TPRGL_HUMAN
ID TPRGL_HUMAN Reviewed; 272 AA.
AC Q5T0D9; A8K1K4; Q8WV04;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
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|HGNC:HGNC:27007}; Synonyms=FAM79A, MOVER;
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 [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=B-cell;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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. Multimerization appears to be important
CC for presynaptic targeting. Interacts with BSN.
CC {ECO:0000250|UniProtKB:A8WCF8, ECO:0000250|UniProtKB:Q9DBS2}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T0D9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T0D9-2; Sequence=VSP_022019;
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; AK289919; BAF82608.1; -; mRNA.
DR EMBL; AL513320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019034; AAH19034.1; -; mRNA.
DR CCDS; CCDS47.1; -. [Q5T0D9-1]
DR RefSeq; NP_877429.2; NM_182752.3. [Q5T0D9-1]
DR AlphaFoldDB; Q5T0D9; -.
DR BioGRID; 126048; 29.
DR IntAct; Q5T0D9; 1.
DR STRING; 9606.ENSP00000367595; -.
DR iPTMnet; Q5T0D9; -.
DR PhosphoSitePlus; Q5T0D9; -.
DR BioMuta; TPRG1L; -.
DR DMDM; 74744290; -.
DR EPD; Q5T0D9; -.
DR jPOST; Q5T0D9; -.
DR MassIVE; Q5T0D9; -.
DR MaxQB; Q5T0D9; -.
DR PaxDb; Q5T0D9; -.
DR PeptideAtlas; Q5T0D9; -.
DR PRIDE; Q5T0D9; -.
DR ProteomicsDB; 64154; -. [Q5T0D9-1]
DR ProteomicsDB; 64155; -. [Q5T0D9-2]
DR Antibodypedia; 26890; 62 antibodies from 15 providers.
DR DNASU; 127262; -.
DR Ensembl; ENST00000344579.5; ENSP00000339714.5; ENSG00000158109.15. [Q5T0D9-2]
DR Ensembl; ENST00000378344.7; ENSP00000367595.2; ENSG00000158109.15. [Q5T0D9-1]
DR GeneID; 127262; -.
DR KEGG; hsa:127262; -.
DR MANE-Select; ENST00000378344.7; ENSP00000367595.2; NM_182752.4; NP_877429.2.
DR UCSC; uc001akm.4; human. [Q5T0D9-1]
DR CTD; 127262; -.
DR DisGeNET; 127262; -.
DR GeneCards; TPRG1L; -.
DR HGNC; HGNC:27007; TPRG1L.
DR HPA; ENSG00000158109; Low tissue specificity.
DR MIM; 611460; gene.
DR neXtProt; NX_Q5T0D9; -.
DR OpenTargets; ENSG00000158109; -.
DR PharmGKB; PA162406855; -.
DR VEuPathDB; HostDB:ENSG00000158109; -.
DR eggNOG; ENOG502QTYQ; Eukaryota.
DR GeneTree; ENSGT00390000001652; -.
DR HOGENOM; CLU_066718_1_0_1; -.
DR InParanoid; Q5T0D9; -.
DR OMA; CQLDNFK; -.
DR OrthoDB; 1377646at2759; -.
DR PhylomeDB; Q5T0D9; -.
DR TreeFam; TF333472; -.
DR PathwayCommons; Q5T0D9; -.
DR SignaLink; Q5T0D9; -.
DR BioGRID-ORCS; 127262; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; TPRG1L; human.
DR GenomeRNAi; 127262; -.
DR Pharos; Q5T0D9; Tbio.
DR PRO; PR:Q5T0D9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T0D9; protein.
DR Bgee; ENSG00000158109; Expressed in ileal mucosa and 174 other tissues.
DR Genevisible; Q5T0D9; HS.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
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 Alternative splicing; Cell projection; Cytoplasmic vesicle; Membrane;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..272
FT /note="Tumor protein p63-regulated gene 1-like protein"
FT /id="PRO_0000269186"
FT DOMAIN 65..238
FT /note="hSac2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01127"
FT REGION 58..97
FT /note="Important for homomultimer formation and
FT localization to presynaptic regions"
FT /evidence="ECO:0000250|UniProtKB:A8WCF8"
FT REGION 186..272
FT /note="Important for homomultimer formation"
FT /evidence="ECO:0000250|UniProtKB:A8WCF8"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBS2"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8WCF8"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 99..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022019"
SQ SEQUENCE 272 AA; 30212 MW; 3324B992F460E83C CRC64;
MLQLRDSVDS AGTSPTAVLA AGEEVGAGGG PGGGRPGAGT PLRQTLWPLS IHDPTRRARV
KEYFVFRPGS IEQAVEEIRV VVRPVEDGEI QGVWLLTEVD HWNNEKERLV LVTEQSLLIC
KYDFISLQCQ QVVRIALNAV DTISYGEFQF PPKSLNKREG FGIRIQWDKQ SRPSFINRWN
PWSTNVPYAT FTEHPMAGAD EKTASLCQLE SFKALLIQAV KKAQKESPLP GQANGVLILE
RPLLIETYVG LMSFINNEAK LGYSMTRGKI GF
