GORS2_RAT
ID GORS2_RAT Reviewed; 454 AA.
AC Q9R064;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Golgi reassembly-stacking protein 2;
DE Short=GRS2;
DE AltName: Full=Golgi reassembly-stacking protein of 55 kDa;
DE Short=GRASP55;
GN Name=Gorasp2;
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], FUNCTION, MUTAGENESIS OF GLY-2, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=10487747; DOI=10.1093/emboj/18.18.4949;
RA Shorter J., Watson R., Giannakou M.-E., Clarke M., Warren G., Barr F.A.;
RT "GRASP55, a second mammalian GRASP protein involved in the stacking of
RT Golgi cisternae in a cell-free system.";
RL EMBO J. 18:4949-4960(1999).
RN [2]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BLZF1.
RX PubMed=11739401; DOI=10.1083/jcb.200108079;
RA Short B., Preisinger C., Koerner R., Kopajtich R., Byron O., Barr F.A.;
RT "A GRASP55-rab2 effector complex linking Golgi structure to membrane
RT traffic.";
RL J. Cell Biol. 155:877-883(2001).
RN [3]
RP INTERACTION WITH TMED2 AND TMED3.
RX PubMed=11739402; DOI=10.1083/jcb.200108102;
RA Barr F.A., Preisinger C., Kopajtich R., Koerner R.;
RT "Golgi matrix proteins interact with p24 cargo receptors and aid their
RT efficient retention in the Golgi apparatus.";
RL J. Cell Biol. 155:885-891(2001).
RN [4]
RP METHYLATION AT ARG-30 AND ARG-47, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15047867; DOI=10.1091/mbc.e04-02-0101;
RA Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
RA Yates J.R. III, Howell K.E.;
RT "Organellar proteomics reveals Golgi arginine dimethylation.";
RL Mol. Biol. Cell 15:2907-2919(2004).
RN [5] {ECO:0007744|PDB:4KFW}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-215, AND FUNCTION.
RX PubMed=23940043; DOI=10.1074/jbc.m113.478024;
RA Feng Y., Yu W., Li X., Lin S., Zhou Y., Hu J., Liu X.;
RT "Structural insight into Golgi membrane stacking by GRASP65 and GRASP55
RT proteins.";
RL J. Biol. Chem. 288:28418-28427(2013).
CC -!- FUNCTION: Plays a role in the assembly and membrane stacking of the
CC Golgi cisternae, and in the process by which Golgi stacks reform after
CC breakdown during mitosis and meiosis (PubMed:10487747,
CC PubMed:23940043). May regulate the intracellular transport and
CC presentation of a defined set of transmembrane proteins, such as
CC transmembrane TGFA (By similarity). Required for normal acrosome
CC formation during spermiogenesis and normal male fertility, probably by
CC promoting colocalization of JAM2 and JAM3 at contact sites between germ
CC cells and Sertoli cells (By similarity). Mediates ER stress-induced
CC unconventional (ER/Golgi-independent) trafficking of core-glycosylated
CC CFTR to cell membrane (By similarity). {ECO:0000250|UniProtKB:Q99JX3,
CC ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747,
CC ECO:0000269|PubMed:23940043}.
CC -!- SUBUNIT: Homodimer. Homooligomer. ER stress induces phosphorylation-
CC dependent monomerization (By similarity). Interacts with BLZF1/Golgin
CC 45 (PubMed:11739401). Identified in a complex with RAB2 and GORASP2 (By
CC similarity). Interacts with JAM2 and JAM3 (By similarity). Interacts
CC with members of the p24 cargo receptors. Interacts with CNIH1 and the
CC cytoplasmic domain of transmembrane TGFA, prior its transit in the
CC trans-Golgi. Interacts with KCTD5 (By similarity). Interacts with TMED2
CC and TMED3 (PubMed:11739402). Interacts with SEC16A in response to ER
CC stress (By similarity). Interacts (via PDZ GRASP-type 1 domain) with
CC core-glycosylated CFTR in response to ER stress (By similarity).
CC {ECO:0000250|UniProtKB:Q99JX3, ECO:0000250|UniProtKB:Q9H8Y8,
CC ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:11739402}.
CC -!- INTERACTION:
CC Q9R064; Q6AYB8: Blzf1; NbExp=5; IntAct=EBI-4422912, EBI-4422894;
CC Q9R064; Q63584: Tmed10; NbExp=2; IntAct=EBI-4422912, EBI-918648;
CC Q9R064; Q63524: Tmed2; NbExp=4; IntAct=EBI-4422912, EBI-918600;
CC Q9R064; Q5I0E7: Tmed9; NbExp=3; IntAct=EBI-4422912, EBI-920903;
CC Q9R064; P50281: MMP14; Xeno; NbExp=14; IntAct=EBI-4422912, EBI-992788;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11739401}; Lipid-
CC anchor {ECO:0000269|PubMed:10487747}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H8Y8}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9H8Y8}. Note=Detected in the intermediate
CC Golgi, membrane-associated (PubMed:10487747). ER stress triggers its
CC relocalization from Golgi to ER membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747}.
