SSH4_DEBHA
ID SSH4_DEBHA Reviewed; 529 AA.
AC Q6BSU1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Protein SSH4;
GN Name=SSH4; OrderedLocusNames=DEHA2D06226g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG86873.2; -; Genomic_DNA.
DR RefSeq; XP_458729.2; XM_458729.1.
DR AlphaFoldDB; Q6BSU1; -.
DR SMR; Q6BSU1; -.
DR STRING; 4959.XP_458729.2; -.
DR EnsemblFungi; CAG86873; CAG86873; DEHA2D06226g.
DR GeneID; 2901608; -.
DR KEGG; dha:DEHA2D06226g; -.
DR VEuPathDB; FungiDB:DEHA2D06226g; -.
DR eggNOG; KOG1477; Eukaryota.
DR HOGENOM; CLU_015116_0_0_1; -.
DR InParanoid; Q6BSU1; -.
DR OMA; FHNNDTP; -.
DR OrthoDB; 962732at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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 CDD; cd12910; SPRY_SSH4_like; 1.
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; IPR035780; SPRY_Ssh4-like.
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..529
FT /note="Protein SSH4"
FT /id="PRO_0000324481"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..529
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 101..309
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 383..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 529 AA; 59649 MW; DF4591B8BDFEDF37 CRC64;
MDPAIILFVF IFVSVCFCLL IFLSAYRVFS GGSERNEYSF LGSEILGSEV PREFLNDEEA
LNHLASEYDF THLSPEEQFS YLRGEEFTKT NPPNFHNTRG KSYSNEDDML LKERGINAFE
FEQDADILRG RYIVADKTEI NFHNNDTPYS TATSILNYSL PVKNRAYSDT VYFEVKVFEF
QNGSENPNGH FAIGLVTKPY PSDFRLPGYN NFSIAYESTG NLKINKPFPT PLQQHQGDNS
QYNALVLPPL QQSDIVGFGY VVSTGTLFIT RNGKKVMDVM RGCFIDLYPA VGCFSSNAKF
QVNLGQLGFV WIEANVRKYG FVSNSDYKKI KGEQGLAALP EYGNSSVAEG DKLLEMGEEL
PPRYPEDELD FFGRSSKDIL KVGSSSKSQN KTKSFSNNEK QDLEEINGEP KVAEEHRSSL
ITDDPEEVMD LRERLYEQNI TGPVSELSSE RAPLIGNNES QSEFYVNAKS ATSSREGNTE
TDLKQVTDEE PNSSQELTKA AQNDSNISKT SRTKKKKKNK KNSKKNKKK
