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Golgi reassembly-stacking protein 2 (GRS2) (Golgi reassembly-stacking protein of 55 kDa) (GRASP55)

 GORS2_RAT               Reviewed;         454 AA.
Q9R064;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 110.
RecName: Full=Golgi reassembly-stacking protein 2;
Short=GRS2;
AltName: Full=Golgi reassembly-stacking protein of 55 kDa;
Short=GRASP55;
Name=Gorasp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-2, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=10487747; DOI=10.1093/emboj/18.18.4949;
Shorter J., Watson R., Giannakou M.-E., Clarke M., Warren G.,
Barr F.A.;
"GRASP55, a second mammalian GRASP protein involved in the stacking of
Golgi cisternae in a cell-free system.";
EMBO J. 18:4949-4960(1999).
[2]
SUBCELLULAR LOCATION, AND INTERACTION WITH BLZF1.
PubMed=11739401; DOI=10.1083/jcb.200108079;
Short B., Preisinger C., Koerner R., Kopajtich R., Byron O.,
Barr F.A.;
"A GRASP55-rab2 effector complex linking Golgi structure to membrane
traffic.";
J. Cell Biol. 155:877-883(2001).
[3]
INTERACTION WITH TMED2 AND TMED3.
PubMed=11739402; DOI=10.1083/jcb.200108102;
Barr F.A., Preisinger C., Kopajtich R., Koerner R.;
"Golgi matrix proteins interact with p24 cargo receptors and aid their
efficient retention in the Golgi apparatus.";
J. Cell Biol. 155:885-891(2001).
[4]
METHYLATION AT ARG-30 AND ARG-47, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15047867; DOI=10.1091/mbc.E04-02-0101;
Wu C.C., MacCoss M.J., Mardones G., Finnigan C., Mogelsvang S.,
Yates J.R. III, Howell K.E.;
"Organellar proteomics reveals Golgi arginine dimethylation.";
Mol. Biol. Cell 15:2907-2919(2004).
[5] {ECO:0000244|PDB:4KFW}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-215, AND FUNCTION.
PubMed=23940043; DOI=10.1074/jbc.M113.478024;
Feng Y., Yu W., Li X., Lin S., Zhou Y., Hu J., Liu X.;
"Structural insight into Golgi membrane stacking by GRASP65 and
GRASP55 proteins.";
J. Biol. Chem. 288:28418-28427(2013).
-!- FUNCTION: Plays a role in the assembly and membrane stacking of
the Golgi cisternae, and in the process by which Golgi stacks
reform after breakdown during mitosis and meiosis
(PubMed:10487747, PubMed:23940043). May regulate the intracellular
transport and presentation of a defined set of transmembrane
proteins, such as transmembrane TGFA (By similarity). Required for
normal acrosome formation during spermiogenesis and normal male
fertility, probably by promoting colocalization of JAM2 and JAM3
at contact sites between germ cells and Sertoli cells (By
similarity). {ECO:0000250|UniProtKB:Q99JX3,
ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747,
ECO:0000269|PubMed:23940043}.
-!- SUBUNIT: Interacts with BLZF1/Golgin 45 (PubMed:11739401).
Identified in a complex with RAB2 and GORASP2 (By similarity).
Interacts with JAM2 and JAM3 (By similarity). Interacts with
members of the p24 cargo receptors. Interacts with CNIH1 and the
cytoplasmic domain of transmembrane TGFA, prior its transit in the
trans-Golgi. Interacts with KCTD5 (By similarity). Interacts with
TMED2 and TMED3 (PubMed:11739402). {ECO:0000250|UniProtKB:Q99JX3,
ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:11739401,
ECO:0000269|PubMed:11739402}.
-!- INTERACTION:
Q6AYB8:Blzf1; NbExp=5; IntAct=EBI-4422912, EBI-4422894;
P50281:MMP14 (xeno); NbExp=14; IntAct=EBI-4422912, EBI-992788;
Q63584:Tmed10; NbExp=2; IntAct=EBI-4422912, EBI-918648;
Q63524:Tmed2; NbExp=4; IntAct=EBI-4422912, EBI-918600;
Q5I0E7:Tmed9; NbExp=3; IntAct=EBI-4422912, EBI-920903;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11739401}; Lipid-
anchor {ECO:0000269|PubMed:10487747}. Note=Detected in the
intermediate Golgi, membrane-associated.
{ECO:0000269|PubMed:10487747}.
-!- TISSUE SPECIFICITY: Detected in lung, brain, heart, liver and
testis. {ECO:0000269|PubMed:10487747}.
-!- PTM: Myristoylated (By similarity). Myristoylation is essential
for the Golgi targeting (PubMed:10487747).
{ECO:0000250|UniProtKB:Q9H8Y8, ECO:0000269|PubMed:10487747}.
