MACOI_MOUSE
ID MACOI_MOUSE Reviewed; 664 AA.
AC Q7TQE6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Macoilin;
DE AltName: Full=Brain-specific adapter protein C61 {ECO:0000303|PubMed:15255972};
DE AltName: Full=Macoilin-1;
DE AltName: Full=Transmembrane protein 57;
GN Name=Maco1; Synonyms=Tmem57 {ECO:0000312|MGI:MGI:1913396};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=15255972; DOI=10.1111/j.1460-9568.2004.03473.x;
RA Kuvbachieva A., Bestel A.M., Tissir F., Maloum I., Guimiot F., Ramoz N.,
RA Bourgeois F., Moalic J.M., Goffinet A.M., Simonneau M.;
RT "Identification of a novel brain-specific and Reelin-regulated gene that
RT encodes a protein colocalized with synapsin.";
RL Eur. J. Neurosci. 20:603-610(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Huang C.-H., Peng J., Chen Y.;
RT "Identification of Macoilin as a novel membrane-associated coiled-coil
RT tetraspanin protein.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in the regulation of neuronal activity.
CC {ECO:0000250|UniProtKB:Q8N5G2}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Detected in the nucleus
CC membrane of non-neuronal cells and in axonal outgrowths of neuronal
CC cells (PubMed:15255972). {ECO:0000269|PubMed:15255972}.
CC -!- TISSUE SPECIFICITY: Strong expression in whole nervous system up to
CC 12.5 dpc. Highly expressed in all neuronal differentiation fields from
CC 14.5 dpc to birth, with highest expression in the telencephalic
CC cortical plate and mitral cells in the olfactory bulb, and lower
CC expression in neuronal progenitor zones. Progressively decreased
CC expression in fields of neuron precursor proliferation from 14.5 dpc
CC and virtually undetectable there by 17.5 dpc. No significant expression
CC detected outside the nervous system. After birth, significant
CC expression remains in the cerebellum, olfactory bulb and hippocampus.
CC {ECO:0000269|PubMed:15255972}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, stronger expression at 15.5 dpc
CC than at 10.5 dpc or 19.5 dpc. Expression decreases after birth although
CC significant expression remains associated with some neuronal structures
CC at P10. {ECO:0000269|PubMed:15255972}.
CC -!- SIMILARITY: Belongs to the macoilin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY364165; AAQ64008.1; -; mRNA.
DR EMBL; AY846873; AAX77385.1; -; mRNA.
DR EMBL; AY846874; AAX77386.1; -; mRNA.
DR EMBL; BC054769; AAH54769.1; -; mRNA.
DR CCDS; CCDS18777.1; -.
DR RefSeq; NP_079658.2; NM_025382.6.
DR AlphaFoldDB; Q7TQE6; -.
DR SMR; Q7TQE6; -.
DR BioGRID; 211249; 1.
DR IntAct; Q7TQE6; 1.
DR STRING; 10090.ENSMUSP00000030628; -.
DR GlyGen; Q7TQE6; 4 sites.
DR iPTMnet; Q7TQE6; -.
DR PhosphoSitePlus; Q7TQE6; -.
DR EPD; Q7TQE6; -.
DR jPOST; Q7TQE6; -.
DR MaxQB; Q7TQE6; -.
DR PaxDb; Q7TQE6; -.
DR PeptideAtlas; Q7TQE6; -.
DR PRIDE; Q7TQE6; -.
DR ProteomicsDB; 292074; -.
DR Antibodypedia; 15928; 78 antibodies from 16 providers.
DR DNASU; 66146; -.
DR Ensembl; ENSMUST00000030628; ENSMUSP00000030628; ENSMUSG00000028826.
DR GeneID; 66146; -.
DR KEGG; mmu:66146; -.
DR UCSC; uc008vfq.2; mouse.
DR CTD; 55219; -.
DR MGI; MGI:1913396; Maco1.
DR VEuPathDB; HostDB:ENSMUSG00000028826; -.
DR eggNOG; KOG1821; Eukaryota.
DR GeneTree; ENSGT00390000016613; -.
DR HOGENOM; CLU_012823_1_0_1; -.
DR InParanoid; Q7TQE6; -.
DR OMA; KIHEMEY; -.
DR OrthoDB; 1227984at2759; -.
DR PhylomeDB; Q7TQE6; -.
DR TreeFam; TF324023; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 66146; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tmem57; mouse.
DR PRO; PR:Q7TQE6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TQE6; protein.
DR Bgee; ENSMUSG00000028826; Expressed in superior cervical ganglion and 221 other tissues.
DR ExpressionAtlas; Q7TQE6; baseline and differential.
DR Genevisible; Q7TQE6; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0044306; C:neuron projection terminus; IDA:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:BHF-UCL.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
DR InterPro; IPR019130; Macoilin.
DR PANTHER; PTHR47464:SF3; PTHR47464:SF3; 1.
DR Pfam; PF09726; Macoilin; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..664
FT /note="Macoilin"
FT /id="PRO_0000070268"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
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 REGION 630..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 630..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5G2"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5G2"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5G2"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 664 AA; 76089 MW; 13C8F0E724F796C8 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 EKQLMEEKKR
KKLEEATAAR AVAFAAASRG ECTETLRSRI RELEAEGKKL TMDMKVKEEQ IRELELKVQE
LRKYKENEKD TEVLMSALSA MQDKTQHLEN SLSAETRIKL DLFSALGDAK RQLEIAQGQI
LQKDQEIKDL KQKIAEVMAV MPSITYSAAT SPLSPVSPHY SSKFVETSPS GLDPNASVYQ
PLKK
