SYNRG_MOUSE
ID SYNRG_MOUSE Reviewed; 1306 AA.
AC Q5SV85; Q5SV84; Q6PHT6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Synergin gamma;
DE AltName: Full=AP1 subunit gamma-binding protein 1;
DE AltName: Full=Gamma-synergin;
GN Name=Synrg; Synonyms=Ap1gbp1, Syng;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=12808037; DOI=10.1091/mbc.e02-11-0735;
RA Lui W.W.Y., Collins B.M., Hirst J., Motley A., Millar C., Schu P.,
RA Owen D.J., Robinson M.S.;
RT "Binding partners for the COOH-terminal appendage domains of the GGAs and
RT gamma-adaptin.";
RL Mol. Biol. Cell 14:2385-2398(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-744; SER-974 AND
RP SER-1067, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-509, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Plays a role in endocytosis and/or membrane trafficking at
CC the trans-Golgi network (TGN) (By similarity). May act by linking the
CC adapter protein complex AP-1 to other proteins (By similarity).
CC Component of clathrin-coated vesicles (By similarity). Component of the
CC aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-
CC 1-mediated protein trafficking including the trafficking of transferrin
CC from early to recycling endosomes, and the membrane trafficking of
CC furin and the lysosomal enzyme cathepsin D between the trans-Golgi
CC network (TGN) and endosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q9UMZ2}.
CC -!- SUBUNIT: Self-associates (By similarity). Interacts with GGA1 (via GAE
CC domain) (By similarity). Interacts with GGA2 and GGA3 (By similarity).
CC Interacts with AP1G1 (via GAE domain), a subunit of adapter protein
CC complex AP-1 (By similarity). Interacts with AP1G2 (via GAE domain) a
CC subunit of adapter protein complex AP-1 (By similarity). Component of
CC the aftiphilin/p200/gamma-synergin complex, at least composed of
CC AFTPH/aftiphilin, HEATR5B/p200a and SYNRG/gamma-synergin, which plays a
CC role in the AP1G1/AP-1-mediated trafficking of transferrin from early
CC to recycling endosomes (By similarity). Within the complex interacts
CC with AFTPH/aftiphilin and HEATR5B/p200a; the interactions are direct
CC (By similarity). Interacts (via EH domain) with SCAMP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JKC9, ECO:0000250|UniProtKB:Q9UMZ2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12808037}.
CC Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:12808037}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12808037}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9UMZ2}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q9UMZ2}. Note=Localization at clathrin-
CC coated vesicles depends on AFTPH/aftiphilin (By similarity). Associates
CC with membranes via the adapter protein complex AP-1 (By similarity).
CC Colocalizes with AP1G1 (By similarity). {ECO:0000250|UniProtKB:Q9JKC9,
CC ECO:0000250|UniProtKB:Q9UMZ2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SV85-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SV85-2; Sequence=VSP_013251, VSP_013252, VSP_013253,
CC VSP_013254;
CC -!- DOMAIN: The DFXDF motifs mediate the interaction with gamma-appendage
CC subunits AP1G1 and AP1G2. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI25511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL645615; CAI25509.1; -; Genomic_DNA.
DR EMBL; AL645615; CAI25510.1; -; Genomic_DNA.
DR EMBL; AL645615; CAI25511.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC056370; AAH56370.1; -; mRNA.
DR CCDS; CCDS25181.1; -. [Q5SV85-2]
DR RefSeq; NP_919322.1; NM_194341.2. [Q5SV85-2]
DR AlphaFoldDB; Q5SV85; -.
DR SMR; Q5SV85; -.
DR BioGRID; 229834; 3.
DR STRING; 10090.ENSMUSP00000059000; -.
DR iPTMnet; Q5SV85; -.
DR PhosphoSitePlus; Q5SV85; -.
DR EPD; Q5SV85; -.
DR jPOST; Q5SV85; -.
DR MaxQB; Q5SV85; -.
DR PaxDb; Q5SV85; -.
DR PeptideAtlas; Q5SV85; -.
DR PRIDE; Q5SV85; -.
DR ProteomicsDB; 254741; -. [Q5SV85-1]
DR ProteomicsDB; 254742; -. [Q5SV85-2]
DR Antibodypedia; 74878; 35 antibodies from 11 providers.
DR DNASU; 217030; -.
DR Ensembl; ENSMUST00000049714; ENSMUSP00000059000; ENSMUSG00000034940. [Q5SV85-1]
DR Ensembl; ENSMUST00000092834; ENSMUSP00000090510; ENSMUSG00000034940. [Q5SV85-2]
DR GeneID; 217030; -.
DR KEGG; mmu:217030; -.
DR UCSC; uc007kqa.3; mouse. [Q5SV85-2]
DR CTD; 11276; -.
DR MGI; MGI:1354742; Synrg.
DR VEuPathDB; HostDB:ENSMUSG00000034940; -.
