SYAP1_MOUSE
ID SYAP1_MOUSE Reviewed; 365 AA.
AC Q9D5V6; Q3UI67; Q9D870;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Synapse-associated protein 1 {ECO:0000305};
DE AltName: Full=BSD domain-containing signal transducer and Akt interactor protein {ECO:0000250|UniProtKB:Q96A49};
DE Short=BSTA {ECO:0000250|UniProtKB:Q96A49};
GN Name=Syap1 {ECO:0000312|MGI:MGI:1914293};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Heart, Small intestine, Spinal ganglion, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262; SER-283 AND SER-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [5]
RP FUNCTION, INTERACTION WITH AKT1, PHOSPHORYLATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=23300339; DOI=10.1126/scisignal.2003295;
RA Yao Y., Suraokar M., Darnay B.G., Hollier B.G., Shaiken T.E., Asano T.,
RA Chen C.H., Chang B.H., Lu Y., Mills G.B., Sarbassov D., Mani S.A.,
RA Abbruzzese J.L., Reddy S.A.;
RT "BSTA promotes mTORC2-mediated phosphorylation of Akt1 to suppress
RT expression of FoxC2 and stimulate adipocyte differentiation.";
RL Sci. Signal. 6:RA2-RA2(2013).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27344443; DOI=10.1007/s00418-016-1457-0;
RA Schmitt D., Funk N., Blum R., Asan E., Andersen L., Ruelicke T.,
RA Sendtner M., Buchner E.;
RT "Initial characterization of a Syap1 knock-out mouse and distribution of
RT Syap1 in mouse brain and cultured motoneurons.";
RL Histochem. Cell Biol. 146:489-512(2016).
CC -!- FUNCTION: Plays a role in adipocyte differentiation by promoting
CC mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth
CC factor stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
CC -!- SUBUNIT: Interacts (via phosphorylated form and BSD domain) with AKT1;
CC this interaction is enhanced in a mTORC2-mediated manner in response to
CC epidermal growth factor (EGF) stimulation and activates AKT1
CC (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:27344443}. Golgi apparatus
CC {ECO:0000269|PubMed:27344443}. Perikaryon
CC {ECO:0000269|PubMed:27344443}. Cell projection, axon
CC {ECO:0000269|PubMed:27344443}. Cell projection, dendrite
CC {ECO:0000269|PubMed:27344443}. Cell projection, growth cone
CC {ECO:0000269|PubMed:27344443}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:27344443}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:27344443}. Membrane {ECO:0000250|UniProtKB:Q96A49}.
CC Note=Localizes to cholinergic neuromuscular junctions and in actin-rich
CC growth cone regions (PubMed:27344443). Membrane-associated in a
CC epidermal growth factor (EGF)-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q96A49, ECO:0000269|PubMed:27344443}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver, kidney, skeletal muscle and
CC in white and brown adipose tissues (PubMed:23300339, PubMed:27344443).
CC Expressed in the cortex, cerebellum, thalamus, hippocampus, braistem,
CC olfactory bulb, spinal cord and striatum of the brain
CC (PubMed:27344443). Expressed in most neuropil regions containing
CC glutamatergic synaptic terminals (PubMed:27344443). Expressed in the
CC CA1, CA2 and CA3 perikarya of the hippocampus (PubMed:27344443).
CC Expressed in neurons and Purkinje cells (at the protein level)
CC (PubMed:27344443). {ECO:0000269|PubMed:23300339,
CC ECO:0000269|PubMed:27344443}.
CC -!- INDUCTION: Up-regulated during adipocyte differentiation (at protein
CC level) (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
CC -!- PTM: Phosphorylated (PubMed:23300339). Phosphorylation increases in a
CC mTORC2-mediated manner in response to epidermal growth factor (EGF)
CC stimulation (PubMed:23300339). {ECO:0000269|PubMed:23300339}.
CC -!- DISRUPTION PHENOTYPE: Mice appear normal and healthy (PubMed:27344443).
CC Display no alteration on the survival or axonal elongation in primary
CC embryonic motoneurons (PubMed:27344443). Show no alteration in total
CC AKT phosphorylation in primary embryonic motoneurons (PubMed:27344443).
CC {ECO:0000269|PubMed:27344443}.
