; EDN60044.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZJ6; -.
DR SMR; A6ZZJ6; -.
DR PRIDE; A6ZZJ6; -.
DR EnsemblFungi; EDN60044; EDN60044; SCY_3256.
DR HOGENOM; CLU_026177_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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 3: Inferred from homology;
KW Endosome; Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein;
KW Protein transport; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation; Vacuole.
FT CHAIN 1..579
FT /note="Protein SSH4"
FT /id="PRO_0000324487"
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:0000250|UniProtKB:P32343"
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:0000250|UniProtKB:P32343"
SQ SEQUENCE 579 AA; 65047 MW; EF3A1DFFF3146311 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 PHDDSDEMTS DEVELHVNLG QVGFVFIEAN VKKYAFGSVY
GQIGIPPAYN GTEIKKDTIL QKGEELPPRY ADTDNFFGSM KVKEGSSSRI TAQTSKPLWS
VGTYERISSN FDRENNVYHD SLETDDNNTD NNVNNNDENA GCNENSPLLE DDGNKRPENS
NTPREVSDGA INKNPRNKST KKRQRNRGKS SKKKNRSRK
