GORS1_RAT
ID GORS1_RAT Reviewed; 451 AA.
AC O35254;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Golgi reassembly-stacking protein 1;
DE AltName: Full=Golgi peripheral membrane protein p65;
DE AltName: Full=Golgi reassembly-stacking protein of 65 kDa {ECO:0000303|PubMed:9346242};
DE Short=GRASP65 {ECO:0000303|PubMed:9346242};
GN Name=Gorasp1; Synonyms=Grasp65 {ECO:0000303|PubMed:9346242};
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, INTERACTION WITH GOLGA2, TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND MYRISTOYLATION AT GLY-2.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9346242; DOI=10.1016/s0092-8674(00)80407-9;
RA Barr F.A., Puype M., Vandekerckhove J., Warren G.;
RT "GRASP65, a protein involved in the stacking of Golgi cisternae.";
RL Cell 91:253-262(1997).
RN [2]
RP SEQUENCE REVISION.
RA Barr F.A.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION.
RX PubMed=11050165; DOI=10.1073/pnas.220423497;
RA Lin C.-Y., Madsen M.L., Yarm F.R., Jang Y.-J., Liu X., Erikson R.L.;
RT "Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase
RT (Plk) and Cdc2.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12589-12594(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11706049; DOI=10.1083/jcb.200107045;
RA Ward T.H., Polishchuk R.S., Caplan S., Hirschberg K.,
RA Lippincott-Schwartz J.;
RT "Maintenance of Golgi structure and function depends on the integrity of ER
RT export.";
RL J. Cell Biol. 155:557-570(2001).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GOLGA2.
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 [6]
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 [7]
RP FUNCTION, CASPASE-MEDIATED CLEAVAGE, AND MUTAGENESIS OF ASP-320; ASP-375
RP AND ASP-393.
RX PubMed=11815631; DOI=10.1083/jcb.200110007;
RA Lane J.D., Lucocq J., Pryde J., Barr F.A., Woodman P.G., Allan V.J.,
RA Lowe M.;
RT "Caspase-mediated cleavage of the stacking protein GRASP65 is required for
RT Golgi fragmentation during apoptosis.";
RL J. Cell Biol. 156:495-509(2002).
RN [8]
RP FUNCTION, ROLE IN GOLGI FRAGMENTATION, AND SUBCELLULAR LOCATION.
RX PubMed=12015985; DOI=10.1016/s0092-8674(02)00720-1;
RA Suetterlin C., Hsu P., Mallabiabarrena A., Malhotra V.;
RT "Fragmentation and dispersal of the pericentriolar Golgi complex is
RT required for entry into mitosis in mammalian cells.";
RL Cell 109:359-369(2002).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, OLIGOMERIZATION, SUBUNIT,
RP AND INTERACTION WITH GOLGA2.
RX PubMed=12839990; DOI=10.1093/emboj/cdg317;
RA Wang Y., Seemann J., Pypaert M., Shorter J., Warren G.;
RT "A direct role for GRASP65 as a mitotically regulated Golgi stacking
RT factor.";
RL EMBO J. 22:3279-3290(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; THR-220; SER-365 AND
RP SER-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [11] {ECO:0007744|PDB:4KFV}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-210 IN COMPLEX WITH ZINC,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-54; PHE-149 AND TYR-209.
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 an important role in assembly and membrane stacking of
CC the Golgi cisternae, and in the reassembly of Golgi stacks after
CC breakdown during mitosis (PubMed:9346242, PubMed:12839990,
CC PubMed:23940043). Key structural protein required for the maintenance
CC of the Golgi apparatus integrity: its caspase-mediated cleavage is
CC required for fragmentation of the Golgi during apoptosis
CC (PubMed:11815631, PubMed:12015985). Also mediates, via its interaction
CC with GOLGA2/GM130, the docking of transport vesicles with the Golgi
CC membranes (By similarity). Mediates ER stress-induced unconventional
CC (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell
CC membrane (By similarity). {ECO:0000250|UniProtKB:Q9BQQ3,
CC ECO:0000269|PubMed:11815631, ECO:0000269|PubMed:12015985,
CC ECO:0000269|PubMed:12839990, ECO:0000269|PubMed:23940043,
CC ECO:0000269|PubMed:9346242}.
CC -!- SUBUNIT: Homodimer (PubMed:12839990, PubMed:23940043). Forms higher-
CC order oligomers under interphase but not mitotic conditions. Dimers of
CC the protein on one membrane might be able to interact with dimers on
CC another and so stack cisternae (PubMed:12839990). Interacts with the C-
CC terminus of GOLGA2/GM130 under both mitotic and non-mitotic conditions
CC (PubMed:9346242, PubMed:11739401, PubMed:12839990). The interaction is
CC critical for the correct targeting of both proteins to the cis-Golgi
CC (PubMed:9346242). Interacts with TMED2 and TMED3 (PubMed:11739402).
CC {ECO:0000250, ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:11739402,
CC ECO:0000269|PubMed:12839990, ECO:0000269|PubMed:23940043,
CC ECO:0000269|PubMed:9346242}.
