SYDE1_RAT
ID SYDE1_RAT Reviewed; 735 AA.
AC D3ZZN9;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP PALMITOYLATION.
RX PubMed=23687301; DOI=10.1074/jbc.m112.431676;
RA Oku S., Takahashi N., Fukata Y., Fukata M.;
RT "In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10
RT (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to
RT Rab5-positive endosomes.";
RL J. Biol. Chem. 288:19816-19829(2013).
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 (PubMed:23687301). Probably palmitoylated by ZDHHC3
CC and ZDHHC7 (PubMed:23687301). {ECO:0000269|PubMed:23687301}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR07055860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178805.1; NM_001191876.1.
DR AlphaFoldDB; D3ZZN9; -.
DR SMR; D3ZZN9; -.
DR STRING; 10116.ENSRNOP00000009606; -.
DR iPTMnet; D3ZZN9; -.
DR PhosphoSitePlus; D3ZZN9; -.
DR PaxDb; D3ZZN9; -.
DR PeptideAtlas; D3ZZN9; -.
DR Ensembl; ENSRNOT00000009606; ENSRNOP00000009606; ENSRNOG00000007307.
DR GeneID; 362842; -.
DR KEGG; rno:362842; -.
DR UCSC; RGD:1305857; rat.
DR CTD; 85360; -.
DR RGD; 1305857; Syde1.
DR eggNOG; KOG1452; Eukaryota.
DR eggNOG; KOG4271; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_005764_1_1_1; -.
DR InParanoid; D3ZZN9; -.
DR OMA; FLQLDHT; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; D3ZZN9; -.
DR TreeFam; TF323458; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:D3ZZN9; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007307; Expressed in heart and 18 other tissues.
DR Genevisible; D3ZZN9; RN.
DR GO; GO:0044300; C:cerebellar mossy fiber; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0030695; F:GTPase regulator activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
DR GO; GO:0060711; P:labyrinthine layer development; ISO:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:RGD.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISO:RGD.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:RGD.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016081; P:synaptic vesicle docking; ISO:RGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISO:RGD.
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..735
FT /note="Rho GTPase-activating protein SYDE1"
FT /id="PRO_0000449472"
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..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..706
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 147..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 680..695
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:0000250|UniProtKB:Q6ZW31"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZW31"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBZ9"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZW31"
SQ SEQUENCE 735 AA; 80378 MW; B2663DF22DBD0F2E CRC64;
MAEPLLRKTF SRLRGREKLP RKKSDAKDRG RPAQRSEPKP PEPEPRVLEG SQAGAEVPLS
PETPRSPARG AYLQSLEPSS RRWVLGGAKP PEEISLGPRT PSSGEPAGEI WYNPIPEEDP
RPPAPEPVGS QLASSEPEGP ILQGAAPTSP PTKTSRTKSP GPARRLSMKM KKLPELRRRL
SLRSTRTSRE RERTAPAGSV ISRYHLDSSV ATPGQASVAG GTRSPRGGYL SDGDSPERPG
GPPSPTAFRP YEVGPSARAP PAALWGRLSL HLYGLGGLRP TPGATPRDLC CLLQVDGVAR
ARTGPLRSGP DFLRLDHTFH LELEAARLLR ALVLAWDPGV RRHRPCAQGT VLLPTIFRGC
QAQQLAVRLE PQGLLYAKLT LSEQQEAPAT VEPRVFGLPL QLLVEREQSP GQVPLIIRKC
VGQIECRGLR VVGLYRLCGS AAVKKELRDA FEQDSAAVCL SEDVYPDINV ITGILKDYLR
ELPTPLITQP LYQVVLEAMA QGHPSRASLG PEGTRGLLSC LPDVERATLT LLLDHLRLVS
SFHTHNRMTP QNLAVCFGPV LLPARQTPSR TRLRGSGPGV SSAVDFKRHI EVLHYLLQSW
PDTRRPSETP DVAPYLRPKR QPPLHLPLDG PEVVTRPRGR GGPESPPSNR YAGDWSVCGG
DLLPRGRDFL SGPDYDHVTG SDSEEDEDES GEPRGTTDFE DEFDAPFNPH LNLKDFDALI
LDLERELSKQ INVCL
