(data stored in ACNUC8465 zone)

SWISSPROT: 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   30-AUG-2017, entry version 70.
DE   RecName: Full=Protein SSH4;
GN   Name=SSH4; OrderedLocusNames=CAGL0M06545g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       that regulates nutrient transport. May be involved in processes
CC       which determine whether plasma membrane proteins are degraded or
CC       routed to the plasma membrane (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass
CC       type II membrane protein {ECO:0000250}. Endosome membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SSH4 family. {ECO:0000305}.
DR   EMBL; CR380959; CAG62608.1; -; Genomic_DNA.
DR   RefSeq; XP_449632.1; XM_449632.1.
DR   ProteinModelPortal; Q6FJG2; -.
DR   SMR; Q6FJG2; -.
DR   STRING; 284593.XP_449632.1; -.
DR   EnsemblFungi; CAG62608; CAG62608; CAGL0M06545g.
DR   KEGG; cgr:CAGL0M06545g; -.
DR   CGD; CAL0136467; CAGL0M06545g.
DR   EuPathDB; FungiDB:CAGL0M06545g; -.
DR   eggNOG; KOG1477; Eukaryota.
DR   eggNOG; ENOG410XPCC; LUCA.
DR   HOGENOM; HOG000154429; -.
DR   InParanoid; Q6FJG2; -.
DR   OMA; IFITHNG; -.
DR   OrthoDB; EOG092C16NT; -.
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 targeting to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR013320; ConA-like_dom.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR027713; Ssh4_Saccharomycetales.
DR   PANTHER; PTHR12864:SF36; PTHR12864:SF36; 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;
DR   PRODOM; Q6FJG2.
DR   SWISS-2DPAGE; Q6FJG2.
KW   Complete proteome; Endosome; Glycoprotein; Membrane;
KW   Protein transport; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN         1    587       Protein SSH4.
FT                                /FTId=PRO_0000324479.
FT   TOPO_DOM      1     33       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     34     54       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     55    587       Lumenal. {ECO:0000255}.
FT   DOMAIN      162    349       B30.2/SPRY. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   CARBOHYD    105    105       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    208    208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    321    321       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    334    334       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    527    527       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    538    538       N-linked (GlcNAc...) asparagine.
FT                                {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
//

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