ID   SSH4_KLULA              Reviewed;         542 AA.
AC   Q6CVE0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Protein SSH4;
GN   Name=SSH4; OrderedLocusNames=KLLA0B12760g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (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; CR382122; CAH02492.1; -; Genomic_DNA.
DR   RefSeq; XP_452099.1; XM_452099.1.
DR   AlphaFoldDB; Q6CVE0; -.
DR   STRING; 28985.XP_452099.1; -.
DR   EnsemblFungi; CAH02492; CAH02492; KLLA0_B12760g.
DR   GeneID; 2896944; -.
DR   KEGG; kla:KLLA0_B12760g; -.
DR   eggNOG; KOG1477; Eukaryota.
DR   HOGENOM; CLU_026177_0_0_1; -.
DR   InParanoid; Q6CVE0; -.
DR   OMA; FIKDRGI; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
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:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
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; Membrane; Protein transport; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..542
FT                   /note="Protein SSH4"
FT                   /id="PRO_0000324482"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..542
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          158..345
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          447..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..542
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   542 AA;  60139 MW;  FAC1E345C0AA12DF CRC64;
     MGLIVLQDGF PNDRPIQGFP SDPVVRVPDD TIPADDAFSL MFLISLSITF GLLLLVLILI
     SIYLTFCGGN DGDDSDDEDE DGTSVSFKFF RKRNSLLLDS SFMTPGKFDD DESLKVREAK
     ELPKMSSFEV ELYERTKEFQ KMSPPMVKPL GSFLNSQDKQ VIKDRGIQSY FFLPSINDNV
     DINGAFLPSF FVEDKLNVSF TKFNISSSAI MNYPLPMNKK DAVYFEVKVY KFKTCSNSIF
     SIGLMTCPYP YFRIPGTAAY SIAYESTGKL RINNAFGADT LLPKLEEGDV VGFGYRYSSG
     TIFITHNGKK MMDVTHKVGI DLFVGLGAMN AAYTRTYTKD GLFEDPDNVS FRQKWSELQA
     FNNGESSSDY IDARNVISKD LLQVHDPKED TVSSDNIELH VNLGQLGFVF IEANVKKYAF
     GSVYGDIGIP PAYNGDDIKQ DMLLQKGDEL PPEYPDDAVD FFGDIHSPAS TSEPPSATFS
     AGLPMDNAAD TPVSTADADA DADADADEEE PLISVKKPAA QTHSKKNNKK KKKKKSNRNR
     RG