SSH4_SCLS1
ID SSH4_SCLS1 Reviewed; 523 AA.
AC A7EQ00;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Protein ssh4;
GN Name=ssh4; ORFNames=SS1G_07399;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476629; EDO04916.1; -; Genomic_DNA.
DR RefSeq; XP_001591953.1; XM_001591903.1.
DR AlphaFoldDB; A7EQ00; -.
DR STRING; 665079.A7EQ00; -.
DR EnsemblFungi; EDO04916; EDO04916; SS1G_07399.
DR GeneID; 5488130; -.
DR KEGG; ssl:SS1G_07399; -.
DR eggNOG; KOG1477; Eukaryota.
DR HOGENOM; CLU_016552_1_1_1; -.
DR InParanoid; A7EQ00; -.
DR OMA; FFFKYTR; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
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..523
FT /note="Protein ssh4"
FT /id="PRO_0000324485"
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..523
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 361..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 523 AA; 57074 MW; 10BA15A1AC540787 CRC64;
MTSVLSSTPT SIPIIAGAQE ALRDTLQQPT SVQYVPAAAT SSLSDNVQLQ SSNDSTINGV
VIGLLSSFGS AILIALIFLI VYFFKYTSSG RILLDRIGRP GEYDDEQAFA KEEAEALEEM
DDLQRTEYLR AKAFVQSNPP DSLPTDISLS QYLAIQEKGV SAWEFEPELE IANCFVEART
EIEFFDSECC TLTNLPVPKQ NEVYYWESKI YDKPENTLIS IGVATKPYPL FRLPGWHKYS
VAYTSTGHRR YNQPFSGPVY GPQYVQGDVI GVGYRPRTGT IFFTRNGKKL EDVAHGLKSQ
NLFPAVGANG PCTVHVNFGQ SGFVFIEANV KKWGLAPMTG SLAPPPPYGS EQGSILLEAG
RESAQSSNGY YQPDPRHGRT RSGNFRHGPP TSPGPLRSPT DISLAQLTHI PSHEEPGEAS
NSSTPAPTGN TTTQPGLSVH DNAQPPPEYT SPLPSEAGSP RGSTDGERTP MLRRKTTPPP
IPSYNDAVAQ RNRSNSHRDQ VGSRRERSDS HQARHGDGSP SRS
