GGA1_MOUSE
ID GGA1_MOUSE Reviewed; 635 AA.
AC Q8R0H9; Q3U2N1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ADP-ribosylation factor-binding protein GGA1;
DE AltName: Full=Gamma-adaptin-related protein 1;
DE AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 1;
GN Name=Gga1;
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 MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Adipose tissue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 INTERACTION WITH ARF1; ARF5 AND ARF6.
RX PubMed=11950392; DOI=10.1042/bj20020428;
RA Takatsu H., Yoshino K., Toda K., Nakayama K.;
RT "GGA proteins associate with Golgi membranes through interaction between
RT their GGAH domains and ADP-ribosylation factors.";
RL Biochem. J. 365:369-378(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, 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 [5]
RP INTERACTION WITH CNST.
RX PubMed=19864490; DOI=10.1093/hmg/ddp490;
RA del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D., Lampe P.D.,
RA Chavrier P., Meda P., Petit C.;
RT "Consortin, a trans-Golgi network cargo receptor for the plasma membrane
RT targeting and recycling of connexins.";
RL Hum. Mol. Genet. 19:262-275(2010).
RN [6]
RP INTERACTION WITH ARF6.
RX PubMed=22522702; DOI=10.1038/emboj.2012.89;
RA Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A.,
RA Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M.,
RA Kawasaki M., Kato R., Wakatsuki S., Nakayama K.;
RT "Structural basis for Arf6-MKLP1 complex formation on the Flemming body
RT responsible for cytokinesis.";
RL EMBO J. 31:2590-2603(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH RABEP1 AND ARL3.
RX PubMed=25405894; DOI=10.1038/ncomms6482;
RA Kim H., Xu H., Yao Q., Li W., Huang Q., Outeda P., Cebotaru V.,
RA Chiaravalli M., Boletta A., Piontek K., Germino G.G., Weinman E.J.,
RA Watnick T., Qian F.;
RT "Ciliary membrane proteins traffic through the Golgi via a
RT Rabep1/GGA1/Arl3-dependent mechanism.";
RL Nat. Commun. 5:5482-5482(2014).
CC -!- FUNCTION: Plays a role in protein sorting and trafficking between the
CC trans-Golgi network (TGN) and endosomes (PubMed:25405894). Mediates the
CC ARF-dependent recruitment of clathrin to the TGN and binds
CC ubiquitinated proteins and membrane cargo molecules with a cytosolic
CC acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR
CC receptor ADRA2B to the cell surface (By similarity). Required for
CC targeting PKD1:PKD2 complex from the trans-Golgi network to the cilium
CC membrane (PubMed:25405894). Regulates retrograde transport of proteins
CC such as phosphorylated form of BACE1 from endosomes to the trans-Golgi
CC network (By similarity). {ECO:0000250|UniProtKB:Q9UJY5,
CC ECO:0000269|PubMed:25405894}.
CC -!- SUBUNIT: Monomer. Interacts with GGA2 and GGA3 (By similarity). Binds
CC to clathrin and activated ARFs, including ARF1, ARF5 and ARF6
CC (PubMed:22522702, PubMed:11950392). Interacts with RABEP1 and RABGEF1
CC (PubMed:25405894). Interacts with the type-I membrane proteins LRP3,
CC M6PR/CD-MPR and IGF2R/CI-MPR. Interacts (via N-terminal VHS domain)
CC with SORL1/sorLA and SORT1 (via C-terminal cytosolic domain) (By
CC similarity). Interacts with EPN4. Interacts with CCDC91 (By
CC similarity). Interacts with HEATR5B/p200a (By similarity). Interacts
CC with SYNRG/gamma-synergin (By similarity). Interacts (via GAE doamin)
CC with NECAP1 and NECAP2 (By similarity). Interacts (via GAE domain) with
CC AFTPH/aftiphilin (By similarity). Interacts with TSG101 and UBC.
CC Interacts with RNF11. Interacts (via VHS domain) with BACE1 (via DXXLL
CC motif); the interaction highly increases when BACE1 is phosphorylated
CC at 'Ser-498' (By similarity). Interacts with CNST (PubMed:19864490).
CC Interacts with ADRA2B (By similarity). Interacts with ARL3; the
CC interaction recruits, in collaboration with RABEP1, PKD1:PKD2 complex
CC to trans-Golgi network and is required for ciliary targeting
CC (PubMed:25405894). {ECO:0000250|UniProtKB:Q9UJY5,
CC ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:19864490,
CC ECO:0000269|PubMed:22522702, ECO:0000269|PubMed:25405894}.
CC -!- INTERACTION:
CC Q8R0H9; Q8CBC4-3: Cnst; NbExp=2; IntAct=EBI-2616212, EBI-2615407;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9UJY5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UJY5}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9UJY5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UJY5}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9UJY5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UJY5}.
CC -!- DOMAIN: The VHS domain functions as a recognition module for sorting
CC signals composed of an acidic cluster followed by two leucines (DXXLL
CC motif).
CC -!- DOMAIN: The GAT domain is responsible for interaction with ARF-GTP, UBC
CC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP
CC hydrolysis. {ECO:0000250|UniProtKB:Q9UJY5}.
CC -!- DOMAIN: The unstructured hinge region contains clathrin-binding but no
CC autoinhibitory (DXXLL) motifs. {ECO:0000250|UniProtKB:Q9UJY5}.
