PRIMA_MOUSE
ID PRIMA_MOUSE Reviewed; 153 AA.
AC Q810F0; Q8VHC4;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Proline-rich membrane anchor 1;
DE Short=PRiMA;
DE Flags: Precursor;
GN Name=Prima1;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH ACHE, AND
RP MUTAGENESIS OF CYS-114.
RC TISSUE=Neuroblastoma;
RX PubMed=11804574; DOI=10.1016/s0896-6273(01)00584-0;
RA Perrier A.L., Massoulie J., Krejci E.;
RT "PRiMA: the membrane anchor of acetylcholinesterase in the brain.";
RL Neuron 33:275-285(2002).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=14622217; DOI=10.1046/j.1460-9568.2003.02914.x;
RA Perrier N.A., Kherif S., Perrier A.L., Dumas S., Mallet J., Massoulie J.;
RT "Expression of PRiMA in the mouse brain: membrane anchoring and
RT accumulation of 'tailed' acetylcholinesterase.";
RL Eur. J. Neurosci. 18:1837-1847(2003).
RN [3]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 109-VAL--LYS-121; CYS-114 AND
RP 138-SER--SER-142.
RX PubMed=20147288; DOI=10.1074/jbc.m109.038711;
RA Xie H.Q., Liang D., Leung K.W., Chen V.P., Zhu K.Y., Chan W.K., Choi R.C.,
RA Massoulie J., Tsim K.W.;
RT "Targeting acetylcholinesterase to membrane rafts: a function mediated by
RT the proline-rich membrane anchor (PRiMA) in neurons.";
RL J. Biol. Chem. 285:11537-11546(2010).
CC -!- FUNCTION: Required to anchor acetylcholinesterase (ACHE) to the basal
CC lamina of the neuromuscular junction and to the membrane of neuronal
CC synapses in brain. Also able to organize ACHE into tetramers.
CC {ECO:0000269|PubMed:11804574}.
CC -!- SUBUNIT: Interacts with ACHE, probably through disulfide bonds.
CC {ECO:0000269|PubMed:11804574}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell junction. Synapse. Note=In the brain, PRIMA linked to
CC ACHE is found in membrane rafts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Variant I;
CC IsoId=Q810F0-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant II;
CC IsoId=Q810F0-2; Sequence=VSP_008496, VSP_008497;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the central nervous
CC system, including in the brain. Also expressed in muscle, heart and
CC kidney. Isoform 1 may be predominant in the cortex and striatum, while
CC isoform 2 is more abundant in the cerebellum.
CC {ECO:0000269|PubMed:11804574, ECO:0000269|PubMed:14622217}.
CC -!- DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE
CC catalytic subunits. {ECO:0000269|PubMed:11804574}.
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DR EMBL; AY043275; AAK85717.1; -; mRNA.
DR EMBL; AY225515; AAO74852.1; -; mRNA.
DR CCDS; CCDS26127.1; -. [Q810F0-1]
DR RefSeq; NP_579942.2; NM_133364.2.
DR AlphaFoldDB; Q810F0; -.
DR STRING; 10090.ENSMUSP00000074017; -.
DR GlyGen; Q810F0; 1 site.
DR PhosphoSitePlus; Q810F0; -.
DR PaxDb; Q810F0; -.
DR PRIDE; Q810F0; -.
DR ProteomicsDB; 291811; -. [Q810F0-1]
DR DNASU; 170952; -.
DR GeneID; 170952; -.
DR KEGG; mmu:170952; -.
DR CTD; 145270; -.
DR MGI; MGI:1926097; Prima1.
DR eggNOG; ENOG502S414; Eukaryota.
DR InParanoid; Q810F0; -.
DR BioGRID-ORCS; 170952; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Prima1; mouse.
DR PRO; PR:Q810F0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q810F0; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0019899; F:enzyme binding; IPI:MGI.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IPI:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Neurotransmitter degradation; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000250"
FT CHAIN 36..153
FT /note="Proline-rich membrane anchor 1"
FT /id="PRO_0000022108"
FT TOPO_DOM 36..92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 56..70
FT /note="PRAD"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 121..124
FT /note="KPLR -> NQAI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11804574"
FT /id="VSP_008496"
FT VAR_SEQ 125..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11804574"
FT /id="VSP_008497"
FT MUTAGEN 109..121
FT /note="VLVIICYKAIKRK->GIAIICLKAISDM: Decrease in ACHE
FT tetramer recruitment to membrane rafts."
FT /evidence="ECO:0000269|PubMed:20147288"
FT MUTAGEN 114
FT /note="C->A: Does not abolish the localization of ACHE."
FT /evidence="ECO:0000269|PubMed:11804574,
FT ECO:0000269|PubMed:20147288"
FT MUTAGEN 114
FT /note="C->S: No effect on ACHE tetramer recruitment to
FT membrane rafts."
FT /evidence="ECO:0000269|PubMed:11804574,
FT ECO:0000269|PubMed:20147288"
FT MUTAGEN 131
FT /note="S->A: No effect on ACHE tetramer recruitment to
FT membrane rafts; when associated with 138-A--A-142."
FT MUTAGEN 138..142
FT /note="SSSQS->AAAQA: No effect on ACHE tetramer recruitment
FT to membrane rafts; when associated with A-131."
FT /evidence="ECO:0000269|PubMed:20147288"
SQ SEQUENCE 153 AA; 16564 MW; F323F7BABD5F28C9 CRC64;
MLLRDLVPRH GCCWPSLLLH CALHPLWGLV QVTHAEPQKS CSKVTDSCQH ICQCRPPPPL
PPPPPPPPPP RLLSAPAPNS TSCPAEDSWW SGLVIIVAVV CASLVFLTVL VIICYKAIKR
KPLRKDENGT SVAEYPMSSS QSHKGVDVNA AVV
