GGA2_MOUSE
ID GGA2_MOUSE Reviewed; 603 AA.
AC Q6P5E6; Q3U374; Q6PFX3; Q6ZPY8; Q8BM76; Q9DC15;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ADP-ribosylation factor-binding protein GGA2;
DE AltName: Full=Gamma-adaptin-related protein 2;
DE AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 2;
GN Name=Gga2; Synonyms=Kiaa1080;
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] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Spleen;
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 [6]
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).
CC -!- FUNCTION: Plays a role in protein sorting and trafficking between the
CC trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent
CC recruitment of clathrin to the TGN and binds ubiquitinated proteins and
CC membrane cargo molecules with a cytosolic acidic cluster-dileucine
CC (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell
CC surface. Regulates retrograde transport of phosphorylated form of BACE1
CC from endosomes to the trans-Golgi network.
CC {ECO:0000250|UniProtKB:Q9UJY4}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with NECAP1, TSG101, UBC
CC and AFTPH/aftiphilin. Interacts with CNST (PubMed:19864490). Interacts
CC with GGA1 and GGA3 (By similarity). Binds to clathrin and activated
CC ARFs, such as ARF1, ARF5 and ARF6 (PubMed:11950392). Binds RABEP1 and
CC RABGEF1. Interacts with the type-I membrane proteins LRP3, M6PR/CD-MPR,
CC IGF2R/CI-MPR and BACE1. Interacts (via N-terminal VHS domain) with
CC SORL1/sorLA and SORT1 (via C-terminal cytosolic domain) (By
CC similarity). Binds the accessory proteins CCDC91, P200, SYNRG, EPN4 and
CC NECAP2. Interacts with ADRA2B. Interacts (via VHS domain) with PIK4B;
CC the interaction is important for PIK4B location at the Golgi apparatus
CC membrane (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UJY4,
CC ECO:0000269|PubMed:11950392, ECO:0000269|PubMed:19864490}.
CC -!- INTERACTION:
CC Q6P5E6; Q8CBC4-3: Cnst; NbExp=2; IntAct=EBI-2616239, EBI-2615407;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UJY4}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UJY4}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UJY4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P5E6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P5E6-2; Sequence=VSP_013255;
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). {ECO:0000250|UniProtKB:Q9UJY4}.
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:Q9UJY4}.
CC -!- DOMAIN: The unstructured hinge region contains clathrin-binding but no
CC autoinhibitory (DXXLL) motifs. {ECO:0000250|UniProtKB:Q9UJY4}.
CC -!- DOMAIN: The GAE domain binds accessory proteins regulating GGAs
CC function. {ECO:0000250|UniProtKB:Q9UJY4}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GGA protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28769.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98090.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK004632; BAB23426.1; -; mRNA.
DR EMBL; AK034612; BAC28769.1; ALT_INIT; mRNA.
DR EMBL; AK129280; BAC98090.1; ALT_INIT; mRNA.
DR EMBL; AK143691; BAE25501.1; -; mRNA.
DR EMBL; AK154904; BAE32915.1; -; mRNA.
DR EMBL; BC057377; AAH57377.1; -; mRNA.
DR EMBL; BC062933; AAH62933.1; -; mRNA.
DR CCDS; CCDS40116.1; -. [Q6P5E6-1]
DR RefSeq; NP_083034.1; NM_028758.2. [Q6P5E6-1]
DR AlphaFoldDB; Q6P5E6; -.
DR SMR; Q6P5E6; -.
DR BioGRID; 216496; 2.
DR IntAct; Q6P5E6; 2.
DR MINT; Q6P5E6; -.
DR STRING; 10090.ENSMUSP00000033160; -.
DR iPTMnet; Q6P5E6; -.
DR PhosphoSitePlus; Q6P5E6; -.
DR EPD; Q6P5E6; -.
DR MaxQB; Q6P5E6; -.
DR PaxDb; Q6P5E6; -.
DR PeptideAtlas; Q6P5E6; -.
DR PRIDE; Q6P5E6; -.
DR ProteomicsDB; 267434; -. [Q6P5E6-1]
DR ProteomicsDB; 267435; -. [Q6P5E6-2]
DR Antibodypedia; 12586; 218 antibodies from 31 providers.
DR DNASU; 74105; -.
DR Ensembl; ENSMUST00000033160; ENSMUSP00000033160; ENSMUSG00000030872. [Q6P5E6-1]
DR Ensembl; ENSMUST00000124566; ENSMUSP00000115581; ENSMUSG00000030872. [Q6P5E6-1]
DR GeneID; 74105; -.
DR KEGG; mmu:74105; -.
DR UCSC; uc009joa.1; mouse. [Q6P5E6-1]
DR CTD; 23062; -.
DR MGI; MGI:1921355; Gga2.
DR VEuPathDB; HostDB:ENSMUSG00000030872; -.
DR eggNOG; KOG1086; Eukaryota.
DR GeneTree; ENSGT00940000159613; -.
DR HOGENOM; CLU_015010_0_0_1; -.
DR InParanoid; Q6P5E6; -.
DR OMA; NCCKEKK; -.
DR OrthoDB; 594067at2759; -.
DR PhylomeDB; Q6P5E6; -.
DR TreeFam; TF318574; -.
DR BioGRID-ORCS; 74105; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Gga2; mouse.
DR PRO; PR:Q6P5E6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6P5E6; protein.
DR Bgee; ENSMUSG00000030872; Expressed in otic placode and 259 other tissues.
DR Genevisible; Q6P5E6; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
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 Alternative splicing; Endosome; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..603
FT /note="ADP-ribosylation factor-binding protein GGA2"
FT /id="PRO_0000212683"
FT DOMAIN 36..166
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 190..317
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT DOMAIN 474..595
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..473
FT /note="Unstructured hinge"
FT VAR_SEQ 1..249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013255"
FT CONFLICT 228
FT /note="E -> G (in Ref. 2; BAB23426)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="P -> A (in Ref. 2; BAB23426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 66049 MW; 0EFCB3905074982C CRC64;
MAATAVAAGT GSPAGTESAE GGPGAAAALE LWLNKATDPS MAEQDWSAIQ KFCEQVNTDP
SGPTHAPWLL AHKIQSPQEK EALYALTVLE ICMNHCGEKF HSEVAKFRFL NELIKVLSPK
YLGAWATEKV KGRVIEILFS WTVWFPEDIK IRDAYQMLKK QGIIKQDPKL PMDKILPPPS
PWPKSIFDAD EEKSKLLTRL LKSNHPEDLQ AANRLIKNLV KEEQEKSEKV SRRVSAVEEV
RSHVRVLREM LSMYRRPGHA LPDQQALQVV YERCEKLRPT LFRLASDTTD DDDALAEILQ
ANDLLTQGVR LYKQVVEGRV SAGNAVPAAV GAIPAPRAFP NPEPCGLNCP LIDLETPSLL
HQDLAALGIN DVPTRNQVVI PSCCNDKKQP GAITLMGGGI QSLSADRNLL DLFSPQPSPG
LNYVPQKSIP KEVPPGTKAS PGWSWEAGPL ASSTASQNTP LAHVFVPLES VKPSSLPPIV
VYDRNGFRIL LHFSQTGAPG HPDVKVLLLT MMSTATQPVW DVMFQVAVPK SMRVKLQPAS
SSKLPAFSPL MPPAVISQTL LLDNPHKEPI RLRYKLTFNQ GGQPFSEVGE VKDFPDLAVL
STA
