SSH4_CANGA
ID SSH4_CANGA Reviewed; 587 AA.
AC Q6FJG2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protein SSH4;
GN Name=SSH4; OrderedLocusNames=CAGL0M06545g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62608.1; -; Genomic_DNA.
DR RefSeq; XP_449632.1; XM_449632.1.
DR AlphaFoldDB; Q6FJG2; -.
DR STRING; 5478.XP_449632.1; -.
DR PRIDE; Q6FJG2; -.
DR EnsemblFungi; CAG62608; CAG62608; CAGL0M06545g.
DR GeneID; 2891680; -.
DR KEGG; cgr:CAGL0M06545g; -.
DR CGD; CAL0136467; CAGL0M06545g.
DR VEuPathDB; FungiDB:CAGL0M06545g; -.
DR eggNOG; KOG1477; Eukaryota.
DR HOGENOM; CLU_026177_0_0_1; -.
DR InParanoid; Q6FJG2; -.
DR OMA; FIKDRGI; -.
DR Proteomes; UP000002428; Chromosome M.
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..587
FT /note="Protein SSH4"
FT /id="PRO_0000324479"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..587
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 162..349
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 509..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..587
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 587 AA; 66218 MW; 0846A0A9EB166E2E CRC64;
MPLIPDSIQS IGVFHVDDPF NPMPDPGDAD PETVAFAFFI GIAVVFSLLL ITLVCTAAYL
VCTSSYEGEY DEELANNGDG SRRGILNFRP LFGKKNSNGL LLDSNFTNPG EFDDNEEFIE
REREALIKMS PFEVDSYMRA KEFQIVSPPA VQEFGTYLDS KDLQMIKDRG IQSYYFIPSI
NDNVDKSGHF LPSFLVQDKL EVEFTRWNKS SSAVLNYPLP YNKKDAVYFE VKVYNHKPNS
NSIFSIGLVT VPYPYFRIPG MCKFSIAYES TGKLRINDPF FPSTLLPKLV EGDVVGFGYR
FKTGTIFITH NGKKLMDVTQ NVSVELFIAL GAMNASYTRT YTKDGLLEDP DNIELRNALA
EGRELKLSKD IQNPHNPMDE TKWDIIDSDE IELHVNLGQT GFVFIEANVK KYGFGSVFGE
IGIPPAYNPN DIQKDKLIQK GEELPPQYPE DTENFGLFGN LKIKSHIKNP LKEVSSNPSA
PELIQKKLKT PIVKTPKVGI YEFTTPIDRK RETNMQPSIN PPVYEINDTR QSSPEITNET
ISNEETVSSS SKAEPALQHG QSNKTPNKRQ NKKTKQRKNK KKGKKNK
