SYNG1_RAT
ID SYNG1_RAT Reviewed; 258 AA.
AC Q58DZ9;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Synapse differentiation-inducing gene protein 1;
DE Short=SynDIG1;
DE AltName: Full=Dispanin subfamily C member 2;
DE Short=DSPC2;
DE AltName: Full=Transmembrane protein 90B;
GN Name=Syndig1; Synonyms=Tmem90b;
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 MRNA].
RC TISSUE=Brain;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=20152115; DOI=10.1016/j.neuron.2009.12.021;
RA Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B., Ishimaru T.,
RA Trimmer J.S., Mohapatra D.P., Diaz E.;
RT "SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane
RT protein that regulates excitatory synapse development.";
RL Neuron 65:80-93(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP 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 [4]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=26660156; DOI=10.1002/cne.23945;
RA Kirk L.M., Ti S.W., Bishop H.I., Orozco-Llamas M., Pham M., Trimmer J.S.,
RA Diaz E.;
RT "Distribution of the SynDIG4/proline-rich transmembrane protein 1 in rat
RT brain.";
RL J. Comp. Neurol. 524:2266-2280(2016).
CC -!- FUNCTION: May regulate AMPA receptor content at nascent synapses, and
CC have a role in postsynaptic development and maturation.
CC {ECO:0000269|PubMed:20152115}.
CC -!- SUBUNIT: Homodimer. Interacts with GRIA1 and GRIA2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20152115};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}.
CC Early endosome membrane {ECO:0000250}; Single-pass type II membrane
CC protein {ECO:0000250}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:26660156}. Synapse {ECO:0000269|PubMed:20152115}.
CC Cell projection, dendrite {ECO:0000269|PubMed:20152115}. Cell
CC projection, dendritic spine {ECO:0000269|PubMed:20152115}.
CC Note=Shuttles between the cell surface and early endosome membrane.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Enriched in the cerebellum and also expressed in
CC the neocortex and modestly in the hippocampus (at protein level)
CC (PubMed:26660156). Expressed in hippocampal neurons, both in cell body
CC and neurites, however its presence is enriched at excitatory synapses
CC and also found in postsynaptic cells (PubMed:20152115).
CC {ECO:0000269|PubMed:20152115, ECO:0000269|PubMed:26660156}.
CC -!- DEVELOPMENTAL STAGE: Expressed during synaptogenesis with levels
CC peaking during the second week of postnatal development
CC (PubMed:20152115). Expression increases between postnatal days 7 and 14
CC and remains high at postnatal day 21 and at 2 months of age
CC (PubMed:26660156). As development proceeds, an increasing percentage
CC becomes localized to excitatory synapses (PubMed:20152115).
CC {ECO:0000269|PubMed:20152115, ECO:0000269|PubMed:26660156}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; BC092131; AAH92131.1; -; mRNA.
DR RefSeq; NP_001020191.1; NM_001025020.1.
DR RefSeq; XP_017447401.1; XM_017591912.1.
DR RefSeq; XP_017447402.1; XM_017591913.1.
DR RefSeq; XP_017447403.1; XM_017591914.1.
DR RefSeq; XP_017447404.1; XM_017591915.1.
DR RefSeq; XP_017447405.1; XM_017591916.1.
DR RefSeq; XP_017447406.1; XM_017591917.1.
DR RefSeq; XP_017447407.1; XM_017591918.1.
DR RefSeq; XP_017447408.1; XM_017591919.1.
DR RefSeq; XP_017447409.1; XM_017591920.1.
DR RefSeq; XP_017447410.1; XM_017591921.1.
DR RefSeq; XP_017447411.1; XM_017591922.1.
DR AlphaFoldDB; Q58DZ9; -.
DR STRING; 10116.ENSRNOP00000060788; -.
DR iPTMnet; Q58DZ9; -.
DR PhosphoSitePlus; Q58DZ9; -.
DR PaxDb; Q58DZ9; -.
DR PRIDE; Q58DZ9; -.
DR ABCD; Q58DZ9; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000068210; ENSRNOP00000060788; ENSRNOG00000031536.
DR GeneID; 362235; -.
DR KEGG; rno:362235; -.
DR UCSC; RGD:1310753; rat.
DR CTD; 79953; -.
DR RGD; 1310753; Syndig1.
DR eggNOG; ENOG502QQXK; Eukaryota.
DR GeneTree; ENSGT00950000183147; -.
DR HOGENOM; CLU_094250_0_0_1; -.
DR InParanoid; Q58DZ9; -.
DR OMA; LGSECCE; -.
DR OrthoDB; 1273993at2759; -.
DR PhylomeDB; Q58DZ9; -.
DR TreeFam; TF331357; -.
DR PRO; PR:Q58DZ9; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000031536; Expressed in cerebellum and 14 other tissues.
DR Genevisible; Q58DZ9; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0035254; F:glutamate receptor binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:UniProtKB.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Endosome; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Signal-anchor; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..258
FT /note="Synapse differentiation-inducing gene protein 1"
FT /id="PRO_0000249458"
FT TOPO_DOM 1..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 258 AA; 28384 MW; EB0B7D2FC7FE0140 CRC64;
MDGIVEQKSV LVHSKIGDAG KRNGLINTRN FMAESRDGLV SVYPAPQYQS HRLVASAAPG
SLEGGRSDPV QQLLDPNTLQ QSVDSHYRPN IILYSDGVLR SWGDGVATDC CETTFIEDRS
PTKDSLEYPD GKFIDLSGDD IKIHTLSYDV EEEEELQELE SDYSSDTESE DNFLMMPPRD
HLGLSVFSML CCFWPLGIAA FYLSHETNKA VAKGDFHQAS TSSRRALFLA VLSITIGTGI
YVGVAVALIA YLSKNNHL
