ID   SSH4_ASPCL              Reviewed;         511 AA.
AC   A1CNW8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Protein ssh4;
GN   Name=ssh4; ORFNames=ACLA_020460;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW07339.1; -; Genomic_DNA.
DR   RefSeq; XP_001268765.1; XM_001268764.1.
DR   AlphaFoldDB; A1CNW8; -.
DR   STRING; 5057.CADACLAP00001982; -.
DR   EnsemblFungi; EAW07339; EAW07339; ACLA_020460.
DR   GeneID; 4701595; -.
DR   KEGG; act:ACLA_020460; -.
DR   VEuPathDB; FungiDB:ACLA_020460; -.
DR   eggNOG; KOG1477; Eukaryota.
DR   HOGENOM; CLU_016552_1_1_1; -.
DR   OMA; FFFKYTR; -.
DR   OrthoDB; 962732at2759; -.
DR   Proteomes; UP000006701; 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..511
FT                   /note="Protein ssh4"
FT                   /id="PRO_0000324476"
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..511
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          432..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        400
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   511 AA;  54917 MW;  0082E8A4E9F366AE CRC64;
     MRGSEASGPG ALLGAASTLT TSVIRNPTSI PTSSAPIPST DAGLVAKNVE HVLMSLTAQN
     DGGLVSVSGN SSGSTGKGIL IGVLSAFGSA VVAVIVLAIF FFFKYTRRGR IMLDRIGRPG
     EFDDEQAFAR EEAEALEVMD DLSRSEYMRA KAFVEAYPPE SMQTDISLSQ FLAIQEKGVS
     AWEFQPELEI ANCFVEGRTE IEFYDSECSV QTNLPVPKQN DVYYWEAKIY DKPENTLVSV
     GMTTKPYPLF RLPGFHKYSV AYSSTGHRRH NQPFASTPYG PPLSQGDVIG VGYRPRSGTI
     FFTRNGKKLE DVVHAAKTQN FFPTVGANGP CTVHVNFGQM GFVFIEANVK KWGLAPMTGS
     LAPPPPYGSE QGSILLESGR ESAAQISQRV YQEAGYARTN STVRIPPSRS PGPVRSPTDI
     SLAQLAHIPS HEDVGEGSSQ ANTIDGEQTP LLNTNDLDDQ VPPPEYSSPD GSRRGSDIAG
     DLPRQGSPPI PSYDAAVGNH SGDTARSDSE P