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Database: UniProt
Entry: K1X177_MARBU
LinkDB: K1X177_MARBU
Original site: K1X177_MARBU 
ID   K1X177_MARBU            Unreviewed;       488 AA.
AC   K1X177;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=C2 domain-containing protein {ECO:0000313|EMBL:EKD18762.1};
GN   ORFNames=MBM_03004 {ECO:0000313|EMBL:EKD18762.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD18762.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD18762.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18762.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; JH921432; EKD18762.1; -; Genomic_DNA.
DR   RefSeq; XP_007290893.1; XM_007290831.1.
DR   AlphaFoldDB; K1X177; -.
DR   GeneID; 18758939; -.
DR   KEGG; mbe:MBM_03004; -.
DR   eggNOG; KOG1012; Eukaryota.
DR   HOGENOM; CLU_048762_0_0_1; -.
DR   InParanoid; K1X177; -.
DR   OMA; DIPDCYC; -.
DR   OrthoDB; 944695at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   CDD; cd00030; C2; 2.
DR   CDD; cd21670; SMP_ESyt; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR031468; SMP_LBD.
DR   InterPro; IPR039010; Synaptotagmin_SMP.
DR   PANTHER; PTHR45761; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR   PANTHER; PTHR45761:SF1; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF17047; SMP_LBD; 1.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51847; SMP; 1.
PE   4: Predicted;
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00023055}.
FT   DOMAIN          13..190
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51847"
FT   DOMAIN          185..314
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   488 AA;  52615 MW;  4D2E442BAE0D48E5 CRC64;
     MASLVEKLTA EGGGESVRFL NDIVAHLWPH INVAASKMTK EIADPMFKTM LPGPLASLHF
     TKIDLGHVPF QLSNVLVTKT EADCIKLDMN VDWAGKCDIE LDGNMIPTLG VEKVALHGRL
     SILLGPTSDI IPLIGAAQIA FVNPPVLKLD FTGAANLADL DMIDGSVRRV ILSIINSMFV
     MPNRFLYKID AANDYFKTQI SPIGIIRLTV EKATGFAEEK QSTGKRLFSK LTGASPDTYC
     KVSVGAEEPW QTSVKNNTTN PSWNEVHDFV VTDLNQCIAV DLLDHDLNSD DKIGLGVTTV
     KDILSAGGKH DLSLVHKEKP VEGKISLSCK FYHFASENSS FSASEHSAEG SLCGVATVLV
     AGAFSVPGKR EEIKPSVVVT WGEKHHFQTA VITDTPGTDI SNPTFDSTFR IPVTADLVGS
     GAQNFRIALM DQKAEIGSVE IPLSDVQEAP NMILQKKFEV GGGATVRASI SLRGIAPASL
     EEISLPRR
//
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