SYDE1_MOUSE
ID SYDE1_MOUSE Reviewed; 737 AA.
AC Q9DBZ9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 29-SEP-2021, entry version 108.
DE RecName: Full=Rho GTPase-activating protein SYDE1;
DE AltName: Full=Synapse defective protein 1 homolog 1;
DE Short=Protein syd-1 homolog 1;
GN Name=Syde1;
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; TISSUE=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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-683 AND SER-685, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, 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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=27917469; DOI=10.1002/path.4835;
RA Lo H.F., Tsai C.Y., Chen C.P., Wang L.J., Lee Y.S., Chen C.Y., Liang C.T.,
RA Cheong M.L., Chen H.;
RT "Association of dysfunctional synapse defective 1 (SYDE1) with restricted
RT fetal growth - SYDE1 regulates placental cell migration and invasion.";
RL J. Pathol. 241:324-336(2017).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases. As a GCM1
CC downstream effector, it is involved in placental development and
CC positively regulates trophoblast cells migration. It regulates
CC cytoskeletal remodeling by controlling the activity of Rho GTPases
CC including RHOA, CDC42 and RAC1. {ECO:0000250|UniProtKB:Q6ZW31}.
CC -!- PTM: Palmitoylated. Probably palmitoylated by ZDHHC3 and ZDHHC7.
CC {ECO:0000250|UniProtKB:D3ZZN9}.
CC -!- DISRUPTION PHENOTYPE: SYDE1 knockout results in small fetuses and
CC aberrant phenotypes in the placental-yolk sac barrier, maternal-
CC trophoblast interface, and placental vascularization. Placental
CC abnormalities include cystic dysplasia and apoptosis in the
CC spongiotrophoblast layer, decreased or absent vascularization in the
CC labyrinthine layer, defective barrier between fetal and maternal blood
CC circulation, and reduced invasiveness of primary trophoblast cells.
CC {ECO:0000269|PubMed:27917469}.
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DR EMBL; AK004654; BAB23445.1; -; mRNA.
DR CCDS; CCDS48613.1; -.
DR IntAct; Q9DBZ9; 1.
DR STRING; 10090.ENSMUSP00000043085; -.
DR iPTMnet; Q9DBZ9; -.
DR PhosphoSitePlus; Q9DBZ9; -.
DR SwissPalm; Q9DBZ9; -.
DR jPOST; Q9DBZ9; -.
DR MaxQB; Q9DBZ9; -.
DR PaxDb; Q9DBZ9; -.
DR PRIDE; Q9DBZ9; -.
DR ProteomicsDB; 257516; -.
DR MGI; MGI:1918959; Syde1.
DR eggNOG; KOG1452; Eukaryota.
DR eggNOG; KOG4271; Eukaryota.
DR InParanoid; Q9DBZ9; -.
DR PhylomeDB; Q9DBZ9; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR PRO; PR:Q9DBZ9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9DBZ9; protein.
DR GO; GO:0044300; C:cerebellar mossy fiber; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0097060; C:synaptic membrane; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0030695; F:GTPase regulator activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR GO; GO:0060711; P:labyrinthine layer development; IMP:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:MGI.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISS:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016081; P:synaptic vesicle docking; IMP:MGI.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:MGI.
DR DisProt; DP01541; -.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Lipoprotein; Palmitate; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..737
FT /note="Rho GTPase-activating protein SYDE1"
FT /id="PRO_0000312159"
FT DOMAIN 249..366
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 398..604
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..697
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZW31"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZW31"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZW31"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZW31"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 737 AA; 80496 MW; 929D6191D05339A1 CRC64;
MAEPLLRKTF SRLRGREKLP RKKSEAKDRG HPAQRSEPKP PEPEPRVLEG SQAGAEVPPS
PETPRSPTRG AYLQSLEPSS RRWVLGGAKP PEEISLGPRT PSSGEPAGEI WYNPIPEEDP
RPPAPEPLGS QLASSEPEGP NIQGAAPTSP PTKTSRTKSP GPARRLSMKM KKLPELRRRL
SLRSTRTGRD RERTAPAGSV ISRYRLDSSV GTPGQASVAG GSRSPRGGYL SDGDSPERPG
GPPSPTAFRP YEVGPSARTP PAALWGRLSL HLYGLGGLRP SPGATPRDLC CLLQVDGVAR
ARTGPLRSGP DFLRLDHTFH LELEAARLLR ALVLAWDPGV RRHRPCAQGT VLLPTIFRGC
QAQQLAVRLE PQGFLYAKLT LSEQQEAPAT AEPRVFGLPL QLLVEREQSP GQVPLIIRKC
VGQIECRGLR VVGLYRLCGS AAVKKELRDA FEQDSAAVCL SEDVYPDINV ITGILKDYLR
ELPTPLITQP LYQVVLEAMA QGHPSRASLG PEGTRGLLRC LPDVERATLT LLLDHLRLVS
SFHTHNRMTP QNXAVCFGPV LLPARQTPSR PRLRSSGPGV TSAVDFKRHI EVLHYLLQSW
PDTRRPSDTP DGAVAPYLRP KRQPPLHLPL AGPEVVTRPR GRGGPESPPS NRYAGDWSVC
GGDLLPCGRD FLSGPDYDHV TGSDSEEDDD ETGEPRGTTD FEDEFDAPFN PHLNLKDFDA
LILDLERELS KQINVCL