CC -!- INTERACTION:
CC O35254; Q62839: Golga2; NbExp=2; IntAct=EBI-4422879, EBI-618335;
CC O35254; Q63524: Tmed2; NbExp=3; IntAct=EBI-4422879, EBI-918600;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:11706049, ECO:0000269|PubMed:11739401,
CC ECO:0000269|PubMed:12015985, ECO:0000269|PubMed:12839990,
CC ECO:0000269|PubMed:9346242}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9346242}; Cytoplasmic side
CC {ECO:0000269|PubMed:9346242}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9346242}.
CC -!- PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis.
CC Phosphorylation cycle correlates with the cisternal stacking cycle.
CC Phosphorylation of the homodimer prevents the association of dimers
CC into higher-order oligomers, leading to cisternal unstacking.
CC {ECO:0000269|PubMed:11050165, ECO:0000269|PubMed:12839990,
CC ECO:0000269|PubMed:9346242}.
CC -!- PTM: Target for caspase-3 cleavage during apoptosis. The cleavage
CC contributes to Golgi fragmentation and occurs very early in the
CC execution phase of apoptosis. {ECO:0000269|PubMed:11815631}.
CC -!- PTM: Myristoylated. {ECO:0000269|PubMed:9346242}.
CC -!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
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DR EMBL; AF015264; AAB81355.2; -; mRNA.
DR PDB; 4KFV; X-ray; 2.20 A; A=1-210.
DR PDBsum; 4KFV; -.
DR AlphaFoldDB; O35254; -.
DR SMR; O35254; -.
DR CORUM; O35254; -.
DR DIP; DIP-60188N; -.
DR ELM; O35254; -.
DR IntAct; O35254; 5.
DR STRING; 10116.ENSRNOP00000024408; -.
DR iPTMnet; O35254; -.
DR PhosphoSitePlus; O35254; -.
DR PaxDb; O35254; -.
DR UCSC; RGD:621122; rat.
DR RGD; 621122; Gorasp1.
DR eggNOG; KOG3834; Eukaryota.
DR InParanoid; O35254; -.
DR PhylomeDB; O35254; -.
DR Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR PRO; PR:O35254; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; 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:0050774; P:negative regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR DisProt; DP02422; -.
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; Direct protein sequencing; Golgi apparatus; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:9346242"
FT CHAIN 2..451
FT /note="Golgi reassembly-stacking protein 1"
FT /id="PRO_0000087572"
FT DOMAIN 14..104
FT /note="PDZ GRASP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT DOMAIN 110..198
FT /note="PDZ GRASP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 14..214
FT /note="GRASP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01214"
FT REGION 189..201
FT /note="Essential for interaction with GOLGA2/GM130"
FT REGION 204..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23940043,
FT ECO:0007744|PDB:4KFV"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23940043,
FT ECO:0007744|PDB:4KFV"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23940043,
FT ECO:0007744|PDB:4KFV"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 224
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQQ3"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X51"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:9346242"
FT MUTAGEN 54
FT /note="L->A: Strongly reduced ability to promote Golgi
FT stack reassembly."
FT /evidence="ECO:0000269|PubMed:23940043"
FT MUTAGEN 149
FT /note="F->A: Strongly reduced ability to promote Golgi
FT stack reassembly."
FT /evidence="ECO:0000269|PubMed:23940043"
FT MUTAGEN 209
FT /note="Y->A: Strongly reduced ability to promote Golgi
FT stack reassembly."
FT /evidence="ECO:0000269|PubMed:23940043"
FT MUTAGEN 320
FT /note="D->A: Blocks the caspase-mediated cleavage."
FT /evidence="ECO:0000269|PubMed:11815631"
FT MUTAGEN 375
FT /note="D->A: Blocks the caspase-mediated cleavage."
FT /evidence="ECO:0000269|PubMed:11815631"
FT MUTAGEN 393
FT /note="D->A: Blocks the caspase-mediated cleavage."
FT /evidence="ECO:0000269|PubMed:11815631"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:4KFV"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:4KFV"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4KFV"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:4KFV"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4KFV"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:4KFV"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4KFV"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:4KFV"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4KFV"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:4KFV"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4KFV"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:4KFV"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4KFV"
SQ SEQUENCE 451 AA; 47673 MW; 5B38FADF2E255EA3 CRC64;
MGLGASSEQP AGGEGFHLHG VQENSPAQQA GLEPYFDFII TIGHSRLNKE NDTLKALLKA
NVEKPVKLEV FNMKTMRVRE VEVVPSNMWG GQGLLGASVR FCSFRRASEH VWHVLDVEPS
SPAALAGLRP YTDYIVGSDQ ILQESEDFFT LIESHEGKPL KLMVYNSESD SCREVTVTPN
AAWGGEGSLG CGIGYGYLHR IPTQPSSQYK KPPSASSPGT PAKTPQPNAF PLGAPPPWPI
PQDSSGPELG SRQSDYMEAL PQVPGGFMEE QLPGPGSPGH GTADYGGCLH SMEIPLQPPP
PVQRVMDPGF LDVSGMSLLD SNNTSVCPSL SSSSLLTPTA VSALGPEDIG SSSSSHERGG
EATWSGSEFE ISFPDSPGSQ AQVDHLPRLT LPDGLTSAAS PEEGLSAELL EAQTEEPAHT
ASLDCMAQTE GPAGQVQAAP DPEPGLCEGP W