DR eggNOG; KOG0998; Eukaryota.
DR GeneTree; ENSGT00390000010789; -.
DR HOGENOM; CLU_263817_0_0_1; -.
DR InParanoid; Q5SV85; -.
DR OrthoDB; 226328at2759; -.
DR PhylomeDB; Q5SV85; -.
DR TreeFam; TF316700; -.
DR BioGRID-ORCS; 217030; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Synrg; mouse.
DR PRO; PR:Q5SV85; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SV85; protein.
DR Bgee; ENSMUSG00000034940; Expressed in animal zygote and 218 other tissues.
DR ExpressionAtlas; Q5SV85; baseline and differential.
DR Genevisible; Q5SV85; MM.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR039656; SYNRG.
DR PANTHER; PTHR15463; PTHR15463; 1.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50031; EH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endocytosis; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1306
FT /note="Synergin gamma"
FT /id="PRO_0000072388"
FT DOMAIN 293..404
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT REGION 176..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..778
FT /note="Interaction with AP1G1"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT REGION 559..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..673
FT /note="Interaction with AP1G1, AP1G2 and GGA1"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT REGION 697..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 113..153
FT /evidence="ECO:0000255"
FT MOTIF 455..459
FT /note="DFXDF motif 1"
FT MOTIF 685..689
FT /note="DFXDF motif 2"
FT MOTIF 767..771
FT /note="DFXDF motif 3"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 509
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 736
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKC9"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 1092
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT VAR_SEQ 38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013251"
FT VAR_SEQ 195..272
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013252"
FT VAR_SEQ 862..938
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013253"
FT VAR_SEQ 1252..1263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013254"
SQ SEQUENCE 1306 AA; 139616 MW; EB149A0B7ADAE2D7 CRC64;
MALRPGAGAS GAAGAGAGPG GAGSFMFPVA GGMRPPQAGL IPMQQQGFPM VSVMQPNMQG
MMGMNYSSQM SQGPIAMQAG IPMGPMPAAG VPFLGQPPFL SMRPAGPQYT PDMQKQFAEE
QQKRFEQQQK LLEEERKRRQ FEEQKQKLRL LSSVKPKTGE KNRDDALEAI KGNLDGFSRD
AKMHPTPASH PKKQGPSLEE KLLVSCDVSA SGQEHIKLNT PDAGHKAIVP GSSKNCPGLM
AHNRGAVDGC VSGPASAEAE KTSDQTLSKE ESGVGVFPSQ DPAQSRMPPW IYNESLVPDA
YKKILETTMT PTGIDTAKLY PILMSSGLPR ETLGQIWALA NRTTPGRLTK EELYTVLAMV
AVTQRGVPAM SPDALSQFPA APIPTLSGFP MTLPTPVSQP TAMPSGPTGS MPLTLGQPIM
GINLVGPVGG AAAPTSSGFM PAYPSNQVGK TEEDDFQDFQ DASKSGSIDD SFTDFQEMPA
SSKTSNSQHG NSAPSLLIPF PGTKASTDKY AVFKGISTDK PSENPASFGE SGDKYSAFRE
LEQTTDSKPL GESFAEFRST GTDDGFTDFK TADSVSPLEP PTKDTFPSAF ASGAAQQTQT
QVKTPLNLED LDMFSSVDCS GEKQVPFSAT FSTAKSVSTR PQPAGSAAAS AALASTKTSS
LADDFGEFNL FGEYSNPASA GEQDDFADFM AFGNSSISSE PKASDKYEAL REEVSPSPLS
SSTVEGAQHP PAAATKYDVF KQLSLEGAGL AMEEFKENTS STKSEDDFAD FHSSKFSSTS
SDKSLGEKAV AFRHAKEDSS SVKSLDLPSI GGSSVGKEDS EDALSVQFDM KLADVGGDLK
HVMSDSSLDL PTVSGQHPPA ADTEDLSCAA FGSCSSHFTV STLTSCEWSD RADALQGRKL
SPFVLSAGSR SFSATSNLHT KEISFGSSEN ITMSSLSKGS ALASEDALPE TAFPAFASFK
DMMPQTTEQK EFESGDFQDF TRQDMPTVDR SQETSCPSPA SSVASHETPK EGADDFGEFQ
SEKSKISKFD FLVANSQSKM KSSEEMIKSE LATFDLSVQG SHKRSLSLGD KEISRSSPSP
ALEQPFRDRS NTLSERAALP VIRDKYKDLT GEVEENERYA YEWQRCLGSA LDVIKKANDT
LNGISSSAVC TEVIQSAQGM EYLLGVVEVY RVTKRVELGI KATAVCSEKL QQLLKDIDKV
WNNLIGFMSL ATLTPDENSL DFSSCMLRPG IKNAQELACG VCLLNVDSRS RKEETPAEEQ
PKKAFNSETD SFKLAYGGHQ YHASCANFWI NCVEPKPPGL LLPDLL
