ID A0A178EYN3_TRIRU Unreviewed; 1487 AA.
AC A0A178EYN3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Membrane bound C2 domain-containing protein {ECO:0000313|EMBL:OAL65242.1};
GN ORFNames=A7C99_3726 {ECO:0000313|EMBL:OAL65242.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL65242.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL65242.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAL65242.1}.
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DR EMBL; LHPM01000014; OAL65242.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TERG_06871; -.
DR OMA; HETIKIN; -.
DR OrthoDB; 2787577at2759; -.
DR Proteomes; UP000243015; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd04044; C2A_Tricalbin-like; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR CDD; cd04045; C2C_Tricalbin-like; 1.
DR CDD; cd04040; C2D_Tricalbin-like; 1.
DR CDD; cd21678; SMP_TCB; 1.
DR Gene3D; 2.60.40.150; C2 domain; 4.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037761; C2A_Tricalbin.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR037762; C2C_Tricalbin.
DR InterPro; IPR037756; C2D_Tricalbin.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR017147; Tricalbin.
DR PANTHER; PTHR46980; TRICALBIN-1-RELATED; 1.
DR PANTHER; PTHR46980:SF2; TRICALBIN-1-RELATED; 1.
DR Pfam; PF00168; C2; 5.
DR PIRSF; PIRSF037232; Tricalbin; 1.
DR SMART; SM00239; C2; 5.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 4.
DR PROSITE; PS50004; C2; 4.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243015};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 169..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 229..434
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 429..548
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 573..693
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 699..829
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1056..1176
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 24..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 162448 MW; 3B5A79FE4A17AFD2 CRC64;
MATQAESPAT DAARPAPETI EQKLVDESKK AGVPAFQFDP DASPEKKAEQ AKMAIPAGFQ
QNGTNGTNGS QAVNGKTVDA VAPATDMGAT NGTEKPAEME KADEADKPKM EVKELTEEEK
FAPGRTGWAP QFSAPAAEDG TGEEPGLPPT LLEGKLEDKF FGDWYHNTAV IIFACLASWI
IALFGGGLGW VFLVMAACGT YYRTSVRRVR RNFRDDITRE LAKNKLETDT ETLEWINSFL
AKFWPIYAPN LAHSIICSVD QVLSTSTPAF LDSLRLKTFT LGSKPPRLEH VKTYPKTEPD
IVLMDWKFSF TPADKMDLTA RQIKDKINPK VVLEVRVGKG IVSKGLDVIV EDFAFSGLMR
VKVKLQIQFP HVERIDISFL GKPEIDYVCK PIGGETLGFD INFIPGLETF ITEQIHGNLA
PMMYDPNVFP VEIAKMLAGN PVDQAIGVLA VTIHGANGLK KADQFSGTPD PYTLVSINSR
AELGRTKTVS DTSNPKWNET LYVIITSFTD ALTLQVFDWN EFRKDVELGT ATFSLESLET
EEVHENLNLD IMQNGRNRGV MQADVRFFPV LTSKKTDGGA IEPPPELNTG IAKFTVEQAK
DLDGSKSFIG QLNPYAVLLL NGKEVHITKK LKRTNNPIFP DPSKEILITD RKTARLGMMI
KDDRDLATDP ILGKQQIKLN DMLKMMDKGK EWFELAGAKT GRVKMRLEWK PVALKGVVGT
GGYINPIGVM RLHIKNAKDL RNVETMGKSD PYLRVMKSGM EVRRTVTWLN NLNPEWDEVL
YVPVNSAREK LVLEVMDDES IGKDRPLGLV ELNVGEYIKE GEDGEYEVHD EKRDLSTPLK
LDGRSHQKGI LNYTVAFYPT LNVVDPDEEA DELEAQKELA AAAAEEEGKP TDADTTANAE
ATTNGDARPS TDGLVNGEKA EKEVPKIRLT PQDVHKYESG LIVFKLEEGD FSSTGTQLEV
LMDDNLYPSY TSPTIQSKHM VFGDVGDAFV PEMEFSKITL RLVAKHDRPN DDSEDHSIAK
LSGPTLTTLQ QSLYKPTELV LRGSDGINSK VTVSLKYLPV KMKLDPSESI NNMGNLRVDI
LDAADLPSAD RNGFSDPYCK FKLGDKEVFK TKVQKKTLHP AWNEFFETPI KSRIAANFRA
DVYDWDFGDK ADYLGGTSID LTHLDPFQAQ EISLPLDGKS GAIRLKLLFK PAYVTRSRQG
SSTFSGTFAA PGKIVGAPVK GVTMLGGGVV KGASFLKHGF KRSSRAQVET EAEPEAATAA
TATNGTHGHT PSVEVSAPGT PQRAGALADS PSGSPVMSHS RSRSSASQAG LGVSSIKGET
GAANITIVSA TGYPRSTNVR IVVKQQTSKG MKEIHKSKAH KAHGSSSETE SVVQFDPGHE
TIKINSVTAD AQFQLQVKDH AVFGSDDILG EALFFLDDQG SNAGKERNVK VGNGFVTIKT
VFTSSESSSL RPGTSHSNTG PEESTADSPK PRRSFLSKRS VSGVGAS
//