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DR EMBL; AK008390; BAB25643.1; -; mRNA.
DR EMBL; AK014893; BAB29608.1; -; mRNA.
DR EMBL; AK051251; BAC34575.1; -; mRNA.
DR EMBL; AK147055; BAE27639.1; -; mRNA.
DR EMBL; BC021373; AAH21373.1; -; mRNA.
DR CCDS; CCDS30511.1; -.
DR RefSeq; NP_080208.2; NM_025932.2.
DR AlphaFoldDB; Q9D5V6; -.
DR SMR; Q9D5V6; -.
DR IntAct; Q9D5V6; 1.
DR MINT; Q9D5V6; -.
DR STRING; 10090.ENSMUSP00000033723; -.
DR iPTMnet; Q9D5V6; -.
DR PhosphoSitePlus; Q9D5V6; -.
DR REPRODUCTION-2DPAGE; IPI00317599; -.
DR EPD; Q9D5V6; -.
DR jPOST; Q9D5V6; -.
DR MaxQB; Q9D5V6; -.
DR PaxDb; Q9D5V6; -.
DR PeptideAtlas; Q9D5V6; -.
DR PRIDE; Q9D5V6; -.
DR ProteomicsDB; 258784; -.
DR Antibodypedia; 395; 130 antibodies from 25 providers.
DR DNASU; 67043; -.
DR Ensembl; ENSMUST00000033723; ENSMUSP00000033723; ENSMUSG00000031357.
DR GeneID; 67043; -.
DR KEGG; mmu:67043; -.
DR UCSC; uc009uun.2; mouse.
DR CTD; 94056; -.
DR MGI; MGI:1914293; Syap1.
DR VEuPathDB; HostDB:ENSMUSG00000031357; -.
DR eggNOG; KOG4310; Eukaryota.
DR GeneTree; ENSGT00390000007662; -.
DR HOGENOM; CLU_046184_1_1_1; -.
DR InParanoid; Q9D5V6; -.
DR OMA; FGSYLFN; -.
DR OrthoDB; 782515at2759; -.
DR PhylomeDB; Q9D5V6; -.
DR TreeFam; TF319666; -.
DR BioGRID-ORCS; 67043; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Syap1; mouse.
DR PRO; PR:Q9D5V6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D5V6; protein.
DR Bgee; ENSMUSG00000031357; Expressed in white adipose tissue and 246 other tissues.
DR Genevisible; Q9D5V6; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IBA:GO_Central.
DR GO; GO:0038203; P:TORC2 signaling; IMP:UniProtKB.
DR Gene3D; 1.10.3970.10; -; 1.
DR InterPro; IPR005607; BSD_dom.
DR InterPro; IPR035925; BSD_dom_sf.
DR Pfam; PF03909; BSD; 1.
DR SMART; SM00751; BSD; 1.
DR SUPFAM; SSF140383; SSF140383; 1.
DR PROSITE; PS50858; BSD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Differentiation;
KW Golgi apparatus; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Synapse.
FT CHAIN 1..365
FT /note="Synapse-associated protein 1"
FT /id="PRO_0000072356"
FT DOMAIN 172..224
FT /note="BSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96A49"
FT CONFLICT 243
FT /note="E -> K (in Ref. 1; BAB25643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 41350 MW; 7553E79C0C50E96B CRC64;
MFGGLSSWLG LKPPEGAAAE GEEPPSRDGD KLSAGAAPSE ESPERPVEPT EEQQQQPPTE
DPQFLHQAKG LGNYLYNFAS AATKKITESV TETAQTIKKS VEEGKIDDIL DKTILGDFQK
EQKKFVEEQN TKKSEAAVPP WVESHDEETI QQQILALSAD KRNFLRDPPA GVQFNFDFDQ
MYPVALVMLQ EDELLSKMRF ALVPKLVKEE VFWRNYFYRI SLIKQSAQLT ALAAQQQASG
KEEKSSNRDD NLPLTEAVRP KTPPVVIKSQ LKSQEDEEEI STSPGVSEFV SDAFDTCSLN
QEDLRKEMEQ LVLDKKQEEA TALEEDSTDW EKELQQELQE YEVVAESEKR DENWDKEIEK
MLQES
