ID Q05D13_MOUSE Unreviewed; 482 AA.
AC Q05D13;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Macoilin {ECO:0000256|ARBA:ARBA00021882};
DE AltName: Full=Transmembrane protein 57 {ECO:0000256|ARBA:ARBA00031129};
DE Flags: Fragment;
GN Name=Maco1 {ECO:0000313|MGI:MGI:1913396};
GN Synonyms=C61 {ECO:0000313|EMBL:AAH19186.1}, RP23-191E19.1
GN {ECO:0000313|EMBL:AAH19186.1}, Tmem57 {ECO:0000313|EMBL:AAH19186.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH19186.1};
RN [1] {ECO:0000313|EMBL:AAH19186.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Mix FVB/N {ECO:0000313|EMBL:AAH19186.1};
RC TISSUE=Mammary tumor. WAP-TGF alpha model. 7 months old
RC {ECO:0000313|EMBL:AAH19186.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC -!- SIMILARITY: Belongs to the macoilin family.
CC {ECO:0000256|ARBA:ARBA00008298}.
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DR EMBL; BC019186; AAH19186.1; -; mRNA.
DR AlphaFoldDB; Q05D13; -.
DR PeptideAtlas; Q05D13; -.
DR UCSC; uc008vfr.1; mouse.
DR AGR; MGI:1913396; -.
DR MGI; MGI:1913396; Maco1.
DR ChiTaRS; Tmem57; mouse.
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 2: Evidence at transcript level;
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 253..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..480
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 482
FT /evidence="ECO:0000313|EMBL:AAH19186.1"
SQ SEQUENCE 482 AA; 55766 MW; FD18CCF91E0900B1 CRC64;
MKRRNADCSK LRRPLKRNRI TEGIYGSTFL YLKFLVVWAL VLLADFVLEF RFEYLWPFWL
FIRSVYDSFR YQGLAFSVFF VCVAFTSNII CLLFIPIQWL FFAASTYVWV QYVWHTERGV
CLPTVSLWIL FVYIEAAIRF KDLKNFHVDL CRPFAAHCIG YPVVTLGFGF KSYVSYKMRL
RKQKEVQKEN EFYMQLLQQA LPPEQQMLQK QEKEAEEAAK GLPDMDSSIL IHHNGGIPAN
KKLSTTLPEI EYREKGKEKD KDAKKHNLGI NNNNILQPVD SKIQEIEYME NHINSKRLNN
DLVGSTENLL KEDSCTASSK NYKNASGVVN SSPRSHSATN GSIPSSSSKN EKKQKCTSKG
PSAHKDLMEN CIPNNQLSKP DALVRLEQDI KKLKADLQAS RQVEQELRSQ ISALSSTERG
IRSEMGQLRQ ENELLQNKLH NAVQMKQKDK QNISQLEKKL KAEQEARSFV EKQLMEEKKK
KK
//
