SYNRG_RAT
ID SYNRG_RAT Reviewed; 1329 AA.
AC Q9JKC9; A1EC70; A1EC72; A1EC74; A1EC75; Q9R145;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
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 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 [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=Lewis;
RX PubMed=17218081; DOI=10.1016/j.ygeno.2006.12.005;
RA Saad Y., Garrett M.R., Manickavasagam E., Yerga-Woolwine S., Farms P.,
RA Radecki T., Joe B.;
RT "Fine-mapping and comprehensive transcript analysis reveals nonsynonymous
RT variants within a novel 1.17 Mb blood pressure QTL region on rat chromosome
RT 10.";
RL Genomics 89:343-353(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-879 (ISOFORMS 2/3), AND INTERACTION WITH
RP SCAMP1.
RX PubMed=10777571; DOI=10.1074/jbc.275.17.12752;
RA Fernandez-Chacon R., Achiriloaie M., Janz R., Albanesi J.P., Suedhof T.C.;
RT "SCAMP1 function in endocytosis.";
RL J. Biol. Chem. 275:12752-12756(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-879 (ISOFORMS 2/3), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10477754; DOI=10.1083/jcb.146.5.993;
RA Page L.J., Sowerby P.J., Lui W.W.Y., Robinson M.S.;
RT "Gamma-synergin: an EH domain-containing protein that interacts with gamma-
RT adaptin.";
RL J. Cell Biol. 146:993-1004(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844; SER-904; SER-997;
RP SER-1088 AND SER-1090, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
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
CC (PubMed:10777571). {ECO:0000250|UniProtKB:Q9UMZ2,
CC ECO:0000269|PubMed:10777571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10477754}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10477754};
CC Peripheral membrane protein {ECO:0000269|PubMed:10477754}. Cytoplasm,
CC perinuclear region {ECO:0000250|UniProtKB:Q9UMZ2}. Cytoplasmic vesicle,
CC clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UMZ2}.
CC Note=Localization at clathrin-coated vesicles depends on
CC AFTPH/aftiphilin (By similarity). Associates with membranes via the
CC adapter protein complex AP-1 (PubMed:10477754). Colocalizes with AP1G1
CC (PubMed:10477754). {ECO:0000250|UniProtKB:Q9UMZ2,
CC ECO:0000269|PubMed:10477754}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9JKC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JKC9-2; Sequence=VSP_023017;
CC Name=3;
CC IsoId=Q9JKC9-3; Sequence=VSP_023017, VSP_023019;
CC Name=4;
CC IsoId=Q9JKC9-4; Sequence=VSP_023018, VSP_023019;
CC -!- TISSUE SPECIFICITY: Detected in brain and liver (at protein level).
CC Ubiquitously expressed. {ECO:0000269|PubMed:10477754}.
CC -!- DOMAIN: The DFXDF motifs mediate the interaction with gamma-appendage
CC subunits AP1G1 and AP1G2. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF61257.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF121979; ABL63418.1; -; mRNA.
DR EMBL; EF121977; ABL63416.1; -; mRNA.
DR EMBL; EF121978; ABL63417.1; -; mRNA.
DR EMBL; EF121980; ABL63419.1; -; mRNA.
DR EMBL; EF121981; ABL63420.1; -; mRNA.
DR EMBL; EF121982; ABL63421.1; -; mRNA.
DR EMBL; AF242544; AAF61257.1; ALT_INIT; mRNA.
DR EMBL; AF169549; AAD49733.1; -; mRNA.
DR RefSeq; NP_445871.1; NM_053419.1. [Q9JKC9-1]
DR AlphaFoldDB; Q9JKC9; -.
DR SMR; Q9JKC9; -.
DR BioGRID; 249979; 3.
DR STRING; 10116.ENSRNOP00000052759; -.
DR CarbonylDB; Q9JKC9; -.
DR iPTMnet; Q9JKC9; -.
DR PhosphoSitePlus; Q9JKC9; -.
DR jPOST; Q9JKC9; -.
DR PaxDb; Q9JKC9; -.
DR PRIDE; Q9JKC9; -.
DR GeneID; 84479; -.
DR KEGG; rno:84479; -.
DR CTD; 11276; -.
DR RGD; 620684; Synrg.
DR eggNOG; KOG0998; Eukaryota.
DR InParanoid; Q9JKC9; -.
DR OrthoDB; 226328at2759; -.
