ID   SSH4_COCIM              Reviewed;         494 AA.
AC   Q1E2D2; J3KB88;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Protein SSH4;
GN   Name=SSH4; ORFNames=CIMG_03281;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG704916; EAS32257.3; -; Genomic_DNA.
DR   RefSeq; XP_001243840.1; XM_001243839.2.
DR   AlphaFoldDB; Q1E2D2; -.
DR   SMR; Q1E2D2; -.
DR   STRING; 246410.Q1E2D2; -.
DR   EnsemblFungi; EAS32257; EAS32257; CIMG_03281.
DR   GeneID; 4564914; -.
DR   KEGG; cim:CIMG_03281; -.
DR   VEuPathDB; FungiDB:CIMG_03281; -.
DR   InParanoid; Q1E2D2; -.
DR   OMA; FFFKYTR; -.
DR   OrthoDB; 962732at2759; -.
DR   Proteomes; UP000001261; 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..494
FT                   /note="Protein SSH4"
FT                   /id="PRO_0000324480"
FT   TOPO_DOM        1..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..494
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          140..336
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          374..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   494 AA;  53847 MW;  E9F775EF5B325BB6 CRC64;
     MFSRDDLVTT LTTSLIQGTP APSSQSSIHR RFGSFQQATE PVNHGYRPSR VSASEKSIMF
     SLGGNVGSTG KGILIGILSA LGSAGIAIIV LSLVFFLRYT HRGRIILDRL GRPGEYDDEQ
     AFAREEAEAL ESMDELQQAE YMRAKAFIQA NPPESAQTDI SLSQFLAIQE KGVSAWEFEP
     ELEIANCFVE ARTEIEFFDS ECSVQSNLPV PKQNEVYYWE AKIYDKPETS LISIGMTTKP
     YPLFRLPGFH KTSISYQSTG HRRHNQPFTP TLYGPEFVQG DVVGVGYRPR SGTIFFTRNG
     KKLEDVAHGL KSQNFFPTVG ANGPCTVHVN FGQLGFVFIE ANVKKWGLAP MTGSLAPPPP
     YGSEQGSILL ETGRENSQTP QWWGSAHSRT RSGTIRLGQG GPVRSPTDIS LAPLPHISPP
     HDVGEGTSNS AQAGENDSDV DAAILDQPPP EYSSPATSPP NGQSGDARID IHPDPNDPPI
     PSYDAAVLQQ QQQV