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Database: UniProt
Entry: A0A183SGU1_SCHSO
LinkDB: A0A183SGU1_SCHSO
Original site: A0A183SGU1_SCHSO 
ID   A0A183SGU1_SCHSO        Unreviewed;      1249 AA.
AC   A0A183SGU1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Macoilin {ECO:0000256|ARBA:ARBA00021882};
DE   AltName: Full=Transmembrane protein 57 {ECO:0000256|ARBA:ARBA00031129};
GN   ORFNames=SSLN_LOCUS3439 {ECO:0000313|EMBL:VDL89824.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000354201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0000354201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL89824.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDL89824.1,
RC   ECO:0000313|Proteomes:UP000275846};
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; UYSU01032538; VDL89824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183SGU1; -.
DR   STRING; 70667.A0A183SGU1; -.
DR   WBParaSite; SSLN_0000354201-mRNA-1; SSLN_0000354201-mRNA-1; SSLN_0000354201.
DR   Proteomes; UP000050788; Unplaced.
DR   Proteomes; UP000275846; 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   InterPro; IPR019130; Macoilin.
DR   PANTHER; PTHR47464; MACOILIN; 1.
DR   PANTHER; PTHR47464:SF2; MACOILIN; 1.
DR   Pfam; PF09726; Macoilin; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275846};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          105..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          912..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1063..1092
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1143..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1092
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1249 AA;  130602 MW;  04ED3E4B45B5F580 CRC64;
     MRKSKQCVLA KEFACTQLLD ILKITTVRTK TASDCEHRQR QVQSQNLKYF YLLASALPEE
     ARSHNRIGEL ANGELPSSSA SVIPAALPSI PSSSAAGHTN LLQSGAFASD RERERPSASG
     GGGGGKERST RKNLSTGKSG AAVTAAAGES GGGGGGAGLT SRSDAATSTS RGSLHPATIP
     AAACDSTLNS FRVRLGVEFP PLAIIKDPYC PSPRVSYLPL SIYAFTMFQC PEDGCGAVID
     VGTCVTHDLG PSFTPTTLRI GQTVRVKCDS MNVQNLLVCG LSRRGRPASL GHVMVVQRAP
     QMSDRAFFAN DADSIVLKGA DGCSPSVCST NWGDAGSPTA SSNSSLSGHE DISAAMTVMS
     GSANTNKKAV ASGTPLSHQG TSPCSKSSRG GQSADSSTVS ASSSSPTAIV TSSTTTKSGA
     NGRQKDSSLS KLEEELRRLR SERQNLHATE VDLRSQVARL TAIERASLTE NSQMRQELEQ
     LQSKLSSANQ RLQQHFAVPS GTEVGNRKLT LLTGSSSPEL FIGWYLTVKL LDRSTFSPFC
     TTDTERSNLQ ALEKRLAEER RQRTTLEQQL VAEKRARKEA EEKEAAKTVP ASSQSSKAVG
     KLVGTNRPGT GTAAPGRGAV GSPSSTVNTN ACTSETCSSR LRELEAQLKS VTRDLAAKEV
     QLASLRSSRA TAAPATSSTT NSVFSSSSSG TSNAAGTTEG QQKMRKQQQQ QQQQQLVSAA
     QTNTERRISE LAMQLSEMQE ENMRLTAILK GEDKMKQELL TAYHTSLKEI TELTSTLTRK
     EFQIVDLSSR LDGLVPPNCD YLCGVVNSVS GGKSVALGYH HSAQSSDPSS LCRRPSASDS
     YCGGVPDPIT SRYNPVSTRH IPYMNGSGNG FGGNAGADSG GSNVFLNRNS DLDSLFAVSD
     FGGLSSPSSA VAATFSSSPW PKQPSATPCS STSALNASLS SSCTFQFPPS NTPSFDPPCM
     DYVGGSGGGS TGGRNGFSDS LLSAAAGGSV AFTRSHTSAD ERLHADSFGP ESLLSQHQHN
     HPPPSHHHHQ QQQQQSHRMM MEEEYRFPST GSSFGGAKRI LSASAHAPSP PPPASSSSSA
     FHHHHQQQQQ HQYLHGAFNV SLAPTCLSNF ASHQQSAAYS GGGGGPENMS TPAYLNQLRS
     QLAQTAAGAA PGSSSPPTGL DHHQSQSHHL GEMPGSGGGC RGPSPAFSAL SRATDKIVGD
     CADDEDNVGV GGEMLVTSSA AADSSAESVA ATATTTTTSD ASMAALATT
//
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