DR PhylomeDB; Q9JKC9; -.
DR PRO; PR:Q9JKC9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IDA:RGD.
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..1329
FT /note="Synergin gamma"
FT /id="PRO_0000072389"
FT DOMAIN 393..504
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT REGION 175..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..878
FT /note="Interaction with AP1G1"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT REGION 661..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..773
FT /note="Interaction with AP1G1, AP1G2 and GGA1"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT REGION 797..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 112..152
FT /evidence="ECO:0000255"
FT MOTIF 555..559
FT /note="DFXDF motif 1"
FT MOTIF 785..789
FT /note="DFXDF motif 2"
FT MOTIF 867..871
FT /note="DFXDF motif 3"
FT COMPBIAS 192..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 836
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 997
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT MOD_RES 1115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMZ2"
FT VAR_SEQ 194..372
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17218081"
FT /id="VSP_023017"
FT VAR_SEQ 194..294
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17218081"
FT /id="VSP_023018"
FT VAR_SEQ 1275..1286
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:17218081"
FT /id="VSP_023019"
SQ SEQUENCE 1329 AA; 141359 MW; D0B06BBF0CDAE083 CRC64;
MALRPGAGAS GAAGAGTGPG GAGSFMFPVA GGMRPPQGLI PMQQQGFPMV SVMQPNMQGM
MGMNYSSQMS QGPIAMQAGI PMGPMPAAGV PFLGQPPFLG MRPAAPQYTP DMQKQFAEEQ
QKRFEQQQKL LEEERKRRQF EEQKQKLRLL SSVKPKTGEK NRDDALEAIK GNLDGFSRDA
KMHPTPASHP KKPDCPTSSH STKTVSPSSA FLGEDEFSGF MQGPVELPTC GPSSTAQPFQ
SFLPSTPLGQ LHTQKAGAQP LPPGQAPVSF AVHGVHGQIP CLSAASASHS MQKAGPSLEE
KLLVSCDISA SGQEHIKLSS PEAGHRAVVP GSSKNSPGLM AHNGGAVDGC VSGPTTAVAE
KTSDQNLSKE ESGVGVFPSQ DPVQPRMPPW IYNESLVPDA YKKILETTMT PTGIDTAKLY
PILMSSGLPR ETLGQIWALA NRTTPGKLTK EELYTVLAMV AVTQRGVPAM SPDTLNQFPA
APIPTLSGFP MTLPTPVSQP TAMTSGPAGS IPLSLGQPIM GINLVGPVGG AAAPTSSGFM
PAYPSNQVGK TEEDDFQDFQ DASKSGSIDD SFTDFQEVPA SSKTSNSQHG NSAPSLLIPL
PGTKASTDKY AVFKGISAEK PSENPASFGE SGDKYSAFRE LEPTADSKPL GESFAEFRST
GTDDGFTDFK TADSVSPLEP PTKDSFPSAF ASGAAQQTQT QVKTPLNLAD LDMFSSVDCS
GEKPVPFSAA FSTSKSVSSR PQPAGSAAAP ASLASTKASS LADDFGEFNL FGEYSNPASV
GEQDDFADFM AFGNSSIPSE PKADDKYEAL REEGSPGALS TSTVEGAHNP PVSSSKYDVF
KQLSLEGAGL AIEEFKENTP STKSDGDFAD FHSSKFSSTS SDKSLGEKAV AFRHAKEDSA
SVKSLDLPSI GGSSVGKEDS EDALSVQFDM KLADVGGDLK HVMSDSSLDL PTVSGQHPPA
AGSALASEDA LPETPFPAFA SFKDMMPQTT EQKEYESGDF QDFTRQDMPM VDRSQENTCP
SPASSVASHE TPKEGADDFG EFQSEKPKIS KFDFLVANSQ SKMKSSEEMI KSELATFDLS
VQGSHKRSLS LGDKEISRSS PSPALEQPFR DRSNTLSERA ALPVIRDKYK DLTGEVEENE
RYAYEWQRCL GSALDVIKKA NDTLNGISSS AVCTEVIQSA QGMEYLLGVV EVYRVTKRVE
LGIKATAVCS EKLQQLLKDI DKVWNNLIGF MSLTTLTPDE NSLDFSSCML RPGIKNAQEL
ACGVCLLNVD SRSRKEETPA EEQPKKAFNS ETDSFKLAYG GHQYHASCAN FWINCVEPKP
PGLLLPDLL
