ID A0A183ALP2_9TREM Unreviewed; 329 AA.
AC A0A183ALP2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Macoilin {ECO:0000256|ARBA:ARBA00021882};
DE AltName: Full=Transmembrane protein 57 {ECO:0000256|ARBA:ARBA00031129};
GN ORFNames=ECPE_LOCUS7877 {ECO:0000313|EMBL:VDP82243.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000789601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000789601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP82243.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP82243.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the regulation of neuronal activity.
CC {ECO:0000256|ARBA:ARBA00003440}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004232}. Rough endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004269}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004269}.
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DR EMBL; UZAN01045212; VDP82243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183ALP2; -.
DR WBParaSite; ECPE_0000789601-mRNA-1; ECPE_0000789601-mRNA-1; ECPE_0000789601.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; Unassembled WGS sequence.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0023041; P:neuronal signal transduction; IEA:InterPro.
DR Gene3D; 1.20.5.1700; -; 1.
DR InterPro; IPR019130; Macoilin.
DR PANTHER; PTHR47464; MACOILIN; 1.
DR PANTHER; PTHR47464:SF2; MACOILIN; 1.
DR Pfam; PF09726; Macoilin; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000272942};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 126..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..289
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 175..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 34598 MW; 20DB9EB895A80DD1 CRC64;
MIPVDRGVYG PTMVFCFLFV YVEVAVRLRD PKTLPLSIDL CRPFAAHCIG YPAVTLGFGL
KTMVAHHLRL RRQRSVEAQN MTFFAMLEEA LPKEFRYYFK PASVASSTSS LSSSSSSSTC
LSHSHLLSST GPSCPTRASA SGDSRNSNVV SVTKSIATGT TGAGCGGGGG GSGAAGNAST
VTTSTAKSGS SATATSAGTG GKPNPGGGGG GGGGGGGGKH PQKDEYTLKL ETELRRLKSE
LQSLRALEID LRTQVQQLTA AERTYRSESA QARQEYESLQ TKLNQLTQRL QVIFSVCLSI
RLTIHLCFLH SLTTSGFIES KICGIAPLC
//