PRIMA_HUMAN
ID PRIMA_HUMAN Reviewed; 153 AA.
AC Q86XR5; Q86XR6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Proline-rich membrane anchor 1;
DE Short=PRiMA;
DE Flags: Precursor;
GN Name=PRIMA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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 INDUCTION.
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 GLYCOSYLATION AT ASN-79.
RX PubMed=22750213; DOI=10.1016/j.neulet.2012.06.045;
RA Chan W.K., Chen V.P., Luk W.K., Choi R.C., Tsim K.W.;
RT "N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not
RT required for assembly and trafficking of globular tetrameric
RT acetylcholinesterase.";
RL Neurosci. Lett. 523:71-75(2012).
RN [4]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-22.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACHE, probably through disulfide bonds.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Synapse
CC {ECO:0000250}. Note=In the brain, PRIMA linked to ACHE is found in
CC membrane rafts. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Variant I;
CC IsoId=Q86XR5-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant II;
CC IsoId=Q86XR5-2; Sequence=VSP_008494, VSP_008495;
CC -!- INDUCTION: By RAF1. {ECO:0000269|PubMed:19368807}.
CC -!- DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE
CC catalytic subunits. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {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; AY225516; AAO74853.1; -; mRNA.
DR EMBL; AY225517; AAO74854.1; -; mRNA.
DR CCDS; CCDS9912.1; -. [Q86XR5-1]
DR RefSeq; NP_821092.1; NM_178013.3. [Q86XR5-1]
DR RefSeq; XP_011534758.1; XM_011536456.2. [Q86XR5-1]
DR AlphaFoldDB; Q86XR5; -.
DR SMR; Q86XR5; -.
DR BioGRID; 126902; 6.
DR STRING; 9606.ENSP00000376848; -.
DR GlyGen; Q86XR5; 1 site.
DR iPTMnet; Q86XR5; -.
DR PhosphoSitePlus; Q86XR5; -.
DR BioMuta; PRIMA1; -.
DR DMDM; 37537937; -.
DR MassIVE; Q86XR5; -.
DR PaxDb; Q86XR5; -.
DR PeptideAtlas; Q86XR5; -.
DR PRIDE; Q86XR5; -.
DR ProteomicsDB; 70321; -. [Q86XR5-1]
DR Antibodypedia; 72168; 8 antibodies from 4 providers.
DR DNASU; 145270; -.
DR Ensembl; ENST00000316227.3; ENSP00000320948.3; ENSG00000175785.13. [Q86XR5-2]
DR Ensembl; ENST00000393140.6; ENSP00000376848.1; ENSG00000175785.13. [Q86XR5-1]
DR Ensembl; ENST00000393143.5; ENSP00000376851.1; ENSG00000175785.13. [Q86XR5-1]
DR Ensembl; ENST00000477603.5; ENSP00000434370.1; ENSG00000175785.13. [Q86XR5-2]
DR Ensembl; ENST00000611347.2; ENSP00000479082.1; ENSG00000274089.4. [Q86XR5-1]
DR Ensembl; ENST00000617019.3; ENSP00000479855.1; ENSG00000274089.4. [Q86XR5-2]
DR Ensembl; ENST00000627063.2; ENSP00000486875.1; ENSG00000274089.4. [Q86XR5-2]
DR Ensembl; ENST00000629961.2; ENSP00000486953.1; ENSG00000274089.4. [Q86XR5-1]
DR GeneID; 145270; -.
DR KEGG; hsa:145270; -.
DR MANE-Select; ENST00000393140.6; ENSP00000376848.1; NM_178013.4; NP_821092.1.
DR UCSC; uc001ybw.2; human. [Q86XR5-1]
DR CTD; 145270; -.
DR DisGeNET; 145270; -.
DR GeneCards; PRIMA1; -.
DR HGNC; HGNC:18319; PRIMA1.
DR HPA; ENSG00000175785; Tissue enhanced (intestine).
DR MIM; 613851; gene.
DR neXtProt; NX_Q86XR5; -.
DR OpenTargets; ENSG00000175785; -.
DR PharmGKB; PA38315; -.
DR VEuPathDB; HostDB:ENSG00000175785; -.
DR eggNOG; ENOG502S414; Eukaryota.
DR GeneTree; ENSGT00390000006240; -.
DR HOGENOM; CLU_144252_0_0_1; -.
DR InParanoid; Q86XR5; -.
DR OMA; LIICYKA; -.
DR PhylomeDB; Q86XR5; -.
DR TreeFam; TF337232; -.
DR PathwayCommons; Q86XR5; -.
DR SignaLink; Q86XR5; -.
DR BioGRID-ORCS; 145270; 12 hits in 1056 CRISPR screens.
DR ChiTaRS; PRIMA1; human.
DR GeneWiki; PRIMA1; -.
DR GenomeRNAi; 145270; -.
DR Pharos; Q86XR5; Tbio.
DR PRO; PR:Q86XR5; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86XR5; protein.
DR Bgee; ENSG00000175785; Expressed in tibial nerve and 93 other tissues.
DR ExpressionAtlas; Q86XR5; baseline and differential.
DR Genevisible; Q86XR5; HS.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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_0000022107"
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 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:0000269|PubMed:22750213"
FT VAR_SEQ 121..124
FT /note="KPLR -> NHAI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11804574"
FT /id="VSP_008494"
FT VAR_SEQ 125..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11804574"
FT /id="VSP_008495"
FT VARIANT 22
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035980"
SQ SEQUENCE 153 AA; 16689 MW; 2F82EA50F0F87EC1 CRC64;
MLLRDLVLRR GCCWSSLLLH CALHPLWGFV QVTHGEPQKS CSKVTDSCRH VCQCRPPPPL
PPPPPPPPPP RLLSAPAPNS TSCPTEESWW SGLVIIIAVC CASLVFLTVL VIICYKAIKR
KPLRKDENGT SVAEYPMSAS QSNKGVDVNN AVV
