TPRGL_RAT
ID TPRGL_RAT Reviewed; 266 AA.
AC A8WCF8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Tumor protein p63-regulated gene 1-like protein {ECO:0000250|UniProtKB:Q5T0D9};
DE AltName: Full=Mossy fiber terminal-associated vertebrate-specific presynaptic protein {ECO:0000312|EMBL:ABW83994.1};
GN Name=Tprg1l {ECO:0000312|RGD:1590079};
GN Synonyms=Mover {ECO:0000303|PubMed:17869247, ECO:0000303|PubMed:23723986,
GN ECO:0000303|PubMed:26212709};
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] {ECO:0000305, ECO:0000312|EMBL:ABW83994.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar {ECO:0000312|EMBL:ABW83994.1};
RC TISSUE=Hippocampus {ECO:0000312|EMBL:ABW83994.1};
RX PubMed=17869247; DOI=10.1016/j.febslet.2007.08.070;
RA Kremer T., Kempf C., Wittenmayer N., Nawrotzki R., Kuner T., Kirsch J.,
RA Dresbach T.;
RT "Mover is a novel vertebrate-specific presynaptic protein with differential
RT distribution at subsets of CNS synapses.";
RL FEBS Lett. 581:4727-4733(2007).
RN [2] {ECO:0000312|EMBL:AAI60865.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAI60865.1};
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23723986; DOI=10.1371/journal.pone.0063474;
RA Ahmed S., Wittenmayer N., Kremer T., Hoeber J., Kiran Akula A., Urlaub H.,
RA Islinger M., Kirsch J., Dean C., Dresbach T.;
RT "Mover is a homomeric phospho-protein present on synaptic vesicles.";
RL PLoS ONE 8:E63474-E63474(2013).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26212709; DOI=10.1016/j.neuron.2015.07.001;
RA Koerber C., Horstmann H., Venkataramani V., Herrmannsdoerfer F., Kremer T.,
RA Kaiser M., Schwenger D.B., Ahmed S., Dean C., Dresbach T., Kuner T.;
RT "Modulation of Presynaptic Release Probability by the Vertebrate-Specific
RT Protein Mover.";
RL Neuron 87:521-533(2015).
CC -!- FUNCTION: Presynaptic protein involved in the synaptic transmission
CC tuning. Regulates synaptic release probability by decreasing the
CC calcium sensitivity of release. {ECO:0000269|PubMed:26212709}.
CC -!- SUBUNIT: Forms homomultimers (PubMed:23723986). Multimerization appears
CC to be important for presynaptic targeting (PubMed:23723986). Interacts
CC with BSN (By similarity). {ECO:0000250|UniProtKB:Q9DBS2,
CC ECO:0000269|PubMed:23723986}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:17869247,
CC ECO:0000269|PubMed:23723986, ECO:0000269|PubMed:26212709}; Peripheral
CC membrane protein {ECO:0000269|PubMed:23723986,
CC ECO:0000269|PubMed:26212709}. Presynaptic active zone
CC {ECO:0000269|PubMed:17869247, ECO:0000269|PubMed:26212709}.
CC -!- TISSUE SPECIFICITY: Highest levels in brain with lower levels in
CC testis. Weakly expressed in heart, spleen and liver. In the hippocampal
CC CA3 region, localizes to mossy fiber terminals but is absent from
CC inhibitory nerve terminals. Localizes to inhibitory terminals
CC throughout the cerebellar cortex (at protein level) (PubMed:17869247).
CC Expressed in the calyx of Held (PubMed:26212709).
CC {ECO:0000269|PubMed:17869247, ECO:0000269|PubMed:26212709}.
CC -!- PTM: Phosphorylated. Phosphorylation promotes association with synaptic
CC vesicle membranes. {ECO:0000269|PubMed:23723986}.
CC -!- SIMILARITY: Belongs to the TPRG1 family. {ECO:0000255}.
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DR EMBL; EU220430; ABW83994.1; -; mRNA.
DR EMBL; BC160865; AAI60865.1; -; mRNA.
DR RefSeq; NP_001103788.1; NM_001110318.2.
DR RefSeq; NP_001258014.1; NM_001271085.1.
DR AlphaFoldDB; A8WCF8; -.
DR STRING; 10116.ENSRNOP00000064778; -.
DR iPTMnet; A8WCF8; -.
DR PhosphoSitePlus; A8WCF8; -.
DR jPOST; A8WCF8; -.
DR PaxDb; A8WCF8; -.
DR PeptideAtlas; A8WCF8; -.
DR PRIDE; A8WCF8; -.
DR GeneID; 687090; -.
DR KEGG; rno:687090; -.
DR CTD; 127262; -.
DR RGD; 1590079; Tprg1l.
DR VEuPathDB; HostDB:ENSRNOG00000046227; -.
DR eggNOG; ENOG502QTYQ; Eukaryota.
DR HOGENOM; CLU_066718_1_0_1; -.
DR InParanoid; A8WCF8; -.
DR OMA; CQLDNFK; -.
DR OrthoDB; 1377646at2759; -.
DR PhylomeDB; A8WCF8; -.
DR PRO; PR:A8WCF8; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000046227; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; A8WCF8; baseline and differential.
DR Genevisible; A8WCF8; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
DR InterPro; IPR034753; hSac2.
DR InterPro; IPR022158; Inositol_phosphatase.
DR InterPro; IPR040242; TPRG1-like.
DR PANTHER; PTHR31108; PTHR31108; 1.
DR Pfam; PF12456; hSac2; 1.
DR PROSITE; PS51791; HSAC2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasmic vesicle; Membrane; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..266
FT /note="Tumor protein p63-regulated gene 1-like protein"
FT /id="PRO_0000347273"
FT DOMAIN 59..239
FT /note="hSac2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01127"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..91
FT /note="Important for homomultimer formation and
FT localization to presynaptic regions"
FT /evidence="ECO:0000269|PubMed:23723986"
FT REGION 180..266
FT /note="Important for homomultimer formation"
FT /evidence="ECO:0000269|PubMed:23723986"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBS2"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0D9"
SQ SEQUENCE 266 AA; 29844 MW; 9CF5266828B048C8 CRC64;
MLQLRDTVDS AGTSPTAVLA AGEDAGAGRQ GAGTPLRQTL WPLNVHDPTR RARVKEYFVF
RPGTIEQAVE EIRAVVRPVE DGEIQGVWLL TEVDHWNNEK ERLVLVTDQS LLICKYDFIS
LQCQQVVRVA LSAVDTISCG EFQFPPKSLN KREGFGVRIQ WDKQSRPSFI NRWNPWSTNM
PYATFIEHPM AGMDEKTASL CHLESFKALL IQAVKKAQKE SPLPGQANNV LVLDRPLLIE
TYVGLMSFIN NEAKLGYSMT RGKIGF
