SSH4_VANPO
ID SSH4_VANPO Reviewed; 556 AA.
AC A7TE03;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Protein SSH4;
GN Name=SSH4; ORFNames=Kpol_1018p163;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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 (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; DS480378; EDO19623.1; -; Genomic_DNA.
DR RefSeq; XP_001647481.1; XM_001647431.1.
DR AlphaFoldDB; A7TE03; -.
DR STRING; 436907.A7TE03; -.
DR PRIDE; A7TE03; -.
DR EnsemblFungi; EDO19623; EDO19623; Kpol_1018p163.
DR GeneID; 5547987; -.
DR KEGG; vpo:Kpol_1018p163; -.
DR eggNOG; KOG1477; Eukaryota.
DR HOGENOM; CLU_026177_0_0_1; -.
DR InParanoid; A7TE03; -.
DR OMA; FIKDRGI; -.
DR OrthoDB; 962732at2759; -.
DR PhylomeDB; A7TE03; -.
DR Proteomes; UP000000267; 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; Membrane; Protein transport; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..556
FT /note="Protein SSH4"
FT /id="PRO_0000324486"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..556
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 127..323
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 500..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..556
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 556 AA; 62296 MW; 859729D08E8C8072 CRC64;
MMIIEGDISG QEAVKNVIYG TFLPVDDPYP VTPPIDHDNE TVSLAFLISL SVTFALLMIL
LVATAAYVMF CGADEAEYDE ETGEGSSSSV TGIHTFFGKK GGGILLDSTF CSPGQFDDEE
ALREQEEQEL PKMSKFEIEL YKRSREFQNL NPPLVKEFGT YLNTSDRQFI KDRGIQSYYF
YPSINDNVDK YGNFLPSFLV QDKLDVTFTE YNKSSSTLLN YPLPFNKKEA VYFEVKIFKF
PTNSNTIFSI GLVTCPYPYF RIPGMSRYSI AYESTGKLRI NNPFGASTLL PRLQEGDVVG
FGYRYKMGTV FITHNGKKMM DVTHNVGVDL FVGLGALNAS YTRTYTKDGL LEDPDNVDIR
EALSQGREVE LPDAIQKVYD PENLTPVAAD EVELQVNLGQ VGFVFIEANV KKYGFGSVLG
EIGIPPAYNG DEIKRNAIIQ KGEEMPPKYG FEEGDRNSFF GDIHIYEGHH QLEAEELPEG
NGGVTTTQDA GARAATDYER VSSAFDRENN DTTKDPADEI LHNQTAANTT KPNKTSNNNN
KNHNNKKRNK RNKRRK