-!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q9H8Y8}.
-!- PTM: Phosphorylated in mitotic cells.
{ECO:0000250|UniProtKB:Q9H8Y8}.
-!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF110267; AAD55350.1; -; mRNA.
UniGene; Rn.145137; -.
PDB; 4KFW; X-ray; 2.70 A; A/B=1-215.
PDBsum; 4KFW; -.
SMR; Q9R064; -.
IntAct; Q9R064; 17.
MINT; Q9R064; -.
STRING; 10116.ENSRNOP00000036881; -.
iPTMnet; Q9R064; -.
PhosphoSitePlus; Q9R064; -.
PaxDb; Q9R064; -.
PRIDE; Q9R064; -.
UCSC; RGD:619911; rat.
RGD; 619911; Gorasp2.
eggNOG; KOG3834; Eukaryota.
eggNOG; COG5233; LUCA.
HOGENOM; HOG000231920; -.
HOVERGEN; HBG051826; -.
InParanoid; Q9R064; -.
PhylomeDB; Q9R064; -.
PRO; PR:Q9R064; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0005797; C:Golgi medial cisterna; IDA:RGD.
GO; GO:0007030; P:Golgi organization; IDA:RGD.
GO; GO:0006996; P:organelle organization; ISS:UniProtKB.
InterPro; IPR024958; GRASP55/65_PDZ.
InterPro; IPR007583; GRASP55_65.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR12893; PTHR12893; 1.
Pfam; PF04495; GRASP55_65; 1.
SUPFAM; SSF50156; SSF50156; 2.
PROSITE; PS51865; PDZ_GRASP; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Differentiation; Golgi apparatus;
Lipoprotein; Membrane; Methylation; Myristate; Palmitate;
Phosphoprotein; Reference proteome; Repeat; Spermatogenesis.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9H8Y8}.
CHAIN 2 454 Golgi reassembly-stacking protein 2.
/FTId=PRO_0000087547.
DOMAIN 15 105 PDZ GRASP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU01212}.
DOMAIN 111 199 PDZ GRASP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU01212}.
REGION 15 215 GRASP. {ECO:0000255|PROSITE-
ProRule:PRU01214}.
REGION 194 199 Important for membrane binding.
{ECO:0000250}.
COMPBIAS 278 377 Pro-rich.
MOD_RES 30 30 Dimethylated arginine.
{ECO:0000269|PubMed:15047867}.
MOD_RES 47 47 Dimethylated arginine.
{ECO:0000269|PubMed:15047867}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H8Y8}.
MOD_RES 222 222 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9H8Y8}.
MOD_RES 225 225 Phosphothreonine; by MAPK.
{ECO:0000250|UniProtKB:Q9H8Y8}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JX3}.
MOD_RES 435 435 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9H8Y8}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JX3}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H8Y8}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:Q9H8Y8}.
MUTAGEN 2 2 G->A: No or few Golgi targeting,
accumulates in the cytoplasm.
{ECO:0000269|PubMed:10487747}.
STRAND 14 22 {ECO:0000244|PDB:4KFW}.
HELIX 27 30 {ECO:0000244|PDB:4KFW}.
TURN 35 37 {ECO:0000244|PDB:4KFW}.
STRAND 38 43 {ECO:0000244|PDB:4KFW}.
STRAND 50 53 {ECO:0000244|PDB:4KFW}.
HELIX 54 61 {ECO:0000244|PDB:4KFW}.
TURN 62 64 {ECO:0000244|PDB:4KFW}.
STRAND 67 73 {ECO:0000244|PDB:4KFW}.
TURN 74 76 {ECO:0000244|PDB:4KFW}.
STRAND 79 84 {ECO:0000244|PDB:4KFW}.
STRAND 88 96 {ECO:0000244|PDB:4KFW}.
STRAND 98 104 {ECO:0000244|PDB:4KFW}.
TURN 106 110 {ECO:0000244|PDB:4KFW}.
STRAND 113 118 {ECO:0000244|PDB:4KFW}.
HELIX 123 127 {ECO:0000244|PDB:4KFW}.
TURN 131 133 {ECO:0000244|PDB:4KFW}.
STRAND 134 140 {ECO:0000244|PDB:4KFW}.
HELIX 149 155 {ECO:0000244|PDB:4KFW}.
TURN 156 158 {ECO:0000244|PDB:4KFW}.
STRAND 161 167 {ECO:0000244|PDB:4KFW}.
TURN 168 171 {ECO:0000244|PDB:4KFW}.
STRAND 172 178 {ECO:0000244|PDB:4KFW}.
STRAND 184 197 {ECO:0000244|PDB:4KFW}.
STRAND 207 210 {ECO:0000244|PDB:4KFW}.
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


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