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 22-FEB-2023, entry version 76.
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 GlyCosmos; Q1E2D2; 1 site, No reported glycans.
DR GeneID; 4564914; -.
DR KEGG; cim:CIMG_03281; -.
DR VEuPathDB; FungiDB:CIMG_03281; -.
DR InParanoid; Q1E2D2; -.
DR OMA; FFFKYTR; -.
DR OrthoDB; 5479594at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR PANTHER; PTHR12864:SF54; SPRY DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//
