GSG1L_HUMAN
ID GSG1L_HUMAN Reviewed; 331 AA.
AC Q6UXU4; Q7Z6F8; Q8TB81;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Germ cell-specific gene 1-like protein;
DE Short=GSG1-like protein;
GN Name=GSG1L; ORFNames=UNQ5831/PRO19651;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Li H., Li S., Zhou G., Shen C., Li M., Xiao W., Lin L., Yang S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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).
CC -!- FUNCTION: As a component of the inner core of AMPAR complex, modifies
CC AMPA receptor (AMPAR) gating. {ECO:0000250}.
CC -!- SUBUNIT: Component of the inner core of AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents. Alone or in combination, these auxiliary
CC subunits control the gating and pharmacology of the AMPAR complex and
CC profoundly impact their biogenesis and protein processing (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6UXU4; Q9BS40: LXN; NbExp=3; IntAct=EBI-10297401, EBI-1044504;
CC Q6UXU4-2; P21145: MAL; NbExp=3; IntAct=EBI-18632127, EBI-3932027;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6UXU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UXU4-3; Sequence=VSP_033004;
CC Name=3;
CC IsoId=Q6UXU4-4; Sequence=VSP_033516, VSP_033517;
CC Name=4;
CC IsoId=Q6UXU4-2; Sequence=VSP_033516;
CC -!- SIMILARITY: Belongs to the GSG1 family. {ECO:0000305}.
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DR EMBL; AY358206; AAQ88573.1; -; mRNA.
DR EMBL; AY302134; AAP57626.1; -; mRNA.
DR EMBL; AC008732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471145; EAW55740.1; -; Genomic_DNA.
DR EMBL; BC016460; AAH16460.1; -; mRNA.
DR CCDS; CCDS10631.1; -. [Q6UXU4-2]
DR CCDS; CCDS45450.1; -. [Q6UXU4-1]
DR CCDS; CCDS81960.1; -. [Q6UXU4-3]
DR RefSeq; NP_001103233.1; NM_001109763.1. [Q6UXU4-1]
DR RefSeq; NP_001310830.1; NM_001323901.1. [Q6UXU4-3]
DR RefSeq; NP_653276.1; NM_144675.2. [Q6UXU4-2]
DR AlphaFoldDB; Q6UXU4; -.
DR SMR; Q6UXU4; -.
DR BioGRID; 126983; 2.
DR IntAct; Q6UXU4; 2.
DR STRING; 9606.ENSP00000394954; -.
DR TCDB; 8.A.16.5.3; the ca(+) channel auxiliary subunit Gama1-Gama8 (ccaGama) family.
DR iPTMnet; Q6UXU4; -.
DR PhosphoSitePlus; Q6UXU4; -.
DR BioMuta; GSG1L; -.
DR DMDM; 187471161; -.
DR MassIVE; Q6UXU4; -.
DR PaxDb; Q6UXU4; -.
DR PeptideAtlas; Q6UXU4; -.
DR PRIDE; Q6UXU4; -.
DR ProteomicsDB; 67660; -. [Q6UXU4-1]
DR ProteomicsDB; 67661; -. [Q6UXU4-2]
DR ProteomicsDB; 67662; -. [Q6UXU4-3]
DR ProteomicsDB; 67663; -. [Q6UXU4-4]
DR Antibodypedia; 3053; 96 antibodies from 19 providers.
DR DNASU; 146395; -.
DR Ensembl; ENST00000380897.7; ENSP00000370282.3; ENSG00000169181.13. [Q6UXU4-2]
DR Ensembl; ENST00000395724.7; ENSP00000379074.3; ENSG00000169181.13. [Q6UXU4-3]
DR Ensembl; ENST00000447459.7; ENSP00000394954.2; ENSG00000169181.13. [Q6UXU4-1]
DR Ensembl; ENST00000569166.1; ENSP00000454880.1; ENSG00000169181.13. [Q6UXU4-4]
DR GeneID; 146395; -.
DR KEGG; hsa:146395; -.
DR MANE-Select; ENST00000447459.7; ENSP00000394954.2; NM_001109763.2; NP_001103233.1.
DR UCSC; uc002doy.3; human. [Q6UXU4-1]
DR CTD; 146395; -.
DR DisGeNET; 146395; -.
DR GeneCards; GSG1L; -.
DR HGNC; HGNC:28283; GSG1L.
DR HPA; ENSG00000169181; Group enriched (brain, heart muscle).
DR neXtProt; NX_Q6UXU4; -.
DR OpenTargets; ENSG00000169181; -.
DR PharmGKB; PA145148734; -.
DR VEuPathDB; HostDB:ENSG00000169181; -.
DR eggNOG; ENOG502QRSH; Eukaryota.
DR GeneTree; ENSGT01050000244814; -.
DR HOGENOM; CLU_063057_0_0_1; -.
DR InParanoid; Q6UXU4; -.
DR OMA; REPWESD; -.
DR OrthoDB; 957556at2759; -.
DR PhylomeDB; Q6UXU4; -.
DR TreeFam; TF331388; -.
DR PathwayCommons; Q6UXU4; -.
DR SignaLink; Q6UXU4; -.
DR BioGRID-ORCS; 146395; 7 hits in 1056 CRISPR screens.
DR ChiTaRS; GSG1L; human.
DR GenomeRNAi; 146395; -.
DR Pharos; Q6UXU4; Tbio.
DR PRO; PR:Q6UXU4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6UXU4; protein.
DR Bgee; ENSG00000169181; Expressed in sural nerve and 114 other tissues.
DR ExpressionAtlas; Q6UXU4; baseline and differential.
DR Genevisible; Q6UXU4; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IBA:GO_Central.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR InterPro; IPR012478; GSG-1.
DR Pfam; PF07803; GSG-1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..331
FT /note="Germ cell-specific gene 1-like protein"
FT /id="PRO_0000329464"
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..132
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..155
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_033516"
FT VAR_SEQ 133..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_033004"
FT VAR_SEQ 277
FT /note="R -> RWQIEAQRGRATCPRSHSW (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_033517"
SQ SEQUENCE 331 AA; 36774 MW; 7CAC097C9DF7FBCB CRC64;
MKTSRRGRAL LAVALNLLAL LFATTAFLTT HWCQGTQRVP KPGCGQGGRA NCPNSGANAT
ANGTAAPAAA AAAATASGNG PPGGALYSWE TGDDRFLFRN FHTGIWYSCE EELSGLGEKC
RSFIDLAPAS EKGVLWLSVV SEVLYILLLV VGFSLMCLEL FHSSNVIDGL KLNAFAAVFT
VLSGLLGMVA HMMYTQVFQV TVSLGPEDWR PHSWDYGWSF CLAWGSFTCC MAASVTTLNS
YTKTVIEFRH KRKVFEQGYR EEPTFIDPEA IKYFRERMEK RDGSEEDFHL DCRHERYPAR
HQPHMADSWP RSSAQEAPEL NRQCWVLGHW V
