ID A0A1E3I1J5_9TREE Unreviewed; 1421 AA.
AC A0A1E3I1J5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Transmembrane protein {ECO:0000313|EMBL:ODN82408.1};
GN ORFNames=L203_05502 {ECO:0000313|EMBL:ODN82408.1};
OS Cryptococcus depauperatus CBS 7841.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN82408.1, ECO:0000313|Proteomes:UP000094043};
RN [1] {ECO:0000313|EMBL:ODN82408.1, ECO:0000313|Proteomes:UP000094043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN82408.1,
RC ECO:0000313|Proteomes:UP000094043};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-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:ODN82408.1}.
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DR EMBL; AWGK01000026; ODN82408.1; -; Genomic_DNA.
DR STRING; 1295531.A0A1E3I1J5; -.
DR VEuPathDB; FungiDB:L203_05502; -.
DR OrthoDB; 2787577at2759; -.
DR Proteomes; UP000094043; 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; cd00030; C2; 1.
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; 5.
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; 3.
DR SMART; SM00239; C2; 5.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 5.
DR PROSITE; PS50004; C2; 5.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000094043};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000313|EMBL:ODN82408.1};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 144..361
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 352..475
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 500..625
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 631..763
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1027..1145
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1246..1364
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 841..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 153836 MW; 33C8853D7DFEEEC9 CRC64;
MPSIKAFDHA SPNGETFPNI AKVPDAMTGE LTSAVGSLLS QDEKKGAAVH TFDPDASPAQ
KAAVTAKAKA SLGLPNRQKV KEKLSGDGGG GRAVTIDTSA SARAPQPTIT LTDVDKASRD
EGQGLGTDEM PGAIPANTAP AVPTWVKAGW RQVAGLDQGA TAREEASILQ TYLYEPVLSQ
TIIASTDSAL AGMAPAGVDS IRLTTFTLGT KAPRIDYVRT FPKTPEDIVI MDWAISFTPT
DIQDITPRQQ EKQVNPKVVL TIRLGKGAIS KGIPVLLEDM SFSGKMRVKL KLMTNFPHVQ
TVDISFIEKP TFDYVLKPLG GETLGFDINN IPALAPFIRD QVHSNLGPMM YDPNVFTIDL
EQLLSGTPLD AAIGVLRVTV LDARGLKAVK FGGGEPDPYV TFSLGSKPNI AQTKIVPSTS
NPTFNETQFL LINSLADVLN LNVYDYNDHR PDSLLGTVSH ELGTLADDAE QEGIVGKILG
GGKDRGGLRY DLSYFPVLKS EKNPDGSIEP LPDTQTGIVR LTIHQAKDLN MSKSVSGLSG
NALNPFARVF LGGSKHEVHK TKTLKHANQP IWEEACEFLV PEKNKSIVTI DLTDHKDFAI
DPSLGQVTIR LTDLLEAKER HQDWFPLKNS RQGKIRLTAE WKPVAMTGAI GGAGSYIPPI
GILRIWLKKA VDVKNVEAAL GGKSDPYVKV LGNNRVMART EVVHNNLNPE WDQIVYVPVH
TTREQFILEL MDYQNIGKDR PLGYVDMNAG DYIEKGDDQK YPYVSKGVQN KRDHIRLDKT
NHYKGELLYE VDFKPAISLR GGVSFDVQKN ELEVAAEAAQ QKSAAEDSKA NGVAQITPAA
NGSIQVQTEN KTSQEVQMAS EQIANGHKPS QSIENASMTT VTSQLDGDNQ PETAAEDPEE
GVSMTVEEIL SHQSGVLVFQ VISGQLARRG SLEVMIDDGY WPAFTSGKAR STHPTWDQVG
EGFIRELDFS RTWLRINAAD ENSKEDVVAE FKCETKDFLE QCINTPCDFL LTDEAGSNKS
IIKMAARFVP INIVLKPRES INNMGLLRVD VIEAKGIYGA DRSGKSDPYV VFSLNGMKVF
KSETKKKTLH PVWNENFETV IPSRVAAKFV FEIFDWDRVG AATSLGGGVI DLAGLEPFEL
TEKILPVISE KRGEAGTFTF RMLFTPEIIA RVRHNTSSFA TAGRAITHIG GVPLGVGKGV
IHGGGAVADP STGTISSDTT TPNGNDIAAG QTSAPTGTNV EGVVPTSNAT TLPVGEGASP
LEPGTLGVTV ISAKDLKSDR EGNAKPYVQV RVGGKTSKTD HVKGQGPTPE WNETFSFNIS
PNTKTFTVTV FDHHTLGKDP ELGEAEVDIW RHIQPAVPNA DVWVELSQGT GLLRLRIDWN
TGVASPIGPM RLGSRIRTSS ISLKSTPESP SRFSMSKKSR E
//
