ID A0A3N2PLZ5_9PEZI Unreviewed; 501 AA.
AC A0A3N2PLZ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Protein SSH4 {ECO:0000256|ARBA:ARBA00017626};
DE AltName: Full=Protein ssh4 {ECO:0000256|ARBA:ARBA00016528};
GN ORFNames=SODALDRAFT_337511 {ECO:0000313|EMBL:ROT35551.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT35551.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT35551.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT35551.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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. {ECO:0000256|ARBA:ARBA00025244}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004639}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004639}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004576}.
CC -!- SIMILARITY: Belongs to the SSH4 family.
CC {ECO:0000256|ARBA:ARBA00006990}.
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DR EMBL; ML119061; ROT35551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2PLZ5; -.
DR STRING; 1314773.A0A3N2PLZ5; -.
DR OrthoDB; 5479594at2759; -.
DR Proteomes; UP000272025; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000272025};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..276
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 313..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 54302 MW; AC3FC703C59D0F52 CRC64;
MAPTPPNSAL NGVIIGLLSS FGSAILIALI FLVIYFFRYT DTGRIFLDRI GRPGEYDDEQ
AFAREEAEAL ETMDDLQRTE YLRAKAFIAA NPPESLQTDI SLSQYLAIQE KGVSAWEFEP
ELEIANCFVE GRTEIEFFDS ECTVMSNLPV PKQNEVYYWE AKIFDKPENT LLSIGMATKP
YPLFRLPGYH KYSVAYMSTG HRRFNQPFNP TPYAPSYVQG DVIGVGYRPR TGTIFFTRNG
RKLDDVVHGF KSHNFFPAVG ANGPCSVHVN FGQAGFVFIE ANVKKWGLAP MTGNLAPPPP
YGSEQGDILL EAGRKDGYSG SSSSAVQTHH VSSHSVQPSR DNAGQTLSAA HGHGRTRSGN
FRVLPPRSPG PTTSPTDISL AHFVPTDDGG ESSSSAPAVH PRHDEHVVGL GMQDALNPPP
EYTSPEQSEA GSRRNSTDSD NTPLIRVINR SRGSSAAAAA GSSQPPIPSY SDAIRDGAGS
ALGNGPGITR HVSRSRSHSA Q
//
