TPRGL_MOUSE
ID TPRGL_MOUSE Reviewed; 266 AA.
AC Q9DBS2; B1AX99; Q8BTC6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tumor protein p63-regulated gene 1-like protein {ECO:0000305};
DE AltName: Full=Mossy fiber terminal-associated vertebrate-specific presynaptic protein;
DE AltName: Full=Protein FAM79A;
GN Name=Tprg1l {ECO:0000312|MGI:MGI:1915058};
GN Synonyms=Fam79a, Mover {ECO:0000303|PubMed:17869247}, Tprgl;
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], AND INTERACTION WITH BSN.
RC TISSUE=Brain;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Embryo, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND THR-34, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Presynaptic protein involved in the synaptic transmission
CC tuning. Regulates synaptic release probability by decreasing the
CC calcium sensitivity of release. {ECO:0000250|UniProtKB:A8WCF8}.
CC -!- SUBUNIT: Forms homomultimers (By similarity). Multimerization appears
CC to be important for presynaptic targeting (By similarity). Interacts
CC with BSN (PubMed:17869247). {ECO:0000250|UniProtKB:A8WCF8,
CC ECO:0000269|PubMed:17869247}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:A8WCF8}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:A8WCF8}. Presynaptic active zone
CC {ECO:0000250|UniProtKB:A8WCF8}.
CC -!- PTM: Phosphorylated. Phosphorylation promotes association with synaptic
CC vesicle membranes. {ECO:0000250|UniProtKB:A8WCF8}.
CC -!- SIMILARITY: Belongs to the TPRG1 family. {ECO:0000305}.
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DR EMBL; AK004324; BAC25076.1; -; mRNA.
DR EMBL; AK004777; BAB23555.1; -; mRNA.
DR EMBL; AK155413; BAE33252.1; -; mRNA.
DR EMBL; AL806525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX465212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019544; AAH19544.1; -; mRNA.
DR CCDS; CCDS19011.1; -.
DR RefSeq; NP_080664.1; NM_026388.2.
DR AlphaFoldDB; Q9DBS2; -.
DR BioGRID; 212453; 8.
DR MINT; Q9DBS2; -.
DR STRING; 10090.ENSMUSP00000030896; -.
DR iPTMnet; Q9DBS2; -.
DR PhosphoSitePlus; Q9DBS2; -.
DR EPD; Q9DBS2; -.
DR MaxQB; Q9DBS2; -.
DR PaxDb; Q9DBS2; -.
DR PeptideAtlas; Q9DBS2; -.
DR PRIDE; Q9DBS2; -.
DR ProteomicsDB; 259071; -.
DR Antibodypedia; 26890; 62 antibodies from 15 providers.
DR Ensembl; ENSMUST00000030896; ENSMUSP00000030896; ENSMUSG00000029030.
DR GeneID; 67808; -.
DR KEGG; mmu:67808; -.
DR UCSC; uc008wbm.2; mouse.
DR CTD; 67808; -.
DR MGI; MGI:1915058; Tprgl.
DR VEuPathDB; HostDB:ENSMUSG00000029030; -.
DR eggNOG; ENOG502QTYQ; Eukaryota.
DR GeneTree; ENSGT00390000001652; -.
DR HOGENOM; CLU_066718_1_0_1; -.
DR InParanoid; Q9DBS2; -.
DR OMA; CQLDNFK; -.
DR OrthoDB; 1377646at2759; -.
DR PhylomeDB; Q9DBS2; -.
DR TreeFam; TF333472; -.
DR BioGRID-ORCS; 67808; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tprgl; mouse.
DR PRO; PR:Q9DBS2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9DBS2; protein.
DR Bgee; ENSMUSG00000029030; Expressed in external carotid artery and 267 other tissues.
DR ExpressionAtlas; Q9DBS2; baseline and differential.
DR Genevisible; Q9DBS2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; ISS: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; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS: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_0000269187"
FT DOMAIN 59..246
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:0000250|UniProtKB:A8WCF8"
FT REGION 180..266
FT /note="Important for homomultimer formation"
FT /evidence="ECO:0000250|UniProtKB:A8WCF8"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8WCF8"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 266 AA; 29814 MW; 3885516EF3995459 CRC64;
MLQLRDTVDS AGTSPTAVLA AGEDAGAGRP GAGTPLRQTL WPLNVHDPTR RARVKEYFVF
RPGTIEQAVE EIRAVVRPVE DGEIQGVWLL TEVDHWNNEK ERLVLVTDQS LLICKYDFIS
LQCQQVVRVA LSAVDTISCG EFQFPPKSLN KREGFGVRIQ WDKQSRPSFI NRWNPWSTNM
PYATFIEHPM AGMDEKTASL CHLESFKALL IQAVKKAQKE SPLPGQANTV LVLERPLLIE
TYVGLMSFIN NEAKLGYSMT RGKIGF
