ID   SSH4_NEOFI              Reviewed;         507 AA.
AC   A1D1S7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Protein ssh4;
GN   Name=ssh4; ORFNames=NFIA_010510;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22370.1; -; Genomic_DNA.
DR   RefSeq; XP_001264267.1; XM_001264266.1.
DR   AlphaFoldDB; A1D1S7; -.
DR   SMR; A1D1S7; -.
DR   STRING; 36630.CADNFIAP00001479; -.
DR   EnsemblFungi; EAW22370; EAW22370; NFIA_010510.
DR   GeneID; 4592081; -.
DR   KEGG; nfi:NFIA_010510; -.
DR   VEuPathDB; FungiDB:NFIA_010510; -.
DR   eggNOG; KOG1477; Eukaryota.
DR   HOGENOM; CLU_016552_1_1_1; -.
DR   OMA; FFFKYTR; -.
DR   OrthoDB; 962732at2759; -.
DR   Proteomes; UP000006702; 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   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..507
FT                   /note="Protein ssh4"
FT                   /id="PRO_0000324483"
FT   TOPO_DOM        1..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..507
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          146..342
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          385..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   507 AA;  54641 MW;  D005290DB078AD50 CRC64;
     MRGSEASGPG AIFGAPSTLT TSVIRNPTSF LSSSTPLPST DADVVAQNVE HVLLSLTSHN
     DGGLVGVSGN SSGSTGKGIL IGVLSAFGSA TVAVLVLAIF FFFKYTRRGR IFLDRIGRPG
     EFDDEQAFAR EEAEALEVMD DMSRSEYMRA KSFVEANPPE SMQTDISLSQ FLAIQEKGVS
     AWEFQPELEI ANCFVEGRTE IEFYDSECSV QTNLPVPKQN DVYYWEAKIY EKPESTHISI
     GMTTKPYPLF RLPGFHKTSV AYLSTGHRRY NQPFSATPYG PPLAQGDVVG VGYRPRSGTI
     FFTRNGKKLE DVVHGAKTQN FFPTVGANGP CTVHVNFGQM GFVFIEANVK KWGLAPMTGS
     LAPPPPYGSE QGSILLESGR ESAAQISQRV YQDARTNSTV RIPPSRSPGP VRSPTDISLA
     PLAHIPSHED VGEGSSHANT IADEQTPLLN TSDLDQVPPP EYSSPDGSRR GSDITGDLPN
     QNSPPIPSYD AAVGNQADNT STPDGDH