PRIMA_RAT
ID PRIMA_RAT Reviewed; 153 AA.
AC D3ZZP4; D4ACH8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Proline-rich membrane anchor 1;
DE Short=PRiMA;
DE Flags: Precursor;
GN Name=Prima1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kube M., Klages S., Kuhl H., Thiel J., Beck A., Reinhardt R.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=19368807; DOI=10.1016/j.brainres.2009.01.065;
RA Xie H.Q., Choi R.C., Leung K.W., Chen V.P., Chu G.K., Tsim K.W.;
RT "Transcriptional regulation of proline-rich membrane anchor (PRiMA) of
RT globular form acetylcholinesterase in neuron: an inductive effect of neuron
RT differentiation.";
RL Brain Res. 1265:13-23(2009).
RN [3]
RP INTERACTION WITH ACHE TETRAMERS, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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. Organizes ACHE into tetramers (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACHE, probably through disulfide bonds.
CC {ECO:0000269|PubMed:20147288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20147288};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:20147288}. Cell
CC junction {ECO:0000250}. Synapse {ECO:0000250}. Note=In the brain, PRIMA
CC linked to ACHE is found in membrane rafts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Variant I;
CC IsoId=D3ZZP4-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant II;
CC IsoId=D3ZZP4-2; Sequence=VSP_041497, VSP_041498;
CC -!- TISSUE SPECIFICITY: Isoforms 1 and 2 are expressed in the adult brain.
CC In matured cortical neurons, only isoform 1 is detectable.
CC {ECO:0000269|PubMed:19368807, ECO:0000269|PubMed:20147288}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during the differentiation of in
CC vitro cultured cortical neurons.
CC -!- DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE
CC catalytic subunits. {ECO:0000250}.
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DR EMBL; FM029865; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001102191.2; NM_001108721.2. [D3ZZP4-1]
DR RefSeq; XP_006240557.1; XM_006240495.3. [D3ZZP4-1]
DR AlphaFoldDB; D3ZZP4; -.
DR STRING; 10116.ENSRNOP00000011906; -.
DR GlyGen; D3ZZP4; 1 site.
DR PaxDb; D3ZZP4; -.
DR GeneID; 690195; -.
DR KEGG; rno:690195; -.
DR CTD; 145270; -.
DR RGD; 1583978; Prima1.
DR VEuPathDB; HostDB:ENSRNOG00000008915; -.
DR eggNOG; ENOG502S414; Eukaryota.
DR HOGENOM; CLU_144252_0_0_1; -.
DR InParanoid; D3ZZP4; -.
DR OMA; LIICYKA; -.
DR OrthoDB; 1626013at2759; -.
DR TreeFam; TF337232; -.
DR PRO; PR:D3ZZP4; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008915; Expressed in adult mammalian kidney and 15 other tissues.
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; ISO:RGD.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
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:0000255"
FT CHAIN 36..153
FT /note="Proline-rich membrane anchor 1"
FT /id="PRO_0000410722"
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 133..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 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:0000305"
FT /id="VSP_041497"
FT VAR_SEQ 125..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041498"
SQ SEQUENCE 153 AA; 16495 MW; F3B330ACBD5A28C6 CRC64;
MLLRDLVLRH GCCWPSLLLH CALHPLWGLV QVTHAEPQKS CSKVTDSCQH ICQCRPPPPL
PPPPPPPPPP RLLSAPAPNS TSCPAEDSWW SGLVIIVAVV CASLVFLTVL VIICYKAIKR
KPLRKDENGA SVAEYPMSSS PSNKGVDVNA AVV
