ID   SSH4_BOTFB              Reviewed;         537 AA.
AC   A6S3E0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Protein ssh4;
GN   Name=ssh4; ORFNames=BC1G_07322;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
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; CH476880; EDN26976.1; -; Genomic_DNA.
DR   RefSeq; XP_001554185.1; XM_001554135.1.
DR   AlphaFoldDB; A6S3E0; -.
DR   SMR; A6S3E0; -.
DR   GeneID; 5434764; -.
DR   KEGG; bfu:BCIN_10g00340; -.
DR   VEuPathDB; FungiDB:Bcin10g00340; -.
DR   OMA; FFFKYTR; -.
DR   OrthoDB; 962732at2759; -.
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; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..537
FT                   /note="Protein ssh4"
FT                   /id="PRO_0000324478"
FT   TOPO_DOM        1..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..537
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          141..337
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          375..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        435
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   537 AA;  58619 MW;  F9BDEDE14F2B9185 CRC64;
     MEDFLRGMQQ STLTTSVLFA TPTSIPIIAA AQEALRDTLQ QPTSLQRAAA AVATSTSSDN
     VQLKSSNDST INGVVIGLLS SFGSAILIAF IFLIVYFFKY TSSGRILLDR IGRPGEYDDE
     QAFAKEEAEA LEEMDDLQRT EYLRAKAFVQ SNPPDSLPTD ISLSQYLAIQ EKGVSAWEFE
     PELEIANCFV EARTEIEFFD SECCTLTNLP VPKQNEVYYW ESKIYDKPEN TLISIGVATK
     PYPLFRLPGW HKYSVAYTST GHRRYNQPFS GPVYGPQYVQ GDVIGVGYRP RTGTIFFTRN
     GKKLEDVAHG LKSQNLFPAV GANGPCTVHV NFGQSGFVFI EANVKKWGLA PMTGSLAPPP
     PYGSEQGSIL LEAGREGAQS SNGHYQPDPR HGRTRSGNFR HGPPTSPGPI RSPTDISLAQ
     LTHFPSHEEP GEASNSSTPA PTGGVTQQSG LGVHDNAQPP PEYTSPLPSA AGSPRGSTDS
     ERTPMLRRKT TPPPIPSYND AVAQRNRSHS HRDRSGGRRE RSDSHRARQG DGNPSQS