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Database: UniProt
Entry: A0A218Z5N6_9HELO
LinkDB: A0A218Z5N6_9HELO
Original site: A0A218Z5N6_9HELO 
ID   A0A218Z5N6_9HELO        Unreviewed;       668 AA.
AC   A0A218Z5N6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Protein SSH4 {ECO:0000256|ARBA:ARBA00017626};
DE   AltName: Full=Protein ssh4 {ECO:0000256|ARBA:ARBA00016528};
GN   ORFNames=B2J93_7397 {ECO:0000313|EMBL:OWP03379.1};
OS   Marssonina coronariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP03379.1, ECO:0000313|Proteomes:UP000242519};
RN   [1] {ECO:0000313|EMBL:OWP03379.1, ECO:0000313|Proteomes:UP000242519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:OWP03379.1,
RC   ECO:0000313|Proteomes:UP000242519};
RA   Cheng Q.;
RT   "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT   blotch.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWP03379.1}.
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DR   EMBL; MZNU01000176; OWP03379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218Z5N6; -.
DR   STRING; 503106.A0A218Z5N6; -.
DR   InParanoid; A0A218Z5N6; -.
DR   OrthoDB; 5479594at2759; -.
DR   Proteomes; UP000242519; 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:UP000242519};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        212..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          273..475
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          1..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  72594 MW;  E89DCF7217112C32 CRC64;
     MAGTGLLHRQ WRRLETSTEA PARGRFARSA QVRFPISSNP SIRSPGSVKS ERRHRRPPNA
     VALAQMTPAN RPDSHRDDSS SSSSSLPSNI DNTTPHCAVT EPPPSPRIET GSLAETADPV
     SPPQPRPSLE LPEAPSHGRR ATRPQHGTMK EPPRGTTHTT LLTSLTTPSP TRAALADDAA
     RKIQALLALQ TTDFRPTDSE IRIQSDSTIN GVMIGLLSSF GSAILIALIF LVVYFFRYTS
     SGRIFLDRIG RPGEYDDEQA YAREEADALE EMDDLQRAEY FRARAFIEAN PPDSLPTDIS
     MSQHLVIQEK GVSAWEFEPE LEIANCFVEG RTEIEFFDSE CSTLTNLPIP KQNEVYYWES
     KIYDKPETTL ISIGVATKPY PLFRLPGWHK YSVAYTSTGH RRYNQPFSGP AYGPQFVQGD
     VIGVGYRPRT GTIFFTRNGK KLEDVAHGLK SHNLFPAVGA NGPCTVHVNF GQSGFVFIEA
     NVKKWGLAPM TGSLAPPPPY GSEQGSILLE AGREGAQSSH GHHPDPRHGR TRSGNVRYGP
     PTSPGPVRSP TDISLAHLTH VPSNYEPGES SIAAALAPEA AAPTVSRVGL GVSEPPPPEY
     TSPHQSSTNS PRGSVDSARA PLMGRESTPP PIPTYNDTVA GDRARDRARS RSQGTRDRSG
     STRAPGSG
//
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