CC -!- TISSUE SPECIFICITY: Detected in lung, brain, heart, liver and testis.
CC {ECO:0000269|PubMed:10487747}.
CC -!- PTM: Myristoylated (By similarity). Myristoylation is essential for the
CC Golgi targeting (PubMed:10487747). {ECO:0000250|UniProtKB:Q9H8Y8,
CC ECO:0000269|PubMed:10487747}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q9H8Y8}.
CC -!- PTM: Phosphorylated in mitotic cells. ER stress-induced phosphorylation
CC at Ser-443 induces monomerization and subsequent relocalization from
CC Golgi to ER which is essential for mediating unconventional (ER/Golgi-
CC independent) trafficking of CFTR to the cell membrane.
CC {ECO:0000250|UniProtKB:Q9H8Y8}.
CC -!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
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DR EMBL; AF110267; AAD55350.1; -; mRNA.
DR PDB; 4KFW; X-ray; 2.70 A; A/B=1-215.
DR PDBsum; 4KFW; -.
DR AlphaFoldDB; Q9R064; -.
DR SMR; Q9R064; -.
DR CORUM; Q9R064; -.
DR IntAct; Q9R064; 17.
DR MINT; Q9R064; -.
DR iPTMnet; Q9R064; -.
DR PhosphoSitePlus; Q9R064; -.
DR jPOST; Q9R064; -.
DR PaxDb; Q9R064; -.
DR PRIDE; Q9R064; -.
DR UCSC; RGD:619911; rat.
DR RGD; 619911; Gorasp2.
DR eggNOG; KOG3834; Eukaryota.
DR InParanoid; Q9R064; -.
DR PhylomeDB; Q9R064; -.
DR Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR PRO; PR:Q9R064; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IDA:RGD.
DR GO; GO:0070925; P:organelle assembly; ISO:RGD.
DR GO; GO:0006996; P:organelle organization; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR007583; GRASP55_65.
DR InterPro; IPR024958; GRASP_PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12893; PTHR12893; 1.
DR Pfam; PF04495; GRASP55_65; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS51865; PDZ_GRASP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Differentiation; Endoplasmic reticulum; Golgi apparatus;
KW Lipoprotein; Membrane; Methylation; Myristate; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT CHAIN 2..454
FT /note="Golgi reassembly-stacking protein 2"
FT /id="PRO_0000087547"
FT DOMAIN 15..105
FT /note="PDZ GRASP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT DOMAIN 111..199
FT /note="PDZ GRASP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT REGION 15..215
FT /note="GRASP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01214"
FT REGION 194..199
FT /note="Important for membrane binding"
FT /evidence="ECO:0000250"
FT REGION 377..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:15047867"
FT MOD_RES 47
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:15047867"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 225
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JX3"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JX3"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MUTAGEN 2
FT /note="G->A: No or few Golgi targeting, accumulates in the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:10487747"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:4KFW"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4KFW"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4KFW"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:4KFW"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4KFW"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4KFW"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4KFW"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:4KFW"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:4KFW"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:4KFW"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4KFW"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 184..197
FT /evidence="ECO:0007829|PDB:4KFW"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:4KFW"
SQ SEQUENCE 454 AA; 47221 MW; BB6898C85CB6221C CRC64;
MGSSQSVEIP GGGTEGYHVL RVQENSPGHR AGLEPFFDFI VSISGSRLNK DNDTLKDLLK
ANVEKPVKML IYSSKTLELR EASVTPSNLW GGQGLLGVSI RFCSFDGANE NVWHVLEVES
NSPAALAGLR PHSDYIIGAD TVMNESEDLF SLIETHEAKP LKLYVYNTDT DNCREVIITP
NSAWGGEGSL GCGIGYGYLH RIPTRPFEEG KKISLPGQMT GTPITPLKDG FTQVQLSSVS
PPSLSPPGTA GVEQSLSGLS ISSAPPAVSN VLSTGVPTVP LLPPQVNQSL ASVPPMNPAA
TLPSLMPLSA GLPNLPNLPS LSNFNLPAPH IMPGVGLPEL GKPGLPPLPS LPPRNVPGIA
PLPMPSDFLP SFPLVPEGSS AASAGEPLSS LPAMGPPSDP VMTTAKADTS SLTVDVMSPA
SKVPTTVEDR VSDCTPAMEK PVSAVTDANA SGAS
