GSG1L_RAT
ID GSG1L_RAT Reviewed; 322 AA.
AC D3ZK93;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Germ cell-specific gene 1-like protein;
DE Short=GSG1-like protein;
GN Name=Gsg1l;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, 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 [3]
RP FUNCTION, IDENTIFICATION IN AMPAR COMPLEX, TOPOLOGY, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
CC -!- FUNCTION: As a component of the inner core of AMPAR complexes, modifies
CC AMPA receptor (AMPAR) gating. {ECO:0000269|PubMed:22632720}.
CC -!- SUBUNIT: Component of the inner core of AMPAR complexes. AMPAR
CC complexes consist of an inner core made of 4 pore-forming GluA/GRIA
CC proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits
CC arranged in a twofold symmetry. One of the two pairs of distinct
CC binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The
CC other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core
CC of AMPAR complexes is complemented by outer core constituents binding
CC directly to the GluA/GRIA proteins at sites distinct from the
CC interaction sites of the inner core constituents. Outer core
CC constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and
CC NRN1. The proteins of the inner and outer core serve as a platform for
CC other, more peripherally associated AMPAR constituents. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complexes and profoundly impact their
CC biogenesis and protein processing. {ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22632720};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22632720}. Synapse
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:22632720}.
CC -!- SIMILARITY: Belongs to the GSG1 family. {ECO:0000305}.
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DR PDB; 5VHW; EM; 7.80 A; A/B/C/D=2-238.
DR PDB; 5VHX; EM; 8.30 A; A/B/C/D/E=2-238.
DR PDB; 5VHY; EM; 4.60 A; A/B/C/D/E/F=2-238.
DR PDB; 5VHZ; EM; 8.40 A; A/B/C/D/E/F=2-238.
DR PDBsum; 5VHW; -.
DR PDBsum; 5VHX; -.
DR PDBsum; 5VHY; -.
DR PDBsum; 5VHZ; -.
DR AlphaFoldDB; D3ZK93; -.
DR SMR; D3ZK93; -.
DR CORUM; D3ZK93; -.
DR STRING; 10116.ENSRNOP00000022392; -.
DR iPTMnet; D3ZK93; -.
DR PhosphoSitePlus; D3ZK93; -.
DR PaxDb; D3ZK93; -.
DR PRIDE; D3ZK93; -.
DR Ensembl; ENSRNOT00000108837; ENSRNOP00000081015; ENSRNOG00000065255.
DR UCSC; RGD:1562278; rat.
DR RGD; 1562278; Gsg1l.
DR eggNOG; ENOG502QRSH; Eukaryota.
DR GeneTree; ENSGT01050000244814; -.
DR InParanoid; D3ZK93; -.
DR PhylomeDB; D3ZK93; -.
DR TreeFam; TF331388; -.
DR PRO; PR:D3ZK93; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:SynGO.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IC:SynGO.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR InterPro; IPR012478; GSG-1.
DR Pfam; PF07803; GSG-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..322
FT /note="Germ cell-specific gene 1-like protein"
FT /id="PRO_0000420685"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 322 AA; 35903 MW; 30388DA6545A5EA1 CRC64;
MKTSRRGRAL LAVALNLLAL LFATTAFLTT YWCQGTQRVP KPGCGQGGGA NCPNSGANAT
ANSTAAPVAA SPAGAPYSWE AGDERFQLRR FHTGIWYSCE EELGGPGEKC RSFIDLAPAS
EKGVLWLSVV SEVLYILLLV VGFSLMCLEL LHSSSVIDGL KLNAFAAVFT VLSGLLGMVA
HMMYTQVFQV TVSLGPEDWR PHSWDYGWSF CLAWGSFTCC MAASVTTLNS YTKTVIEFRH
KRKVFEQGYR EEPTFIDPEA IKYFRERIEK GDVSEEEDFR LACRHERYPT RHQPHMGDSW
PRSSAHEAAE LNRQCWVLGH WV
