PRRT2_PONAB
ID PRRT2_PONAB Reviewed; 340 AA.
AC Q5RAC1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Proline-rich transmembrane protein 2;
DE AltName: Full=Dispanin subfamily B member 3;
DE Short=DSPB3;
GN Name=PRRT2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
CC -!- FUNCTION: As a component of the outer core of AMPAR complex, may be
CC involved in synaptic transmission in the central nervous system. In
CC hippocampal neurons, in presynaptic terminals, plays an important role
CC in the final steps of neurotransmitter release, possibly by regulating
CC Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation
CC and down-regulate short-term facilitation.
CC {ECO:0000250|UniProtKB:E9PUL5}.
CC -!- SUBUNIT: Component of the outer core of AMPAR complex (By similarity).
CC AMPAR complex consists of an inner core made of 4 pore-forming
CC GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major
CC auxiliary subunits arranged in a twofold symmetry. One of the two pairs
CC of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2,
CC CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This
CC inner core of AMPAR complex is complemented by outer core constituents
CC binding directly to the GluA/GRIA proteins at sites distinct from the
CC interaction sites of the inner core constituents. Outer core
CC constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and
CC NRN1. The proteins of the inner and outer core serve as a platform for
CC other, more peripherally associated AMPAR constituents. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing (By similarity). Interacts with
CC intersectin 1/ITSN1. Interacts with SNARE complex components, including
CC SNAP25, STX1A, SYT1 and SYT2; this interaction may inhibit SNARE
CC complex formation (By similarity). {ECO:0000250|UniProtKB:E9PUL5,
CC ECO:0000250|UniProtKB:Q7Z6L0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7Z6L0};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}.
CC Presynaptic cell membrane {ECO:0000250|UniProtKB:E9PUL5}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Synapse
CC {ECO:0000250|UniProtKB:E9PUL5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q7Z6L0}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:D3ZFB6}. Postsynaptic
CC density membrane {ECO:0000250|UniProtKB:D3ZFB6}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:D3ZFB6}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; CR859097; CAH91289.1; -; mRNA.
DR RefSeq; NP_001125763.1; NM_001132291.1.
DR AlphaFoldDB; Q5RAC1; -.
DR STRING; 9601.ENSPPYP00000008205; -.
DR PRIDE; Q5RAC1; -.
DR GeneID; 100444066; -.
DR KEGG; pon:100444066; -.
DR CTD; 112476; -.
DR eggNOG; ENOG502S2U1; Eukaryota.
DR InParanoid; Q5RAC1; -.
DR OrthoDB; 1101977at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0017075; F:syntaxin-1 binding; ISS:UniProtKB.
DR GO; GO:1905513; P:negative regulation of short-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; ISS:UniProtKB.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; ISS:UniProtKB.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Membrane; Methylation;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Proline-rich transmembrane protein 2"
FT /id="PRO_0000307746"
FT TOPO_DOM 1..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT INTRAMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TOPO_DOM 290..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TOPO_DOM 339..340
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZFB6"
FT MOD_RES 240
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
SQ SEQUENCE 340 AA; 34970 MW; 0C6007545C09A31A CRC64;
MAASSSEISE MKGVEESPEV PGEGPGHSEA ETGPPQVLAG VPDQPEALQP GPDTTAALVD
SGPKAELAPE TTETPAGASE TAQATDLSLS PGGESKANCS PEDLCQETVS KPEVSKETTA
DQGSRLESAA PPEPAPEPAP QPDPQPDSQP TPKPALQPEL PTQEDPTPEI LSESVGEKQE
NGAVVPLQAG DGEEGPAPEP HSPPSKKSPP ANGAPPRVLQ QLVEEDRMGR AHSGHPGSPR
GSLSRHPSSQ LAGPGVEGGE GTQKPRDYII LAILSCFCPM WPVNIVAFAY AVMSRNSLQQ
GDVDGAQRLG RVAKLLSIVA LVGGVLIIIA SCVINLGVYK
