(data stored in ACNUC14577 zone)

HOGENOM: MOUSE15_PE798

ID   MOUSE15_PE798                        STANDARD;      PRT;   635 AA.
AC   MOUSE15_PE798; Q8R0H9; Q3U2N1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ADP-ribosylation factor-binding protein GGA1;AltName:
DE   Full=Gamma-adaptin-related protein 1;AltName: Full=Golgi-localized, gamma
DE   ear-containing, ARF-binding protein 1; (MOUSE15.PE798).
GN   Name=Gga1;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE15.PE798.
CC       Mus musculus chromosome 15 NCBIM37  sequence 1..103494974 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:GGA1_MOUSE
CC   -!- FUNCTION: Plays a role in protein sorting and trafficking between
CC       the trans-Golgi network (TGN) and endosomes. Mediates the ARF-
CC       dependent recruitment of clathrin to the TGN and binds
CC       ubiquitinated proteins and membrane cargo molecules with a
CC       cytosolic acidic cluster-dileucine (AC-LL) motif (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with NECAP1 (By similarity). Interacts
CC       with GGA2 and GGA3. Binds to clathrin and activated ARFs.
CC       Interacts with RABEP1 and RABGEF1. Interacts with the type-I
CC       membrane proteins SORT1, SORL1, LRP3, M6PR/CD-MPR, IGF2R/CI-MPR
CC       and BACE1. Binds CCDC91, P200, SYNRG, EPN4, NECAP2 and
CC       AFTPH/aftiphilin. Interacts with TSG101 and UBC (By similarity).
CC       Interacts with CNST.
CC   -!- INTERACTION:
CC       Q8CBC4-3:Cnst; NbExp=2; IntAct=EBI-2616212, EBI-2615407;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Peripheral membrane protein (By similarity). Endosome
CC       membrane; Peripheral membrane protein (By similarity).
CC   -!- DOMAIN: The VHS domain functions as a recognition module for
CC       sorting signals composed of an acidic cluster followed by two
CC       leucines (AC-LL motif) (By similarity).
CC   -!- DOMAIN: The GAT domain is responsible for interaction with ARF-
CC       GTP, UBC and RABEP1. Required for recruitment to the TGN it
CC       prevents ARF-GTP hydrolysis (By similarity).
CC   -!- DOMAIN: The unstructured hinge region contains clathrin-binding
CC       but no autoinhibitory (AC-LL) motifs (By similarity).
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 AC-LL motif to bind
CC       the VHS domain and to inhibit the recognition of cargo signals.
CC       Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Ubiquitinated (By similarity).
CC   -!- SIMILARITY: Belongs to the GGA protein family.
CC   -!- SIMILARITY: Contains 1 GAE domain.
CC   -!- SIMILARITY: Contains 1 GAT domain.
CC   -!- SIMILARITY: Contains 1 VHS domain.
CC   -!- GENE_FAMILY: HOG000231169 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000033128;ENSMUST00000041587;ENSMUSP00000035992.
DR   EMBL; AK080881; - ;
DR   EMBL; AK155195; - ;
DR   EMBL; AK171534; - ;
DR   EMBL; BC026802; - ;
DR   UniProtKB/Swiss-Prot; Q8R0H9; Q3U2N1; -.
DR   EMBL; AK080881; BAC38058.1; -; mRNA.
DR   EMBL; AK155195; BAE33109.1; -; mRNA.
DR   EMBL; BC026802; AAH26802.1; -; mRNA.
DR   IPI; IPI00153201; -.
DR   RefSeq; NP_666041.1; NM_145929.2.
DR   UniGene; Mm.251331; -.
DR   ProteinModelPortal; Q8R0H9; -.
DR   SMR; Q8R0H9; 2-147, 168-301, 508-635.
DR   IntAct; Q8R0H9; 2.
DR   STRING; Q8R0H9; -.
DR   PhosphoSite; Q8R0H9; -.
DR   PRIDE; Q8R0H9; -.
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   GeneTree; ENSGT00600000084107; -.
DR   InParanoid; Q8R0H9; -.
DR   OMA; LRYKLIF; -.
DR   OrthoDB; EOG4J117V; -.
DR   PhylomeDB; Q8R0H9; -.
DR   NextBio; 358026; -.
DR   ArrayExpress; Q8R0H9; -.
DR   Bgee; Q8R0H9; -.
DR   Genevestigator; Q8R0H9; -.
DR   GermOnline; ENSMUSG00000033128; Mus musculus.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044431; C:Golgi apparatus part; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR013041; Clathrin/coatomer_app_Ig-like.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR008153; Clathrin_g-adaptin_app.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR004152; GAT.
DR   InterPro; IPR002014; VHS.
DR   InterPro; IPR018205; VHS_subgr.
DR   Gene3D; G3DSA:2.60.40.1230; Clathrin_g-adaptin_app; 1.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   Pfam; PF03127; GAT; 1.
DR   Pfam; PF00790; VHS; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF49348; Clath_adapt; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50180; GAE; 1.
DR   PROSITE; PS50909; GAT; 1.
DR   PROSITE; PS50179; VHS; 1.
DR   HOGENOMDNA; MOUSE15.PE798; -.
KW   ENSMUSG000000331285old_1320000031; ENSMUSP000000359921old_1320000031;
KW   Q3TB03_MOUSE; AK080881; AK155195; AK171534; BC026802;
KW   Acetylation; Complete proteome; Endosome; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation.
SQ   SEQUENCE   635 AA;  UNKNOWN MW;  UNKNOWN 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
//

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