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   24-JAN-2024, entry version 137.
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,
RC   and 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; 5.
DR   STRING; 10090.ENSMUSP00000090510; -.
DR   GlyGen; Q5SV85; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q5SV85; -.
DR   PhosphoSitePlus; Q5SV85; -.
DR   EPD; Q5SV85; -.
DR   jPOST; Q5SV85; -.
DR   MaxQB; Q5SV85; -.
DR   PaxDb; 10090-ENSMUSP00000059000; -.
DR   PeptideAtlas; Q5SV85; -.
DR   ProteomicsDB; 254741; -. [Q5SV85-1]
DR   ProteomicsDB; 254742; -. [Q5SV85-2]
DR   Pumba; Q5SV85; -.
DR   Antibodypedia; 74878; 37 antibodies from 12 providers.
DR   DNASU; 217030; -.
DR   Ensembl; ENSMUST00000049714.15; ENSMUSP00000059000.9; ENSMUSG00000034940.16. [Q5SV85-1]
DR   Ensembl; ENSMUST00000092834.12; ENSMUSP00000090510.6; ENSMUSG00000034940.16. [Q5SV85-2]
DR   GeneID; 217030; -.
DR   KEGG; mmu:217030; -.
DR   UCSC; uc007kqa.3; mouse. [Q5SV85-2]
DR   AGR; MGI:1354742; -.
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; 2878149at2759; -.
DR   PhylomeDB; Q5SV85; -.
DR   TreeFam; TF316700; -.
DR   BioGRID-ORCS; 217030; 3 hits in 78 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 220 other cell types or tissues.
DR   ExpressionAtlas; Q5SV85; baseline and differential.
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   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR000261; EH_dom.
DR   InterPro; IPR039656; SYNRG.
DR   PANTHER; PTHR15463; AP1 GAMMA SUBUNIT BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR15463:SF2; SYNERGIN GAMMA; 1.
DR   SMART; SM00027; EH; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50031; EH; 1.
DR   Genevisible; Q5SV85; MM.
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
//