CC -!- DOMAIN: The GAE domain binds accessory proteins regulating GGAs
CC function.
CC -!- PTM: Phosphorylated by CK2 and dephosphorylated by PP2A.
CC Phosphorylation of GGA1 allows the internal DXXLL motif to bind the VHS
CC domain and to inhibit the recognition of cargo signals.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9UJY5}.
CC -!- SIMILARITY: Belongs to the GGA protein family. {ECO:0000305}.
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DR EMBL; AK080881; BAC38058.1; -; mRNA.
DR EMBL; AK155195; BAE33109.1; -; mRNA.
DR EMBL; BC026802; AAH26802.1; -; mRNA.
DR CCDS; CCDS27625.1; -.
DR RefSeq; NP_666041.1; NM_145929.2.
DR AlphaFoldDB; Q8R0H9; -.
DR SMR; Q8R0H9; -.
DR BioGRID; 222979; 15.
DR ELM; Q8R0H9; -.
DR IntAct; Q8R0H9; 2.
DR STRING; 10090.ENSMUSP00000035992; -.
DR iPTMnet; Q8R0H9; -.
DR PhosphoSitePlus; Q8R0H9; -.
DR EPD; Q8R0H9; -.
DR MaxQB; Q8R0H9; -.
DR PaxDb; Q8R0H9; -.
DR PeptideAtlas; Q8R0H9; -.
DR PRIDE; Q8R0H9; -.
DR ProteomicsDB; 268872; -.
DR Antibodypedia; 12029; 239 antibodies from 28 providers.
DR DNASU; 106039; -.
DR Ensembl; ENSMUST00000041587; ENSMUSP00000035992; ENSMUSG00000033128.
DR GeneID; 106039; -.
DR KEGG; mmu:106039; -.
DR UCSC; uc007wrn.2; mouse.
DR CTD; 26088; -.
DR MGI; MGI:2146207; Gga1.
DR VEuPathDB; HostDB:ENSMUSG00000033128; -.
DR eggNOG; KOG1086; Eukaryota.
DR GeneTree; ENSGT00940000156448; -.
DR HOGENOM; CLU_015010_0_0_1; -.
DR InParanoid; Q8R0H9; -.
DR OMA; KGYRFPN; -.
DR OrthoDB; 594067at2759; -.
DR PhylomeDB; Q8R0H9; -.
DR TreeFam; TF318574; -.
DR BioGRID-ORCS; 106039; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Gga1; mouse.
DR PRO; PR:Q8R0H9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8R0H9; protein.
DR Bgee; ENSMUSG00000033128; Expressed in granulocyte and 215 other tissues.
DR ExpressionAtlas; Q8R0H9; baseline and differential.
DR Genevisible; Q8R0H9; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:MGI.
DR GO; GO:0030163; P:protein catabolic process; IGI:MGI.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:1903441; P:protein localization to ciliary membrane; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR008153; GAE_dom.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR041198; GGA_N-GAT.
DR InterPro; IPR002014; VHS_dom.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF18308; GGA_N-GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR PROSITE; PS50180; GAE; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..635
FT /note="ADP-ribosylation factor-binding protein GGA1"
FT /id="PRO_0000212681"
FT DOMAIN 17..147
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 171..298
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT DOMAIN 506..627
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 114..273
FT /note="Interaction with ARF3"
FT /evidence="ECO:0000250"
FT REGION 299..505
FT /note="Unstructured hinge"
FT REGION 305..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 357..361
FT /note="Autoinhibitory"
FT /evidence="ECO:0000250"
FT COMPBIAS 367..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY5"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY5"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY5"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJY5"
SQ SEQUENCE 635 AA; 69972 MW; 9F5F1C37F41ECCC6 CRC64;
MEPAMEPETL EARINRATNP LNKELNWASI NSFCEQLNED FEGPPLATRL LAHKIQSPQE
WEAIQALTVL ETCMKSCGKR FHDEVGKFRF LNELIKVVSP KYLGSRTSEK VKSKILELLY
SWTVCLPEEV KIAEAYQMLK KQGIVKSDPK LPEDAIFPLP PPRPKNVIFE DEEKSKMLAR
LLKSSHPEDL RAANKLIKEM VQEDQKRMEK ISKRVNAIEE VNNNVKLLTE MVMSHSQGAA
SSSSEDLMKE LYQRCERMRP TLFRLASDTE DNDEALAEIL QANDNLTQVI NLYKQLVRGE
EVNGDATASS IPGSTSALLD LSGLDLPPPG TTQPATPTRP GNQSSPEQLS ASVSLLDDEL
MSLGLSDPTP PSGTSSDSVG WDNFQSSDGT ESSVPPPAQA PSMDCRPPAQ APPPTSSGLD
DLDLLGKTLM QQALPPEAQQ VRWEKQQPAP RLTLRDLQSK SSSPSPGAAS LLHTTSPEPP
GPPPQATPTE FSLTSITVPL ESIKPSSILP VTVYDQHGFR VLFHFARDPL PGRSDVLVVV
VSMLSTAPQP IRNIVFQSAV PKVMKVRLQP PSGTELPAFN PIVHPSAITQ VLLLANPQKE
KVRLRYKLIF TMGDQTYNEM GDVDQFPPPE TWGSL
