SYT12_MOUSE
ID SYT12_MOUSE Reviewed; 421 AA.
AC Q920N7;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Synaptotagmin-12 {ECO:0000303|PubMed:17190793};
DE AltName: Full=Synaptotagmin XII {ECO:0000303|PubMed:11514560};
DE Short=SytXII {ECO:0000303|PubMed:11514560};
GN Name=Syt12 {ECO:0000303|PubMed:17190793};
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].
RC TISSUE=Brain;
RX PubMed=11514560; DOI=10.1074/jbc.m105356200;
RA Fukuda M., Kanno E., Ogata Y., Mikoshiba K.;
RT "Mechanism of the SDS-resistant synaptotagmin clustering mediated by the
RT cysteine cluster at the interface between the transmembrane and spacer
RT domains.";
RL J. Biol. Chem. 276:40319-40325(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Hippocampus;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17190793; DOI=10.1083/jcb.200607021;
RA Maximov A., Shin O.H., Liu X., Suedhof T.C.;
RT "Synaptotagmin-12, a synaptic vesicle phosphoprotein that modulates
RT spontaneous neurotransmitter release.";
RL J. Cell Biol. 176:113-124(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT
RP SER-97, AND MUTAGENESIS OF SER-97.
RX PubMed=23739973; DOI=10.1523/jneurosci.5814-12.2013;
RA Kaeser-Woo Y.J., Younts T.J., Yang X., Zhou P., Wu D., Castillo P.E.,
RA Suedhof T.C.;
RT "Synaptotagmin-12 phosphorylation by cAMP-dependent protein kinase is
RT essential for hippocampal mossy fiber LTP.";
RL J. Neurosci. 33:9769-9780(2013).
CC -!- FUNCTION: Synaptic vesicle phosphoprotein that enhances spontaneous
CC neurotransmitter release but does not effect induced neurotransmitter
CC release (By similarity). Unlike other synaptotagmins, it does not bind
CC Ca(2+) or phospholipids (By similarity). Essential for mossy-fiber
CC long-term potentiation in the hippocampus (PubMed:23739973).
CC {ECO:0000250|UniProtKB:P97610, ECO:0000269|PubMed:23739973}.
CC -!- SUBUNIT: Homodimer (By similarity). Can also form heterodimers (By
CC similarity). Interacts with SYT1 (By similarity).
CC {ECO:0000250|UniProtKB:P97610, ECO:0000250|UniProtKB:Q9R0N7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:17190793}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, specifically by neurons in
CC the hippocampus, and in the adrenal medulla (at protein level).
CC {ECO:0000269|PubMed:17190793, ECO:0000269|PubMed:23739973}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in the brain at postnatal
CC day 5 (at protein level) (PubMed:17190793). Expression in the brain is
CC increased by postnatal days 9 and 10, and continues to increase at
CC postnatal days 15 and 20 (at protein level) (PubMed:17190793).
CC {ECO:0000269|PubMed:17190793}.
CC -!- PTM: Phosphorylation of Ser-97 is required for mossy-fiber long-term
CC potentiation. {ECO:0000269|PubMed:23739973}.
CC -!- DISRUPTION PHENOTYPE: No measurable change in basal synaptic strength
CC or short-term neuronal plasticity (PubMed:23739973). Neurons from the
CC CA3 hippocampal region exhibit an impairment of cAMP-dependent long-
CC term potentiation in mossy-fiber synapses (PubMed:23739973).
CC {ECO:0000269|PubMed:23739973}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC -!- CAUTION: Unlike classical synaptotagmins, lacks Ca(2+)-binding
CC sequences and does not bind phospholipids.
CC {ECO:0000250|UniProtKB:P97610}.
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DR EMBL; AB062804; BAB69674.1; -; mRNA.
DR EMBL; AK046627; BAC32812.1; -; mRNA.
DR EMBL; AK083139; BAC38779.1; -; mRNA.
DR CCDS; CCDS29428.1; -.
DR RefSeq; NP_598925.1; NM_134164.5.
DR AlphaFoldDB; Q920N7; -.
DR SMR; Q920N7; -.
DR BioGRID; 228489; 1.
DR STRING; 10090.ENSMUSP00000055237; -.
DR iPTMnet; Q920N7; -.
DR PhosphoSitePlus; Q920N7; -.
DR MaxQB; Q920N7; -.
DR PaxDb; Q920N7; -.
DR PRIDE; Q920N7; -.
DR ProteomicsDB; 254616; -.
DR ABCD; Q920N7; 1 sequenced antibody.
DR Antibodypedia; 2614; 195 antibodies from 30 providers.
DR DNASU; 171180; -.
DR Ensembl; ENSMUST00000059295; ENSMUSP00000055237; ENSMUSG00000049303.
DR GeneID; 171180; -.
DR KEGG; mmu:171180; -.
DR UCSC; uc008gad.1; mouse.
DR CTD; 91683; -.
DR MGI; MGI:2159601; Syt12.
DR VEuPathDB; HostDB:ENSMUSG00000049303; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158627; -.
DR HOGENOM; CLU_053862_0_0_1; -.
DR InParanoid; Q920N7; -.
DR OMA; LQPFGGW; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q920N7; -.
DR TreeFam; TF315600; -.
DR BioGRID-ORCS; 171180; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Syt12; mouse.
DR PRO; PR:Q920N7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q920N7; protein.
DR Bgee; ENSMUSG00000049303; Expressed in lumbar subsegment of spinal cord and 74 other tissues.
DR ExpressionAtlas; Q920N7; baseline and differential.
DR Genevisible; Q920N7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IEA:InterPro.
DR GO; GO:0048792; P:spontaneous exocytosis of neurotransmitter; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR030537; SYT12.
DR PANTHER; PTHR10024:SF252; PTHR10024:SF252; 1.
DR Pfam; PF00168; C2; 2.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Synaptotagmin-12"
FT /id="PRO_0000183973"
FT TOPO_DOM 1..18
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 152..272
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 283..416
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 97
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:23739973"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97610"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 97
FT /note="S->A: Loss of phosphorylation by PKA. Reduces long-
FT term potentiation in mossy-fiber synapses in the
FT hippocampus but has no effect on short-term potentiation.
FT Inhibits the effect of forskolin on synaptic transmission
FT and inhibitory post-synaptic currents. No effect on
FT excitatory and inhibitory synaptic transmission in the
FT hippocampus. No effect on brain structure."
FT /evidence="ECO:0000269|PubMed:23739973"
SQ SEQUENCE 421 AA; 46680 MW; 4E854C7B2089597C CRC64;
MAVDVTEYHL SVIKSPPGWE VGVYAAGALA LLGIAAVSLW KLWTSGSFPS PSPFPNYDYR
YLQQKYGEAY VEAKLKRVPP WNDQRTTTRG PPSRKGSLSI EDTFESISEL GPLELMGREL
DLAPYGTLRK SQSADSLNSI SSVSNTFGQD FTLGQVEVSM DYDGASHTLH VAVLQGKDLL
EREEATFESC FMRVSLLPDE QIVGISRIQR NAYSIFFDEK FSVPLDPTAL EEKSLRFSVF
GIDEDERNVS TGVVELKLSV LDLPLQPFSG WLYLQDQNKA ADAVGEILLS LSYLPTAERL
TVVVVKAKNL IWTNEKSTAD PFVKVYLLQD GRKMSKKKTA VKRDDPNPVF NEAMIFSVPA
IVLQDLSLRV TVAESSSDGR GDNVGHVIIG PGVSGMGTTH WNQMLATLRR PVSMWHPVRR
N
